data_9B4S
# 
_entry.id   9B4S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9B4S         pdb_00009b4s 10.2210/pdb9b4s/pdb 
WWPDB D_1000282603 ?            ?                   
# 
_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       2025-01-22 
# 
_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                        9B4S 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dhirendra.simanshu@nih.gov 
_pdbx_contact_author.name_first         Dhirendra 
_pdbx_contact_author.name_last          Simanshu 
_pdbx_contact_author.name_mi            K 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9717-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Czyzyk, D.J.'   1 ? 
'Simanshu, D.K.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                525 
_citation.page_last                 525 
_citation.title                     
'Structural insights into isoform-specific RAS-PI3K alpha interactions and the role of RAS in PI3K alpha activation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55766-x 
_citation.pdbx_database_id_PubMed   39788953 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Czyzyk, D.'     1  0000-0002-2398-5784 
primary 'Yan, W.'        2  ?                   
primary 'Messing, S.'    3  0000-0001-8991-2097 
primary 'Gillette, W.'   4  ?                   
primary 'Tsuji, T.'      5  ?                   
primary 'Yamaguchi, M.'  6  ?                   
primary 'Furuzono, S.'   7  ?                   
primary 'Turner, D.M.'   8  ?                   
primary 'Esposito, D.'   9  0000-0002-9987-1687 
primary 'Nissley, D.V.'  10 0000-0001-7523-116X 
primary 'McCormick, F.'  11 0000-0002-6619-7120 
primary 'Simanshu, D.K.' 12 0000-0002-9717-4618 
# 
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 'Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform' 112033.430 1 
2.7.1.137,2.7.1.153,2.7.11.1 'W1057A, I1058A, F1059A' ? ? 
2 polymer     man 'Ras-related protein R-Ras2' 20557.266  1 3.6.5.-                      Q36A                     ? ? 
3 non-polymer syn 
'(2S)-2-({2-[1-(propan-2-yl)-1H-1,2,4-triazol-5-yl]-5,6-dihydroimidazo[1,2-d][1,4]benzoxazepin-9-yl}oxy)propanamide' 382.416    1 
?                            ?                        ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196    1 ?                            ?                        
? ? 
5 non-polymer syn 'MAGNESIUM ION' 24.305     1 ?                            ?                        ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;PI3-kinase subunit alpha,PI3K-alpha,PI3Kalpha,PtdIns-3-kinase subunit alpha,Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha,PtdIns-3-kinase subunit p110-alpha,p110alpha,Phosphoinositide 3-kinase alpha,Phosphoinositide-3-kinase catalytic alpha polypeptide,Serine/threonine protein kinase PIK3CA
;
2 'Ras-like protein TC21,Teratocarcinoma oncogene' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYN
KLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLE
KYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATY
VNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLA
WGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSRE
AGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQM
YCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRI
GHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPD
FMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENI
WQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAG
YCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEM
CYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDAAAHTIK
QHALN
;
;GVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYN
KLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLE
KYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATY
VNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLA
WGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSRE
AGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQM
YCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRI
GHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPD
FMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENI
WQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAG
YCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEM
CYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDAAAHTIK
QHALN
;
A ? 
2 'polypeptide(L)' no no 
;GMAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIASYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMR
EQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAK
IRMNVDQAFHELVRVIRKFQ
;
;GMAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIASYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMR
EQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAK
IRMNVDQAFHELVRVIRKFQ
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(2S)-2-({2-[1-(propan-2-yl)-1H-1,2,4-triazol-5-yl]-5,6-dihydroimidazo[1,2-d][1,4]benzoxazepin-9-yl}oxy)propanamide' 5H5 
4 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                                                                        GNP 
5 'MAGNESIUM ION'                                                                                                      MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   VAL n 
1 3   GLY n 
1 4   ASN n 
1 5   ARG n 
1 6   GLU n 
1 7   GLU n 
1 8   LYS n 
1 9   ILE n 
1 10  LEU n 
1 11  ASN n 
1 12  ARG n 
1 13  GLU n 
1 14  ILE n 
1 15  GLY n 
1 16  PHE n 
1 17  ALA n 
1 18  ILE n 
1 19  GLY n 
1 20  MET n 
1 21  PRO n 
1 22  VAL n 
1 23  CYS n 
1 24  GLU n 
1 25  PHE n 
1 26  ASP n 
1 27  MET n 
1 28  VAL n 
1 29  LYS n 
1 30  ASP n 
1 31  PRO n 
1 32  GLU n 
1 33  VAL n 
1 34  GLN n 
1 35  ASP n 
1 36  PHE n 
1 37  ARG n 
1 38  ARG n 
1 39  ASN n 
1 40  ILE n 
1 41  LEU n 
1 42  ASN n 
1 43  VAL n 
1 44  CYS n 
1 45  LYS n 
1 46  GLU n 
1 47  ALA n 
1 48  VAL n 
1 49  ASP n 
1 50  LEU n 
1 51  ARG n 
1 52  ASP n 
1 53  LEU n 
1 54  ASN n 
1 55  SER n 
1 56  PRO n 
1 57  HIS n 
1 58  SER n 
1 59  ARG n 
1 60  ALA n 
1 61  MET n 
1 62  TYR n 
1 63  VAL n 
1 64  TYR n 
1 65  PRO n 
1 66  PRO n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  SER n 
1 71  SER n 
1 72  PRO n 
1 73  GLU n 
1 74  LEU n 
1 75  PRO n 
1 76  LYS n 
1 77  HIS n 
1 78  ILE n 
1 79  TYR n 
1 80  ASN n 
1 81  LYS n 
1 82  LEU n 
1 83  ASP n 
1 84  LYS n 
1 85  GLY n 
1 86  GLN n 
1 87  ILE n 
1 88  ILE n 
1 89  VAL n 
1 90  VAL n 
1 91  ILE n 
1 92  TRP n 
1 93  VAL n 
1 94  ILE n 
1 95  VAL n 
1 96  SER n 
1 97  PRO n 
1 98  ASN n 
1 99  ASN n 
1 100 ASP n 
1 101 LYS n 
1 102 GLN n 
1 103 LYS n 
1 104 TYR n 
1 105 THR n 
1 106 LEU n 
1 107 LYS n 
1 108 ILE n 
1 109 ASN n 
1 110 HIS n 
1 111 ASP n 
1 112 CYS n 
1 113 VAL n 
1 114 PRO n 
1 115 GLU n 
1 116 GLN n 
1 117 VAL n 
1 118 ILE n 
1 119 ALA n 
1 120 GLU n 
1 121 ALA n 
1 122 ILE n 
1 123 ARG n 
1 124 LYS n 
1 125 LYS n 
1 126 THR n 
1 127 ARG n 
1 128 SER n 
1 129 MET n 
1 130 LEU n 
1 131 LEU n 
1 132 SER n 
1 133 SER n 
1 134 GLU n 
1 135 GLN n 
1 136 LEU n 
1 137 LYS n 
1 138 LEU n 
1 139 CYS n 
1 140 VAL n 
1 141 LEU n 
1 142 GLU n 
1 143 TYR n 
1 144 GLN n 
1 145 GLY n 
1 146 LYS n 
1 147 TYR n 
1 148 ILE n 
1 149 LEU n 
1 150 LYS n 
1 151 VAL n 
1 152 CYS n 
1 153 GLY n 
1 154 CYS n 
1 155 ASP n 
1 156 GLU n 
1 157 TYR n 
1 158 PHE n 
1 159 LEU n 
1 160 GLU n 
1 161 LYS n 
1 162 TYR n 
1 163 PRO n 
1 164 LEU n 
1 165 SER n 
1 166 GLN n 
1 167 TYR n 
1 168 LYS n 
1 169 TYR n 
1 170 ILE n 
1 171 ARG n 
1 172 SER n 
1 173 CYS n 
1 174 ILE n 
1 175 MET n 
1 176 LEU n 
1 177 GLY n 
1 178 ARG n 
1 179 MET n 
1 180 PRO n 
1 181 ASN n 
1 182 LEU n 
1 183 MET n 
1 184 LEU n 
1 185 MET n 
1 186 ALA n 
1 187 LYS n 
1 188 GLU n 
1 189 SER n 
1 190 LEU n 
1 191 TYR n 
1 192 SER n 
1 193 GLN n 
1 194 LEU n 
1 195 PRO n 
1 196 MET n 
1 197 ASP n 
1 198 CYS n 
1 199 PHE n 
1 200 THR n 
1 201 MET n 
1 202 PRO n 
1 203 SER n 
1 204 TYR n 
1 205 SER n 
1 206 ARG n 
1 207 ARG n 
1 208 ILE n 
1 209 SER n 
1 210 THR n 
1 211 ALA n 
1 212 THR n 
1 213 PRO n 
1 214 TYR n 
1 215 MET n 
1 216 ASN n 
1 217 GLY n 
1 218 GLU n 
1 219 THR n 
1 220 SER n 
1 221 THR n 
1 222 LYS n 
1 223 SER n 
1 224 LEU n 
1 225 TRP n 
1 226 VAL n 
1 227 ILE n 
1 228 ASN n 
1 229 SER n 
1 230 ALA n 
1 231 LEU n 
1 232 ARG n 
1 233 ILE n 
1 234 LYS n 
1 235 ILE n 
1 236 LEU n 
1 237 CYS n 
1 238 ALA n 
1 239 THR n 
1 240 TYR n 
1 241 VAL n 
1 242 ASN n 
1 243 VAL n 
1 244 ASN n 
1 245 ILE n 
1 246 ARG n 
1 247 ASP n 
1 248 ILE n 
1 249 ASP n 
1 250 LYS n 
1 251 ILE n 
1 252 TYR n 
1 253 VAL n 
1 254 ARG n 
1 255 THR n 
1 256 GLY n 
1 257 ILE n 
1 258 TYR n 
1 259 HIS n 
1 260 GLY n 
1 261 GLY n 
1 262 GLU n 
1 263 PRO n 
1 264 LEU n 
1 265 CYS n 
1 266 ASP n 
1 267 ASN n 
1 268 VAL n 
1 269 ASN n 
1 270 THR n 
1 271 GLN n 
1 272 ARG n 
1 273 VAL n 
1 274 PRO n 
1 275 CYS n 
1 276 SER n 
1 277 ASN n 
1 278 PRO n 
1 279 ARG n 
1 280 TRP n 
1 281 ASN n 
1 282 GLU n 
1 283 TRP n 
1 284 LEU n 
1 285 ASN n 
1 286 TYR n 
1 287 ASP n 
1 288 ILE n 
1 289 TYR n 
1 290 ILE n 
1 291 PRO n 
1 292 ASP n 
1 293 LEU n 
1 294 PRO n 
1 295 ARG n 
1 296 ALA n 
1 297 ALA n 
1 298 ARG n 
1 299 LEU n 
1 300 CYS n 
1 301 LEU n 
1 302 SER n 
1 303 ILE n 
1 304 CYS n 
1 305 SER n 
1 306 VAL n 
1 307 LYS n 
1 308 GLY n 
1 309 ARG n 
1 310 LYS n 
1 311 GLY n 
1 312 ALA n 
1 313 LYS n 
1 314 GLU n 
1 315 GLU n 
1 316 HIS n 
1 317 CYS n 
1 318 PRO n 
1 319 LEU n 
1 320 ALA n 
1 321 TRP n 
1 322 GLY n 
1 323 ASN n 
1 324 ILE n 
1 325 ASN n 
1 326 LEU n 
1 327 PHE n 
1 328 ASP n 
1 329 TYR n 
1 330 THR n 
1 331 ASP n 
1 332 THR n 
1 333 LEU n 
1 334 VAL n 
1 335 SER n 
1 336 GLY n 
1 337 LYS n 
1 338 MET n 
1 339 ALA n 
1 340 LEU n 
1 341 ASN n 
1 342 LEU n 
1 343 TRP n 
1 344 PRO n 
1 345 VAL n 
1 346 PRO n 
1 347 HIS n 
1 348 GLY n 
1 349 LEU n 
1 350 GLU n 
1 351 ASP n 
1 352 LEU n 
1 353 LEU n 
1 354 ASN n 
1 355 PRO n 
1 356 ILE n 
1 357 GLY n 
1 358 VAL n 
1 359 THR n 
1 360 GLY n 
1 361 SER n 
1 362 ASN n 
1 363 PRO n 
1 364 ASN n 
1 365 LYS n 
1 366 GLU n 
1 367 THR n 
1 368 PRO n 
1 369 CYS n 
1 370 LEU n 
1 371 GLU n 
1 372 LEU n 
1 373 GLU n 
1 374 PHE n 
1 375 ASP n 
1 376 TRP n 
1 377 PHE n 
1 378 SER n 
1 379 SER n 
1 380 VAL n 
1 381 VAL n 
1 382 LYS n 
1 383 PHE n 
1 384 PRO n 
1 385 ASP n 
1 386 MET n 
1 387 SER n 
1 388 VAL n 
1 389 ILE n 
1 390 GLU n 
1 391 GLU n 
1 392 HIS n 
1 393 ALA n 
1 394 ASN n 
1 395 TRP n 
1 396 SER n 
1 397 VAL n 
1 398 SER n 
1 399 ARG n 
1 400 GLU n 
1 401 ALA n 
1 402 GLY n 
1 403 PHE n 
1 404 SER n 
1 405 TYR n 
1 406 SER n 
1 407 HIS n 
1 408 ALA n 
1 409 GLY n 
1 410 LEU n 
1 411 SER n 
1 412 ASN n 
1 413 ARG n 
1 414 LEU n 
1 415 ALA n 
1 416 ARG n 
1 417 ASP n 
1 418 ASN n 
1 419 GLU n 
1 420 LEU n 
1 421 ARG n 
1 422 GLU n 
1 423 ASN n 
1 424 ASP n 
1 425 LYS n 
1 426 GLU n 
1 427 GLN n 
1 428 LEU n 
1 429 LYS n 
1 430 ALA n 
1 431 ILE n 
1 432 SER n 
1 433 THR n 
1 434 ARG n 
1 435 ASP n 
1 436 PRO n 
1 437 LEU n 
1 438 SER n 
1 439 GLU n 
1 440 ILE n 
1 441 THR n 
1 442 GLU n 
1 443 GLN n 
1 444 GLU n 
1 445 LYS n 
1 446 ASP n 
1 447 PHE n 
1 448 LEU n 
1 449 TRP n 
1 450 SER n 
1 451 HIS n 
1 452 ARG n 
1 453 HIS n 
1 454 TYR n 
1 455 CYS n 
1 456 VAL n 
1 457 THR n 
1 458 ILE n 
1 459 PRO n 
1 460 GLU n 
1 461 ILE n 
1 462 LEU n 
1 463 PRO n 
1 464 LYS n 
1 465 LEU n 
1 466 LEU n 
1 467 LEU n 
1 468 SER n 
1 469 VAL n 
1 470 LYS n 
1 471 TRP n 
1 472 ASN n 
1 473 SER n 
1 474 ARG n 
1 475 ASP n 
1 476 GLU n 
1 477 VAL n 
1 478 ALA n 
1 479 GLN n 
1 480 MET n 
1 481 TYR n 
1 482 CYS n 
1 483 LEU n 
1 484 VAL n 
1 485 LYS n 
1 486 ASP n 
1 487 TRP n 
1 488 PRO n 
1 489 PRO n 
1 490 ILE n 
1 491 LYS n 
1 492 PRO n 
1 493 GLU n 
1 494 GLN n 
1 495 ALA n 
1 496 MET n 
1 497 GLU n 
1 498 LEU n 
1 499 LEU n 
1 500 ASP n 
1 501 CYS n 
1 502 ASN n 
1 503 TYR n 
1 504 PRO n 
1 505 ASP n 
1 506 PRO n 
1 507 MET n 
1 508 VAL n 
1 509 ARG n 
1 510 GLY n 
1 511 PHE n 
1 512 ALA n 
1 513 VAL n 
1 514 ARG n 
1 515 CYS n 
1 516 LEU n 
1 517 GLU n 
1 518 LYS n 
1 519 TYR n 
1 520 LEU n 
1 521 THR n 
1 522 ASP n 
1 523 ASP n 
1 524 LYS n 
1 525 LEU n 
1 526 SER n 
1 527 GLN n 
1 528 TYR n 
1 529 LEU n 
1 530 ILE n 
1 531 GLN n 
1 532 LEU n 
1 533 VAL n 
1 534 GLN n 
1 535 VAL n 
1 536 LEU n 
1 537 LYS n 
1 538 TYR n 
1 539 GLU n 
1 540 GLN n 
1 541 TYR n 
1 542 LEU n 
1 543 ASP n 
1 544 ASN n 
1 545 LEU n 
1 546 LEU n 
1 547 VAL n 
1 548 ARG n 
1 549 PHE n 
1 550 LEU n 
1 551 LEU n 
1 552 LYS n 
1 553 LYS n 
1 554 ALA n 
1 555 LEU n 
1 556 THR n 
1 557 ASN n 
1 558 GLN n 
1 559 ARG n 
1 560 ILE n 
1 561 GLY n 
1 562 HIS n 
1 563 PHE n 
1 564 PHE n 
1 565 PHE n 
1 566 TRP n 
1 567 HIS n 
1 568 LEU n 
1 569 LYS n 
1 570 SER n 
1 571 GLU n 
1 572 MET n 
1 573 HIS n 
1 574 ASN n 
1 575 LYS n 
1 576 THR n 
1 577 VAL n 
1 578 SER n 
1 579 GLN n 
1 580 ARG n 
1 581 PHE n 
1 582 GLY n 
1 583 LEU n 
1 584 LEU n 
1 585 LEU n 
1 586 GLU n 
1 587 SER n 
1 588 TYR n 
1 589 CYS n 
1 590 ARG n 
1 591 ALA n 
1 592 CYS n 
1 593 GLY n 
1 594 MET n 
1 595 TYR n 
1 596 LEU n 
1 597 LYS n 
1 598 HIS n 
1 599 LEU n 
1 600 ASN n 
1 601 ARG n 
1 602 GLN n 
1 603 VAL n 
1 604 GLU n 
1 605 ALA n 
1 606 MET n 
1 607 GLU n 
1 608 LYS n 
1 609 LEU n 
1 610 ILE n 
1 611 ASN n 
1 612 LEU n 
1 613 THR n 
1 614 ASP n 
1 615 ILE n 
1 616 LEU n 
1 617 LYS n 
1 618 GLN n 
1 619 GLU n 
1 620 LYS n 
1 621 LYS n 
1 622 ASP n 
1 623 GLU n 
1 624 THR n 
1 625 GLN n 
1 626 LYS n 
1 627 VAL n 
1 628 GLN n 
1 629 MET n 
1 630 LYS n 
1 631 PHE n 
1 632 LEU n 
1 633 VAL n 
1 634 GLU n 
1 635 GLN n 
1 636 MET n 
1 637 ARG n 
1 638 ARG n 
1 639 PRO n 
1 640 ASP n 
1 641 PHE n 
1 642 MET n 
1 643 ASP n 
1 644 ALA n 
1 645 LEU n 
1 646 GLN n 
1 647 GLY n 
1 648 PHE n 
1 649 LEU n 
1 650 SER n 
1 651 PRO n 
1 652 LEU n 
1 653 ASN n 
1 654 PRO n 
1 655 ALA n 
1 656 HIS n 
1 657 GLN n 
1 658 LEU n 
1 659 GLY n 
1 660 ASN n 
1 661 LEU n 
1 662 ARG n 
1 663 LEU n 
1 664 GLU n 
1 665 GLU n 
1 666 CYS n 
1 667 ARG n 
1 668 ILE n 
1 669 MET n 
1 670 SER n 
1 671 SER n 
1 672 ALA n 
1 673 LYS n 
1 674 ARG n 
1 675 PRO n 
1 676 LEU n 
1 677 TRP n 
1 678 LEU n 
1 679 ASN n 
1 680 TRP n 
1 681 GLU n 
1 682 ASN n 
1 683 PRO n 
1 684 ASP n 
1 685 ILE n 
1 686 MET n 
1 687 SER n 
1 688 GLU n 
1 689 LEU n 
1 690 LEU n 
1 691 PHE n 
1 692 GLN n 
1 693 ASN n 
1 694 ASN n 
1 695 GLU n 
1 696 ILE n 
1 697 ILE n 
1 698 PHE n 
1 699 LYS n 
1 700 ASN n 
1 701 GLY n 
1 702 ASP n 
1 703 ASP n 
1 704 LEU n 
1 705 ARG n 
1 706 GLN n 
1 707 ASP n 
1 708 MET n 
1 709 LEU n 
1 710 THR n 
1 711 LEU n 
1 712 GLN n 
1 713 ILE n 
1 714 ILE n 
1 715 ARG n 
1 716 ILE n 
1 717 MET n 
1 718 GLU n 
1 719 ASN n 
1 720 ILE n 
1 721 TRP n 
1 722 GLN n 
1 723 ASN n 
1 724 GLN n 
1 725 GLY n 
1 726 LEU n 
1 727 ASP n 
1 728 LEU n 
1 729 ARG n 
1 730 MET n 
1 731 LEU n 
1 732 PRO n 
1 733 TYR n 
1 734 GLY n 
1 735 CYS n 
1 736 LEU n 
1 737 SER n 
1 738 ILE n 
1 739 GLY n 
1 740 ASP n 
1 741 CYS n 
1 742 VAL n 
1 743 GLY n 
1 744 LEU n 
1 745 ILE n 
1 746 GLU n 
1 747 VAL n 
1 748 VAL n 
1 749 ARG n 
1 750 ASN n 
1 751 SER n 
1 752 HIS n 
1 753 THR n 
1 754 ILE n 
1 755 MET n 
1 756 GLN n 
1 757 ILE n 
1 758 GLN n 
1 759 CYS n 
1 760 LYS n 
1 761 GLY n 
1 762 GLY n 
1 763 LEU n 
1 764 LYS n 
1 765 GLY n 
1 766 ALA n 
1 767 LEU n 
1 768 GLN n 
1 769 PHE n 
1 770 ASN n 
1 771 SER n 
1 772 HIS n 
1 773 THR n 
1 774 LEU n 
1 775 HIS n 
1 776 GLN n 
1 777 TRP n 
1 778 LEU n 
1 779 LYS n 
1 780 ASP n 
1 781 LYS n 
1 782 ASN n 
1 783 LYS n 
1 784 GLY n 
1 785 GLU n 
1 786 ILE n 
1 787 TYR n 
1 788 ASP n 
1 789 ALA n 
1 790 ALA n 
1 791 ILE n 
1 792 ASP n 
1 793 LEU n 
1 794 PHE n 
1 795 THR n 
1 796 ARG n 
1 797 SER n 
1 798 CYS n 
1 799 ALA n 
1 800 GLY n 
1 801 TYR n 
1 802 CYS n 
1 803 VAL n 
1 804 ALA n 
1 805 THR n 
1 806 PHE n 
1 807 ILE n 
1 808 LEU n 
1 809 GLY n 
1 810 ILE n 
1 811 GLY n 
1 812 ASP n 
1 813 ARG n 
1 814 HIS n 
1 815 ASN n 
1 816 SER n 
1 817 ASN n 
1 818 ILE n 
1 819 MET n 
1 820 VAL n 
1 821 LYS n 
1 822 ASP n 
1 823 ASP n 
1 824 GLY n 
1 825 GLN n 
1 826 LEU n 
1 827 PHE n 
1 828 HIS n 
1 829 ILE n 
1 830 ASP n 
1 831 PHE n 
1 832 GLY n 
1 833 HIS n 
1 834 PHE n 
1 835 LEU n 
1 836 ASP n 
1 837 HIS n 
1 838 LYS n 
1 839 LYS n 
1 840 LYS n 
1 841 LYS n 
1 842 PHE n 
1 843 GLY n 
1 844 TYR n 
1 845 LYS n 
1 846 ARG n 
1 847 GLU n 
1 848 ARG n 
1 849 VAL n 
1 850 PRO n 
1 851 PHE n 
1 852 VAL n 
1 853 LEU n 
1 854 THR n 
1 855 GLN n 
1 856 ASP n 
1 857 PHE n 
1 858 LEU n 
1 859 ILE n 
1 860 VAL n 
1 861 ILE n 
1 862 SER n 
1 863 LYS n 
1 864 GLY n 
1 865 ALA n 
1 866 GLN n 
1 867 GLU n 
1 868 CYS n 
1 869 THR n 
1 870 LYS n 
1 871 THR n 
1 872 ARG n 
1 873 GLU n 
1 874 PHE n 
1 875 GLU n 
1 876 ARG n 
1 877 PHE n 
1 878 GLN n 
1 879 GLU n 
1 880 MET n 
1 881 CYS n 
1 882 TYR n 
1 883 LYS n 
1 884 ALA n 
1 885 TYR n 
1 886 LEU n 
1 887 ALA n 
1 888 ILE n 
1 889 ARG n 
1 890 GLN n 
1 891 HIS n 
1 892 ALA n 
1 893 ASN n 
1 894 LEU n 
1 895 PHE n 
1 896 ILE n 
1 897 ASN n 
1 898 LEU n 
1 899 PHE n 
1 900 SER n 
1 901 MET n 
1 902 MET n 
1 903 LEU n 
1 904 GLY n 
1 905 SER n 
1 906 GLY n 
1 907 MET n 
1 908 PRO n 
1 909 GLU n 
1 910 LEU n 
1 911 GLN n 
1 912 SER n 
1 913 PHE n 
1 914 ASP n 
1 915 ASP n 
1 916 ILE n 
1 917 ALA n 
1 918 TYR n 
1 919 ILE n 
1 920 ARG n 
1 921 LYS n 
1 922 THR n 
1 923 LEU n 
1 924 ALA n 
1 925 LEU n 
1 926 ASP n 
1 927 LYS n 
1 928 THR n 
1 929 GLU n 
1 930 GLN n 
1 931 GLU n 
1 932 ALA n 
1 933 LEU n 
1 934 GLU n 
1 935 TYR n 
1 936 PHE n 
1 937 MET n 
1 938 LYS n 
1 939 GLN n 
1 940 MET n 
1 941 ASN n 
1 942 ASP n 
1 943 ALA n 
1 944 HIS n 
1 945 HIS n 
1 946 GLY n 
1 947 GLY n 
1 948 TRP n 
1 949 THR n 
1 950 THR n 
1 951 LYS n 
1 952 MET n 
1 953 ASP n 
1 954 ALA n 
1 955 ALA n 
1 956 ALA n 
1 957 HIS n 
1 958 THR n 
1 959 ILE n 
1 960 LYS n 
1 961 GLN n 
1 962 HIS n 
1 963 ALA n 
1 964 LEU n 
1 965 ASN n 
2 1   GLY n 
2 2   MET n 
2 3   ALA n 
2 4   ALA n 
2 5   ALA n 
2 6   GLY n 
2 7   TRP n 
2 8   ARG n 
2 9   ASP n 
2 10  GLY n 
2 11  SER n 
2 12  GLY n 
2 13  GLN n 
2 14  GLU n 
2 15  LYS n 
2 16  TYR n 
2 17  ARG n 
2 18  LEU n 
2 19  VAL n 
2 20  VAL n 
2 21  VAL n 
2 22  GLY n 
2 23  GLY n 
2 24  GLY n 
2 25  GLY n 
2 26  VAL n 
2 27  GLY n 
2 28  LYS n 
2 29  SER n 
2 30  ALA n 
2 31  LEU n 
2 32  THR n 
2 33  ILE n 
2 34  GLN n 
2 35  PHE n 
2 36  ILE n 
2 37  ALA n 
2 38  SER n 
2 39  TYR n 
2 40  PHE n 
2 41  VAL n 
2 42  THR n 
2 43  ASP n 
2 44  TYR n 
2 45  ASP n 
2 46  PRO n 
2 47  THR n 
2 48  ILE n 
2 49  GLU n 
2 50  ASP n 
2 51  SER n 
2 52  TYR n 
2 53  THR n 
2 54  LYS n 
2 55  GLN n 
2 56  CYS n 
2 57  VAL n 
2 58  ILE n 
2 59  ASP n 
2 60  ASP n 
2 61  ARG n 
2 62  ALA n 
2 63  ALA n 
2 64  ARG n 
2 65  LEU n 
2 66  ASP n 
2 67  ILE n 
2 68  LEU n 
2 69  ASP n 
2 70  THR n 
2 71  ALA n 
2 72  GLY n 
2 73  GLN n 
2 74  GLU n 
2 75  GLU n 
2 76  PHE n 
2 77  GLY n 
2 78  ALA n 
2 79  MET n 
2 80  ARG n 
2 81  GLU n 
2 82  GLN n 
2 83  TYR n 
2 84  MET n 
2 85  ARG n 
2 86  THR n 
2 87  GLY n 
2 88  GLU n 
2 89  GLY n 
2 90  PHE n 
2 91  LEU n 
2 92  LEU n 
2 93  VAL n 
2 94  PHE n 
2 95  SER n 
2 96  VAL n 
2 97  THR n 
2 98  ASP n 
2 99  ARG n 
2 100 GLY n 
2 101 SER n 
2 102 PHE n 
2 103 GLU n 
2 104 GLU n 
2 105 ILE n 
2 106 TYR n 
2 107 LYS n 
2 108 PHE n 
2 109 GLN n 
2 110 ARG n 
2 111 GLN n 
2 112 ILE n 
2 113 LEU n 
2 114 ARG n 
2 115 VAL n 
2 116 LYS n 
2 117 ASP n 
2 118 ARG n 
2 119 ASP n 
2 120 GLU n 
2 121 PHE n 
2 122 PRO n 
2 123 MET n 
2 124 ILE n 
2 125 LEU n 
2 126 ILE n 
2 127 GLY n 
2 128 ASN n 
2 129 LYS n 
2 130 ALA n 
2 131 ASP n 
2 132 LEU n 
2 133 ASP n 
2 134 HIS n 
2 135 GLN n 
2 136 ARG n 
2 137 GLN n 
2 138 VAL n 
2 139 THR n 
2 140 GLN n 
2 141 GLU n 
2 142 GLU n 
2 143 GLY n 
2 144 GLN n 
2 145 GLN n 
2 146 LEU n 
2 147 ALA n 
2 148 ARG n 
2 149 GLN n 
2 150 LEU n 
2 151 LYS n 
2 152 VAL n 
2 153 THR n 
2 154 TYR n 
2 155 MET n 
2 156 GLU n 
2 157 ALA n 
2 158 SER n 
2 159 ALA n 
2 160 LYS n 
2 161 ILE n 
2 162 ARG n 
2 163 MET n 
2 164 ASN n 
2 165 VAL n 
2 166 ASP n 
2 167 GLN n 
2 168 ALA n 
2 169 PHE n 
2 170 HIS n 
2 171 GLU n 
2 172 LEU n 
2 173 VAL n 
2 174 ARG n 
2 175 VAL n 
2 176 ILE n 
2 177 ARG n 
2 178 LYS n 
2 179 PHE n 
2 180 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 965 human ? PIK3CA        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? Trichoplacea 3043702 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 180 human ? 'RRAS2, TC21' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? Trichoplacea 3043702 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
5H5 non-polymer         . 
'(2S)-2-({2-[1-(propan-2-yl)-1H-1,2,4-triazol-5-yl]-5,6-dihydroimidazo[1,2-d][1,4]benzoxazepin-9-yl}oxy)propanamide' GDC-0326 
'C19 H22 N6 O3'     382.416 
ALA 'L-peptide linking' y ALANINE ?        'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?        'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?        'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?        'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?        'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?        'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?        'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?        'C2 H5 N O2'        75.067  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ?        'C10 H17 N6 O13 P3' 522.196 
HIS 'L-peptide linking' y HISTIDINE ?        'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE ?        'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?        'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?        'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?        'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?        'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?        'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?        'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?        'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?        'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?        'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?        'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?        'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   104  ?    ?   ?   A . n 
A 1 2   VAL 2   105  ?    ?   ?   A . n 
A 1 3   GLY 3   106  ?    ?   ?   A . n 
A 1 4   ASN 4   107  107  ASN ASN A . n 
A 1 5   ARG 5   108  108  ARG ARG A . n 
A 1 6   GLU 6   109  109  GLU GLU A . n 
A 1 7   GLU 7   110  110  GLU GLU A . n 
A 1 8   LYS 8   111  111  LYS LYS A . n 
A 1 9   ILE 9   112  112  ILE ILE A . n 
A 1 10  LEU 10  113  113  LEU LEU A . n 
A 1 11  ASN 11  114  114  ASN ASN A . n 
A 1 12  ARG 12  115  115  ARG ARG A . n 
A 1 13  GLU 13  116  116  GLU GLU A . n 
A 1 14  ILE 14  117  117  ILE ILE A . n 
A 1 15  GLY 15  118  118  GLY GLY A . n 
A 1 16  PHE 16  119  119  PHE PHE A . n 
A 1 17  ALA 17  120  120  ALA ALA A . n 
A 1 18  ILE 18  121  121  ILE ILE A . n 
A 1 19  GLY 19  122  122  GLY GLY A . n 
A 1 20  MET 20  123  123  MET MET A . n 
A 1 21  PRO 21  124  124  PRO PRO A . n 
A 1 22  VAL 22  125  125  VAL VAL A . n 
A 1 23  CYS 23  126  126  CYS CYS A . n 
A 1 24  GLU 24  127  127  GLU GLU A . n 
A 1 25  PHE 25  128  128  PHE PHE A . n 
A 1 26  ASP 26  129  129  ASP ASP A . n 
A 1 27  MET 27  130  130  MET MET A . n 
A 1 28  VAL 28  131  131  VAL VAL A . n 
A 1 29  LYS 29  132  132  LYS LYS A . n 
A 1 30  ASP 30  133  133  ASP ASP A . n 
A 1 31  PRO 31  134  134  PRO PRO A . n 
A 1 32  GLU 32  135  135  GLU GLU A . n 
A 1 33  VAL 33  136  136  VAL VAL A . n 
A 1 34  GLN 34  137  137  GLN GLN A . n 
A 1 35  ASP 35  138  138  ASP ASP A . n 
A 1 36  PHE 36  139  139  PHE PHE A . n 
A 1 37  ARG 37  140  140  ARG ARG A . n 
A 1 38  ARG 38  141  141  ARG ARG A . n 
A 1 39  ASN 39  142  142  ASN ASN A . n 
A 1 40  ILE 40  143  143  ILE ILE A . n 
A 1 41  LEU 41  144  144  LEU LEU A . n 
A 1 42  ASN 42  145  145  ASN ASN A . n 
A 1 43  VAL 43  146  146  VAL VAL A . n 
A 1 44  CYS 44  147  147  CYS CYS A . n 
A 1 45  LYS 45  148  148  LYS LYS A . n 
A 1 46  GLU 46  149  149  GLU GLU A . n 
A 1 47  ALA 47  150  150  ALA ALA A . n 
A 1 48  VAL 48  151  151  VAL VAL A . n 
A 1 49  ASP 49  152  152  ASP ASP A . n 
A 1 50  LEU 50  153  153  LEU LEU A . n 
A 1 51  ARG 51  154  154  ARG ARG A . n 
A 1 52  ASP 52  155  155  ASP ASP A . n 
A 1 53  LEU 53  156  156  LEU LEU A . n 
A 1 54  ASN 54  157  157  ASN ASN A . n 
A 1 55  SER 55  158  158  SER SER A . n 
A 1 56  PRO 56  159  159  PRO PRO A . n 
A 1 57  HIS 57  160  160  HIS HIS A . n 
A 1 58  SER 58  161  161  SER SER A . n 
A 1 59  ARG 59  162  162  ARG ARG A . n 
A 1 60  ALA 60  163  163  ALA ALA A . n 
A 1 61  MET 61  164  164  MET MET A . n 
A 1 62  TYR 62  165  165  TYR TYR A . n 
A 1 63  VAL 63  166  166  VAL VAL A . n 
A 1 64  TYR 64  167  167  TYR TYR A . n 
A 1 65  PRO 65  168  168  PRO PRO A . n 
A 1 66  PRO 66  169  169  PRO PRO A . n 
A 1 67  ASN 67  170  170  ASN ASN A . n 
A 1 68  VAL 68  171  171  VAL VAL A . n 
A 1 69  GLU 69  172  172  GLU GLU A . n 
A 1 70  SER 70  173  173  SER SER A . n 
A 1 71  SER 71  174  174  SER SER A . n 
A 1 72  PRO 72  175  175  PRO PRO A . n 
A 1 73  GLU 73  176  176  GLU GLU A . n 
A 1 74  LEU 74  177  177  LEU LEU A . n 
A 1 75  PRO 75  178  178  PRO PRO A . n 
A 1 76  LYS 76  179  179  LYS LYS A . n 
A 1 77  HIS 77  180  180  HIS HIS A . n 
A 1 78  ILE 78  181  181  ILE ILE A . n 
A 1 79  TYR 79  182  182  TYR TYR A . n 
A 1 80  ASN 80  183  183  ASN ASN A . n 
A 1 81  LYS 81  184  184  LYS LYS A . n 
A 1 82  LEU 82  185  185  LEU LEU A . n 
A 1 83  ASP 83  186  186  ASP ASP A . n 
A 1 84  LYS 84  187  187  LYS LYS A . n 
A 1 85  GLY 85  188  188  GLY GLY A . n 
A 1 86  GLN 86  189  189  GLN GLN A . n 
A 1 87  ILE 87  190  190  ILE ILE A . n 
A 1 88  ILE 88  191  191  ILE ILE A . n 
A 1 89  VAL 89  192  192  VAL VAL A . n 
A 1 90  VAL 90  193  193  VAL VAL A . n 
A 1 91  ILE 91  194  194  ILE ILE A . n 
A 1 92  TRP 92  195  195  TRP TRP A . n 
A 1 93  VAL 93  196  196  VAL VAL A . n 
A 1 94  ILE 94  197  197  ILE ILE A . n 
A 1 95  VAL 95  198  198  VAL VAL A . n 
A 1 96  SER 96  199  199  SER SER A . n 
A 1 97  PRO 97  200  200  PRO PRO A . n 
A 1 98  ASN 98  201  201  ASN ASN A . n 
A 1 99  ASN 99  202  202  ASN ASN A . n 
A 1 100 ASP 100 203  203  ASP ASP A . n 
A 1 101 LYS 101 204  204  LYS LYS A . n 
A 1 102 GLN 102 205  205  GLN GLN A . n 
A 1 103 LYS 103 206  206  LYS LYS A . n 
A 1 104 TYR 104 207  207  TYR TYR A . n 
A 1 105 THR 105 208  208  THR THR A . n 
A 1 106 LEU 106 209  209  LEU LEU A . n 
A 1 107 LYS 107 210  210  LYS LYS A . n 
A 1 108 ILE 108 211  211  ILE ILE A . n 
A 1 109 ASN 109 212  212  ASN ASN A . n 
A 1 110 HIS 110 213  213  HIS HIS A . n 
A 1 111 ASP 111 214  214  ASP ASP A . n 
A 1 112 CYS 112 215  215  CYS CYS A . n 
A 1 113 VAL 113 216  216  VAL VAL A . n 
A 1 114 PRO 114 217  217  PRO PRO A . n 
A 1 115 GLU 115 218  218  GLU GLU A . n 
A 1 116 GLN 116 219  219  GLN GLN A . n 
A 1 117 VAL 117 220  220  VAL VAL A . n 
A 1 118 ILE 118 221  221  ILE ILE A . n 
A 1 119 ALA 119 222  222  ALA ALA A . n 
A 1 120 GLU 120 223  223  GLU GLU A . n 
A 1 121 ALA 121 224  224  ALA ALA A . n 
A 1 122 ILE 122 225  225  ILE ILE A . n 
A 1 123 ARG 123 226  226  ARG ARG A . n 
A 1 124 LYS 124 227  227  LYS LYS A . n 
A 1 125 LYS 125 228  228  LYS LYS A . n 
A 1 126 THR 126 229  229  THR THR A . n 
A 1 127 ARG 127 230  230  ARG ARG A . n 
A 1 128 SER 128 231  231  SER SER A . n 
A 1 129 MET 129 232  232  MET MET A . n 
A 1 130 LEU 130 233  233  LEU LEU A . n 
A 1 131 LEU 131 234  234  LEU LEU A . n 
A 1 132 SER 132 235  235  SER SER A . n 
A 1 133 SER 133 236  236  SER SER A . n 
A 1 134 GLU 134 237  237  GLU GLU A . n 
A 1 135 GLN 135 238  238  GLN GLN A . n 
A 1 136 LEU 136 239  239  LEU LEU A . n 
A 1 137 LYS 137 240  240  LYS LYS A . n 
A 1 138 LEU 138 241  241  LEU LEU A . n 
A 1 139 CYS 139 242  242  CYS CYS A . n 
A 1 140 VAL 140 243  243  VAL VAL A . n 
A 1 141 LEU 141 244  244  LEU LEU A . n 
A 1 142 GLU 142 245  245  GLU GLU A . n 
A 1 143 TYR 143 246  246  TYR TYR A . n 
A 1 144 GLN 144 247  247  GLN GLN A . n 
A 1 145 GLY 145 248  248  GLY GLY A . n 
A 1 146 LYS 146 249  249  LYS LYS A . n 
A 1 147 TYR 147 250  250  TYR TYR A . n 
A 1 148 ILE 148 251  251  ILE ILE A . n 
A 1 149 LEU 149 252  252  LEU LEU A . n 
A 1 150 LYS 150 253  253  LYS LYS A . n 
A 1 151 VAL 151 254  254  VAL VAL A . n 
A 1 152 CYS 152 255  255  CYS CYS A . n 
A 1 153 GLY 153 256  256  GLY GLY A . n 
A 1 154 CYS 154 257  257  CYS CYS A . n 
A 1 155 ASP 155 258  258  ASP ASP A . n 
A 1 156 GLU 156 259  259  GLU GLU A . n 
A 1 157 TYR 157 260  260  TYR TYR A . n 
A 1 158 PHE 158 261  261  PHE PHE A . n 
A 1 159 LEU 159 262  262  LEU LEU A . n 
A 1 160 GLU 160 263  263  GLU GLU A . n 
A 1 161 LYS 161 264  264  LYS LYS A . n 
A 1 162 TYR 162 265  265  TYR TYR A . n 
A 1 163 PRO 163 266  266  PRO PRO A . n 
A 1 164 LEU 164 267  267  LEU LEU A . n 
A 1 165 SER 165 268  268  SER SER A . n 
A 1 166 GLN 166 269  269  GLN GLN A . n 
A 1 167 TYR 167 270  270  TYR TYR A . n 
A 1 168 LYS 168 271  271  LYS LYS A . n 
A 1 169 TYR 169 272  272  TYR TYR A . n 
A 1 170 ILE 170 273  273  ILE ILE A . n 
A 1 171 ARG 171 274  274  ARG ARG A . n 
A 1 172 SER 172 275  275  SER SER A . n 
A 1 173 CYS 173 276  276  CYS CYS A . n 
A 1 174 ILE 174 277  277  ILE ILE A . n 
A 1 175 MET 175 278  278  MET MET A . n 
A 1 176 LEU 176 279  279  LEU LEU A . n 
A 1 177 GLY 177 280  280  GLY GLY A . n 
A 1 178 ARG 178 281  281  ARG ARG A . n 
A 1 179 MET 179 282  282  MET MET A . n 
A 1 180 PRO 180 283  283  PRO PRO A . n 
A 1 181 ASN 181 284  284  ASN ASN A . n 
A 1 182 LEU 182 285  285  LEU LEU A . n 
A 1 183 MET 183 286  286  MET MET A . n 
A 1 184 LEU 184 287  287  LEU LEU A . n 
A 1 185 MET 185 288  288  MET MET A . n 
A 1 186 ALA 186 289  289  ALA ALA A . n 
A 1 187 LYS 187 290  290  LYS LYS A . n 
A 1 188 GLU 188 291  291  GLU GLU A . n 
A 1 189 SER 189 292  292  SER SER A . n 
A 1 190 LEU 190 293  293  LEU LEU A . n 
A 1 191 TYR 191 294  294  TYR TYR A . n 
A 1 192 SER 192 295  295  SER SER A . n 
A 1 193 GLN 193 296  296  GLN GLN A . n 
A 1 194 LEU 194 297  297  LEU LEU A . n 
A 1 195 PRO 195 298  298  PRO PRO A . n 
A 1 196 MET 196 299  299  MET MET A . n 
A 1 197 ASP 197 300  300  ASP ASP A . n 
A 1 198 CYS 198 301  301  CYS CYS A . n 
A 1 199 PHE 199 302  302  PHE PHE A . n 
A 1 200 THR 200 303  303  THR THR A . n 
A 1 201 MET 201 304  304  MET MET A . n 
A 1 202 PRO 202 305  305  PRO PRO A . n 
A 1 203 SER 203 306  306  SER SER A . n 
A 1 204 TYR 204 307  307  TYR TYR A . n 
A 1 205 SER 205 308  308  SER SER A . n 
A 1 206 ARG 206 309  309  ARG ARG A . n 
A 1 207 ARG 207 310  310  ARG ARG A . n 
A 1 208 ILE 208 311  ?    ?   ?   A . n 
A 1 209 SER 209 312  ?    ?   ?   A . n 
A 1 210 THR 210 313  ?    ?   ?   A . n 
A 1 211 ALA 211 314  ?    ?   ?   A . n 
A 1 212 THR 212 315  ?    ?   ?   A . n 
A 1 213 PRO 213 316  ?    ?   ?   A . n 
A 1 214 TYR 214 317  ?    ?   ?   A . n 
A 1 215 MET 215 318  ?    ?   ?   A . n 
A 1 216 ASN 216 319  ?    ?   ?   A . n 
A 1 217 GLY 217 320  ?    ?   ?   A . n 
A 1 218 GLU 218 321  ?    ?   ?   A . n 
A 1 219 THR 219 322  ?    ?   ?   A . n 
A 1 220 SER 220 323  323  SER SER A . n 
A 1 221 THR 221 324  324  THR THR A . n 
A 1 222 LYS 222 325  325  LYS LYS A . n 
A 1 223 SER 223 326  326  SER SER A . n 
A 1 224 LEU 224 327  327  LEU LEU A . n 
A 1 225 TRP 225 328  328  TRP TRP A . n 
A 1 226 VAL 226 329  329  VAL VAL A . n 
A 1 227 ILE 227 330  330  ILE ILE A . n 
A 1 228 ASN 228 331  331  ASN ASN A . n 
A 1 229 SER 229 332  332  SER SER A . n 
A 1 230 ALA 230 333  333  ALA ALA A . n 
A 1 231 LEU 231 334  334  LEU LEU A . n 
A 1 232 ARG 232 335  335  ARG ARG A . n 
A 1 233 ILE 233 336  336  ILE ILE A . n 
A 1 234 LYS 234 337  337  LYS LYS A . n 
A 1 235 ILE 235 338  338  ILE ILE A . n 
A 1 236 LEU 236 339  339  LEU LEU A . n 
A 1 237 CYS 237 340  340  CYS CYS A . n 
A 1 238 ALA 238 341  341  ALA ALA A . n 
A 1 239 THR 239 342  342  THR THR A . n 
A 1 240 TYR 240 343  343  TYR TYR A . n 
A 1 241 VAL 241 344  ?    ?   ?   A . n 
A 1 242 ASN 242 345  ?    ?   ?   A . n 
A 1 243 VAL 243 346  ?    ?   ?   A . n 
A 1 244 ASN 244 347  ?    ?   ?   A . n 
A 1 245 ILE 245 348  ?    ?   ?   A . n 
A 1 246 ARG 246 349  ?    ?   ?   A . n 
A 1 247 ASP 247 350  ?    ?   ?   A . n 
A 1 248 ILE 248 351  ?    ?   ?   A . n 
A 1 249 ASP 249 352  ?    ?   ?   A . n 
A 1 250 LYS 250 353  353  LYS LYS A . n 
A 1 251 ILE 251 354  354  ILE ILE A . n 
A 1 252 TYR 252 355  355  TYR TYR A . n 
A 1 253 VAL 253 356  356  VAL VAL A . n 
A 1 254 ARG 254 357  357  ARG ARG A . n 
A 1 255 THR 255 358  358  THR THR A . n 
A 1 256 GLY 256 359  359  GLY GLY A . n 
A 1 257 ILE 257 360  360  ILE ILE A . n 
A 1 258 TYR 258 361  361  TYR TYR A . n 
A 1 259 HIS 259 362  362  HIS HIS A . n 
A 1 260 GLY 260 363  363  GLY GLY A . n 
A 1 261 GLY 261 364  364  GLY GLY A . n 
A 1 262 GLU 262 365  365  GLU GLU A . n 
A 1 263 PRO 263 366  366  PRO PRO A . n 
A 1 264 LEU 264 367  367  LEU LEU A . n 
A 1 265 CYS 265 368  368  CYS CYS A . n 
A 1 266 ASP 266 369  369  ASP ASP A . n 
A 1 267 ASN 267 370  370  ASN ASN A . n 
A 1 268 VAL 268 371  371  VAL VAL A . n 
A 1 269 ASN 269 372  372  ASN ASN A . n 
A 1 270 THR 270 373  373  THR THR A . n 
A 1 271 GLN 271 374  374  GLN GLN A . n 
A 1 272 ARG 272 375  375  ARG ARG A . n 
A 1 273 VAL 273 376  376  VAL VAL A . n 
A 1 274 PRO 274 377  377  PRO PRO A . n 
A 1 275 CYS 275 378  378  CYS CYS A . n 
A 1 276 SER 276 379  379  SER SER A . n 
A 1 277 ASN 277 380  380  ASN ASN A . n 
A 1 278 PRO 278 381  381  PRO PRO A . n 
A 1 279 ARG 279 382  382  ARG ARG A . n 
A 1 280 TRP 280 383  383  TRP TRP A . n 
A 1 281 ASN 281 384  384  ASN ASN A . n 
A 1 282 GLU 282 385  385  GLU GLU A . n 
A 1 283 TRP 283 386  386  TRP TRP A . n 
A 1 284 LEU 284 387  387  LEU LEU A . n 
A 1 285 ASN 285 388  388  ASN ASN A . n 
A 1 286 TYR 286 389  389  TYR TYR A . n 
A 1 287 ASP 287 390  390  ASP ASP A . n 
A 1 288 ILE 288 391  391  ILE ILE A . n 
A 1 289 TYR 289 392  392  TYR TYR A . n 
A 1 290 ILE 290 393  393  ILE ILE A . n 
A 1 291 PRO 291 394  394  PRO PRO A . n 
A 1 292 ASP 292 395  395  ASP ASP A . n 
A 1 293 LEU 293 396  396  LEU LEU A . n 
A 1 294 PRO 294 397  397  PRO PRO A . n 
A 1 295 ARG 295 398  398  ARG ARG A . n 
A 1 296 ALA 296 399  399  ALA ALA A . n 
A 1 297 ALA 297 400  400  ALA ALA A . n 
A 1 298 ARG 298 401  401  ARG ARG A . n 
A 1 299 LEU 299 402  402  LEU LEU A . n 
A 1 300 CYS 300 403  403  CYS CYS A . n 
A 1 301 LEU 301 404  404  LEU LEU A . n 
A 1 302 SER 302 405  405  SER SER A . n 
A 1 303 ILE 303 406  406  ILE ILE A . n 
A 1 304 CYS 304 407  407  CYS CYS A . n 
A 1 305 SER 305 408  408  SER SER A . n 
A 1 306 VAL 306 409  409  VAL VAL A . n 
A 1 307 LYS 307 410  410  LYS LYS A . n 
A 1 308 GLY 308 411  ?    ?   ?   A . n 
A 1 309 ARG 309 412  ?    ?   ?   A . n 
A 1 310 LYS 310 413  ?    ?   ?   A . n 
A 1 311 GLY 311 414  ?    ?   ?   A . n 
A 1 312 ALA 312 415  ?    ?   ?   A . n 
A 1 313 LYS 313 416  416  LYS LYS A . n 
A 1 314 GLU 314 417  417  GLU GLU A . n 
A 1 315 GLU 315 418  418  GLU GLU A . n 
A 1 316 HIS 316 419  419  HIS HIS A . n 
A 1 317 CYS 317 420  420  CYS CYS A . n 
A 1 318 PRO 318 421  421  PRO PRO A . n 
A 1 319 LEU 319 422  422  LEU LEU A . n 
A 1 320 ALA 320 423  423  ALA ALA A . n 
A 1 321 TRP 321 424  424  TRP TRP A . n 
A 1 322 GLY 322 425  425  GLY GLY A . n 
A 1 323 ASN 323 426  426  ASN ASN A . n 
A 1 324 ILE 324 427  427  ILE ILE A . n 
A 1 325 ASN 325 428  428  ASN ASN A . n 
A 1 326 LEU 326 429  429  LEU LEU A . n 
A 1 327 PHE 327 430  430  PHE PHE A . n 
A 1 328 ASP 328 431  431  ASP ASP A . n 
A 1 329 TYR 329 432  432  TYR TYR A . n 
A 1 330 THR 330 433  433  THR THR A . n 
A 1 331 ASP 331 434  434  ASP ASP A . n 
A 1 332 THR 332 435  435  THR THR A . n 
A 1 333 LEU 333 436  436  LEU LEU A . n 
A 1 334 VAL 334 437  437  VAL VAL A . n 
A 1 335 SER 335 438  438  SER SER A . n 
A 1 336 GLY 336 439  439  GLY GLY A . n 
A 1 337 LYS 337 440  440  LYS LYS A . n 
A 1 338 MET 338 441  441  MET MET A . n 
A 1 339 ALA 339 442  442  ALA ALA A . n 
A 1 340 LEU 340 443  443  LEU LEU A . n 
A 1 341 ASN 341 444  444  ASN ASN A . n 
A 1 342 LEU 342 445  445  LEU LEU A . n 
A 1 343 TRP 343 446  446  TRP TRP A . n 
A 1 344 PRO 344 447  447  PRO PRO A . n 
A 1 345 VAL 345 448  448  VAL VAL A . n 
A 1 346 PRO 346 449  449  PRO PRO A . n 
A 1 347 HIS 347 450  450  HIS HIS A . n 
A 1 348 GLY 348 451  451  GLY GLY A . n 
A 1 349 LEU 349 452  452  LEU LEU A . n 
A 1 350 GLU 350 453  453  GLU GLU A . n 
A 1 351 ASP 351 454  454  ASP ASP A . n 
A 1 352 LEU 352 455  455  LEU LEU A . n 
A 1 353 LEU 353 456  456  LEU LEU A . n 
A 1 354 ASN 354 457  457  ASN ASN A . n 
A 1 355 PRO 355 458  458  PRO PRO A . n 
A 1 356 ILE 356 459  459  ILE ILE A . n 
A 1 357 GLY 357 460  460  GLY GLY A . n 
A 1 358 VAL 358 461  461  VAL VAL A . n 
A 1 359 THR 359 462  462  THR THR A . n 
A 1 360 GLY 360 463  463  GLY GLY A . n 
A 1 361 SER 361 464  464  SER SER A . n 
A 1 362 ASN 362 465  465  ASN ASN A . n 
A 1 363 PRO 363 466  466  PRO PRO A . n 
A 1 364 ASN 364 467  467  ASN ASN A . n 
A 1 365 LYS 365 468  468  LYS LYS A . n 
A 1 366 GLU 366 469  469  GLU GLU A . n 
A 1 367 THR 367 470  470  THR THR A . n 
A 1 368 PRO 368 471  471  PRO PRO A . n 
A 1 369 CYS 369 472  472  CYS CYS A . n 
A 1 370 LEU 370 473  473  LEU LEU A . n 
A 1 371 GLU 371 474  474  GLU GLU A . n 
A 1 372 LEU 372 475  475  LEU LEU A . n 
A 1 373 GLU 373 476  476  GLU GLU A . n 
A 1 374 PHE 374 477  477  PHE PHE A . n 
A 1 375 ASP 375 478  478  ASP ASP A . n 
A 1 376 TRP 376 479  479  TRP TRP A . n 
A 1 377 PHE 377 480  480  PHE PHE A . n 
A 1 378 SER 378 481  481  SER SER A . n 
A 1 379 SER 379 482  482  SER SER A . n 
A 1 380 VAL 380 483  483  VAL VAL A . n 
A 1 381 VAL 381 484  484  VAL VAL A . n 
A 1 382 LYS 382 485  485  LYS LYS A . n 
A 1 383 PHE 383 486  486  PHE PHE A . n 
A 1 384 PRO 384 487  487  PRO PRO A . n 
A 1 385 ASP 385 488  488  ASP ASP A . n 
A 1 386 MET 386 489  489  MET MET A . n 
A 1 387 SER 387 490  490  SER SER A . n 
A 1 388 VAL 388 491  491  VAL VAL A . n 
A 1 389 ILE 389 492  492  ILE ILE A . n 
A 1 390 GLU 390 493  493  GLU GLU A . n 
A 1 391 GLU 391 494  494  GLU GLU A . n 
A 1 392 HIS 392 495  495  HIS HIS A . n 
A 1 393 ALA 393 496  496  ALA ALA A . n 
A 1 394 ASN 394 497  497  ASN ASN A . n 
A 1 395 TRP 395 498  498  TRP TRP A . n 
A 1 396 SER 396 499  499  SER SER A . n 
A 1 397 VAL 397 500  500  VAL VAL A . n 
A 1 398 SER 398 501  501  SER SER A . n 
A 1 399 ARG 399 502  502  ARG ARG A . n 
A 1 400 GLU 400 503  503  GLU GLU A . n 
A 1 401 ALA 401 504  ?    ?   ?   A . n 
A 1 402 GLY 402 505  ?    ?   ?   A . n 
A 1 403 PHE 403 506  ?    ?   ?   A . n 
A 1 404 SER 404 507  ?    ?   ?   A . n 
A 1 405 TYR 405 508  ?    ?   ?   A . n 
A 1 406 SER 406 509  ?    ?   ?   A . n 
A 1 407 HIS 407 510  ?    ?   ?   A . n 
A 1 408 ALA 408 511  ?    ?   ?   A . n 
A 1 409 GLY 409 512  ?    ?   ?   A . n 
A 1 410 LEU 410 513  ?    ?   ?   A . n 
A 1 411 SER 411 514  ?    ?   ?   A . n 
A 1 412 ASN 412 515  ?    ?   ?   A . n 
A 1 413 ARG 413 516  ?    ?   ?   A . n 
A 1 414 LEU 414 517  ?    ?   ?   A . n 
A 1 415 ALA 415 518  ?    ?   ?   A . n 
A 1 416 ARG 416 519  ?    ?   ?   A . n 
A 1 417 ASP 417 520  ?    ?   ?   A . n 
A 1 418 ASN 418 521  ?    ?   ?   A . n 
A 1 419 GLU 419 522  ?    ?   ?   A . n 
A 1 420 LEU 420 523  523  LEU LEU A . n 
A 1 421 ARG 421 524  524  ARG ARG A . n 
A 1 422 GLU 422 525  525  GLU GLU A . n 
A 1 423 ASN 423 526  526  ASN ASN A . n 
A 1 424 ASP 424 527  527  ASP ASP A . n 
A 1 425 LYS 425 528  528  LYS LYS A . n 
A 1 426 GLU 426 529  529  GLU GLU A . n 
A 1 427 GLN 427 530  530  GLN GLN A . n 
A 1 428 LEU 428 531  531  LEU LEU A . n 
A 1 429 LYS 429 532  532  LYS LYS A . n 
A 1 430 ALA 430 533  533  ALA ALA A . n 
A 1 431 ILE 431 534  534  ILE ILE A . n 
A 1 432 SER 432 535  535  SER SER A . n 
A 1 433 THR 433 536  536  THR THR A . n 
A 1 434 ARG 434 537  537  ARG ARG A . n 
A 1 435 ASP 435 538  538  ASP ASP A . n 
A 1 436 PRO 436 539  539  PRO PRO A . n 
A 1 437 LEU 437 540  540  LEU LEU A . n 
A 1 438 SER 438 541  541  SER SER A . n 
A 1 439 GLU 439 542  542  GLU GLU A . n 
A 1 440 ILE 440 543  543  ILE ILE A . n 
A 1 441 THR 441 544  544  THR THR A . n 
A 1 442 GLU 442 545  545  GLU GLU A . n 
A 1 443 GLN 443 546  546  GLN GLN A . n 
A 1 444 GLU 444 547  547  GLU GLU A . n 
A 1 445 LYS 445 548  548  LYS LYS A . n 
A 1 446 ASP 446 549  549  ASP ASP A . n 
A 1 447 PHE 447 550  550  PHE PHE A . n 
A 1 448 LEU 448 551  551  LEU LEU A . n 
A 1 449 TRP 449 552  552  TRP TRP A . n 
A 1 450 SER 450 553  553  SER SER A . n 
A 1 451 HIS 451 554  554  HIS HIS A . n 
A 1 452 ARG 452 555  555  ARG ARG A . n 
A 1 453 HIS 453 556  556  HIS HIS A . n 
A 1 454 TYR 454 557  557  TYR TYR A . n 
A 1 455 CYS 455 558  558  CYS CYS A . n 
A 1 456 VAL 456 559  559  VAL VAL A . n 
A 1 457 THR 457 560  560  THR THR A . n 
A 1 458 ILE 458 561  561  ILE ILE A . n 
A 1 459 PRO 459 562  562  PRO PRO A . n 
A 1 460 GLU 460 563  563  GLU GLU A . n 
A 1 461 ILE 461 564  564  ILE ILE A . n 
A 1 462 LEU 462 565  565  LEU LEU A . n 
A 1 463 PRO 463 566  566  PRO PRO A . n 
A 1 464 LYS 464 567  567  LYS LYS A . n 
A 1 465 LEU 465 568  568  LEU LEU A . n 
A 1 466 LEU 466 569  569  LEU LEU A . n 
A 1 467 LEU 467 570  570  LEU LEU A . n 
A 1 468 SER 468 571  571  SER SER A . n 
A 1 469 VAL 469 572  572  VAL VAL A . n 
A 1 470 LYS 470 573  573  LYS LYS A . n 
A 1 471 TRP 471 574  574  TRP TRP A . n 
A 1 472 ASN 472 575  575  ASN ASN A . n 
A 1 473 SER 473 576  576  SER SER A . n 
A 1 474 ARG 474 577  577  ARG ARG A . n 
A 1 475 ASP 475 578  578  ASP ASP A . n 
A 1 476 GLU 476 579  579  GLU GLU A . n 
A 1 477 VAL 477 580  580  VAL VAL A . n 
A 1 478 ALA 478 581  581  ALA ALA A . n 
A 1 479 GLN 479 582  582  GLN GLN A . n 
A 1 480 MET 480 583  583  MET MET A . n 
A 1 481 TYR 481 584  584  TYR TYR A . n 
A 1 482 CYS 482 585  585  CYS CYS A . n 
A 1 483 LEU 483 586  586  LEU LEU A . n 
A 1 484 VAL 484 587  587  VAL VAL A . n 
A 1 485 LYS 485 588  588  LYS LYS A . n 
A 1 486 ASP 486 589  589  ASP ASP A . n 
A 1 487 TRP 487 590  590  TRP TRP A . n 
A 1 488 PRO 488 591  591  PRO PRO A . n 
A 1 489 PRO 489 592  592  PRO PRO A . n 
A 1 490 ILE 490 593  593  ILE ILE A . n 
A 1 491 LYS 491 594  594  LYS LYS A . n 
A 1 492 PRO 492 595  595  PRO PRO A . n 
A 1 493 GLU 493 596  596  GLU GLU A . n 
A 1 494 GLN 494 597  597  GLN GLN A . n 
A 1 495 ALA 495 598  598  ALA ALA A . n 
A 1 496 MET 496 599  599  MET MET A . n 
A 1 497 GLU 497 600  600  GLU GLU A . n 
A 1 498 LEU 498 601  601  LEU LEU A . n 
A 1 499 LEU 499 602  602  LEU LEU A . n 
A 1 500 ASP 500 603  603  ASP ASP A . n 
A 1 501 CYS 501 604  604  CYS CYS A . n 
A 1 502 ASN 502 605  605  ASN ASN A . n 
A 1 503 TYR 503 606  606  TYR TYR A . n 
A 1 504 PRO 504 607  607  PRO PRO A . n 
A 1 505 ASP 505 608  608  ASP ASP A . n 
A 1 506 PRO 506 609  609  PRO PRO A . n 
A 1 507 MET 507 610  610  MET MET A . n 
A 1 508 VAL 508 611  611  VAL VAL A . n 
A 1 509 ARG 509 612  612  ARG ARG A . n 
A 1 510 GLY 510 613  613  GLY GLY A . n 
A 1 511 PHE 511 614  614  PHE PHE A . n 
A 1 512 ALA 512 615  615  ALA ALA A . n 
A 1 513 VAL 513 616  616  VAL VAL A . n 
A 1 514 ARG 514 617  617  ARG ARG A . n 
A 1 515 CYS 515 618  618  CYS CYS A . n 
A 1 516 LEU 516 619  619  LEU LEU A . n 
A 1 517 GLU 517 620  620  GLU GLU A . n 
A 1 518 LYS 518 621  621  LYS LYS A . n 
A 1 519 TYR 519 622  622  TYR TYR A . n 
A 1 520 LEU 520 623  623  LEU LEU A . n 
A 1 521 THR 521 624  624  THR THR A . n 
A 1 522 ASP 522 625  625  ASP ASP A . n 
A 1 523 ASP 523 626  626  ASP ASP A . n 
A 1 524 LYS 524 627  627  LYS LYS A . n 
A 1 525 LEU 525 628  628  LEU LEU A . n 
A 1 526 SER 526 629  629  SER SER A . n 
A 1 527 GLN 527 630  630  GLN GLN A . n 
A 1 528 TYR 528 631  631  TYR TYR A . n 
A 1 529 LEU 529 632  632  LEU LEU A . n 
A 1 530 ILE 530 633  633  ILE ILE A . n 
A 1 531 GLN 531 634  634  GLN GLN A . n 
A 1 532 LEU 532 635  635  LEU LEU A . n 
A 1 533 VAL 533 636  636  VAL VAL A . n 
A 1 534 GLN 534 637  637  GLN GLN A . n 
A 1 535 VAL 535 638  638  VAL VAL A . n 
A 1 536 LEU 536 639  639  LEU LEU A . n 
A 1 537 LYS 537 640  640  LYS LYS A . n 
A 1 538 TYR 538 641  641  TYR TYR A . n 
A 1 539 GLU 539 642  642  GLU GLU A . n 
A 1 540 GLN 540 643  643  GLN GLN A . n 
A 1 541 TYR 541 644  644  TYR TYR A . n 
A 1 542 LEU 542 645  645  LEU LEU A . n 
A 1 543 ASP 543 646  646  ASP ASP A . n 
A 1 544 ASN 544 647  647  ASN ASN A . n 
A 1 545 LEU 545 648  648  LEU LEU A . n 
A 1 546 LEU 546 649  649  LEU LEU A . n 
A 1 547 VAL 547 650  650  VAL VAL A . n 
A 1 548 ARG 548 651  651  ARG ARG A . n 
A 1 549 PHE 549 652  652  PHE PHE A . n 
A 1 550 LEU 550 653  653  LEU LEU A . n 
A 1 551 LEU 551 654  654  LEU LEU A . n 
A 1 552 LYS 552 655  655  LYS LYS A . n 
A 1 553 LYS 553 656  656  LYS LYS A . n 
A 1 554 ALA 554 657  657  ALA ALA A . n 
A 1 555 LEU 555 658  658  LEU LEU A . n 
A 1 556 THR 556 659  659  THR THR A . n 
A 1 557 ASN 557 660  660  ASN ASN A . n 
A 1 558 GLN 558 661  661  GLN GLN A . n 
A 1 559 ARG 559 662  662  ARG ARG A . n 
A 1 560 ILE 560 663  663  ILE ILE A . n 
A 1 561 GLY 561 664  664  GLY GLY A . n 
A 1 562 HIS 562 665  665  HIS HIS A . n 
A 1 563 PHE 563 666  666  PHE PHE A . n 
A 1 564 PHE 564 667  667  PHE PHE A . n 
A 1 565 PHE 565 668  668  PHE PHE A . n 
A 1 566 TRP 566 669  669  TRP TRP A . n 
A 1 567 HIS 567 670  670  HIS HIS A . n 
A 1 568 LEU 568 671  671  LEU LEU A . n 
A 1 569 LYS 569 672  672  LYS LYS A . n 
A 1 570 SER 570 673  673  SER SER A . n 
A 1 571 GLU 571 674  674  GLU GLU A . n 
A 1 572 MET 572 675  675  MET MET A . n 
A 1 573 HIS 573 676  676  HIS HIS A . n 
A 1 574 ASN 574 677  677  ASN ASN A . n 
A 1 575 LYS 575 678  678  LYS LYS A . n 
A 1 576 THR 576 679  679  THR THR A . n 
A 1 577 VAL 577 680  680  VAL VAL A . n 
A 1 578 SER 578 681  681  SER SER A . n 
A 1 579 GLN 579 682  682  GLN GLN A . n 
A 1 580 ARG 580 683  683  ARG ARG A . n 
A 1 581 PHE 581 684  684  PHE PHE A . n 
A 1 582 GLY 582 685  685  GLY GLY A . n 
A 1 583 LEU 583 686  686  LEU LEU A . n 
A 1 584 LEU 584 687  687  LEU LEU A . n 
A 1 585 LEU 585 688  688  LEU LEU A . n 
A 1 586 GLU 586 689  689  GLU GLU A . n 
A 1 587 SER 587 690  690  SER SER A . n 
A 1 588 TYR 588 691  691  TYR TYR A . n 
A 1 589 CYS 589 692  692  CYS CYS A . n 
A 1 590 ARG 590 693  693  ARG ARG A . n 
A 1 591 ALA 591 694  694  ALA ALA A . n 
A 1 592 CYS 592 695  695  CYS CYS A . n 
A 1 593 GLY 593 696  696  GLY GLY A . n 
A 1 594 MET 594 697  697  MET MET A . n 
A 1 595 TYR 595 698  698  TYR TYR A . n 
A 1 596 LEU 596 699  699  LEU LEU A . n 
A 1 597 LYS 597 700  700  LYS LYS A . n 
A 1 598 HIS 598 701  701  HIS HIS A . n 
A 1 599 LEU 599 702  702  LEU LEU A . n 
A 1 600 ASN 600 703  703  ASN ASN A . n 
A 1 601 ARG 601 704  704  ARG ARG A . n 
A 1 602 GLN 602 705  705  GLN GLN A . n 
A 1 603 VAL 603 706  706  VAL VAL A . n 
A 1 604 GLU 604 707  707  GLU GLU A . n 
A 1 605 ALA 605 708  708  ALA ALA A . n 
A 1 606 MET 606 709  709  MET MET A . n 
A 1 607 GLU 607 710  710  GLU GLU A . n 
A 1 608 LYS 608 711  711  LYS LYS A . n 
A 1 609 LEU 609 712  712  LEU LEU A . n 
A 1 610 ILE 610 713  713  ILE ILE A . n 
A 1 611 ASN 611 714  714  ASN ASN A . n 
A 1 612 LEU 612 715  715  LEU LEU A . n 
A 1 613 THR 613 716  716  THR THR A . n 
A 1 614 ASP 614 717  717  ASP ASP A . n 
A 1 615 ILE 615 718  718  ILE ILE A . n 
A 1 616 LEU 616 719  719  LEU LEU A . n 
A 1 617 LYS 617 720  720  LYS LYS A . n 
A 1 618 GLN 618 721  721  GLN GLN A . n 
A 1 619 GLU 619 722  722  GLU GLU A . n 
A 1 620 LYS 620 723  723  LYS LYS A . n 
A 1 621 LYS 621 724  724  LYS LYS A . n 
A 1 622 ASP 622 725  725  ASP ASP A . n 
A 1 623 GLU 623 726  726  GLU GLU A . n 
A 1 624 THR 624 727  727  THR THR A . n 
A 1 625 GLN 625 728  728  GLN GLN A . n 
A 1 626 LYS 626 729  729  LYS LYS A . n 
A 1 627 VAL 627 730  730  VAL VAL A . n 
A 1 628 GLN 628 731  731  GLN GLN A . n 
A 1 629 MET 629 732  732  MET MET A . n 
A 1 630 LYS 630 733  733  LYS LYS A . n 
A 1 631 PHE 631 734  734  PHE PHE A . n 
A 1 632 LEU 632 735  735  LEU LEU A . n 
A 1 633 VAL 633 736  736  VAL VAL A . n 
A 1 634 GLU 634 737  737  GLU GLU A . n 
A 1 635 GLN 635 738  738  GLN GLN A . n 
A 1 636 MET 636 739  739  MET MET A . n 
A 1 637 ARG 637 740  740  ARG ARG A . n 
A 1 638 ARG 638 741  741  ARG ARG A . n 
A 1 639 PRO 639 742  742  PRO PRO A . n 
A 1 640 ASP 640 743  743  ASP ASP A . n 
A 1 641 PHE 641 744  744  PHE PHE A . n 
A 1 642 MET 642 745  745  MET MET A . n 
A 1 643 ASP 643 746  746  ASP ASP A . n 
A 1 644 ALA 644 747  747  ALA ALA A . n 
A 1 645 LEU 645 748  748  LEU LEU A . n 
A 1 646 GLN 646 749  749  GLN GLN A . n 
A 1 647 GLY 647 750  750  GLY GLY A . n 
A 1 648 PHE 648 751  751  PHE PHE A . n 
A 1 649 LEU 649 752  752  LEU LEU A . n 
A 1 650 SER 650 753  753  SER SER A . n 
A 1 651 PRO 651 754  754  PRO PRO A . n 
A 1 652 LEU 652 755  755  LEU LEU A . n 
A 1 653 ASN 653 756  756  ASN ASN A . n 
A 1 654 PRO 654 757  757  PRO PRO A . n 
A 1 655 ALA 655 758  758  ALA ALA A . n 
A 1 656 HIS 656 759  759  HIS HIS A . n 
A 1 657 GLN 657 760  760  GLN GLN A . n 
A 1 658 LEU 658 761  761  LEU LEU A . n 
A 1 659 GLY 659 762  762  GLY GLY A . n 
A 1 660 ASN 660 763  763  ASN ASN A . n 
A 1 661 LEU 661 764  764  LEU LEU A . n 
A 1 662 ARG 662 765  765  ARG ARG A . n 
A 1 663 LEU 663 766  766  LEU LEU A . n 
A 1 664 GLU 664 767  767  GLU GLU A . n 
A 1 665 GLU 665 768  768  GLU GLU A . n 
A 1 666 CYS 666 769  769  CYS CYS A . n 
A 1 667 ARG 667 770  770  ARG ARG A . n 
A 1 668 ILE 668 771  771  ILE ILE A . n 
A 1 669 MET 669 772  772  MET MET A . n 
A 1 670 SER 670 773  773  SER SER A . n 
A 1 671 SER 671 774  774  SER SER A . n 
A 1 672 ALA 672 775  775  ALA ALA A . n 
A 1 673 LYS 673 776  776  LYS LYS A . n 
A 1 674 ARG 674 777  777  ARG ARG A . n 
A 1 675 PRO 675 778  778  PRO PRO A . n 
A 1 676 LEU 676 779  779  LEU LEU A . n 
A 1 677 TRP 677 780  780  TRP TRP A . n 
A 1 678 LEU 678 781  781  LEU LEU A . n 
A 1 679 ASN 679 782  782  ASN ASN A . n 
A 1 680 TRP 680 783  783  TRP TRP A . n 
A 1 681 GLU 681 784  784  GLU GLU A . n 
A 1 682 ASN 682 785  785  ASN ASN A . n 
A 1 683 PRO 683 786  786  PRO PRO A . n 
A 1 684 ASP 684 787  787  ASP ASP A . n 
A 1 685 ILE 685 788  788  ILE ILE A . n 
A 1 686 MET 686 789  789  MET MET A . n 
A 1 687 SER 687 790  790  SER SER A . n 
A 1 688 GLU 688 791  791  GLU GLU A . n 
A 1 689 LEU 689 792  792  LEU LEU A . n 
A 1 690 LEU 690 793  793  LEU LEU A . n 
A 1 691 PHE 691 794  794  PHE PHE A . n 
A 1 692 GLN 692 795  795  GLN GLN A . n 
A 1 693 ASN 693 796  796  ASN ASN A . n 
A 1 694 ASN 694 797  797  ASN ASN A . n 
A 1 695 GLU 695 798  798  GLU GLU A . n 
A 1 696 ILE 696 799  799  ILE ILE A . n 
A 1 697 ILE 697 800  800  ILE ILE A . n 
A 1 698 PHE 698 801  801  PHE PHE A . n 
A 1 699 LYS 699 802  802  LYS LYS A . n 
A 1 700 ASN 700 803  803  ASN ASN A . n 
A 1 701 GLY 701 804  804  GLY GLY A . n 
A 1 702 ASP 702 805  805  ASP ASP A . n 
A 1 703 ASP 703 806  806  ASP ASP A . n 
A 1 704 LEU 704 807  807  LEU LEU A . n 
A 1 705 ARG 705 808  808  ARG ARG A . n 
A 1 706 GLN 706 809  809  GLN GLN A . n 
A 1 707 ASP 707 810  810  ASP ASP A . n 
A 1 708 MET 708 811  811  MET MET A . n 
A 1 709 LEU 709 812  812  LEU LEU A . n 
A 1 710 THR 710 813  813  THR THR A . n 
A 1 711 LEU 711 814  814  LEU LEU A . n 
A 1 712 GLN 712 815  815  GLN GLN A . n 
A 1 713 ILE 713 816  816  ILE ILE A . n 
A 1 714 ILE 714 817  817  ILE ILE A . n 
A 1 715 ARG 715 818  818  ARG ARG A . n 
A 1 716 ILE 716 819  819  ILE ILE A . n 
A 1 717 MET 717 820  820  MET MET A . n 
A 1 718 GLU 718 821  821  GLU GLU A . n 
A 1 719 ASN 719 822  822  ASN ASN A . n 
A 1 720 ILE 720 823  823  ILE ILE A . n 
A 1 721 TRP 721 824  824  TRP TRP A . n 
A 1 722 GLN 722 825  825  GLN GLN A . n 
A 1 723 ASN 723 826  826  ASN ASN A . n 
A 1 724 GLN 724 827  827  GLN GLN A . n 
A 1 725 GLY 725 828  828  GLY GLY A . n 
A 1 726 LEU 726 829  829  LEU LEU A . n 
A 1 727 ASP 727 830  830  ASP ASP A . n 
A 1 728 LEU 728 831  831  LEU LEU A . n 
A 1 729 ARG 729 832  832  ARG ARG A . n 
A 1 730 MET 730 833  833  MET MET A . n 
A 1 731 LEU 731 834  834  LEU LEU A . n 
A 1 732 PRO 732 835  835  PRO PRO A . n 
A 1 733 TYR 733 836  836  TYR TYR A . n 
A 1 734 GLY 734 837  837  GLY GLY A . n 
A 1 735 CYS 735 838  838  CYS CYS A . n 
A 1 736 LEU 736 839  839  LEU LEU A . n 
A 1 737 SER 737 840  840  SER SER A . n 
A 1 738 ILE 738 841  841  ILE ILE A . n 
A 1 739 GLY 739 842  842  GLY GLY A . n 
A 1 740 ASP 740 843  843  ASP ASP A . n 
A 1 741 CYS 741 844  844  CYS CYS A . n 
A 1 742 VAL 742 845  845  VAL VAL A . n 
A 1 743 GLY 743 846  846  GLY GLY A . n 
A 1 744 LEU 744 847  847  LEU LEU A . n 
A 1 745 ILE 745 848  848  ILE ILE A . n 
A 1 746 GLU 746 849  849  GLU GLU A . n 
A 1 747 VAL 747 850  850  VAL VAL A . n 
A 1 748 VAL 748 851  851  VAL VAL A . n 
A 1 749 ARG 749 852  852  ARG ARG A . n 
A 1 750 ASN 750 853  853  ASN ASN A . n 
A 1 751 SER 751 854  854  SER SER A . n 
A 1 752 HIS 752 855  855  HIS HIS A . n 
A 1 753 THR 753 856  856  THR THR A . n 
A 1 754 ILE 754 857  857  ILE ILE A . n 
A 1 755 MET 755 858  858  MET MET A . n 
A 1 756 GLN 756 859  859  GLN GLN A . n 
A 1 757 ILE 757 860  860  ILE ILE A . n 
A 1 758 GLN 758 861  861  GLN GLN A . n 
A 1 759 CYS 759 862  862  CYS CYS A . n 
A 1 760 LYS 760 863  ?    ?   ?   A . n 
A 1 761 GLY 761 864  ?    ?   ?   A . n 
A 1 762 GLY 762 865  ?    ?   ?   A . n 
A 1 763 LEU 763 866  ?    ?   ?   A . n 
A 1 764 LYS 764 867  ?    ?   ?   A . n 
A 1 765 GLY 765 868  ?    ?   ?   A . n 
A 1 766 ALA 766 869  ?    ?   ?   A . n 
A 1 767 LEU 767 870  ?    ?   ?   A . n 
A 1 768 GLN 768 871  ?    ?   ?   A . n 
A 1 769 PHE 769 872  872  PHE PHE A . n 
A 1 770 ASN 770 873  873  ASN ASN A . n 
A 1 771 SER 771 874  874  SER SER A . n 
A 1 772 HIS 772 875  875  HIS HIS A . n 
A 1 773 THR 773 876  876  THR THR A . n 
A 1 774 LEU 774 877  877  LEU LEU A . n 
A 1 775 HIS 775 878  878  HIS HIS A . n 
A 1 776 GLN 776 879  879  GLN GLN A . n 
A 1 777 TRP 777 880  880  TRP TRP A . n 
A 1 778 LEU 778 881  881  LEU LEU A . n 
A 1 779 LYS 779 882  882  LYS LYS A . n 
A 1 780 ASP 780 883  883  ASP ASP A . n 
A 1 781 LYS 781 884  884  LYS LYS A . n 
A 1 782 ASN 782 885  885  ASN ASN A . n 
A 1 783 LYS 783 886  886  LYS LYS A . n 
A 1 784 GLY 784 887  887  GLY GLY A . n 
A 1 785 GLU 785 888  888  GLU GLU A . n 
A 1 786 ILE 786 889  889  ILE ILE A . n 
A 1 787 TYR 787 890  890  TYR TYR A . n 
A 1 788 ASP 788 891  891  ASP ASP A . n 
A 1 789 ALA 789 892  892  ALA ALA A . n 
A 1 790 ALA 790 893  893  ALA ALA A . n 
A 1 791 ILE 791 894  894  ILE ILE A . n 
A 1 792 ASP 792 895  895  ASP ASP A . n 
A 1 793 LEU 793 896  896  LEU LEU A . n 
A 1 794 PHE 794 897  897  PHE PHE A . n 
A 1 795 THR 795 898  898  THR THR A . n 
A 1 796 ARG 796 899  899  ARG ARG A . n 
A 1 797 SER 797 900  900  SER SER A . n 
A 1 798 CYS 798 901  901  CYS CYS A . n 
A 1 799 ALA 799 902  902  ALA ALA A . n 
A 1 800 GLY 800 903  903  GLY GLY A . n 
A 1 801 TYR 801 904  904  TYR TYR A . n 
A 1 802 CYS 802 905  905  CYS CYS A . n 
A 1 803 VAL 803 906  906  VAL VAL A . n 
A 1 804 ALA 804 907  907  ALA ALA A . n 
A 1 805 THR 805 908  908  THR THR A . n 
A 1 806 PHE 806 909  909  PHE PHE A . n 
A 1 807 ILE 807 910  910  ILE ILE A . n 
A 1 808 LEU 808 911  911  LEU LEU A . n 
A 1 809 GLY 809 912  912  GLY GLY A . n 
A 1 810 ILE 810 913  913  ILE ILE A . n 
A 1 811 GLY 811 914  914  GLY GLY A . n 
A 1 812 ASP 812 915  915  ASP ASP A . n 
A 1 813 ARG 813 916  916  ARG ARG A . n 
A 1 814 HIS 814 917  917  HIS HIS A . n 
A 1 815 ASN 815 918  918  ASN ASN A . n 
A 1 816 SER 816 919  919  SER SER A . n 
A 1 817 ASN 817 920  920  ASN ASN A . n 
A 1 818 ILE 818 921  921  ILE ILE A . n 
A 1 819 MET 819 922  922  MET MET A . n 
A 1 820 VAL 820 923  923  VAL VAL A . n 
A 1 821 LYS 821 924  924  LYS LYS A . n 
A 1 822 ASP 822 925  925  ASP ASP A . n 
A 1 823 ASP 823 926  926  ASP ASP A . n 
A 1 824 GLY 824 927  927  GLY GLY A . n 
A 1 825 GLN 825 928  928  GLN GLN A . n 
A 1 826 LEU 826 929  929  LEU LEU A . n 
A 1 827 PHE 827 930  930  PHE PHE A . n 
A 1 828 HIS 828 931  931  HIS HIS A . n 
A 1 829 ILE 829 932  932  ILE ILE A . n 
A 1 830 ASP 830 933  933  ASP ASP A . n 
A 1 831 PHE 831 934  934  PHE PHE A . n 
A 1 832 GLY 832 935  935  GLY GLY A . n 
A 1 833 HIS 833 936  936  HIS HIS A . n 
A 1 834 PHE 834 937  937  PHE PHE A . n 
A 1 835 LEU 835 938  938  LEU LEU A . n 
A 1 836 ASP 836 939  939  ASP ASP A . n 
A 1 837 HIS 837 940  940  HIS HIS A . n 
A 1 838 LYS 838 941  941  LYS LYS A . n 
A 1 839 LYS 839 942  ?    ?   ?   A . n 
A 1 840 LYS 840 943  ?    ?   ?   A . n 
A 1 841 LYS 841 944  ?    ?   ?   A . n 
A 1 842 PHE 842 945  ?    ?   ?   A . n 
A 1 843 GLY 843 946  ?    ?   ?   A . n 
A 1 844 TYR 844 947  ?    ?   ?   A . n 
A 1 845 LYS 845 948  ?    ?   ?   A . n 
A 1 846 ARG 846 949  ?    ?   ?   A . n 
A 1 847 GLU 847 950  ?    ?   ?   A . n 
A 1 848 ARG 848 951  ?    ?   ?   A . n 
A 1 849 VAL 849 952  952  VAL VAL A . n 
A 1 850 PRO 850 953  953  PRO PRO A . n 
A 1 851 PHE 851 954  954  PHE PHE A . n 
A 1 852 VAL 852 955  955  VAL VAL A . n 
A 1 853 LEU 853 956  956  LEU LEU A . n 
A 1 854 THR 854 957  957  THR THR A . n 
A 1 855 GLN 855 958  958  GLN GLN A . n 
A 1 856 ASP 856 959  959  ASP ASP A . n 
A 1 857 PHE 857 960  960  PHE PHE A . n 
A 1 858 LEU 858 961  961  LEU LEU A . n 
A 1 859 ILE 859 962  962  ILE ILE A . n 
A 1 860 VAL 860 963  963  VAL VAL A . n 
A 1 861 ILE 861 964  964  ILE ILE A . n 
A 1 862 SER 862 965  965  SER SER A . n 
A 1 863 LYS 863 966  966  LYS LYS A . n 
A 1 864 GLY 864 967  967  GLY GLY A . n 
A 1 865 ALA 865 968  968  ALA ALA A . n 
A 1 866 GLN 866 969  969  GLN GLN A . n 
A 1 867 GLU 867 970  970  GLU GLU A . n 
A 1 868 CYS 868 971  971  CYS CYS A . n 
A 1 869 THR 869 972  972  THR THR A . n 
A 1 870 LYS 870 973  973  LYS LYS A . n 
A 1 871 THR 871 974  974  THR THR A . n 
A 1 872 ARG 872 975  975  ARG ARG A . n 
A 1 873 GLU 873 976  976  GLU GLU A . n 
A 1 874 PHE 874 977  977  PHE PHE A . n 
A 1 875 GLU 875 978  978  GLU GLU A . n 
A 1 876 ARG 876 979  979  ARG ARG A . n 
A 1 877 PHE 877 980  980  PHE PHE A . n 
A 1 878 GLN 878 981  981  GLN GLN A . n 
A 1 879 GLU 879 982  982  GLU GLU A . n 
A 1 880 MET 880 983  983  MET MET A . n 
A 1 881 CYS 881 984  984  CYS CYS A . n 
A 1 882 TYR 882 985  985  TYR TYR A . n 
A 1 883 LYS 883 986  986  LYS LYS A . n 
A 1 884 ALA 884 987  987  ALA ALA A . n 
A 1 885 TYR 885 988  988  TYR TYR A . n 
A 1 886 LEU 886 989  989  LEU LEU A . n 
A 1 887 ALA 887 990  990  ALA ALA A . n 
A 1 888 ILE 888 991  991  ILE ILE A . n 
A 1 889 ARG 889 992  992  ARG ARG A . n 
A 1 890 GLN 890 993  993  GLN GLN A . n 
A 1 891 HIS 891 994  994  HIS HIS A . n 
A 1 892 ALA 892 995  995  ALA ALA A . n 
A 1 893 ASN 893 996  996  ASN ASN A . n 
A 1 894 LEU 894 997  997  LEU LEU A . n 
A 1 895 PHE 895 998  998  PHE PHE A . n 
A 1 896 ILE 896 999  999  ILE ILE A . n 
A 1 897 ASN 897 1000 1000 ASN ASN A . n 
A 1 898 LEU 898 1001 1001 LEU LEU A . n 
A 1 899 PHE 899 1002 1002 PHE PHE A . n 
A 1 900 SER 900 1003 1003 SER SER A . n 
A 1 901 MET 901 1004 1004 MET MET A . n 
A 1 902 MET 902 1005 1005 MET MET A . n 
A 1 903 LEU 903 1006 1006 LEU LEU A . n 
A 1 904 GLY 904 1007 1007 GLY GLY A . n 
A 1 905 SER 905 1008 1008 SER SER A . n 
A 1 906 GLY 906 1009 1009 GLY GLY A . n 
A 1 907 MET 907 1010 1010 MET MET A . n 
A 1 908 PRO 908 1011 1011 PRO PRO A . n 
A 1 909 GLU 909 1012 1012 GLU GLU A . n 
A 1 910 LEU 910 1013 1013 LEU LEU A . n 
A 1 911 GLN 911 1014 1014 GLN GLN A . n 
A 1 912 SER 912 1015 1015 SER SER A . n 
A 1 913 PHE 913 1016 1016 PHE PHE A . n 
A 1 914 ASP 914 1017 1017 ASP ASP A . n 
A 1 915 ASP 915 1018 1018 ASP ASP A . n 
A 1 916 ILE 916 1019 1019 ILE ILE A . n 
A 1 917 ALA 917 1020 1020 ALA ALA A . n 
A 1 918 TYR 918 1021 1021 TYR TYR A . n 
A 1 919 ILE 919 1022 1022 ILE ILE A . n 
A 1 920 ARG 920 1023 1023 ARG ARG A . n 
A 1 921 LYS 921 1024 1024 LYS LYS A . n 
A 1 922 THR 922 1025 1025 THR THR A . n 
A 1 923 LEU 923 1026 1026 LEU LEU A . n 
A 1 924 ALA 924 1027 1027 ALA ALA A . n 
A 1 925 LEU 925 1028 1028 LEU LEU A . n 
A 1 926 ASP 926 1029 1029 ASP ASP A . n 
A 1 927 LYS 927 1030 1030 LYS LYS A . n 
A 1 928 THR 928 1031 1031 THR THR A . n 
A 1 929 GLU 929 1032 1032 GLU GLU A . n 
A 1 930 GLN 930 1033 1033 GLN GLN A . n 
A 1 931 GLU 931 1034 1034 GLU GLU A . n 
A 1 932 ALA 932 1035 1035 ALA ALA A . n 
A 1 933 LEU 933 1036 1036 LEU LEU A . n 
A 1 934 GLU 934 1037 1037 GLU GLU A . n 
A 1 935 TYR 935 1038 1038 TYR TYR A . n 
A 1 936 PHE 936 1039 1039 PHE PHE A . n 
A 1 937 MET 937 1040 1040 MET MET A . n 
A 1 938 LYS 938 1041 1041 LYS LYS A . n 
A 1 939 GLN 939 1042 1042 GLN GLN A . n 
A 1 940 MET 940 1043 1043 MET MET A . n 
A 1 941 ASN 941 1044 1044 ASN ASN A . n 
A 1 942 ASP 942 1045 1045 ASP ASP A . n 
A 1 943 ALA 943 1046 1046 ALA ALA A . n 
A 1 944 HIS 944 1047 1047 HIS HIS A . n 
A 1 945 HIS 945 1048 1048 HIS HIS A . n 
A 1 946 GLY 946 1049 1049 GLY GLY A . n 
A 1 947 GLY 947 1050 1050 GLY GLY A . n 
A 1 948 TRP 948 1051 1051 TRP TRP A . n 
A 1 949 THR 949 1052 1052 THR THR A . n 
A 1 950 THR 950 1053 1053 THR THR A . n 
A 1 951 LYS 951 1054 ?    ?   ?   A . n 
A 1 952 MET 952 1055 ?    ?   ?   A . n 
A 1 953 ASP 953 1056 ?    ?   ?   A . n 
A 1 954 ALA 954 1057 ?    ?   ?   A . n 
A 1 955 ALA 955 1058 ?    ?   ?   A . n 
A 1 956 ALA 956 1059 ?    ?   ?   A . n 
A 1 957 HIS 957 1060 ?    ?   ?   A . n 
A 1 958 THR 958 1061 ?    ?   ?   A . n 
A 1 959 ILE 959 1062 ?    ?   ?   A . n 
A 1 960 LYS 960 1063 ?    ?   ?   A . n 
A 1 961 GLN 961 1064 ?    ?   ?   A . n 
A 1 962 HIS 962 1065 ?    ?   ?   A . n 
A 1 963 ALA 963 1066 ?    ?   ?   A . n 
A 1 964 LEU 964 1067 ?    ?   ?   A . n 
A 1 965 ASN 965 1068 ?    ?   ?   A . n 
B 2 1   GLY 1   0    ?    ?   ?   B . n 
B 2 2   MET 2   1    ?    ?   ?   B . n 
B 2 3   ALA 3   2    ?    ?   ?   B . n 
B 2 4   ALA 4   3    ?    ?   ?   B . n 
B 2 5   ALA 5   4    ?    ?   ?   B . n 
B 2 6   GLY 6   5    ?    ?   ?   B . n 
B 2 7   TRP 7   6    ?    ?   ?   B . n 
B 2 8   ARG 8   7    ?    ?   ?   B . n 
B 2 9   ASP 9   8    ?    ?   ?   B . n 
B 2 10  GLY 10  9    ?    ?   ?   B . n 
B 2 11  SER 11  10   ?    ?   ?   B . n 
B 2 12  GLY 12  11   ?    ?   ?   B . n 
B 2 13  GLN 13  12   12   GLN GLN B . n 
B 2 14  GLU 14  13   13   GLU GLU B . n 
B 2 15  LYS 15  14   14   LYS LYS B . n 
B 2 16  TYR 16  15   15   TYR TYR B . n 
B 2 17  ARG 17  16   16   ARG ARG B . n 
B 2 18  LEU 18  17   17   LEU LEU B . n 
B 2 19  VAL 19  18   18   VAL VAL B . n 
B 2 20  VAL 20  19   19   VAL VAL B . n 
B 2 21  VAL 21  20   20   VAL VAL B . n 
B 2 22  GLY 22  21   21   GLY GLY B . n 
B 2 23  GLY 23  22   22   GLY GLY B . n 
B 2 24  GLY 24  23   23   GLY GLY B . n 
B 2 25  GLY 25  24   24   GLY GLY B . n 
B 2 26  VAL 26  25   25   VAL VAL B . n 
B 2 27  GLY 27  26   26   GLY GLY B . n 
B 2 28  LYS 28  27   27   LYS LYS B . n 
B 2 29  SER 29  28   28   SER SER B . n 
B 2 30  ALA 30  29   29   ALA ALA B . n 
B 2 31  LEU 31  30   30   LEU LEU B . n 
B 2 32  THR 32  31   31   THR THR B . n 
B 2 33  ILE 33  32   32   ILE ILE B . n 
B 2 34  GLN 34  33   33   GLN GLN B . n 
B 2 35  PHE 35  34   34   PHE PHE B . n 
B 2 36  ILE 36  35   35   ILE ILE B . n 
B 2 37  ALA 37  36   36   ALA ALA B . n 
B 2 38  SER 38  37   37   SER SER B . n 
B 2 39  TYR 39  38   38   TYR TYR B . n 
B 2 40  PHE 40  39   39   PHE PHE B . n 
B 2 41  VAL 41  40   40   VAL VAL B . n 
B 2 42  THR 42  41   41   THR THR B . n 
B 2 43  ASP 43  42   42   ASP ASP B . n 
B 2 44  TYR 44  43   43   TYR TYR B . n 
B 2 45  ASP 45  44   44   ASP ASP B . n 
B 2 46  PRO 46  45   45   PRO PRO B . n 
B 2 47  THR 47  46   46   THR THR B . n 
B 2 48  ILE 48  47   47   ILE ILE B . n 
B 2 49  GLU 49  48   48   GLU GLU B . n 
B 2 50  ASP 50  49   49   ASP ASP B . n 
B 2 51  SER 51  50   50   SER SER B . n 
B 2 52  TYR 52  51   51   TYR TYR B . n 
B 2 53  THR 53  52   52   THR THR B . n 
B 2 54  LYS 54  53   53   LYS LYS B . n 
B 2 55  GLN 55  54   54   GLN GLN B . n 
B 2 56  CYS 56  55   55   CYS CYS B . n 
B 2 57  VAL 57  56   56   VAL VAL B . n 
B 2 58  ILE 58  57   57   ILE ILE B . n 
B 2 59  ASP 59  58   58   ASP ASP B . n 
B 2 60  ASP 60  59   59   ASP ASP B . n 
B 2 61  ARG 61  60   60   ARG ARG B . n 
B 2 62  ALA 62  61   61   ALA ALA B . n 
B 2 63  ALA 63  62   62   ALA ALA B . n 
B 2 64  ARG 64  63   63   ARG ARG B . n 
B 2 65  LEU 65  64   64   LEU LEU B . n 
B 2 66  ASP 66  65   65   ASP ASP B . n 
B 2 67  ILE 67  66   66   ILE ILE B . n 
B 2 68  LEU 68  67   67   LEU LEU B . n 
B 2 69  ASP 69  68   68   ASP ASP B . n 
B 2 70  THR 70  69   69   THR THR B . n 
B 2 71  ALA 71  70   70   ALA ALA B . n 
B 2 72  GLY 72  71   71   GLY GLY B . n 
B 2 73  GLN 73  72   72   GLN GLN B . n 
B 2 74  GLU 74  73   73   GLU GLU B . n 
B 2 75  GLU 75  74   74   GLU GLU B . n 
B 2 76  PHE 76  75   75   PHE PHE B . n 
B 2 77  GLY 77  76   76   GLY GLY B . n 
B 2 78  ALA 78  77   77   ALA ALA B . n 
B 2 79  MET 79  78   78   MET MET B . n 
B 2 80  ARG 80  79   79   ARG ARG B . n 
B 2 81  GLU 81  80   80   GLU GLU B . n 
B 2 82  GLN 82  81   81   GLN GLN B . n 
B 2 83  TYR 83  82   82   TYR TYR B . n 
B 2 84  MET 84  83   83   MET MET B . n 
B 2 85  ARG 85  84   84   ARG ARG B . n 
B 2 86  THR 86  85   85   THR THR B . n 
B 2 87  GLY 87  86   86   GLY GLY B . n 
B 2 88  GLU 88  87   87   GLU GLU B . n 
B 2 89  GLY 89  88   88   GLY GLY B . n 
B 2 90  PHE 90  89   89   PHE PHE B . n 
B 2 91  LEU 91  90   90   LEU LEU B . n 
B 2 92  LEU 92  91   91   LEU LEU B . n 
B 2 93  VAL 93  92   92   VAL VAL B . n 
B 2 94  PHE 94  93   93   PHE PHE B . n 
B 2 95  SER 95  94   94   SER SER B . n 
B 2 96  VAL 96  95   95   VAL VAL B . n 
B 2 97  THR 97  96   96   THR THR B . n 
B 2 98  ASP 98  97   97   ASP ASP B . n 
B 2 99  ARG 99  98   98   ARG ARG B . n 
B 2 100 GLY 100 99   99   GLY GLY B . n 
B 2 101 SER 101 100  100  SER SER B . n 
B 2 102 PHE 102 101  101  PHE PHE B . n 
B 2 103 GLU 103 102  102  GLU GLU B . n 
B 2 104 GLU 104 103  103  GLU GLU B . n 
B 2 105 ILE 105 104  104  ILE ILE B . n 
B 2 106 TYR 106 105  105  TYR TYR B . n 
B 2 107 LYS 107 106  106  LYS LYS B . n 
B 2 108 PHE 108 107  107  PHE PHE B . n 
B 2 109 GLN 109 108  108  GLN GLN B . n 
B 2 110 ARG 110 109  109  ARG ARG B . n 
B 2 111 GLN 111 110  110  GLN GLN B . n 
B 2 112 ILE 112 111  111  ILE ILE B . n 
B 2 113 LEU 113 112  112  LEU LEU B . n 
B 2 114 ARG 114 113  113  ARG ARG B . n 
B 2 115 VAL 115 114  114  VAL VAL B . n 
B 2 116 LYS 116 115  115  LYS LYS B . n 
B 2 117 ASP 117 116  116  ASP ASP B . n 
B 2 118 ARG 118 117  117  ARG ARG B . n 
B 2 119 ASP 119 118  118  ASP ASP B . n 
B 2 120 GLU 120 119  119  GLU GLU B . n 
B 2 121 PHE 121 120  120  PHE PHE B . n 
B 2 122 PRO 122 121  121  PRO PRO B . n 
B 2 123 MET 123 122  122  MET MET B . n 
B 2 124 ILE 124 123  123  ILE ILE B . n 
B 2 125 LEU 125 124  124  LEU LEU B . n 
B 2 126 ILE 126 125  125  ILE ILE B . n 
B 2 127 GLY 127 126  126  GLY GLY B . n 
B 2 128 ASN 128 127  127  ASN ASN B . n 
B 2 129 LYS 129 128  128  LYS LYS B . n 
B 2 130 ALA 130 129  129  ALA ALA B . n 
B 2 131 ASP 131 130  130  ASP ASP B . n 
B 2 132 LEU 132 131  131  LEU LEU B . n 
B 2 133 ASP 133 132  132  ASP ASP B . n 
B 2 134 HIS 134 133  133  HIS HIS B . n 
B 2 135 GLN 135 134  134  GLN GLN B . n 
B 2 136 ARG 136 135  135  ARG ARG B . n 
B 2 137 GLN 137 136  136  GLN GLN B . n 
B 2 138 VAL 138 137  137  VAL VAL B . n 
B 2 139 THR 139 138  138  THR THR B . n 
B 2 140 GLN 140 139  139  GLN GLN B . n 
B 2 141 GLU 141 140  140  GLU GLU B . n 
B 2 142 GLU 142 141  141  GLU GLU B . n 
B 2 143 GLY 143 142  142  GLY GLY B . n 
B 2 144 GLN 144 143  143  GLN GLN B . n 
B 2 145 GLN 145 144  144  GLN GLN B . n 
B 2 146 LEU 146 145  145  LEU LEU B . n 
B 2 147 ALA 147 146  146  ALA ALA B . n 
B 2 148 ARG 148 147  147  ARG ARG B . n 
B 2 149 GLN 149 148  148  GLN GLN B . n 
B 2 150 LEU 150 149  149  LEU LEU B . n 
B 2 151 LYS 151 150  150  LYS LYS B . n 
B 2 152 VAL 152 151  151  VAL VAL B . n 
B 2 153 THR 153 152  152  THR THR B . n 
B 2 154 TYR 154 153  153  TYR TYR B . n 
B 2 155 MET 155 154  154  MET MET B . n 
B 2 156 GLU 156 155  155  GLU GLU B . n 
B 2 157 ALA 157 156  156  ALA ALA B . n 
B 2 158 SER 158 157  157  SER SER B . n 
B 2 159 ALA 159 158  158  ALA ALA B . n 
B 2 160 LYS 160 159  159  LYS LYS B . n 
B 2 161 ILE 161 160  160  ILE ILE B . n 
B 2 162 ARG 162 161  161  ARG ARG B . n 
B 2 163 MET 163 162  162  MET MET B . n 
B 2 164 ASN 164 163  163  ASN ASN B . n 
B 2 165 VAL 165 164  164  VAL VAL B . n 
B 2 166 ASP 166 165  165  ASP ASP B . n 
B 2 167 GLN 167 166  166  GLN GLN B . n 
B 2 168 ALA 168 167  167  ALA ALA B . n 
B 2 169 PHE 169 168  168  PHE PHE B . n 
B 2 170 HIS 170 169  169  HIS HIS B . n 
B 2 171 GLU 171 170  170  GLU GLU B . n 
B 2 172 LEU 172 171  171  LEU LEU B . n 
B 2 173 VAL 173 172  172  VAL VAL B . n 
B 2 174 ARG 174 173  173  ARG ARG B . n 
B 2 175 VAL 175 174  174  VAL VAL B . n 
B 2 176 ILE 176 175  175  ILE ILE B . n 
B 2 177 ARG 177 176  176  ARG ARG B . n 
B 2 178 LYS 178 177  177  LYS LYS B . n 
B 2 179 PHE 179 178  178  PHE PHE B . n 
B 2 180 GLN 180 179  179  GLN GLN B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 5H5 ? ? 5H5 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GNP ? ? GNP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 5H5 1 1101 1071 5H5 GDC A . 
D 4 GNP 1 201  500  GNP GNP B . 
E 5 MG  1 202  1    MG  MG  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 148  ? CG  ? A LYS 45  CG  
2  1 Y 1 A LYS 148  ? CD  ? A LYS 45  CD  
3  1 Y 1 A LYS 148  ? CE  ? A LYS 45  CE  
4  1 Y 1 A LYS 148  ? NZ  ? A LYS 45  NZ  
5  1 Y 1 A ILE 181  ? CD1 ? A ILE 78  CD1 
6  1 Y 1 A ILE 211  ? CD1 ? A ILE 108 CD1 
7  1 Y 1 A LYS 353  ? CG  ? A LYS 250 CG  
8  1 Y 1 A LYS 353  ? CD  ? A LYS 250 CD  
9  1 Y 1 A LYS 353  ? CE  ? A LYS 250 CE  
10 1 Y 1 A LYS 353  ? NZ  ? A LYS 250 NZ  
11 1 Y 1 A GLN 374  ? CG  ? A GLN 271 CG  
12 1 Y 1 A GLN 374  ? CD  ? A GLN 271 CD  
13 1 Y 1 A GLN 374  ? OE1 ? A GLN 271 OE1 
14 1 Y 1 A GLN 374  ? NE2 ? A GLN 271 NE2 
15 1 Y 1 A ASN 380  ? CG  ? A ASN 277 CG  
16 1 Y 1 A ASN 380  ? OD1 ? A ASN 277 OD1 
17 1 Y 1 A ASN 380  ? ND2 ? A ASN 277 ND2 
18 1 Y 1 A ILE 391  ? CD1 ? A ILE 288 CD1 
19 1 Y 1 A ARG 502  ? CG  ? A ARG 399 CG  
20 1 Y 1 A ARG 502  ? CD  ? A ARG 399 CD  
21 1 Y 1 A ARG 502  ? NE  ? A ARG 399 NE  
22 1 Y 1 A ARG 502  ? CZ  ? A ARG 399 CZ  
23 1 Y 1 A ARG 502  ? NH1 ? A ARG 399 NH1 
24 1 Y 1 A ARG 502  ? NH2 ? A ARG 399 NH2 
25 1 Y 1 A GLU 503  ? CG  ? A GLU 400 CG  
26 1 Y 1 A GLU 503  ? CD  ? A GLU 400 CD  
27 1 Y 1 A GLU 503  ? OE1 ? A GLU 400 OE1 
28 1 Y 1 A GLU 503  ? OE2 ? A GLU 400 OE2 
29 1 Y 1 A ILE 543  ? CD1 ? A ILE 440 CD1 
30 1 Y 1 A ILE 561  ? CD1 ? A ILE 458 CD1 
31 1 Y 1 A ILE 564  ? CD1 ? A ILE 461 CD1 
32 1 Y 1 A LYS 776  ? CG  ? A LYS 673 CG  
33 1 Y 1 A LYS 776  ? CD  ? A LYS 673 CD  
34 1 Y 1 A LYS 776  ? CE  ? A LYS 673 CE  
35 1 Y 1 A LYS 776  ? NZ  ? A LYS 673 NZ  
36 1 Y 1 A PHE 872  ? CG  ? A PHE 769 CG  
37 1 Y 1 A PHE 872  ? CD1 ? A PHE 769 CD1 
38 1 Y 1 A PHE 872  ? CD2 ? A PHE 769 CD2 
39 1 Y 1 A PHE 872  ? CE1 ? A PHE 769 CE1 
40 1 Y 1 A PHE 872  ? CE2 ? A PHE 769 CE2 
41 1 Y 1 A PHE 872  ? CZ  ? A PHE 769 CZ  
42 1 Y 1 A ILE 913  ? CD1 ? A ILE 810 CD1 
43 1 Y 1 A LYS 941  ? CG  ? A LYS 838 CG  
44 1 Y 1 A LYS 941  ? CD  ? A LYS 838 CD  
45 1 Y 1 A LYS 941  ? CE  ? A LYS 838 CE  
46 1 Y 1 A LYS 941  ? NZ  ? A LYS 838 NZ  
47 1 Y 1 A PHE 954  ? CG  ? A PHE 851 CG  
48 1 Y 1 A PHE 954  ? CD1 ? A PHE 851 CD1 
49 1 Y 1 A PHE 954  ? CD2 ? A PHE 851 CD2 
50 1 Y 1 A PHE 954  ? CE1 ? A PHE 851 CE1 
51 1 Y 1 A PHE 954  ? CE2 ? A PHE 851 CE2 
52 1 Y 1 A PHE 954  ? CZ  ? A PHE 851 CZ  
53 1 Y 1 A GLN 958  ? CG  ? A GLN 855 CG  
54 1 Y 1 A GLN 958  ? CD  ? A GLN 855 CD  
55 1 Y 1 A GLN 958  ? OE1 ? A GLN 855 OE1 
56 1 Y 1 A GLN 958  ? NE2 ? A GLN 855 NE2 
57 1 Y 1 A LYS 966  ? CG  ? A LYS 863 CG  
58 1 Y 1 A LYS 966  ? CD  ? A LYS 863 CD  
59 1 Y 1 A LYS 966  ? CE  ? A LYS 863 CE  
60 1 Y 1 A LYS 966  ? NZ  ? A LYS 863 NZ  
61 1 Y 1 A ARG 1023 ? CZ  ? A ARG 920 CZ  
62 1 Y 1 A ARG 1023 ? NH1 ? A ARG 920 NH1 
63 1 Y 1 A ARG 1023 ? NH2 ? A ARG 920 NH2 
64 1 Y 1 B LYS 177  ? CG  ? B LYS 178 CG  
65 1 Y 1 B LYS 177  ? CD  ? B LYS 178 CD  
66 1 Y 1 B LYS 177  ? CE  ? B LYS 178 CE  
67 1 Y 1 B LYS 177  ? NZ  ? B LYS 178 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 ? ? ? '(1.21_5207: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B4S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     181.488 
_cell.length_a_esd                 ? 
_cell.length_b                     181.488 
_cell.length_b_esd                 ? 
_cell.length_c                     96.030 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9B4S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_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                   9B4S 
_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             2.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '0.1 M (Bicine/Tris), 0.06 M Divalent mix, 30% (40%v/v PEG MME 500, 20%w/v PEG 20000)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B4S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.1 
_reflns.d_resolution_low                               49.26 
_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                                     28076 
_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                           94.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.12 
_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                                0.071 
_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                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
3.10 3.29  ? ? ? ? ? ? 4491 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.154               ? ? 1 1 0.435              ? ? ? ? 
2.0380000000000003   ? ? ? ? ? ? ? ? ? 
3.29 3.51  ? ? ? ? ? ? 4240 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.018               ? ? 2 1 0.826              ? ? ? ? 
0.9640000000000001   ? ? ? ? ? ? ? ? ? 
3.51 3.79  ? ? ? ? ? ? 3939 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.40399999999999997 ? ? 3 1 0.973              ? ? ? ? 0.381 ? ? ? ? ? ? 
? ? ? 
3.79 4.15  ? ? ? ? ? ? 3639 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.18100000000000002 ? ? 4 1 0.993              ? ? ? ? 0.171 ? ? ? ? ? ? 
? ? ? 
4.15 4.64  ? ? ? ? ? ? 3275 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.08900000000000001 ? ? 5 1 0.997              ? ? ? ? 0.084 ? ? ? ? ? ? 
? ? ? 
4.64 5.35  ? ? ? ? ? ? 2908 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.061               ? ? 6 1 0.998              ? ? ? ? 0.057 ? ? ? ? ? ? 
? ? ? 
5.35 6.53  ? ? ? ? ? ? 2475 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.055               ? ? 7 1 0.9990000000000001 ? ? ? ? 
0.052000000000000005 ? ? ? ? ? ? ? ? ? 
6.53 9.16  ? ? ? ? ? ? 1951 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.038               ? ? 8 1 0.9990000000000001 ? ? ? ? 
0.036000000000000004 ? ? ? ? ? ? ? ? ? 
9.16 49.26 ? ? ? ? ? ? 1158 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03                ? ? 9 1 0.9990000000000001 ? ? ? ? 
0.027999999999999997 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9B4S 
_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                            3.10 
_refine.ls_d_res_low                             49.26 
_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                     28056 
_refine.ls_number_reflns_R_free                  1404 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.76 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2322 
_refine.ls_R_factor_R_free                       0.2717 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2302 
_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             1.10 
_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                 32.14 
_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                            0.56 
_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                       3.10 
_refine_hist.d_res_low                        49.26 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               8585 
_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        8524 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         61 
_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' ? 0.001  ? 8768  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.385  ? 11859 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.730 ? 3320  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 1297  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 1516  ? 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' 3.10 3.21  . . 139 2642 96.00 . . . . 0.3441 . . . . . . . . . . . 0.4087 
'X-RAY DIFFRACTION' 3.21 3.34  . . 140 2655 96.00 . . . . 0.3417 . . . . . . . . . . . 0.3819 
'X-RAY DIFFRACTION' 3.34 3.49  . . 138 2629 96.00 . . . . 0.3176 . . . . . . . . . . . 0.3812 
'X-RAY DIFFRACTION' 3.49 3.68  . . 140 2664 96.00 . . . . 0.2791 . . . . . . . . . . . 0.3491 
'X-RAY DIFFRACTION' 3.68 3.91  . . 140 2642 95.00 . . . . 0.2481 . . . . . . . . . . . 0.3711 
'X-RAY DIFFRACTION' 3.91 4.21  . . 140 2668 95.00 . . . . 0.2537 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 4.21 4.63  . . 139 2651 95.00 . . . . 0.2147 . . . . . . . . . . . 0.2652 
'X-RAY DIFFRACTION' 4.63 5.30  . . 140 2648 94.00 . . . . 0.2110 . . . . . . . . . . . 0.2609 
'X-RAY DIFFRACTION' 5.30 6.67  . . 142 2685 94.00 . . . . 0.2572 . . . . . . . . . . . 0.2903 
'X-RAY DIFFRACTION' 6.68 49.26 . . 146 2768 92.00 . . . . 0.1912 . . . . . . . . . . . 0.2148 
# 
_struct.entry_id                     9B4S 
_struct.title                        'Crystal structure of the RRAS2-p110alpha 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        9B4S 
_struct_keywords.text            'RAS, RRAS2, TC21, p110alpha, PIK3CA, PI3Kalpha, ONCOPROTEIN, PI3Ka, PI3K' 
_struct_keywords.pdbx_keywords   ONCOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP PK3CA_HUMAN P42336 ? 1 
;VGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNK
LDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEK
YPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYV
NVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAW
GNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREA
GFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMY
CLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIG
HFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDF
MDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIW
QNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGY
CVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEMC
YKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQ
HALN
;
105 
2 UNP RRAS2_HUMAN P62070 ? 2 
;MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMRE
QYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKI
RMNVDQAFHELVRVIRKFQ
;
1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9B4S A 2 ? 965 ? P42336 105 ? 1068 ? 105 1068 
2 2 9B4S B 2 ? 180 ? P62070 1   ? 179  ? 1   179  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9B4S GLY A 1   ? UNP P42336 ?   ?    'expression tag'      104  1 
1 9B4S ALA A 954 ? UNP P42336 TRP 1057 'engineered mutation' 1057 2 
1 9B4S ALA A 955 ? UNP P42336 ILE 1058 'engineered mutation' 1058 3 
1 9B4S ALA A 956 ? UNP P42336 PHE 1059 'engineered mutation' 1059 4 
2 9B4S GLY B 1   ? UNP P62070 ?   ?    'expression tag'      0    5 
2 9B4S ALA B 37  ? UNP P62070 GLN 36   'engineered mutation' 36   6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 6   ? GLY A 19  ? GLU A 109  GLY A 122  1 ? 14 
HELX_P HELX_P2  AA2 VAL A 22  ? MET A 27  ? VAL A 125  MET A 130  1 ? 6  
HELX_P HELX_P3  AA3 ASP A 30  ? ILE A 40  ? ASP A 133  ILE A 143  1 ? 11 
HELX_P HELX_P4  AA4 ILE A 40  ? ASP A 49  ? ILE A 143  ASP A 152  1 ? 10 
HELX_P HELX_P5  AA5 PRO A 56  ? TYR A 64  ? PRO A 159  TYR A 167  1 ? 9  
HELX_P HELX_P6  AA6 PRO A 75  ? ASN A 80  ? PRO A 178  ASN A 183  1 ? 6  
HELX_P HELX_P7  AA7 LYS A 81  ? LYS A 84  ? LYS A 184  LYS A 187  5 ? 4  
HELX_P HELX_P8  AA8 VAL A 113 ? ARG A 127 ? VAL A 216  ARG A 230  1 ? 15 
HELX_P HELX_P9  AA9 GLN A 135 ? LEU A 141 ? GLN A 238  LEU A 244  1 ? 7  
HELX_P HELX_P10 AB1 GLU A 142 ? GLN A 144 ? GLU A 245  GLN A 247  5 ? 3  
HELX_P HELX_P11 AB2 PRO A 163 ? GLN A 166 ? PRO A 266  GLN A 269  5 ? 4  
HELX_P HELX_P12 AB3 TYR A 167 ? GLY A 177 ? TYR A 270  GLY A 280  1 ? 11 
HELX_P HELX_P13 AB4 LYS A 187 ? SER A 192 ? LYS A 290  SER A 295  1 ? 6  
HELX_P HELX_P14 AB5 SER A 223 ? ILE A 227 ? SER A 326  ILE A 330  5 ? 5  
HELX_P HELX_P15 AB6 PRO A 291 ? LEU A 293 ? PRO A 394  LEU A 396  5 ? 3  
HELX_P HELX_P16 AB7 ASP A 385 ? ARG A 399 ? ASP A 488  ARG A 502  1 ? 15 
HELX_P HELX_P17 AB8 ARG A 421 ? THR A 433 ? ARG A 524  THR A 536  1 ? 13 
HELX_P HELX_P18 AB9 THR A 441 ? HIS A 451 ? THR A 544  HIS A 554  1 ? 11 
HELX_P HELX_P19 AC1 ILE A 458 ? GLU A 460 ? ILE A 561  GLU A 563  5 ? 3  
HELX_P HELX_P20 AC2 ILE A 461 ? LEU A 467 ? ILE A 564  LEU A 570  1 ? 7  
HELX_P HELX_P21 AC3 ASP A 475 ? ASP A 486 ? ASP A 578  ASP A 589  1 ? 12 
HELX_P HELX_P22 AC4 LYS A 491 ? MET A 496 ? LYS A 594  MET A 599  1 ? 6  
HELX_P HELX_P23 AC5 GLU A 497 ? ASP A 500 ? GLU A 600  ASP A 603  5 ? 4  
HELX_P HELX_P24 AC6 ASP A 505 ? GLU A 517 ? ASP A 608  GLU A 620  1 ? 13 
HELX_P HELX_P25 AC7 THR A 521 ? TYR A 528 ? THR A 624  TYR A 631  1 ? 8  
HELX_P HELX_P26 AC8 TYR A 528 ? VAL A 535 ? TYR A 631  VAL A 638  1 ? 8  
HELX_P HELX_P27 AC9 ASN A 544 ? LEU A 555 ? ASN A 647  LEU A 658  1 ? 12 
HELX_P HELX_P28 AD1 ASN A 557 ? SER A 570 ? ASN A 660  SER A 673  1 ? 14 
HELX_P HELX_P29 AD2 VAL A 577 ? CYS A 592 ? VAL A 680  CYS A 695  1 ? 16 
HELX_P HELX_P30 AD3 MET A 594 ? GLN A 618 ? MET A 697  GLN A 721  1 ? 25 
HELX_P HELX_P31 AD4 LYS A 626 ? ARG A 637 ? LYS A 729  ARG A 740  1 ? 12 
HELX_P HELX_P32 AD5 ARG A 638 ? ASP A 643 ? ARG A 741  ASP A 746  1 ? 6  
HELX_P HELX_P33 AD6 ALA A 644 ? GLN A 646 ? ALA A 747  GLN A 749  5 ? 3  
HELX_P HELX_P34 AD7 LEU A 704 ? ASN A 723 ? LEU A 807  ASN A 826  1 ? 20 
HELX_P HELX_P35 AD8 THR A 773 ? ASN A 782 ? THR A 876  ASN A 885  1 ? 10 
HELX_P HELX_P36 AD9 GLU A 785 ? GLY A 809 ? GLU A 888  GLY A 912  1 ? 25 
HELX_P HELX_P37 AE1 THR A 854 ? SER A 862 ? THR A 957  SER A 965  1 ? 9  
HELX_P HELX_P38 AE2 THR A 871 ? HIS A 891 ? THR A 974  HIS A 994  1 ? 21 
HELX_P HELX_P39 AE3 HIS A 891 ? MET A 901 ? HIS A 994  MET A 1004 1 ? 11 
HELX_P HELX_P40 AE4 MET A 902 ? GLY A 906 ? MET A 1005 GLY A 1009 5 ? 5  
HELX_P HELX_P41 AE5 SER A 912 ? LEU A 923 ? SER A 1015 LEU A 1026 1 ? 12 
HELX_P HELX_P42 AE6 THR A 928 ? HIS A 944 ? THR A 1031 HIS A 1047 1 ? 17 
HELX_P HELX_P43 AE7 GLY B 27  ? ALA B 37  ? GLY B 26   ALA B 36   1 ? 11 
HELX_P HELX_P44 AE8 PHE B 76  ? ALA B 78  ? PHE B 75   ALA B 77   5 ? 3  
HELX_P HELX_P45 AE9 MET B 79  ? GLY B 87  ? MET B 78   GLY B 86   1 ? 9  
HELX_P HELX_P46 AF1 ASP B 98  ? GLU B 103 ? ASP B 97   GLU B 102  1 ? 6  
HELX_P HELX_P47 AF2 GLU B 104 ? ASP B 117 ? GLU B 103  ASP B 116  1 ? 14 
HELX_P HELX_P48 AF3 LEU B 132 ? ARG B 136 ? LEU B 131  ARG B 135  5 ? 5  
HELX_P HELX_P49 AF4 THR B 139 ? LYS B 151 ? THR B 138  LYS B 150  1 ? 13 
HELX_P HELX_P50 AF5 ASN B 164 ? LYS B 178 ? ASN B 163  LYS B 177  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 
metalc1 metalc ? ? B SER 29 OG  ? ? ? 1_555 E MG . MG ? ? B SER 28  B MG 202 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2 metalc ? ? B THR 47 OG1 ? ? ? 1_555 E MG . MG ? ? B THR 46  B MG 202 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc3 metalc ? ? D GNP .  O2G ? ? ? 1_555 E MG . MG ? ? B GNP 201 B MG 202 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc4 metalc ? ? D GNP .  O2B ? ? ? 1_555 E MG . MG ? ? B GNP 201 B MG 202 1_555 ? ? ? ? ? ? ? 1.943 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG  ? B SER 29 ? B SER 28  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 OG1 ? B THR 47 ? B THR 46  ? 1_555 75.8  ? 
2 OG  ? B SER 29 ? B SER 28  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2G ? D GNP .  ? B GNP 201 ? 1_555 135.9 ? 
3 OG1 ? B THR 47 ? B THR 46  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2G ? D GNP .  ? B GNP 201 ? 1_555 93.7  ? 
4 OG  ? B SER 29 ? B SER 28  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2B ? D GNP .  ? B GNP 201 ? 1_555 82.4  ? 
5 OG1 ? B THR 47 ? B THR 46  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2B ? D GNP .  ? B GNP 201 ? 1_555 157.6 ? 
6 O2G ? D GNP .  ? B GNP 201 ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2B ? D GNP .  ? B GNP 201 ? 1_555 105.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? 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 LYS A 101 ? ASN A 109 ? LYS A 204 ASN A 212 
AA1 2 GLN A 86  ? ILE A 94  ? GLN A 189 ILE A 197 
AA1 3 ASN A 181 ? ALA A 186 ? ASN A 284 ALA A 289 
AA1 4 TYR A 147 ? VAL A 151 ? TYR A 250 VAL A 254 
AA2 1 ARG A 279 ? TYR A 289 ? ARG A 382 TYR A 392 
AA2 2 ALA A 230 ? ALA A 238 ? ALA A 333 ALA A 341 
AA2 3 CYS A 369 ? PHE A 374 ? CYS A 472 PHE A 477 
AA2 4 GLY A 336 ? ASN A 341 ? GLY A 439 ASN A 444 
AA3 1 GLU A 262 ? PRO A 263 ? GLU A 365 PRO A 366 
AA3 2 ILE A 251 ? HIS A 259 ? ILE A 354 HIS A 362 
AA3 3 VAL A 268 ? ASN A 269 ? VAL A 371 ASN A 372 
AA4 1 GLU A 262 ? PRO A 263 ? GLU A 365 PRO A 366 
AA4 2 ILE A 251 ? HIS A 259 ? ILE A 354 HIS A 362 
AA4 3 ARG A 298 ? SER A 305 ? ARG A 401 SER A 408 
AA4 4 CYS A 317 ? ASN A 325 ? CYS A 420 ASN A 428 
AA4 5 TRP A 343 ? PRO A 344 ? TRP A 446 PRO A 447 
AA5 1 PHE A 648 ? LEU A 649 ? PHE A 751 LEU A 752 
AA5 2 GLN A 657 ? LEU A 658 ? GLN A 760 LEU A 761 
AA6 1 ARG A 667 ? ILE A 668 ? ARG A 770 ILE A 771 
AA6 2 LEU A 676 ? GLU A 681 ? LEU A 779 GLU A 784 
AA6 3 ASN A 693 ? PHE A 698 ? ASN A 796 PHE A 801 
AA6 4 VAL A 742 ? GLU A 746 ? VAL A 845 GLU A 849 
AA6 5 CYS A 735 ? ILE A 738 ? CYS A 838 ILE A 841 
AA7 1 SER A 751 ? THR A 753 ? SER A 854 THR A 856 
AA7 2 ILE A 818 ? LYS A 821 ? ILE A 921 LYS A 924 
AA7 3 LEU A 826 ? HIS A 828 ? LEU A 929 HIS A 931 
AA8 1 GLU B 49  ? GLN B 55  ? GLU B 48  GLN B 54  
AA8 2 ARG B 64  ? THR B 70  ? ARG B 63  THR B 69  
AA8 3 LYS B 15  ? GLY B 22  ? LYS B 14  GLY B 21  
AA8 4 GLY B 89  ? SER B 95  ? GLY B 88  SER B 94  
AA8 5 MET B 123 ? ASN B 128 ? MET B 122 ASN B 127 
AA8 6 THR B 153 ? GLU B 156 ? THR B 152 GLU B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 108 ? O ILE A 211 N ILE A 87  ? N ILE A 190 
AA1 2 3 N TRP A 92  ? N TRP A 195 O LEU A 184 ? O LEU A 287 
AA1 3 4 O MET A 183 ? O MET A 286 N LYS A 150 ? N LYS A 253 
AA2 1 2 O LEU A 284 ? O LEU A 387 N ILE A 233 ? N ILE A 336 
AA2 2 3 N LYS A 234 ? N LYS A 337 O GLU A 373 ? O GLU A 476 
AA2 3 4 O PHE A 374 ? O PHE A 477 N GLY A 336 ? N GLY A 439 
AA3 1 2 O GLU A 262 ? O GLU A 365 N HIS A 259 ? N HIS A 362 
AA3 2 3 N THR A 255 ? N THR A 358 O VAL A 268 ? O VAL A 371 
AA4 1 2 O GLU A 262 ? O GLU A 365 N HIS A 259 ? N HIS A 362 
AA4 2 3 N GLY A 256 ? N GLY A 359 O CYS A 300 ? O CYS A 403 
AA4 3 4 N LEU A 301 ? N LEU A 404 O GLY A 322 ? O GLY A 425 
AA4 4 5 N TRP A 321 ? N TRP A 424 O TRP A 343 ? O TRP A 446 
AA5 1 2 N PHE A 648 ? N PHE A 751 O LEU A 658 ? O LEU A 761 
AA6 1 2 N ARG A 667 ? N ARG A 770 O TRP A 677 ? O TRP A 780 
AA6 2 3 N LEU A 678 ? N LEU A 781 O ILE A 696 ? O ILE A 799 
AA6 3 4 N ILE A 697 ? N ILE A 800 O ILE A 745 ? O ILE A 848 
AA6 4 5 O VAL A 742 ? O VAL A 845 N ILE A 738 ? N ILE A 841 
AA7 1 2 N HIS A 752 ? N HIS A 855 O VAL A 820 ? O VAL A 923 
AA7 2 3 N MET A 819 ? N MET A 922 O PHE A 827 ? O PHE A 930 
AA8 1 2 N TYR B 52  ? N TYR B 51  O ILE B 67  ? O ILE B 66  
AA8 2 3 O ASP B 66  ? O ASP B 65  N TYR B 16  ? N TYR B 15  
AA8 3 4 N VAL B 19  ? N VAL B 18  O GLY B 89  ? O GLY B 88  
AA8 4 5 N PHE B 94  ? N PHE B 93  O ASN B 128 ? O ASN B 127 
AA8 5 6 N LEU B 125 ? N LEU B 124 O THR B 153 ? O THR B 152 
# 
_pdbx_entry_details.entry_id                   9B4S 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 170  ? ? -67.12  95.73   
2  1 VAL A 198  ? ? -106.46 -64.22  
3  1 ASP A 214  ? ? -93.41  41.62   
4  1 ARG A 230  ? ? 59.88   -115.20 
5  1 MET A 232  ? ? -108.26 -150.31 
6  1 SER A 236  ? ? -69.28  2.67    
7  1 LYS A 249  ? ? -134.16 -33.71  
8  1 ILE A 251  ? ? -119.46 -166.96 
9  1 LYS A 264  ? ? -82.57  36.47   
10 1 SER A 308  ? ? -99.25  36.88   
11 1 THR A 324  ? ? 54.57   70.64   
12 1 LEU A 339  ? ? -81.17  -73.35  
13 1 TRP A 383  ? ? -136.29 -62.48  
14 1 ALA A 399  ? ? -99.23  31.31   
15 1 LEU A 422  ? ? -139.63 -52.55  
16 1 PRO A 449  ? ? -69.26  -175.05 
17 1 GLU A 453  ? ? -92.50  -69.73  
18 1 PRO A 466  ? ? -89.08  31.61   
19 1 LYS A 468  ? ? 47.34   19.48   
20 1 PHE A 480  ? ? 68.13   -1.25   
21 1 LYS A 723  ? ? 56.29   -127.77 
22 1 GLN A 728  ? ? -132.40 -66.22  
23 1 LYS A 733  ? ? -91.48  -71.41  
24 1 SER A 774  ? ? -93.78  -159.11 
25 1 ARG A 777  ? ? 53.44   76.44   
26 1 PRO A 786  ? ? -68.66  2.75    
27 1 LEU A 793  ? ? -102.14 -168.28 
28 1 ASP A 843  ? ? -72.41  -72.68  
29 1 HIS A 917  ? ? -109.68 -167.15 
30 1 ASP A 933  ? ? 57.93   72.15   
31 1 HIS A 940  ? ? -148.45 -11.15  
32 1 LYS A 966  ? ? 53.83   -112.89 
33 1 GLU A 970  ? ? -118.61 -89.61  
34 1 THR A 974  ? ? -118.99 -161.57 
35 1 HIS A 1048 ? ? -55.74  103.43  
36 1 TRP A 1051 ? ? -115.04 60.98   
37 1 ILE B 35   ? ? -105.27 -65.11  
38 1 TYR B 43   ? ? -113.30 76.86   
39 1 ILE B 47   ? ? -107.02 -63.99  
40 1 GLU B 48   ? ? -164.46 110.07  
41 1 GLU B 73   ? ? 65.00   -8.69   
42 1 GLN B 81   ? ? -95.34  -60.71  
43 1 MET B 154  ? ? -160.98 118.44  
44 1 PHE B 178  ? ? -86.05  -75.65  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -42.8857 
_pdbx_refine_tls.origin_y         -9.2009 
_pdbx_refine_tls.origin_z         -21.0239 
_pdbx_refine_tls.T[1][1]          0.9559 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0450 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.2052 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.9217 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.1949 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          1.0302 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.3499 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          1.1936 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.8216 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.5771 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.7089 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.2268 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.2977 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0912 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.1232 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.6710 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.2061 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.5331 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1625 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.2750 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0822 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 104  ? A GLY 1   
2  1 Y 1 A VAL 105  ? A VAL 2   
3  1 Y 1 A GLY 106  ? A GLY 3   
4  1 Y 1 A ILE 311  ? A ILE 208 
5  1 Y 1 A SER 312  ? A SER 209 
6  1 Y 1 A THR 313  ? A THR 210 
7  1 Y 1 A ALA 314  ? A ALA 211 
8  1 Y 1 A THR 315  ? A THR 212 
9  1 Y 1 A PRO 316  ? A PRO 213 
10 1 Y 1 A TYR 317  ? A TYR 214 
11 1 Y 1 A MET 318  ? A MET 215 
12 1 Y 1 A ASN 319  ? A ASN 216 
13 1 Y 1 A GLY 320  ? A GLY 217 
14 1 Y 1 A GLU 321  ? A GLU 218 
15 1 Y 1 A THR 322  ? A THR 219 
16 1 Y 1 A VAL 344  ? A VAL 241 
17 1 Y 1 A ASN 345  ? A ASN 242 
18 1 Y 1 A VAL 346  ? A VAL 243 
19 1 Y 1 A ASN 347  ? A ASN 244 
20 1 Y 1 A ILE 348  ? A ILE 245 
21 1 Y 1 A ARG 349  ? A ARG 246 
22 1 Y 1 A ASP 350  ? A ASP 247 
23 1 Y 1 A ILE 351  ? A ILE 248 
24 1 Y 1 A ASP 352  ? A ASP 249 
25 1 Y 1 A GLY 411  ? A GLY 308 
26 1 Y 1 A ARG 412  ? A ARG 309 
27 1 Y 1 A LYS 413  ? A LYS 310 
28 1 Y 1 A GLY 414  ? A GLY 311 
29 1 Y 1 A ALA 415  ? A ALA 312 
30 1 Y 1 A ALA 504  ? A ALA 401 
31 1 Y 1 A GLY 505  ? A GLY 402 
32 1 Y 1 A PHE 506  ? A PHE 403 
33 1 Y 1 A SER 507  ? A SER 404 
34 1 Y 1 A TYR 508  ? A TYR 405 
35 1 Y 1 A SER 509  ? A SER 406 
36 1 Y 1 A HIS 510  ? A HIS 407 
37 1 Y 1 A ALA 511  ? A ALA 408 
38 1 Y 1 A GLY 512  ? A GLY 409 
39 1 Y 1 A LEU 513  ? A LEU 410 
40 1 Y 1 A SER 514  ? A SER 411 
41 1 Y 1 A ASN 515  ? A ASN 412 
42 1 Y 1 A ARG 516  ? A ARG 413 
43 1 Y 1 A LEU 517  ? A LEU 414 
44 1 Y 1 A ALA 518  ? A ALA 415 
45 1 Y 1 A ARG 519  ? A ARG 416 
46 1 Y 1 A ASP 520  ? A ASP 417 
47 1 Y 1 A ASN 521  ? A ASN 418 
48 1 Y 1 A GLU 522  ? A GLU 419 
49 1 Y 1 A LYS 863  ? A LYS 760 
50 1 Y 1 A GLY 864  ? A GLY 761 
51 1 Y 1 A GLY 865  ? A GLY 762 
52 1 Y 1 A LEU 866  ? A LEU 763 
53 1 Y 1 A LYS 867  ? A LYS 764 
54 1 Y 1 A GLY 868  ? A GLY 765 
55 1 Y 1 A ALA 869  ? A ALA 766 
56 1 Y 1 A LEU 870  ? A LEU 767 
57 1 Y 1 A GLN 871  ? A GLN 768 
58 1 Y 1 A LYS 942  ? A LYS 839 
59 1 Y 1 A LYS 943  ? A LYS 840 
60 1 Y 1 A LYS 944  ? A LYS 841 
61 1 Y 1 A PHE 945  ? A PHE 842 
62 1 Y 1 A GLY 946  ? A GLY 843 
63 1 Y 1 A TYR 947  ? A TYR 844 
64 1 Y 1 A LYS 948  ? A LYS 845 
65 1 Y 1 A ARG 949  ? A ARG 846 
66 1 Y 1 A GLU 950  ? A GLU 847 
67 1 Y 1 A ARG 951  ? A ARG 848 
68 1 Y 1 A LYS 1054 ? A LYS 951 
69 1 Y 1 A MET 1055 ? A MET 952 
70 1 Y 1 A ASP 1056 ? A ASP 953 
71 1 Y 1 A ALA 1057 ? A ALA 954 
72 1 Y 1 A ALA 1058 ? A ALA 955 
73 1 Y 1 A ALA 1059 ? A ALA 956 
74 1 Y 1 A HIS 1060 ? A HIS 957 
75 1 Y 1 A THR 1061 ? A THR 958 
76 1 Y 1 A ILE 1062 ? A ILE 959 
77 1 Y 1 A LYS 1063 ? A LYS 960 
78 1 Y 1 A GLN 1064 ? A GLN 961 
79 1 Y 1 A HIS 1065 ? A HIS 962 
80 1 Y 1 A ALA 1066 ? A ALA 963 
81 1 Y 1 A LEU 1067 ? A LEU 964 
82 1 Y 1 A ASN 1068 ? A ASN 965 
83 1 Y 1 B GLY 0    ? B GLY 1   
84 1 Y 1 B MET 1    ? B MET 2   
85 1 Y 1 B ALA 2    ? B ALA 3   
86 1 Y 1 B ALA 3    ? B ALA 4   
87 1 Y 1 B ALA 4    ? B ALA 5   
88 1 Y 1 B GLY 5    ? B GLY 6   
89 1 Y 1 B TRP 6    ? B TRP 7   
90 1 Y 1 B ARG 7    ? B ARG 8   
91 1 Y 1 B ASP 8    ? B ASP 9   
92 1 Y 1 B GLY 9    ? B GLY 10  
93 1 Y 1 B SER 10   ? B SER 11  
94 1 Y 1 B GLY 11   ? B GLY 12  
# 
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 
5H5 C2     C  N N 1   
5H5 C4     C  N S 2   
5H5 C6     C  N N 3   
5H5 C8     C  Y N 4   
5H5 C12    C  N N 5   
5H5 C15    C  Y N 6   
5H5 C16    C  Y N 7   
5H5 C18    C  Y N 8   
5H5 C19    C  Y N 9   
5H5 C21    C  Y N 10  
5H5 C24    C  Y N 11  
5H5 C27    C  N N 12  
5H5 N1     N  N N 13  
5H5 O3     O  N N 14  
5H5 O7     O  N N 15  
5H5 C9     C  Y N 16  
5H5 C10    C  Y N 17  
5H5 O11    O  N N 18  
5H5 C13    C  N N 19  
5H5 N14    N  Y N 20  
5H5 N17    N  Y N 21  
5H5 C20    C  Y N 22  
5H5 C22    C  Y N 23  
5H5 N23    N  Y N 24  
5H5 N25    N  Y N 25  
5H5 N26    N  Y N 26  
5H5 C28    C  N N 27  
5H5 C29    C  N N 28  
5H5 H1     H  N N 29  
5H5 H2     H  N N 30  
5H5 H3     H  N N 31  
5H5 H4     H  N N 32  
5H5 H5     H  N N 33  
5H5 H6     H  N N 34  
5H5 H7     H  N N 35  
5H5 H8     H  N N 36  
5H5 H9     H  N N 37  
5H5 H10    H  N N 38  
5H5 H11    H  N N 39  
5H5 H12    H  N N 40  
5H5 H13    H  N N 41  
5H5 H14    H  N N 42  
5H5 H15    H  N N 43  
5H5 H16    H  N N 44  
5H5 H17    H  N N 45  
5H5 H18    H  N N 46  
5H5 H19    H  N N 47  
5H5 H20    H  N N 48  
5H5 H21    H  N N 49  
5H5 H22    H  N N 50  
ALA N      N  N N 51  
ALA CA     C  N S 52  
ALA C      C  N N 53  
ALA O      O  N N 54  
ALA CB     C  N N 55  
ALA OXT    O  N N 56  
ALA H      H  N N 57  
ALA H2     H  N N 58  
ALA HA     H  N N 59  
ALA HB1    H  N N 60  
ALA HB2    H  N N 61  
ALA HB3    H  N N 62  
ALA HXT    H  N N 63  
ARG N      N  N N 64  
ARG CA     C  N S 65  
ARG C      C  N N 66  
ARG O      O  N N 67  
ARG CB     C  N N 68  
ARG CG     C  N N 69  
ARG CD     C  N N 70  
ARG NE     N  N N 71  
ARG CZ     C  N N 72  
ARG NH1    N  N N 73  
ARG NH2    N  N N 74  
ARG OXT    O  N N 75  
ARG H      H  N N 76  
ARG H2     H  N N 77  
ARG HA     H  N N 78  
ARG HB2    H  N N 79  
ARG HB3    H  N N 80  
ARG HG2    H  N N 81  
ARG HG3    H  N N 82  
ARG HD2    H  N N 83  
ARG HD3    H  N N 84  
ARG HE     H  N N 85  
ARG HH11   H  N N 86  
ARG HH12   H  N N 87  
ARG HH21   H  N N 88  
ARG HH22   H  N N 89  
ARG HXT    H  N N 90  
ASN N      N  N N 91  
ASN CA     C  N S 92  
ASN C      C  N N 93  
ASN O      O  N N 94  
ASN CB     C  N N 95  
ASN CG     C  N N 96  
ASN OD1    O  N N 97  
ASN ND2    N  N N 98  
ASN OXT    O  N N 99  
ASN H      H  N N 100 
ASN H2     H  N N 101 
ASN HA     H  N N 102 
ASN HB2    H  N N 103 
ASN HB3    H  N N 104 
ASN HD21   H  N N 105 
ASN HD22   H  N N 106 
ASN HXT    H  N N 107 
ASP N      N  N N 108 
ASP CA     C  N S 109 
ASP C      C  N N 110 
ASP O      O  N N 111 
ASP CB     C  N N 112 
ASP CG     C  N N 113 
ASP OD1    O  N N 114 
ASP OD2    O  N N 115 
ASP OXT    O  N N 116 
ASP H      H  N N 117 
ASP H2     H  N N 118 
ASP HA     H  N N 119 
ASP HB2    H  N N 120 
ASP HB3    H  N N 121 
ASP HD2    H  N N 122 
ASP HXT    H  N N 123 
CYS N      N  N N 124 
CYS CA     C  N R 125 
CYS C      C  N N 126 
CYS O      O  N N 127 
CYS CB     C  N N 128 
CYS SG     S  N N 129 
CYS OXT    O  N N 130 
CYS H      H  N N 131 
CYS H2     H  N N 132 
CYS HA     H  N N 133 
CYS HB2    H  N N 134 
CYS HB3    H  N N 135 
CYS HG     H  N N 136 
CYS HXT    H  N N 137 
GLN N      N  N N 138 
GLN CA     C  N S 139 
GLN C      C  N N 140 
GLN O      O  N N 141 
GLN CB     C  N N 142 
GLN CG     C  N N 143 
GLN CD     C  N N 144 
GLN OE1    O  N N 145 
GLN NE2    N  N N 146 
GLN OXT    O  N N 147 
GLN H      H  N N 148 
GLN H2     H  N N 149 
GLN HA     H  N N 150 
GLN HB2    H  N N 151 
GLN HB3    H  N N 152 
GLN HG2    H  N N 153 
GLN HG3    H  N N 154 
GLN HE21   H  N N 155 
GLN HE22   H  N N 156 
GLN HXT    H  N N 157 
GLU N      N  N N 158 
GLU CA     C  N S 159 
GLU C      C  N N 160 
GLU O      O  N N 161 
GLU CB     C  N N 162 
GLU CG     C  N N 163 
GLU CD     C  N N 164 
GLU OE1    O  N N 165 
GLU OE2    O  N N 166 
GLU OXT    O  N N 167 
GLU H      H  N N 168 
GLU H2     H  N N 169 
GLU HA     H  N N 170 
GLU HB2    H  N N 171 
GLU HB3    H  N N 172 
GLU HG2    H  N N 173 
GLU HG3    H  N N 174 
GLU HE2    H  N N 175 
GLU HXT    H  N N 176 
GLY N      N  N N 177 
GLY CA     C  N N 178 
GLY C      C  N N 179 
GLY O      O  N N 180 
GLY OXT    O  N N 181 
GLY H      H  N N 182 
GLY H2     H  N N 183 
GLY HA2    H  N N 184 
GLY HA3    H  N N 185 
GLY HXT    H  N N 186 
GNP PG     P  N N 187 
GNP O1G    O  N N 188 
GNP O2G    O  N N 189 
GNP O3G    O  N N 190 
GNP N3B    N  N N 191 
GNP PB     P  N R 192 
GNP O1B    O  N N 193 
GNP O2B    O  N N 194 
GNP O3A    O  N N 195 
GNP PA     P  N S 196 
GNP O1A    O  N N 197 
GNP O2A    O  N N 198 
GNP "O5'"  O  N N 199 
GNP "C5'"  C  N N 200 
GNP "C4'"  C  N R 201 
GNP "O4'"  O  N N 202 
GNP "C3'"  C  N S 203 
GNP "O3'"  O  N N 204 
GNP "C2'"  C  N R 205 
GNP "O2'"  O  N N 206 
GNP "C1'"  C  N R 207 
GNP N9     N  Y N 208 
GNP C8     C  Y N 209 
GNP N7     N  Y N 210 
GNP C5     C  Y N 211 
GNP C6     C  Y N 212 
GNP O6     O  N N 213 
GNP N1     N  Y N 214 
GNP C2     C  Y N 215 
GNP N2     N  N N 216 
GNP N3     N  Y N 217 
GNP C4     C  Y N 218 
GNP HOG2   H  N N 219 
GNP HOG3   H  N N 220 
GNP HNB3   H  N N 221 
GNP HOB2   H  N N 222 
GNP HOA2   H  N N 223 
GNP "H5'2" H  N N 224 
GNP "H5'1" H  N N 225 
GNP "H4'"  H  N N 226 
GNP "H3'"  H  N N 227 
GNP "HO3'" H  N N 228 
GNP "H2'"  H  N N 229 
GNP "HO2'" H  N N 230 
GNP "H1'"  H  N N 231 
GNP H8     H  N N 232 
GNP HN1    H  N N 233 
GNP HN21   H  N N 234 
GNP HN22   H  N N 235 
HIS N      N  N N 236 
HIS CA     C  N S 237 
HIS C      C  N N 238 
HIS O      O  N N 239 
HIS CB     C  N N 240 
HIS CG     C  Y N 241 
HIS ND1    N  Y N 242 
HIS CD2    C  Y N 243 
HIS CE1    C  Y N 244 
HIS NE2    N  Y N 245 
HIS OXT    O  N N 246 
HIS H      H  N N 247 
HIS H2     H  N N 248 
HIS HA     H  N N 249 
HIS HB2    H  N N 250 
HIS HB3    H  N N 251 
HIS HD1    H  N N 252 
HIS HD2    H  N N 253 
HIS HE1    H  N N 254 
HIS HE2    H  N N 255 
HIS HXT    H  N N 256 
ILE N      N  N N 257 
ILE CA     C  N S 258 
ILE C      C  N N 259 
ILE O      O  N N 260 
ILE CB     C  N S 261 
ILE CG1    C  N N 262 
ILE CG2    C  N N 263 
ILE CD1    C  N N 264 
ILE OXT    O  N N 265 
ILE H      H  N N 266 
ILE H2     H  N N 267 
ILE HA     H  N N 268 
ILE HB     H  N N 269 
ILE HG12   H  N N 270 
ILE HG13   H  N N 271 
ILE HG21   H  N N 272 
ILE HG22   H  N N 273 
ILE HG23   H  N N 274 
ILE HD11   H  N N 275 
ILE HD12   H  N N 276 
ILE HD13   H  N N 277 
ILE HXT    H  N N 278 
LEU N      N  N N 279 
LEU CA     C  N S 280 
LEU C      C  N N 281 
LEU O      O  N N 282 
LEU CB     C  N N 283 
LEU CG     C  N N 284 
LEU CD1    C  N N 285 
LEU CD2    C  N N 286 
LEU OXT    O  N N 287 
LEU H      H  N N 288 
LEU H2     H  N N 289 
LEU HA     H  N N 290 
LEU HB2    H  N N 291 
LEU HB3    H  N N 292 
LEU HG     H  N N 293 
LEU HD11   H  N N 294 
LEU HD12   H  N N 295 
LEU HD13   H  N N 296 
LEU HD21   H  N N 297 
LEU HD22   H  N N 298 
LEU HD23   H  N N 299 
LEU HXT    H  N N 300 
LYS N      N  N N 301 
LYS CA     C  N S 302 
LYS C      C  N N 303 
LYS O      O  N N 304 
LYS CB     C  N N 305 
LYS CG     C  N N 306 
LYS CD     C  N N 307 
LYS CE     C  N N 308 
LYS NZ     N  N N 309 
LYS OXT    O  N N 310 
LYS H      H  N N 311 
LYS H2     H  N N 312 
LYS HA     H  N N 313 
LYS HB2    H  N N 314 
LYS HB3    H  N N 315 
LYS HG2    H  N N 316 
LYS HG3    H  N N 317 
LYS HD2    H  N N 318 
LYS HD3    H  N N 319 
LYS HE2    H  N N 320 
LYS HE3    H  N N 321 
LYS HZ1    H  N N 322 
LYS HZ2    H  N N 323 
LYS HZ3    H  N N 324 
LYS HXT    H  N N 325 
MET N      N  N N 326 
MET CA     C  N S 327 
MET C      C  N N 328 
MET O      O  N N 329 
MET CB     C  N N 330 
MET CG     C  N N 331 
MET SD     S  N N 332 
MET CE     C  N N 333 
MET OXT    O  N N 334 
MET H      H  N N 335 
MET H2     H  N N 336 
MET HA     H  N N 337 
MET HB2    H  N N 338 
MET HB3    H  N N 339 
MET HG2    H  N N 340 
MET HG3    H  N N 341 
MET HE1    H  N N 342 
MET HE2    H  N N 343 
MET HE3    H  N N 344 
MET HXT    H  N N 345 
MG  MG     MG N N 346 
PHE N      N  N N 347 
PHE CA     C  N S 348 
PHE C      C  N N 349 
PHE O      O  N N 350 
PHE CB     C  N N 351 
PHE CG     C  Y N 352 
PHE CD1    C  Y N 353 
PHE CD2    C  Y N 354 
PHE CE1    C  Y N 355 
PHE CE2    C  Y N 356 
PHE CZ     C  Y N 357 
PHE OXT    O  N N 358 
PHE H      H  N N 359 
PHE H2     H  N N 360 
PHE HA     H  N N 361 
PHE HB2    H  N N 362 
PHE HB3    H  N N 363 
PHE HD1    H  N N 364 
PHE HD2    H  N N 365 
PHE HE1    H  N N 366 
PHE HE2    H  N N 367 
PHE HZ     H  N N 368 
PHE HXT    H  N N 369 
PRO N      N  N N 370 
PRO CA     C  N S 371 
PRO C      C  N N 372 
PRO O      O  N N 373 
PRO CB     C  N N 374 
PRO CG     C  N N 375 
PRO CD     C  N N 376 
PRO OXT    O  N N 377 
PRO H      H  N N 378 
PRO HA     H  N N 379 
PRO HB2    H  N N 380 
PRO HB3    H  N N 381 
PRO HG2    H  N N 382 
PRO HG3    H  N N 383 
PRO HD2    H  N N 384 
PRO HD3    H  N N 385 
PRO HXT    H  N N 386 
SER N      N  N N 387 
SER CA     C  N S 388 
SER C      C  N N 389 
SER O      O  N N 390 
SER CB     C  N N 391 
SER OG     O  N N 392 
SER OXT    O  N N 393 
SER H      H  N N 394 
SER H2     H  N N 395 
SER HA     H  N N 396 
SER HB2    H  N N 397 
SER HB3    H  N N 398 
SER HG     H  N N 399 
SER HXT    H  N N 400 
THR N      N  N N 401 
THR CA     C  N S 402 
THR C      C  N N 403 
THR O      O  N N 404 
THR CB     C  N R 405 
THR OG1    O  N N 406 
THR CG2    C  N N 407 
THR OXT    O  N N 408 
THR H      H  N N 409 
THR H2     H  N N 410 
THR HA     H  N N 411 
THR HB     H  N N 412 
THR HG1    H  N N 413 
THR HG21   H  N N 414 
THR HG22   H  N N 415 
THR HG23   H  N N 416 
THR HXT    H  N N 417 
TRP N      N  N N 418 
TRP CA     C  N S 419 
TRP C      C  N N 420 
TRP O      O  N N 421 
TRP CB     C  N N 422 
TRP CG     C  Y N 423 
TRP CD1    C  Y N 424 
TRP CD2    C  Y N 425 
TRP NE1    N  Y N 426 
TRP CE2    C  Y N 427 
TRP CE3    C  Y N 428 
TRP CZ2    C  Y N 429 
TRP CZ3    C  Y N 430 
TRP CH2    C  Y N 431 
TRP OXT    O  N N 432 
TRP H      H  N N 433 
TRP H2     H  N N 434 
TRP HA     H  N N 435 
TRP HB2    H  N N 436 
TRP HB3    H  N N 437 
TRP HD1    H  N N 438 
TRP HE1    H  N N 439 
TRP HE3    H  N N 440 
TRP HZ2    H  N N 441 
TRP HZ3    H  N N 442 
TRP HH2    H  N N 443 
TRP HXT    H  N N 444 
TYR N      N  N N 445 
TYR CA     C  N S 446 
TYR C      C  N N 447 
TYR O      O  N N 448 
TYR CB     C  N N 449 
TYR CG     C  Y N 450 
TYR CD1    C  Y N 451 
TYR CD2    C  Y N 452 
TYR CE1    C  Y N 453 
TYR CE2    C  Y N 454 
TYR CZ     C  Y N 455 
TYR OH     O  N N 456 
TYR OXT    O  N N 457 
TYR H      H  N N 458 
TYR H2     H  N N 459 
TYR HA     H  N N 460 
TYR HB2    H  N N 461 
TYR HB3    H  N N 462 
TYR HD1    H  N N 463 
TYR HD2    H  N N 464 
TYR HE1    H  N N 465 
TYR HE2    H  N N 466 
TYR HH     H  N N 467 
TYR HXT    H  N N 468 
VAL N      N  N N 469 
VAL CA     C  N S 470 
VAL C      C  N N 471 
VAL O      O  N N 472 
VAL CB     C  N N 473 
VAL CG1    C  N N 474 
VAL CG2    C  N N 475 
VAL OXT    O  N N 476 
VAL H      H  N N 477 
VAL H2     H  N N 478 
VAL HA     H  N N 479 
VAL HB     H  N N 480 
VAL HG11   H  N N 481 
VAL HG12   H  N N 482 
VAL HG13   H  N N 483 
VAL HG21   H  N N 484 
VAL HG22   H  N N 485 
VAL HG23   H  N N 486 
VAL HXT    H  N N 487 
# 
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 
5H5 C24   N23    sing Y N 1   
5H5 C24   N25    doub Y N 2   
5H5 N23   C22    doub Y N 3   
5H5 N25   N26    sing Y N 4   
5H5 C22   N26    sing Y N 5   
5H5 C22   C16    sing N N 6   
5H5 N26   C27    sing N N 7   
5H5 C29   C27    sing N N 8   
5H5 C15   C16    doub Y N 9   
5H5 C15   N14    sing Y N 10  
5H5 C16   N17    sing Y N 11  
5H5 C27   C28    sing N N 12  
5H5 N14   C13    sing N N 13  
5H5 N14   C18    sing Y N 14  
5H5 N17   C18    doub Y N 15  
5H5 C13   C12    sing N N 16  
5H5 C12   O11    sing N N 17  
5H5 C18   C19    sing N N 18  
5H5 C19   C20    doub Y N 19  
5H5 C19   C10    sing Y N 20  
5H5 O11   C10    sing N N 21  
5H5 C20   C21    sing Y N 22  
5H5 C10   C9     doub Y N 23  
5H5 N1    C2     sing N N 24  
5H5 C21   C8     doub Y N 25  
5H5 C9    C8     sing Y N 26  
5H5 C8    O7     sing N N 27  
5H5 C2    O3     doub N N 28  
5H5 C2    C4     sing N N 29  
5H5 O7    C4     sing N N 30  
5H5 C4    C6     sing N N 31  
5H5 C4    H1     sing N N 32  
5H5 C6    H2     sing N N 33  
5H5 C6    H3     sing N N 34  
5H5 C6    H4     sing N N 35  
5H5 C12   H5     sing N N 36  
5H5 C12   H6     sing N N 37  
5H5 C15   H7     sing N N 38  
5H5 C21   H8     sing N N 39  
5H5 C24   H9     sing N N 40  
5H5 C27   H10    sing N N 41  
5H5 N1    H11    sing N N 42  
5H5 N1    H12    sing N N 43  
5H5 C9    H13    sing N N 44  
5H5 C13   H14    sing N N 45  
5H5 C13   H15    sing N N 46  
5H5 C20   H16    sing N N 47  
5H5 C28   H17    sing N N 48  
5H5 C28   H18    sing N N 49  
5H5 C28   H19    sing N N 50  
5H5 C29   H20    sing N N 51  
5H5 C29   H21    sing N N 52  
5H5 C29   H22    sing N N 53  
ALA N     CA     sing N N 54  
ALA N     H      sing N N 55  
ALA N     H2     sing N N 56  
ALA CA    C      sing N N 57  
ALA CA    CB     sing N N 58  
ALA CA    HA     sing N N 59  
ALA C     O      doub N N 60  
ALA C     OXT    sing N N 61  
ALA CB    HB1    sing N N 62  
ALA CB    HB2    sing N N 63  
ALA CB    HB3    sing N N 64  
ALA OXT   HXT    sing N N 65  
ARG N     CA     sing N N 66  
ARG N     H      sing N N 67  
ARG N     H2     sing N N 68  
ARG CA    C      sing N N 69  
ARG CA    CB     sing N N 70  
ARG CA    HA     sing N N 71  
ARG C     O      doub N N 72  
ARG C     OXT    sing N N 73  
ARG CB    CG     sing N N 74  
ARG CB    HB2    sing N N 75  
ARG CB    HB3    sing N N 76  
ARG CG    CD     sing N N 77  
ARG CG    HG2    sing N N 78  
ARG CG    HG3    sing N N 79  
ARG CD    NE     sing N N 80  
ARG CD    HD2    sing N N 81  
ARG CD    HD3    sing N N 82  
ARG NE    CZ     sing N N 83  
ARG NE    HE     sing N N 84  
ARG CZ    NH1    sing N N 85  
ARG CZ    NH2    doub N N 86  
ARG NH1   HH11   sing N N 87  
ARG NH1   HH12   sing N N 88  
ARG NH2   HH21   sing N N 89  
ARG NH2   HH22   sing N N 90  
ARG OXT   HXT    sing N N 91  
ASN N     CA     sing N N 92  
ASN N     H      sing N N 93  
ASN N     H2     sing N N 94  
ASN CA    C      sing N N 95  
ASN CA    CB     sing N N 96  
ASN CA    HA     sing N N 97  
ASN C     O      doub N N 98  
ASN C     OXT    sing N N 99  
ASN CB    CG     sing N N 100 
ASN CB    HB2    sing N N 101 
ASN CB    HB3    sing N N 102 
ASN CG    OD1    doub N N 103 
ASN CG    ND2    sing N N 104 
ASN ND2   HD21   sing N N 105 
ASN ND2   HD22   sing N N 106 
ASN OXT   HXT    sing N N 107 
ASP N     CA     sing N N 108 
ASP N     H      sing N N 109 
ASP N     H2     sing N N 110 
ASP CA    C      sing N N 111 
ASP CA    CB     sing N N 112 
ASP CA    HA     sing N N 113 
ASP C     O      doub N N 114 
ASP C     OXT    sing N N 115 
ASP CB    CG     sing N N 116 
ASP CB    HB2    sing N N 117 
ASP CB    HB3    sing N N 118 
ASP CG    OD1    doub N N 119 
ASP CG    OD2    sing N N 120 
ASP OD2   HD2    sing N N 121 
ASP OXT   HXT    sing N N 122 
CYS N     CA     sing N N 123 
CYS N     H      sing N N 124 
CYS N     H2     sing N N 125 
CYS CA    C      sing N N 126 
CYS CA    CB     sing N N 127 
CYS CA    HA     sing N N 128 
CYS C     O      doub N N 129 
CYS C     OXT    sing N N 130 
CYS CB    SG     sing N N 131 
CYS CB    HB2    sing N N 132 
CYS CB    HB3    sing N N 133 
CYS SG    HG     sing N N 134 
CYS OXT   HXT    sing N N 135 
GLN N     CA     sing N N 136 
GLN N     H      sing N N 137 
GLN N     H2     sing N N 138 
GLN CA    C      sing N N 139 
GLN CA    CB     sing N N 140 
GLN CA    HA     sing N N 141 
GLN C     O      doub N N 142 
GLN C     OXT    sing N N 143 
GLN CB    CG     sing N N 144 
GLN CB    HB2    sing N N 145 
GLN CB    HB3    sing N N 146 
GLN CG    CD     sing N N 147 
GLN CG    HG2    sing N N 148 
GLN CG    HG3    sing N N 149 
GLN CD    OE1    doub N N 150 
GLN CD    NE2    sing N N 151 
GLN NE2   HE21   sing N N 152 
GLN NE2   HE22   sing N N 153 
GLN OXT   HXT    sing N N 154 
GLU N     CA     sing N N 155 
GLU N     H      sing N N 156 
GLU N     H2     sing N N 157 
GLU CA    C      sing N N 158 
GLU CA    CB     sing N N 159 
GLU CA    HA     sing N N 160 
GLU C     O      doub N N 161 
GLU C     OXT    sing N N 162 
GLU CB    CG     sing N N 163 
GLU CB    HB2    sing N N 164 
GLU CB    HB3    sing N N 165 
GLU CG    CD     sing N N 166 
GLU CG    HG2    sing N N 167 
GLU CG    HG3    sing N N 168 
GLU CD    OE1    doub N N 169 
GLU CD    OE2    sing N N 170 
GLU OE2   HE2    sing N N 171 
GLU OXT   HXT    sing N N 172 
GLY N     CA     sing N N 173 
GLY N     H      sing N N 174 
GLY N     H2     sing N N 175 
GLY CA    C      sing N N 176 
GLY CA    HA2    sing N N 177 
GLY CA    HA3    sing N N 178 
GLY C     O      doub N N 179 
GLY C     OXT    sing N N 180 
GLY OXT   HXT    sing N N 181 
GNP PG    O1G    doub N N 182 
GNP PG    O2G    sing N N 183 
GNP PG    O3G    sing N N 184 
GNP PG    N3B    sing N N 185 
GNP O2G   HOG2   sing N N 186 
GNP O3G   HOG3   sing N N 187 
GNP N3B   PB     sing N N 188 
GNP N3B   HNB3   sing N N 189 
GNP PB    O1B    doub N N 190 
GNP PB    O2B    sing N N 191 
GNP PB    O3A    sing N N 192 
GNP O2B   HOB2   sing N N 193 
GNP O3A   PA     sing N N 194 
GNP PA    O1A    doub N N 195 
GNP PA    O2A    sing N N 196 
GNP PA    "O5'"  sing N N 197 
GNP O2A   HOA2   sing N N 198 
GNP "O5'" "C5'"  sing N N 199 
GNP "C5'" "C4'"  sing N N 200 
GNP "C5'" "H5'2" sing N N 201 
GNP "C5'" "H5'1" sing N N 202 
GNP "C4'" "O4'"  sing N N 203 
GNP "C4'" "C3'"  sing N N 204 
GNP "C4'" "H4'"  sing N N 205 
GNP "O4'" "C1'"  sing N N 206 
GNP "C3'" "O3'"  sing N N 207 
GNP "C3'" "C2'"  sing N N 208 
GNP "C3'" "H3'"  sing N N 209 
GNP "O3'" "HO3'" sing N N 210 
GNP "C2'" "O2'"  sing N N 211 
GNP "C2'" "C1'"  sing N N 212 
GNP "C2'" "H2'"  sing N N 213 
GNP "O2'" "HO2'" sing N N 214 
GNP "C1'" N9     sing N N 215 
GNP "C1'" "H1'"  sing N N 216 
GNP N9    C8     sing Y N 217 
GNP N9    C4     sing Y N 218 
GNP C8    N7     doub Y N 219 
GNP C8    H8     sing N N 220 
GNP N7    C5     sing Y N 221 
GNP C5    C6     sing Y N 222 
GNP C5    C4     doub Y N 223 
GNP C6    O6     doub N N 224 
GNP C6    N1     sing Y N 225 
GNP N1    C2     sing Y N 226 
GNP N1    HN1    sing N N 227 
GNP C2    N2     sing N N 228 
GNP C2    N3     doub Y N 229 
GNP N2    HN21   sing N N 230 
GNP N2    HN22   sing N N 231 
GNP N3    C4     sing Y N 232 
HIS N     CA     sing N N 233 
HIS N     H      sing N N 234 
HIS N     H2     sing N N 235 
HIS CA    C      sing N N 236 
HIS CA    CB     sing N N 237 
HIS CA    HA     sing N N 238 
HIS C     O      doub N N 239 
HIS C     OXT    sing N N 240 
HIS CB    CG     sing N N 241 
HIS CB    HB2    sing N N 242 
HIS CB    HB3    sing N N 243 
HIS CG    ND1    sing Y N 244 
HIS CG    CD2    doub Y N 245 
HIS ND1   CE1    doub Y N 246 
HIS ND1   HD1    sing N N 247 
HIS CD2   NE2    sing Y N 248 
HIS CD2   HD2    sing N N 249 
HIS CE1   NE2    sing Y N 250 
HIS CE1   HE1    sing N N 251 
HIS NE2   HE2    sing N N 252 
HIS OXT   HXT    sing N N 253 
ILE N     CA     sing N N 254 
ILE N     H      sing N N 255 
ILE N     H2     sing N N 256 
ILE CA    C      sing N N 257 
ILE CA    CB     sing N N 258 
ILE CA    HA     sing N N 259 
ILE C     O      doub N N 260 
ILE C     OXT    sing N N 261 
ILE CB    CG1    sing N N 262 
ILE CB    CG2    sing N N 263 
ILE CB    HB     sing N N 264 
ILE CG1   CD1    sing N N 265 
ILE CG1   HG12   sing N N 266 
ILE CG1   HG13   sing N N 267 
ILE CG2   HG21   sing N N 268 
ILE CG2   HG22   sing N N 269 
ILE CG2   HG23   sing N N 270 
ILE CD1   HD11   sing N N 271 
ILE CD1   HD12   sing N N 272 
ILE CD1   HD13   sing N N 273 
ILE OXT   HXT    sing N N 274 
LEU N     CA     sing N N 275 
LEU N     H      sing N N 276 
LEU N     H2     sing N N 277 
LEU CA    C      sing N N 278 
LEU CA    CB     sing N N 279 
LEU CA    HA     sing N N 280 
LEU C     O      doub N N 281 
LEU C     OXT    sing N N 282 
LEU CB    CG     sing N N 283 
LEU CB    HB2    sing N N 284 
LEU CB    HB3    sing N N 285 
LEU CG    CD1    sing N N 286 
LEU CG    CD2    sing N N 287 
LEU CG    HG     sing N N 288 
LEU CD1   HD11   sing N N 289 
LEU CD1   HD12   sing N N 290 
LEU CD1   HD13   sing N N 291 
LEU CD2   HD21   sing N N 292 
LEU CD2   HD22   sing N N 293 
LEU CD2   HD23   sing N N 294 
LEU OXT   HXT    sing N N 295 
LYS N     CA     sing N N 296 
LYS N     H      sing N N 297 
LYS N     H2     sing N N 298 
LYS CA    C      sing N N 299 
LYS CA    CB     sing N N 300 
LYS CA    HA     sing N N 301 
LYS C     O      doub N N 302 
LYS C     OXT    sing N N 303 
LYS CB    CG     sing N N 304 
LYS CB    HB2    sing N N 305 
LYS CB    HB3    sing N N 306 
LYS CG    CD     sing N N 307 
LYS CG    HG2    sing N N 308 
LYS CG    HG3    sing N N 309 
LYS CD    CE     sing N N 310 
LYS CD    HD2    sing N N 311 
LYS CD    HD3    sing N N 312 
LYS CE    NZ     sing N N 313 
LYS CE    HE2    sing N N 314 
LYS CE    HE3    sing N N 315 
LYS NZ    HZ1    sing N N 316 
LYS NZ    HZ2    sing N N 317 
LYS NZ    HZ3    sing N N 318 
LYS OXT   HXT    sing N N 319 
MET N     CA     sing N N 320 
MET N     H      sing N N 321 
MET N     H2     sing N N 322 
MET CA    C      sing N N 323 
MET CA    CB     sing N N 324 
MET CA    HA     sing N N 325 
MET C     O      doub N N 326 
MET C     OXT    sing N N 327 
MET CB    CG     sing N N 328 
MET CB    HB2    sing N N 329 
MET CB    HB3    sing N N 330 
MET CG    SD     sing N N 331 
MET CG    HG2    sing N N 332 
MET CG    HG3    sing N N 333 
MET SD    CE     sing N N 334 
MET CE    HE1    sing N N 335 
MET CE    HE2    sing N N 336 
MET CE    HE3    sing N N 337 
MET OXT   HXT    sing N N 338 
PHE N     CA     sing N N 339 
PHE N     H      sing N N 340 
PHE N     H2     sing N N 341 
PHE CA    C      sing N N 342 
PHE CA    CB     sing N N 343 
PHE CA    HA     sing N N 344 
PHE C     O      doub N N 345 
PHE C     OXT    sing N N 346 
PHE CB    CG     sing N N 347 
PHE CB    HB2    sing N N 348 
PHE CB    HB3    sing N N 349 
PHE CG    CD1    doub Y N 350 
PHE CG    CD2    sing Y N 351 
PHE CD1   CE1    sing Y N 352 
PHE CD1   HD1    sing N N 353 
PHE CD2   CE2    doub Y N 354 
PHE CD2   HD2    sing N N 355 
PHE CE1   CZ     doub Y N 356 
PHE CE1   HE1    sing N N 357 
PHE CE2   CZ     sing Y N 358 
PHE CE2   HE2    sing N N 359 
PHE CZ    HZ     sing N N 360 
PHE OXT   HXT    sing N N 361 
PRO N     CA     sing N N 362 
PRO N     CD     sing N N 363 
PRO N     H      sing N N 364 
PRO CA    C      sing N N 365 
PRO CA    CB     sing N N 366 
PRO CA    HA     sing N N 367 
PRO C     O      doub N N 368 
PRO C     OXT    sing N N 369 
PRO CB    CG     sing N N 370 
PRO CB    HB2    sing N N 371 
PRO CB    HB3    sing N N 372 
PRO CG    CD     sing N N 373 
PRO CG    HG2    sing N N 374 
PRO CG    HG3    sing N N 375 
PRO CD    HD2    sing N N 376 
PRO CD    HD3    sing N N 377 
PRO OXT   HXT    sing N N 378 
SER N     CA     sing N N 379 
SER N     H      sing N N 380 
SER N     H2     sing N N 381 
SER CA    C      sing N N 382 
SER CA    CB     sing N N 383 
SER CA    HA     sing N N 384 
SER C     O      doub N N 385 
SER C     OXT    sing N N 386 
SER CB    OG     sing N N 387 
SER CB    HB2    sing N N 388 
SER CB    HB3    sing N N 389 
SER OG    HG     sing N N 390 
SER OXT   HXT    sing N N 391 
THR N     CA     sing N N 392 
THR N     H      sing N N 393 
THR N     H2     sing N N 394 
THR CA    C      sing N N 395 
THR CA    CB     sing N N 396 
THR CA    HA     sing N N 397 
THR C     O      doub N N 398 
THR C     OXT    sing N N 399 
THR CB    OG1    sing N N 400 
THR CB    CG2    sing N N 401 
THR CB    HB     sing N N 402 
THR OG1   HG1    sing N N 403 
THR CG2   HG21   sing N N 404 
THR CG2   HG22   sing N N 405 
THR CG2   HG23   sing N N 406 
THR OXT   HXT    sing N N 407 
TRP N     CA     sing N N 408 
TRP N     H      sing N N 409 
TRP N     H2     sing N N 410 
TRP CA    C      sing N N 411 
TRP CA    CB     sing N N 412 
TRP CA    HA     sing N N 413 
TRP C     O      doub N N 414 
TRP C     OXT    sing N N 415 
TRP CB    CG     sing N N 416 
TRP CB    HB2    sing N N 417 
TRP CB    HB3    sing N N 418 
TRP CG    CD1    doub Y N 419 
TRP CG    CD2    sing Y N 420 
TRP CD1   NE1    sing Y N 421 
TRP CD1   HD1    sing N N 422 
TRP CD2   CE2    doub Y N 423 
TRP CD2   CE3    sing Y N 424 
TRP NE1   CE2    sing Y N 425 
TRP NE1   HE1    sing N N 426 
TRP CE2   CZ2    sing Y N 427 
TRP CE3   CZ3    doub Y N 428 
TRP CE3   HE3    sing N N 429 
TRP CZ2   CH2    doub Y N 430 
TRP CZ2   HZ2    sing N N 431 
TRP CZ3   CH2    sing Y N 432 
TRP CZ3   HZ3    sing N N 433 
TRP CH2   HH2    sing N N 434 
TRP OXT   HXT    sing N N 435 
TYR N     CA     sing N N 436 
TYR N     H      sing N N 437 
TYR N     H2     sing N N 438 
TYR CA    C      sing N N 439 
TYR CA    CB     sing N N 440 
TYR CA    HA     sing N N 441 
TYR C     O      doub N N 442 
TYR C     OXT    sing N N 443 
TYR CB    CG     sing N N 444 
TYR CB    HB2    sing N N 445 
TYR CB    HB3    sing N N 446 
TYR CG    CD1    doub Y N 447 
TYR CG    CD2    sing Y N 448 
TYR CD1   CE1    sing Y N 449 
TYR CD1   HD1    sing N N 450 
TYR CD2   CE2    doub Y N 451 
TYR CD2   HD2    sing N N 452 
TYR CE1   CZ     doub Y N 453 
TYR CE1   HE1    sing N N 454 
TYR CE2   CZ     sing Y N 455 
TYR CE2   HE2    sing N N 456 
TYR CZ    OH     sing N N 457 
TYR OH    HH     sing N N 458 
TYR OXT   HXT    sing N N 459 
VAL N     CA     sing N N 460 
VAL N     H      sing N N 461 
VAL N     H2     sing N N 462 
VAL CA    C      sing N N 463 
VAL CA    CB     sing N N 464 
VAL CA    HA     sing N N 465 
VAL C     O      doub N N 466 
VAL C     OXT    sing N N 467 
VAL CB    CG1    sing N N 468 
VAL CB    CG2    sing N N 469 
VAL CB    HB     sing N N 470 
VAL CG1   HG11   sing N N 471 
VAL CG1   HG12   sing N N 472 
VAL CG1   HG13   sing N N 473 
VAL CG2   HG21   sing N N 474 
VAL CG2   HG22   sing N N 475 
VAL CG2   HG23   sing N N 476 
VAL OXT   HXT    sing N N 477 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N91019D00024 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 2ERY ? 
2 ? 'experimental model' PDB 5DXT ? 
# 
_atom_sites.entry_id                    9B4S 
_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]   0.005510 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005510 
_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]   0.010413 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ASN A 1 4   ? -25.477 -43.386 -10.819 1.00 224.11 ? 107  ASN A N     1 
ATOM   2    C  CA    . ASN A 1 4   ? -26.472 -42.796 -9.931  1.00 213.83 ? 107  ASN A CA    1 
ATOM   3    C  C     . ASN A 1 4   ? -25.846 -41.749 -9.017  1.00 196.59 ? 107  ASN A C     1 
ATOM   4    O  O     . ASN A 1 4   ? -26.550 -41.058 -8.282  1.00 192.80 ? 107  ASN A O     1 
ATOM   5    C  CB    . ASN A 1 4   ? -27.155 -43.880 -9.094  1.00 216.60 ? 107  ASN A CB    1 
ATOM   6    C  CG    . ASN A 1 4   ? -27.981 -44.832 -9.936  1.00 220.70 ? 107  ASN A CG    1 
ATOM   7    O  OD1   . ASN A 1 4   ? -27.834 -44.888 -11.157 1.00 230.27 ? 107  ASN A OD1   1 
ATOM   8    N  ND2   . ASN A 1 4   ? -28.858 -45.589 -9.285  1.00 194.80 ? 107  ASN A ND2   1 
ATOM   9    N  N     . ARG A 1 5   ? -24.517 -41.635 -9.067  1.00 189.72 ? 108  ARG A N     1 
ATOM   10   C  CA    . ARG A 1 5   ? -23.828 -40.680 -8.206  1.00 182.36 ? 108  ARG A CA    1 
ATOM   11   C  C     . ARG A 1 5   ? -24.088 -39.241 -8.633  1.00 199.17 ? 108  ARG A C     1 
ATOM   12   O  O     . ARG A 1 5   ? -24.151 -38.347 -7.782  1.00 200.48 ? 108  ARG A O     1 
ATOM   13   C  CB    . ARG A 1 5   ? -22.327 -40.972 -8.192  1.00 195.93 ? 108  ARG A CB    1 
ATOM   14   C  CG    . ARG A 1 5   ? -21.701 -41.095 -9.570  1.00 203.34 ? 108  ARG A CG    1 
ATOM   15   C  CD    . ARG A 1 5   ? -20.215 -41.399 -9.475  1.00 223.44 ? 108  ARG A CD    1 
ATOM   16   N  NE    . ARG A 1 5   ? -19.613 -41.594 -10.788 1.00 216.85 ? 108  ARG A NE    1 
ATOM   17   C  CZ    . ARG A 1 5   ? -19.538 -42.762 -11.411 1.00 189.79 ? 108  ARG A CZ    1 
ATOM   18   N  NH1   . ARG A 1 5   ? -20.019 -43.868 -10.867 1.00 170.31 ? 108  ARG A NH1   1 
ATOM   19   N  NH2   . ARG A 1 5   ? -18.965 -42.823 -12.610 1.00 173.94 ? 108  ARG A NH2   1 
ATOM   20   N  N     . GLU A 1 6   ? -24.241 -38.994 -9.937  1.00 218.18 ? 109  GLU A N     1 
ATOM   21   C  CA    . GLU A 1 6   ? -24.554 -37.644 -10.395 1.00 189.92 ? 109  GLU A CA    1 
ATOM   22   C  C     . GLU A 1 6   ? -26.003 -37.277 -10.104 1.00 184.95 ? 109  GLU A C     1 
ATOM   23   O  O     . GLU A 1 6   ? -26.304 -36.107 -9.842  1.00 192.27 ? 109  GLU A O     1 
ATOM   24   C  CB    . GLU A 1 6   ? -24.267 -37.507 -11.892 1.00 188.05 ? 109  GLU A CB    1 
ATOM   25   C  CG    . GLU A 1 6   ? -22.799 -37.629 -12.273 1.00 174.26 ? 109  GLU A CG    1 
ATOM   26   C  CD    . GLU A 1 6   ? -22.340 -39.069 -12.393 1.00 207.09 ? 109  GLU A CD    1 
ATOM   27   O  OE1   . GLU A 1 6   ? -23.187 -39.979 -12.265 1.00 235.50 ? 109  GLU A OE1   1 
ATOM   28   O  OE2   . GLU A 1 6   ? -21.132 -39.292 -12.618 1.00 208.01 ? 109  GLU A OE2   1 
ATOM   29   N  N     . GLU A 1 7   ? -26.910 -38.257 -10.147 1.00 183.68 ? 110  GLU A N     1 
ATOM   30   C  CA    . GLU A 1 7   ? -28.313 -37.980 -9.860  1.00 188.64 ? 110  GLU A CA    1 
ATOM   31   C  C     . GLU A 1 7   ? -28.524 -37.604 -8.400  1.00 177.95 ? 110  GLU A C     1 
ATOM   32   O  O     . GLU A 1 7   ? -29.466 -36.869 -8.081  1.00 162.46 ? 110  GLU A O     1 
ATOM   33   C  CB    . GLU A 1 7   ? -29.170 -39.190 -10.228 1.00 198.49 ? 110  GLU A CB    1 
ATOM   34   C  CG    . GLU A 1 7   ? -29.011 -39.641 -11.670 1.00 195.68 ? 110  GLU A CG    1 
ATOM   35   C  CD    . GLU A 1 7   ? -29.775 -40.913 -11.967 1.00 205.43 ? 110  GLU A CD    1 
ATOM   36   O  OE1   . GLU A 1 7   ? -30.535 -41.368 -11.086 1.00 215.87 ? 110  GLU A OE1   1 
ATOM   37   O  OE2   . GLU A 1 7   ? -29.615 -41.461 -13.077 1.00 217.75 ? 110  GLU A OE2   1 
ATOM   38   N  N     . LYS A 1 8   ? -27.664 -38.092 -7.503  1.00 190.58 ? 111  LYS A N     1 
ATOM   39   C  CA    . LYS A 1 8   ? -27.749 -37.705 -6.101  1.00 183.08 ? 111  LYS A CA    1 
ATOM   40   C  C     . LYS A 1 8   ? -27.444 -36.228 -5.893  1.00 179.35 ? 111  LYS A C     1 
ATOM   41   O  O     . LYS A 1 8   ? -27.812 -35.673 -4.853  1.00 200.37 ? 111  LYS A O     1 
ATOM   42   C  CB    . LYS A 1 8   ? -26.795 -38.555 -5.261  1.00 173.96 ? 111  LYS A CB    1 
ATOM   43   C  CG    . LYS A 1 8   ? -27.081 -40.046 -5.316  1.00 176.17 ? 111  LYS A CG    1 
ATOM   44   C  CD    . LYS A 1 8   ? -25.960 -40.848 -4.677  1.00 190.32 ? 111  LYS A CD    1 
ATOM   45   C  CE    . LYS A 1 8   ? -26.186 -42.341 -4.844  1.00 166.65 ? 111  LYS A CE    1 
ATOM   46   N  NZ    . LYS A 1 8   ? -25.059 -43.137 -4.285  1.00 222.49 ? 111  LYS A NZ    1 
ATOM   47   N  N     . ILE A 1 9   ? -26.785 -35.585 -6.853  1.00 175.85 ? 112  ILE A N     1 
ATOM   48   C  CA    . ILE A 1 9   ? -26.469 -34.165 -6.745  1.00 193.43 ? 112  ILE A CA    1 
ATOM   49   C  C     . ILE A 1 9   ? -27.527 -33.307 -7.428  1.00 169.75 ? 112  ILE A C     1 
ATOM   50   O  O     . ILE A 1 9   ? -27.937 -32.275 -6.892  1.00 172.35 ? 112  ILE A O     1 
ATOM   51   C  CB    . ILE A 1 9   ? -25.066 -33.896 -7.325  1.00 194.25 ? 112  ILE A CB    1 
ATOM   52   C  CG1   . ILE A 1 9   ? -24.020 -34.756 -6.612  1.00 185.53 ? 112  ILE A CG1   1 
ATOM   53   C  CG2   . ILE A 1 9   ? -24.714 -32.421 -7.215  1.00 178.73 ? 112  ILE A CG2   1 
ATOM   54   C  CD1   . ILE A 1 9   ? -22.615 -34.577 -7.146  1.00 148.12 ? 112  ILE A CD1   1 
ATOM   55   N  N     . LEU A 1 10  ? -27.986 -33.720 -8.613  1.00 172.19 ? 113  LEU A N     1 
ATOM   56   C  CA    . LEU A 1 10  ? -28.971 -32.926 -9.342  1.00 181.87 ? 113  LEU A CA    1 
ATOM   57   C  C     . LEU A 1 10  ? -30.323 -32.934 -8.640  1.00 156.14 ? 113  LEU A C     1 
ATOM   58   O  O     . LEU A 1 10  ? -31.019 -31.913 -8.614  1.00 150.66 ? 113  LEU A O     1 
ATOM   59   C  CB    . LEU A 1 10  ? -29.108 -33.443 -10.774 1.00 183.63 ? 113  LEU A CB    1 
ATOM   60   C  CG    . LEU A 1 10  ? -27.871 -33.331 -11.668 1.00 196.94 ? 113  LEU A CG    1 
ATOM   61   C  CD1   . LEU A 1 10  ? -28.167 -33.866 -13.061 1.00 190.05 ? 113  LEU A CD1   1 
ATOM   62   C  CD2   . LEU A 1 10  ? -27.383 -31.892 -11.736 1.00 184.22 ? 113  LEU A CD2   1 
ATOM   63   N  N     . ASN A 1 11  ? -30.712 -34.074 -8.064  1.00 156.26 ? 114  ASN A N     1 
ATOM   64   C  CA    . ASN A 1 11  ? -32.004 -34.168 -7.392  1.00 157.00 ? 114  ASN A CA    1 
ATOM   65   C  C     . ASN A 1 11  ? -32.079 -33.297 -6.145  1.00 168.82 ? 114  ASN A C     1 
ATOM   66   O  O     . ASN A 1 11  ? -33.184 -32.967 -5.702  1.00 137.91 ? 114  ASN A O     1 
ATOM   67   C  CB    . ASN A 1 11  ? -32.305 -35.623 -7.030  1.00 159.28 ? 114  ASN A CB    1 
ATOM   68   C  CG    . ASN A 1 11  ? -32.638 -36.469 -8.245  1.00 171.05 ? 114  ASN A CG    1 
ATOM   69   O  OD1   . ASN A 1 11  ? -33.808 -36.706 -8.548  1.00 163.19 ? 114  ASN A OD1   1 
ATOM   70   N  ND2   . ASN A 1 11  ? -31.610 -36.926 -8.949  1.00 162.89 ? 114  ASN A ND2   1 
ATOM   71   N  N     . ARG A 1 12  ? -30.936 -32.918 -5.569  1.00 180.40 ? 115  ARG A N     1 
ATOM   72   C  CA    . ARG A 1 12  ? -30.946 -32.045 -4.400  1.00 168.63 ? 115  ARG A CA    1 
ATOM   73   C  C     . ARG A 1 12  ? -31.383 -30.634 -4.777  1.00 162.77 ? 115  ARG A C     1 
ATOM   74   O  O     . ARG A 1 12  ? -32.335 -30.089 -4.206  1.00 152.63 ? 115  ARG A O     1 
ATOM   75   C  CB    . ARG A 1 12  ? -29.562 -32.026 -3.748  1.00 168.39 ? 115  ARG A CB    1 
ATOM   76   C  CG    . ARG A 1 12  ? -29.153 -33.342 -3.112  1.00 184.90 ? 115  ARG A CG    1 
ATOM   77   C  CD    . ARG A 1 12  ? -29.895 -33.586 -1.808  1.00 216.37 ? 115  ARG A CD    1 
ATOM   78   N  NE    . ARG A 1 12  ? -29.587 -32.570 -0.809  1.00 215.69 ? 115  ARG A NE    1 
ATOM   79   C  CZ    . ARG A 1 12  ? -29.994 -32.609 0.452   1.00 197.37 ? 115  ARG A CZ    1 
ATOM   80   N  NH1   . ARG A 1 12  ? -30.727 -33.611 0.911   1.00 191.59 ? 115  ARG A NH1   1 
ATOM   81   N  NH2   . ARG A 1 12  ? -29.656 -31.620 1.274   1.00 176.13 ? 115  ARG A NH2   1 
ATOM   82   N  N     . GLU A 1 13  ? -30.696 -30.026 -5.747  1.00 169.99 ? 116  GLU A N     1 
ATOM   83   C  CA    . GLU A 1 13  ? -31.009 -28.659 -6.144  1.00 152.26 ? 116  GLU A CA    1 
ATOM   84   C  C     . GLU A 1 13  ? -32.352 -28.547 -6.853  1.00 154.90 ? 116  GLU A C     1 
ATOM   85   O  O     . GLU A 1 13  ? -32.937 -27.459 -6.872  1.00 147.82 ? 116  GLU A O     1 
ATOM   86   C  CB    . GLU A 1 13  ? -29.896 -28.105 -7.037  1.00 172.44 ? 116  GLU A CB    1 
ATOM   87   C  CG    . GLU A 1 13  ? -29.468 -29.042 -8.155  1.00 173.63 ? 116  GLU A CG    1 
ATOM   88   C  CD    . GLU A 1 13  ? -28.291 -28.504 -8.946  1.00 178.48 ? 116  GLU A CD    1 
ATOM   89   O  OE1   . GLU A 1 13  ? -28.042 -27.282 -8.888  1.00 183.22 ? 116  GLU A OE1   1 
ATOM   90   O  OE2   . GLU A 1 13  ? -27.612 -29.305 -9.622  1.00 158.32 ? 116  GLU A OE2   1 
ATOM   91   N  N     . ILE A 1 14  ? -32.855 -29.639 -7.433  1.00 170.31 ? 117  ILE A N     1 
ATOM   92   C  CA    . ILE A 1 14  ? -34.172 -29.597 -8.061  1.00 135.02 ? 117  ILE A CA    1 
ATOM   93   C  C     . ILE A 1 14  ? -35.259 -29.424 -7.008  1.00 136.32 ? 117  ILE A C     1 
ATOM   94   O  O     . ILE A 1 14  ? -36.198 -28.638 -7.189  1.00 158.72 ? 117  ILE A O     1 
ATOM   95   C  CB    . ILE A 1 14  ? -34.398 -30.857 -8.917  1.00 121.92 ? 117  ILE A CB    1 
ATOM   96   C  CG1   . ILE A 1 14  ? -33.537 -30.804 -10.180 1.00 140.62 ? 117  ILE A CG1   1 
ATOM   97   C  CG2   . ILE A 1 14  ? -35.867 -31.007 -9.280  1.00 114.35 ? 117  ILE A CG2   1 
ATOM   98   C  CD1   . ILE A 1 14  ? -33.740 -31.982 -11.110 1.00 132.42 ? 117  ILE A CD1   1 
ATOM   99   N  N     . GLY A 1 15  ? -35.145 -30.139 -5.887  1.00 143.51 ? 118  GLY A N     1 
ATOM   100  C  CA    . GLY A 1 15  ? -36.121 -30.013 -4.819  1.00 138.26 ? 118  GLY A CA    1 
ATOM   101  C  C     . GLY A 1 15  ? -36.126 -28.660 -4.139  1.00 142.08 ? 118  GLY A C     1 
ATOM   102  O  O     . GLY A 1 15  ? -37.141 -28.280 -3.546  1.00 125.98 ? 118  GLY A O     1 
ATOM   103  N  N     . PHE A 1 16  ? -35.014 -27.923 -4.211  1.00 140.15 ? 119  PHE A N     1 
ATOM   104  C  CA    . PHE A 1 16  ? -34.968 -26.594 -3.610  1.00 140.39 ? 119  PHE A CA    1 
ATOM   105  C  C     . PHE A 1 16  ? -35.822 -25.606 -4.396  1.00 157.18 ? 119  PHE A C     1 
ATOM   106  O  O     . PHE A 1 16  ? -36.573 -24.819 -3.808  1.00 141.04 ? 119  PHE A O     1 
ATOM   107  C  CB    . PHE A 1 16  ? -33.520 -26.108 -3.528  1.00 150.37 ? 119  PHE A CB    1 
ATOM   108  C  CG    . PHE A 1 16  ? -33.316 -24.936 -2.604  1.00 165.42 ? 119  PHE A CG    1 
ATOM   109  C  CD1   . PHE A 1 16  ? -34.304 -24.551 -1.712  1.00 160.86 ? 119  PHE A CD1   1 
ATOM   110  C  CD2   . PHE A 1 16  ? -32.132 -24.218 -2.633  1.00 159.13 ? 119  PHE A CD2   1 
ATOM   111  C  CE1   . PHE A 1 16  ? -34.114 -23.474 -0.866  1.00 162.10 ? 119  PHE A CE1   1 
ATOM   112  C  CE2   . PHE A 1 16  ? -31.936 -23.139 -1.790  1.00 163.58 ? 119  PHE A CE2   1 
ATOM   113  C  CZ    . PHE A 1 16  ? -32.929 -22.767 -0.905  1.00 153.23 ? 119  PHE A CZ    1 
ATOM   114  N  N     . ALA A 1 17  ? -35.722 -25.634 -5.728  1.00 158.70 ? 120  ALA A N     1 
ATOM   115  C  CA    . ALA A 1 17  ? -36.489 -24.703 -6.548  1.00 130.66 ? 120  ALA A CA    1 
ATOM   116  C  C     . ALA A 1 17  ? -37.978 -25.027 -6.532  1.00 147.73 ? 120  ALA A C     1 
ATOM   117  O  O     . ALA A 1 17  ? -38.809 -24.115 -6.599  1.00 115.20 ? 120  ALA A O     1 
ATOM   118  C  CB    . ALA A 1 17  ? -35.961 -24.710 -7.982  1.00 121.14 ? 120  ALA A CB    1 
ATOM   119  N  N     . ILE A 1 18  ? -38.333 -26.309 -6.443  1.00 129.15 ? 121  ILE A N     1 
ATOM   120  C  CA    . ILE A 1 18  ? -39.743 -26.683 -6.431  1.00 124.70 ? 121  ILE A CA    1 
ATOM   121  C  C     . ILE A 1 18  ? -40.369 -26.410 -5.067  1.00 136.24 ? 121  ILE A C     1 
ATOM   122  O  O     . ILE A 1 18  ? -41.562 -26.093 -4.980  1.00 124.46 ? 121  ILE A O     1 
ATOM   123  C  CB    . ILE A 1 18  ? -39.902 -28.158 -6.840  1.00 121.30 ? 121  ILE A CB    1 
ATOM   124  C  CG1   . ILE A 1 18  ? -39.230 -28.409 -8.191  1.00 128.72 ? 121  ILE A CG1   1 
ATOM   125  C  CG2   . ILE A 1 18  ? -41.370 -28.544 -6.911  1.00 135.96 ? 121  ILE A CG2   1 
ATOM   126  C  CD1   . ILE A 1 18  ? -39.336 -29.842 -8.666  1.00 144.92 ? 121  ILE A CD1   1 
ATOM   127  N  N     . GLY A 1 19  ? -39.590 -26.510 -3.993  1.00 125.60 ? 122  GLY A N     1 
ATOM   128  C  CA    . GLY A 1 19  ? -40.107 -26.330 -2.655  1.00 138.54 ? 122  GLY A CA    1 
ATOM   129  C  C     . GLY A 1 19  ? -40.505 -27.607 -1.950  1.00 147.40 ? 122  GLY A C     1 
ATOM   130  O  O     . GLY A 1 19  ? -40.988 -27.542 -0.811  1.00 164.79 ? 122  GLY A O     1 
ATOM   131  N  N     . MET A 1 20  ? -40.323 -28.761 -2.586  1.00 152.58 ? 123  MET A N     1 
ATOM   132  C  CA    . MET A 1 20  ? -40.642 -30.052 -1.997  1.00 157.95 ? 123  MET A CA    1 
ATOM   133  C  C     . MET A 1 20  ? -39.639 -31.071 -2.509  1.00 170.55 ? 123  MET A C     1 
ATOM   134  O  O     . MET A 1 20  ? -39.144 -30.938 -3.635  1.00 141.23 ? 123  MET A O     1 
ATOM   135  C  CB    . MET A 1 20  ? -42.074 -30.492 -2.337  1.00 136.19 ? 123  MET A CB    1 
ATOM   136  C  CG    . MET A 1 20  ? -42.456 -30.315 -3.796  1.00 128.27 ? 123  MET A CG    1 
ATOM   137  S  SD    . MET A 1 20  ? -44.118 -30.924 -4.136  1.00 131.03 ? 123  MET A SD    1 
ATOM   138  C  CE    . MET A 1 20  ? -44.465 -30.112 -5.693  1.00 166.49 ? 123  MET A CE    1 
ATOM   139  N  N     . PRO A 1 21  ? -39.312 -32.087 -1.714  1.00 179.85 ? 124  PRO A N     1 
ATOM   140  C  CA    . PRO A 1 21  ? -38.322 -33.077 -2.149  1.00 162.29 ? 124  PRO A CA    1 
ATOM   141  C  C     . PRO A 1 21  ? -38.827 -33.911 -3.317  1.00 176.44 ? 124  PRO A C     1 
ATOM   142  O  O     . PRO A 1 21  ? -40.030 -34.077 -3.534  1.00 178.98 ? 124  PRO A O     1 
ATOM   143  C  CB    . PRO A 1 21  ? -38.111 -33.941 -0.902  1.00 162.96 ? 124  PRO A CB    1 
ATOM   144  C  CG    . PRO A 1 21  ? -39.369 -33.774 -0.117  1.00 157.42 ? 124  PRO A CG    1 
ATOM   145  C  CD    . PRO A 1 21  ? -39.807 -32.362 -0.354  1.00 160.09 ? 124  PRO A CD    1 
ATOM   146  N  N     . VAL A 1 22  ? -37.868 -34.444 -4.079  1.00 183.75 ? 125  VAL A N     1 
ATOM   147  C  CA    . VAL A 1 22  ? -38.197 -35.259 -5.241  1.00 173.80 ? 125  VAL A CA    1 
ATOM   148  C  C     . VAL A 1 22  ? -38.785 -36.605 -4.836  1.00 181.80 ? 125  VAL A C     1 
ATOM   149  O  O     . VAL A 1 22  ? -39.522 -37.217 -5.619  1.00 177.19 ? 125  VAL A O     1 
ATOM   150  C  CB    . VAL A 1 22  ? -36.947 -35.450 -6.122  1.00 154.46 ? 125  VAL A CB    1 
ATOM   151  C  CG1   . VAL A 1 22  ? -37.323 -36.018 -7.484  1.00 152.01 ? 125  VAL A CG1   1 
ATOM   152  C  CG2   . VAL A 1 22  ? -36.203 -34.133 -6.277  1.00 152.35 ? 125  VAL A CG2   1 
ATOM   153  N  N     . CYS A 1 23  ? -38.492 -37.078 -3.622  1.00 176.00 ? 126  CYS A N     1 
ATOM   154  C  CA    . CYS A 1 23  ? -38.993 -38.375 -3.181  1.00 167.01 ? 126  CYS A CA    1 
ATOM   155  C  C     . CYS A 1 23  ? -40.509 -38.401 -3.038  1.00 169.53 ? 126  CYS A C     1 
ATOM   156  O  O     . CYS A 1 23  ? -41.094 -39.489 -3.014  1.00 188.85 ? 126  CYS A O     1 
ATOM   157  C  CB    . CYS A 1 23  ? -38.342 -38.768 -1.856  1.00 170.55 ? 126  CYS A CB    1 
ATOM   158  S  SG    . CYS A 1 23  ? -36.578 -39.114 -1.980  1.00 203.11 ? 126  CYS A SG    1 
ATOM   159  N  N     . GLU A 1 24  ? -41.158 -37.239 -2.946  1.00 162.34 ? 127  GLU A N     1 
ATOM   160  C  CA    . GLU A 1 24  ? -42.612 -37.205 -2.855  1.00 169.64 ? 127  GLU A CA    1 
ATOM   161  C  C     . GLU A 1 24  ? -43.295 -37.614 -4.153  1.00 167.45 ? 127  GLU A C     1 
ATOM   162  O  O     . GLU A 1 24  ? -44.519 -37.778 -4.162  1.00 164.87 ? 127  GLU A O     1 
ATOM   163  C  CB    . GLU A 1 24  ? -43.083 -35.809 -2.440  1.00 166.90 ? 127  GLU A CB    1 
ATOM   164  C  CG    . GLU A 1 24  ? -42.613 -35.384 -1.059  1.00 184.97 ? 127  GLU A CG    1 
ATOM   165  C  CD    . GLU A 1 24  ? -43.285 -34.113 -0.580  1.00 187.89 ? 127  GLU A CD    1 
ATOM   166  O  OE1   . GLU A 1 24  ? -44.235 -33.653 -1.248  1.00 183.87 ? 127  GLU A OE1   1 
ATOM   167  O  OE2   . GLU A 1 24  ? -42.865 -33.575 0.466   1.00 191.78 ? 127  GLU A OE2   1 
ATOM   168  N  N     . PHE A 1 25  ? -42.540 -37.780 -5.242  1.00 163.75 ? 128  PHE A N     1 
ATOM   169  C  CA    . PHE A 1 25  ? -43.096 -38.239 -6.506  1.00 152.94 ? 128  PHE A CA    1 
ATOM   170  C  C     . PHE A 1 25  ? -42.743 -39.680 -6.839  1.00 162.44 ? 128  PHE A C     1 
ATOM   171  O  O     . PHE A 1 25  ? -43.481 -40.317 -7.597  1.00 178.49 ? 128  PHE A O     1 
ATOM   172  C  CB    . PHE A 1 25  ? -42.631 -37.334 -7.655  1.00 148.01 ? 128  PHE A CB    1 
ATOM   173  C  CG    . PHE A 1 25  ? -43.015 -35.893 -7.482  1.00 165.63 ? 128  PHE A CG    1 
ATOM   174  C  CD1   . PHE A 1 25  ? -44.346 -35.511 -7.499  1.00 148.52 ? 128  PHE A CD1   1 
ATOM   175  C  CD2   . PHE A 1 25  ? -42.045 -34.920 -7.304  1.00 170.33 ? 128  PHE A CD2   1 
ATOM   176  C  CE1   . PHE A 1 25  ? -44.704 -34.187 -7.340  1.00 153.51 ? 128  PHE A CE1   1 
ATOM   177  C  CE2   . PHE A 1 25  ? -42.397 -33.593 -7.146  1.00 140.93 ? 128  PHE A CE2   1 
ATOM   178  C  CZ    . PHE A 1 25  ? -43.728 -33.227 -7.164  1.00 152.25 ? 128  PHE A CZ    1 
ATOM   179  N  N     . ASP A 1 26  ? -41.642 -40.208 -6.298  1.00 165.92 ? 129  ASP A N     1 
ATOM   180  C  CA    . ASP A 1 26  ? -41.307 -41.609 -6.514  1.00 151.75 ? 129  ASP A CA    1 
ATOM   181  C  C     . ASP A 1 26  ? -42.205 -42.544 -5.717  1.00 146.25 ? 129  ASP A C     1 
ATOM   182  O  O     . ASP A 1 26  ? -42.326 -43.721 -6.073  1.00 150.19 ? 129  ASP A O     1 
ATOM   183  C  CB    . ASP A 1 26  ? -39.842 -41.866 -6.155  1.00 139.07 ? 129  ASP A CB    1 
ATOM   184  C  CG    . ASP A 1 26  ? -38.884 -41.033 -6.983  1.00 157.52 ? 129  ASP A CG    1 
ATOM   185  O  OD1   . ASP A 1 26  ? -38.772 -39.818 -6.721  1.00 189.02 ? 129  ASP A OD1   1 
ATOM   186  O  OD2   . ASP A 1 26  ? -38.244 -41.594 -7.897  1.00 161.69 ? 129  ASP A OD2   1 
ATOM   187  N  N     . MET A 1 27  ? -42.837 -42.049 -4.651  1.00 144.28 ? 130  MET A N     1 
ATOM   188  C  CA    . MET A 1 27  ? -43.730 -42.844 -3.818  1.00 167.83 ? 130  MET A CA    1 
ATOM   189  C  C     . MET A 1 27  ? -45.195 -42.665 -4.206  1.00 150.68 ? 130  MET A C     1 
ATOM   190  O  O     . MET A 1 27  ? -46.087 -42.859 -3.373  1.00 157.63 ? 130  MET A O     1 
ATOM   191  C  CB    . MET A 1 27  ? -43.527 -42.498 -2.343  1.00 175.33 ? 130  MET A CB    1 
ATOM   192  C  CG    . MET A 1 27  ? -43.752 -41.032 -2.010  1.00 158.58 ? 130  MET A CG    1 
ATOM   193  S  SD    . MET A 1 27  ? -43.607 -40.690 -0.246  1.00 175.34 ? 130  MET A SD    1 
ATOM   194  C  CE    . MET A 1 27  ? -44.979 -41.645 0.397   1.00 171.08 ? 130  MET A CE    1 
ATOM   195  N  N     . VAL A 1 28  ? -45.460 -42.299 -5.456  1.00 154.02 ? 131  VAL A N     1 
ATOM   196  C  CA    . VAL A 1 28  ? -46.818 -42.103 -5.949  1.00 160.17 ? 131  VAL A CA    1 
ATOM   197  C  C     . VAL A 1 28  ? -47.255 -43.374 -6.663  1.00 158.78 ? 131  VAL A C     1 
ATOM   198  O  O     . VAL A 1 28  ? -46.627 -43.796 -7.642  1.00 148.27 ? 131  VAL A O     1 
ATOM   199  C  CB    . VAL A 1 28  ? -46.907 -40.884 -6.881  1.00 154.69 ? 131  VAL A CB    1 
ATOM   200  C  CG1   . VAL A 1 28  ? -48.315 -40.744 -7.432  1.00 146.86 ? 131  VAL A CG1   1 
ATOM   201  C  CG2   . VAL A 1 28  ? -46.495 -39.623 -6.140  1.00 145.43 ? 131  VAL A CG2   1 
ATOM   202  N  N     . LYS A 1 29  ? -48.334 -43.986 -6.172  1.00 163.00 ? 132  LYS A N     1 
ATOM   203  C  CA    . LYS A 1 29  ? -48.849 -45.217 -6.757  1.00 159.45 ? 132  LYS A CA    1 
ATOM   204  C  C     . LYS A 1 29  ? -49.576 -44.983 -8.076  1.00 161.96 ? 132  LYS A C     1 
ATOM   205  O  O     . LYS A 1 29  ? -49.832 -45.950 -8.803  1.00 193.36 ? 132  LYS A O     1 
ATOM   206  C  CB    . LYS A 1 29  ? -49.782 -45.910 -5.759  1.00 163.52 ? 132  LYS A CB    1 
ATOM   207  C  CG    . LYS A 1 29  ? -50.106 -47.360 -6.086  1.00 181.89 ? 132  LYS A CG    1 
ATOM   208  C  CD    . LYS A 1 29  ? -51.149 -47.919 -5.134  1.00 178.32 ? 132  LYS A CD    1 
ATOM   209  C  CE    . LYS A 1 29  ? -51.552 -49.331 -5.523  1.00 176.11 ? 132  LYS A CE    1 
ATOM   210  N  NZ    . LYS A 1 29  ? -52.613 -49.869 -4.627  1.00 205.97 ? 132  LYS A NZ    1 
ATOM   211  N  N     . ASP A 1 30  ? -49.902 -43.739 -8.404  1.00 140.84 ? 133  ASP A N     1 
ATOM   212  C  CA    . ASP A 1 30  ? -50.634 -43.435 -9.627  1.00 132.04 ? 133  ASP A CA    1 
ATOM   213  C  C     . ASP A 1 30  ? -49.809 -43.831 -10.848 1.00 130.91 ? 133  ASP A C     1 
ATOM   214  O  O     . ASP A 1 30  ? -48.662 -43.377 -10.985 1.00 135.93 ? 133  ASP A O     1 
ATOM   215  C  CB    . ASP A 1 30  ? -50.982 -41.948 -9.677  1.00 131.29 ? 133  ASP A CB    1 
ATOM   216  C  CG    . ASP A 1 30  ? -52.091 -41.635 -10.667 1.00 147.50 ? 133  ASP A CG    1 
ATOM   217  O  OD1   . ASP A 1 30  ? -52.085 -42.196 -11.783 1.00 148.43 ? 133  ASP A OD1   1 
ATOM   218  O  OD2   . ASP A 1 30  ? -52.975 -40.820 -10.326 1.00 153.77 ? 133  ASP A OD2   1 
ATOM   219  N  N     . PRO A 1 31  ? -50.338 -44.668 -11.745 1.00 118.69 ? 134  PRO A N     1 
ATOM   220  C  CA    . PRO A 1 31  ? -49.563 -45.030 -12.942 1.00 131.69 ? 134  PRO A CA    1 
ATOM   221  C  C     . PRO A 1 31  ? -49.400 -43.882 -13.922 1.00 143.22 ? 134  PRO A C     1 
ATOM   222  O  O     . PRO A 1 31  ? -48.410 -43.855 -14.663 1.00 136.98 ? 134  PRO A O     1 
ATOM   223  C  CB    . PRO A 1 31  ? -50.375 -46.182 -13.548 1.00 125.72 ? 134  PRO A CB    1 
ATOM   224  C  CG    . PRO A 1 31  ? -51.769 -45.948 -13.065 1.00 134.16 ? 134  PRO A CG    1 
ATOM   225  C  CD    . PRO A 1 31  ? -51.630 -45.372 -11.684 1.00 124.35 ? 134  PRO A CD    1 
ATOM   226  N  N     . GLU A 1 32  ? -50.341 -42.935 -13.955 1.00 128.46 ? 135  GLU A N     1 
ATOM   227  C  CA    . GLU A 1 32  ? -50.191 -41.783 -14.838 1.00 109.55 ? 135  GLU A CA    1 
ATOM   228  C  C     . GLU A 1 32  ? -49.052 -40.880 -14.386 1.00 120.90 ? 135  GLU A C     1 
ATOM   229  O  O     . GLU A 1 32  ? -48.366 -40.283 -15.224 1.00 127.57 ? 135  GLU A O     1 
ATOM   230  C  CB    . GLU A 1 32  ? -51.497 -40.991 -14.905 1.00 115.08 ? 135  GLU A CB    1 
ATOM   231  C  CG    . GLU A 1 32  ? -51.482 -39.868 -15.933 1.00 154.28 ? 135  GLU A CG    1 
ATOM   232  C  CD    . GLU A 1 32  ? -52.798 -39.115 -16.006 1.00 135.56 ? 135  GLU A CD    1 
ATOM   233  O  OE1   . GLU A 1 32  ? -53.659 -39.326 -15.126 1.00 107.42 ? 135  GLU A OE1   1 
ATOM   234  O  OE2   . GLU A 1 32  ? -52.970 -38.313 -16.947 1.00 102.04 ? 135  GLU A OE2   1 
ATOM   235  N  N     . VAL A 1 33  ? -48.835 -40.770 -13.074 1.00 127.86 ? 136  VAL A N     1 
ATOM   236  C  CA    . VAL A 1 33  ? -47.744 -39.947 -12.564 1.00 127.76 ? 136  VAL A CA    1 
ATOM   237  C  C     . VAL A 1 33  ? -46.397 -40.527 -12.976 1.00 113.57 ? 136  VAL A C     1 
ATOM   238  O  O     . VAL A 1 33  ? -45.501 -39.798 -13.417 1.00 151.06 ? 136  VAL A O     1 
ATOM   239  C  CB    . VAL A 1 33  ? -47.858 -39.803 -11.035 1.00 111.98 ? 136  VAL A CB    1 
ATOM   240  C  CG1   . VAL A 1 33  ? -46.597 -39.179 -10.460 1.00 119.28 ? 136  VAL A CG1   1 
ATOM   241  C  CG2   . VAL A 1 33  ? -49.078 -38.972 -10.675 1.00 114.53 ? 136  VAL A CG2   1 
ATOM   242  N  N     . GLN A 1 34  ? -46.234 -41.846 -12.853 1.00 118.19 ? 137  GLN A N     1 
ATOM   243  C  CA    . GLN A 1 34  ? -44.962 -42.464 -13.210 1.00 135.45 ? 137  GLN A CA    1 
ATOM   244  C  C     . GLN A 1 34  ? -44.752 -42.470 -14.719 1.00 133.13 ? 137  GLN A C     1 
ATOM   245  O  O     . GLN A 1 34  ? -43.626 -42.280 -15.194 1.00 132.01 ? 137  GLN A O     1 
ATOM   246  C  CB    . GLN A 1 34  ? -44.893 -43.883 -12.646 1.00 135.61 ? 137  GLN A CB    1 
ATOM   247  C  CG    . GLN A 1 34  ? -45.116 -43.958 -11.143 1.00 151.08 ? 137  GLN A CG    1 
ATOM   248  C  CD    . GLN A 1 34  ? -44.143 -43.091 -10.362 1.00 172.06 ? 137  GLN A CD    1 
ATOM   249  O  OE1   . GLN A 1 34  ? -42.976 -42.955 -10.731 1.00 157.45 ? 137  GLN A OE1   1 
ATOM   250  N  NE2   . GLN A 1 34  ? -44.624 -42.497 -9.276  1.00 151.95 ? 137  GLN A NE2   1 
ATOM   251  N  N     . ASP A 1 35  ? -45.822 -42.684 -15.490 1.00 116.65 ? 138  ASP A N     1 
ATOM   252  C  CA    . ASP A 1 35  ? -45.700 -42.629 -16.943 1.00 126.72 ? 138  ASP A CA    1 
ATOM   253  C  C     . ASP A 1 35  ? -45.437 -41.210 -17.428 1.00 131.58 ? 138  ASP A C     1 
ATOM   254  O  O     . ASP A 1 35  ? -44.799 -41.022 -18.470 1.00 127.63 ? 138  ASP A O     1 
ATOM   255  C  CB    . ASP A 1 35  ? -46.959 -43.193 -17.603 1.00 140.19 ? 138  ASP A CB    1 
ATOM   256  C  CG    . ASP A 1 35  ? -47.075 -44.695 -17.446 1.00 132.69 ? 138  ASP A CG    1 
ATOM   257  O  OD1   . ASP A 1 35  ? -46.026 -45.364 -17.329 1.00 159.43 ? 138  ASP A OD1   1 
ATOM   258  O  OD2   . ASP A 1 35  ? -48.214 -45.208 -17.442 1.00 135.73 ? 138  ASP A OD2   1 
ATOM   259  N  N     . PHE A 1 36  ? -45.922 -40.206 -16.695 1.00 124.83 ? 139  PHE A N     1 
ATOM   260  C  CA    . PHE A 1 36  ? -45.608 -38.822 -17.033 1.00 105.52 ? 139  PHE A CA    1 
ATOM   261  C  C     . PHE A 1 36  ? -44.111 -38.565 -16.916 1.00 104.29 ? 139  PHE A C     1 
ATOM   262  O  O     . PHE A 1 36  ? -43.478 -38.077 -17.857 1.00 106.29 ? 139  PHE A O     1 
ATOM   263  C  CB    . PHE A 1 36  ? -46.392 -37.871 -16.126 1.00 111.62 ? 139  PHE A CB    1 
ATOM   264  C  CG    . PHE A 1 36  ? -46.218 -36.416 -16.468 1.00 115.86 ? 139  PHE A CG    1 
ATOM   265  C  CD1   . PHE A 1 36  ? -45.946 -36.019 -17.768 1.00 139.32 ? 139  PHE A CD1   1 
ATOM   266  C  CD2   . PHE A 1 36  ? -46.324 -35.446 -15.486 1.00 111.33 ? 139  PHE A CD2   1 
ATOM   267  C  CE1   . PHE A 1 36  ? -45.787 -34.682 -18.080 1.00 118.38 ? 139  PHE A CE1   1 
ATOM   268  C  CE2   . PHE A 1 36  ? -46.164 -34.107 -15.793 1.00 120.12 ? 139  PHE A CE2   1 
ATOM   269  C  CZ    . PHE A 1 36  ? -45.895 -33.725 -17.091 1.00 125.08 ? 139  PHE A CZ    1 
ATOM   270  N  N     . ARG A 1 37  ? -43.527 -38.905 -15.765 1.00 127.33 ? 140  ARG A N     1 
ATOM   271  C  CA    . ARG A 1 37  ? -42.106 -38.657 -15.546 1.00 109.50 ? 140  ARG A CA    1 
ATOM   272  C  C     . ARG A 1 37  ? -41.236 -39.464 -16.501 1.00 126.42 ? 140  ARG A C     1 
ATOM   273  O  O     . ARG A 1 37  ? -40.111 -39.055 -16.811 1.00 154.57 ? 140  ARG A O     1 
ATOM   274  C  CB    . ARG A 1 37  ? -41.748 -38.973 -14.094 1.00 131.51 ? 140  ARG A CB    1 
ATOM   275  C  CG    . ARG A 1 37  ? -42.672 -38.304 -13.090 1.00 122.26 ? 140  ARG A CG    1 
ATOM   276  C  CD    . ARG A 1 37  ? -42.643 -38.984 -11.728 1.00 156.25 ? 140  ARG A CD    1 
ATOM   277  N  NE    . ARG A 1 37  ? -41.576 -38.480 -10.871 1.00 147.62 ? 140  ARG A NE    1 
ATOM   278  C  CZ    . ARG A 1 37  ? -40.488 -39.163 -10.546 1.00 149.76 ? 140  ARG A CZ    1 
ATOM   279  N  NH1   . ARG A 1 37  ? -40.288 -40.395 -10.984 1.00 155.48 ? 140  ARG A NH1   1 
ATOM   280  N  NH2   . ARG A 1 37  ? -39.581 -38.600 -9.753  1.00 159.06 ? 140  ARG A NH2   1 
ATOM   281  N  N     . ARG A 1 38  ? -41.736 -40.603 -16.984 1.00 141.91 ? 141  ARG A N     1 
ATOM   282  C  CA    . ARG A 1 38  ? -40.957 -41.432 -17.898 1.00 140.40 ? 141  ARG A CA    1 
ATOM   283  C  C     . ARG A 1 38  ? -41.025 -40.906 -19.328 1.00 129.76 ? 141  ARG A C     1 
ATOM   284  O  O     . ARG A 1 38  ? -39.992 -40.748 -19.989 1.00 132.23 ? 141  ARG A O     1 
ATOM   285  C  CB    . ARG A 1 38  ? -41.447 -42.881 -17.843 1.00 156.59 ? 141  ARG A CB    1 
ATOM   286  C  CG    . ARG A 1 38  ? -40.826 -43.781 -18.902 1.00 160.93 ? 141  ARG A CG    1 
ATOM   287  C  CD    . ARG A 1 38  ? -41.557 -45.112 -19.013 1.00 157.02 ? 141  ARG A CD    1 
ATOM   288  N  NE    . ARG A 1 38  ? -41.396 -45.935 -17.821 1.00 178.94 ? 141  ARG A NE    1 
ATOM   289  C  CZ    . ARG A 1 38  ? -41.903 -47.152 -17.678 1.00 194.88 ? 141  ARG A CZ    1 
ATOM   290  N  NH1   . ARG A 1 38  ? -42.619 -47.719 -18.636 1.00 216.60 ? 141  ARG A NH1   1 
ATOM   291  N  NH2   . ARG A 1 38  ? -41.687 -47.817 -16.547 1.00 188.09 ? 141  ARG A NH2   1 
ATOM   292  N  N     . ASN A 1 39  ? -42.233 -40.629 -19.821 1.00 122.45 ? 142  ASN A N     1 
ATOM   293  C  CA    . ASN A 1 39  ? -42.410 -40.262 -21.220 1.00 131.27 ? 142  ASN A CA    1 
ATOM   294  C  C     . ASN A 1 39  ? -42.122 -38.793 -21.498 1.00 130.21 ? 142  ASN A C     1 
ATOM   295  O  O     . ASN A 1 39  ? -41.788 -38.450 -22.638 1.00 130.59 ? 142  ASN A O     1 
ATOM   296  C  CB    . ASN A 1 39  ? -43.831 -40.599 -21.675 1.00 117.09 ? 142  ASN A CB    1 
ATOM   297  C  CG    . ASN A 1 39  ? -44.144 -42.075 -21.552 1.00 114.02 ? 142  ASN A CG    1 
ATOM   298  O  OD1   . ASN A 1 39  ? -43.832 -42.863 -22.444 1.00 146.05 ? 142  ASN A OD1   1 
ATOM   299  N  ND2   . ASN A 1 39  ? -44.764 -42.458 -20.442 1.00 138.25 ? 142  ASN A ND2   1 
ATOM   300  N  N     . ILE A 1 40  ? -42.241 -37.919 -20.495 1.00 134.55 ? 143  ILE A N     1 
ATOM   301  C  CA    . ILE A 1 40  ? -41.973 -36.504 -20.724 1.00 113.38 ? 143  ILE A CA    1 
ATOM   302  C  C     . ILE A 1 40  ? -40.490 -36.248 -20.951 1.00 115.55 ? 143  ILE A C     1 
ATOM   303  O  O     . ILE A 1 40  ? -40.117 -35.175 -21.440 1.00 134.40 ? 143  ILE A O     1 
ATOM   304  C  CB    . ILE A 1 40  ? -42.502 -35.652 -19.554 1.00 98.40  ? 143  ILE A CB    1 
ATOM   305  C  CG1   . ILE A 1 40  ? -42.839 -34.240 -20.031 1.00 102.34 ? 143  ILE A CG1   1 
ATOM   306  C  CG2   . ILE A 1 40  ? -41.487 -35.604 -18.422 1.00 114.09 ? 143  ILE A CG2   1 
ATOM   307  C  CD1   . ILE A 1 40  ? -43.887 -34.201 -21.119 1.00 87.83  ? 143  ILE A CD1   1 
ATOM   308  N  N     . LEU A 1 41  ? -39.628 -37.210 -20.612 1.00 116.26 ? 144  LEU A N     1 
ATOM   309  C  CA    . LEU A 1 41  ? -38.206 -37.068 -20.894 1.00 119.30 ? 144  LEU A CA    1 
ATOM   310  C  C     . LEU A 1 41  ? -37.914 -37.092 -22.388 1.00 114.37 ? 144  LEU A C     1 
ATOM   311  O  O     . LEU A 1 41  ? -36.841 -36.643 -22.803 1.00 133.29 ? 144  LEU A O     1 
ATOM   312  C  CB    . LEU A 1 41  ? -37.415 -38.168 -20.186 1.00 120.98 ? 144  LEU A CB    1 
ATOM   313  C  CG    . LEU A 1 41  ? -37.523 -38.186 -18.660 1.00 99.03  ? 144  LEU A CG    1 
ATOM   314  C  CD1   . LEU A 1 41  ? -36.668 -39.295 -18.075 1.00 129.89 ? 144  LEU A CD1   1 
ATOM   315  C  CD2   . LEU A 1 41  ? -37.131 -36.838 -18.076 1.00 113.98 ? 144  LEU A CD2   1 
ATOM   316  N  N     . ASN A 1 42  ? -38.838 -37.612 -23.199 1.00 116.99 ? 145  ASN A N     1 
ATOM   317  C  CA    . ASN A 1 42  ? -38.679 -37.529 -24.647 1.00 125.99 ? 145  ASN A CA    1 
ATOM   318  C  C     . ASN A 1 42  ? -38.704 -36.080 -25.113 1.00 142.92 ? 145  ASN A C     1 
ATOM   319  O  O     . ASN A 1 42  ? -37.989 -35.707 -26.050 1.00 144.31 ? 145  ASN A O     1 
ATOM   320  C  CB    . ASN A 1 42  ? -39.773 -38.338 -25.343 1.00 133.76 ? 145  ASN A CB    1 
ATOM   321  C  CG    . ASN A 1 42  ? -39.748 -39.804 -24.958 1.00 165.80 ? 145  ASN A CG    1 
ATOM   322  O  OD1   . ASN A 1 42  ? -39.096 -40.192 -23.989 1.00 155.25 ? 145  ASN A OD1   1 
ATOM   323  N  ND2   . ASN A 1 42  ? -40.463 -40.627 -25.717 1.00 181.93 ? 145  ASN A ND2   1 
ATOM   324  N  N     . VAL A 1 43  ? -39.523 -35.246 -24.467 1.00 128.69 ? 146  VAL A N     1 
ATOM   325  C  CA    . VAL A 1 43  ? -39.523 -33.820 -24.774 1.00 132.68 ? 146  VAL A CA    1 
ATOM   326  C  C     . VAL A 1 43  ? -38.204 -33.188 -24.353 1.00 125.26 ? 146  VAL A C     1 
ATOM   327  O  O     . VAL A 1 43  ? -37.683 -32.292 -25.027 1.00 127.93 ? 146  VAL A O     1 
ATOM   328  C  CB    . VAL A 1 43  ? -40.722 -33.130 -24.099 1.00 129.04 ? 146  VAL A CB    1 
ATOM   329  C  CG1   . VAL A 1 43  ? -40.831 -31.681 -24.553 1.00 123.99 ? 146  VAL A CG1   1 
ATOM   330  C  CG2   . VAL A 1 43  ? -42.004 -33.888 -24.394 1.00 137.41 ? 146  VAL A CG2   1 
ATOM   331  N  N     . CYS A 1 44  ? -37.641 -33.647 -23.233 1.00 125.88 ? 147  CYS A N     1 
ATOM   332  C  CA    . CYS A 1 44  ? -36.357 -33.122 -22.781 1.00 120.15 ? 147  CYS A CA    1 
ATOM   333  C  C     . CYS A 1 44  ? -35.226 -33.563 -23.702 1.00 118.29 ? 147  CYS A C     1 
ATOM   334  O  O     . CYS A 1 44  ? -34.336 -32.768 -24.024 1.00 127.60 ? 147  CYS A O     1 
ATOM   335  C  CB    . CYS A 1 44  ? -36.088 -33.569 -21.344 1.00 120.38 ? 147  CYS A CB    1 
ATOM   336  S  SG    . CYS A 1 44  ? -37.409 -33.165 -20.178 1.00 128.75 ? 147  CYS A SG    1 
ATOM   337  N  N     . LYS A 1 45  ? -35.245 -34.826 -24.137 1.00 128.22 ? 148  LYS A N     1 
ATOM   338  C  CA    . LYS A 1 45  ? -34.199 -35.318 -25.028 1.00 110.34 ? 148  LYS A CA    1 
ATOM   339  C  C     . LYS A 1 45  ? -34.245 -34.615 -26.378 1.00 142.31 ? 148  LYS A C     1 
ATOM   340  O  O     . LYS A 1 45  ? -33.201 -34.254 -26.932 1.00 140.02 ? 148  LYS A O     1 
ATOM   341  C  CB    . LYS A 1 45  ? -34.326 -36.830 -25.204 1.00 130.97 ? 148  LYS A CB    1 
ATOM   342  N  N     . GLU A 1 46  ? -35.446 -34.411 -26.925 1.00 146.91 ? 149  GLU A N     1 
ATOM   343  C  CA    . GLU A 1 46  ? -35.572 -33.691 -28.186 1.00 143.87 ? 149  GLU A CA    1 
ATOM   344  C  C     . GLU A 1 46  ? -35.197 -32.222 -28.051 1.00 130.22 ? 149  GLU A C     1 
ATOM   345  O  O     . GLU A 1 46  ? -34.865 -31.586 -29.057 1.00 134.74 ? 149  GLU A O     1 
ATOM   346  C  CB    . GLU A 1 46  ? -36.998 -33.816 -28.728 1.00 157.14 ? 149  GLU A CB    1 
ATOM   347  C  CG    . GLU A 1 46  ? -37.376 -35.221 -29.168 1.00 149.34 ? 149  GLU A CG    1 
ATOM   348  C  CD    . GLU A 1 46  ? -38.804 -35.310 -29.669 1.00 157.41 ? 149  GLU A CD    1 
ATOM   349  O  OE1   . GLU A 1 46  ? -39.502 -34.274 -29.665 1.00 165.90 ? 149  GLU A OE1   1 
ATOM   350  O  OE2   . GLU A 1 46  ? -39.229 -36.415 -30.066 1.00 173.82 ? 149  GLU A OE2   1 
ATOM   351  N  N     . ALA A 1 47  ? -35.239 -31.672 -26.838 1.00 142.49 ? 150  ALA A N     1 
ATOM   352  C  CA    . ALA A 1 47  ? -34.880 -30.278 -26.614 1.00 147.90 ? 150  ALA A CA    1 
ATOM   353  C  C     . ALA A 1 47  ? -33.385 -30.092 -26.385 1.00 136.77 ? 150  ALA A C     1 
ATOM   354  O  O     . ALA A 1 47  ? -32.784 -29.176 -26.956 1.00 149.53 ? 150  ALA A O     1 
ATOM   355  C  CB    . ALA A 1 47  ? -35.662 -29.715 -25.425 1.00 123.40 ? 150  ALA A CB    1 
ATOM   356  N  N     . VAL A 1 48  ? -32.770 -30.944 -25.561 1.00 140.77 ? 151  VAL A N     1 
ATOM   357  C  CA    . VAL A 1 48  ? -31.340 -30.807 -25.301 1.00 141.94 ? 151  VAL A CA    1 
ATOM   358  C  C     . VAL A 1 48  ? -30.528 -31.169 -26.538 1.00 159.10 ? 151  VAL A C     1 
ATOM   359  O  O     . VAL A 1 48  ? -29.429 -30.640 -26.743 1.00 178.29 ? 151  VAL A O     1 
ATOM   360  C  CB    . VAL A 1 48  ? -30.926 -31.652 -24.081 1.00 137.60 ? 151  VAL A CB    1 
ATOM   361  C  CG1   . VAL A 1 48  ? -31.689 -31.204 -22.843 1.00 96.25  ? 151  VAL A CG1   1 
ATOM   362  C  CG2   . VAL A 1 48  ? -31.149 -33.135 -24.346 1.00 151.72 ? 151  VAL A CG2   1 
ATOM   363  N  N     . ASP A 1 49  ? -31.044 -32.067 -27.382 1.00 147.43 ? 152  ASP A N     1 
ATOM   364  C  CA    . ASP A 1 49  ? -30.379 -32.362 -28.645 1.00 149.78 ? 152  ASP A CA    1 
ATOM   365  C  C     . ASP A 1 49  ? -30.576 -31.249 -29.664 1.00 137.57 ? 152  ASP A C     1 
ATOM   366  O  O     . ASP A 1 49  ? -29.823 -31.178 -30.641 1.00 145.83 ? 152  ASP A O     1 
ATOM   367  C  CB    . ASP A 1 49  ? -30.882 -33.692 -29.210 1.00 162.61 ? 152  ASP A CB    1 
ATOM   368  C  CG    . ASP A 1 49  ? -30.318 -34.890 -28.469 1.00 155.12 ? 152  ASP A CG    1 
ATOM   369  O  OD1   . ASP A 1 49  ? -30.517 -34.980 -27.239 1.00 146.09 ? 152  ASP A OD1   1 
ATOM   370  O  OD2   . ASP A 1 49  ? -29.678 -35.744 -29.118 1.00 179.39 ? 152  ASP A OD2   1 
ATOM   371  N  N     . LEU A 1 50  ? -31.572 -30.384 -29.460 1.00 138.35 ? 153  LEU A N     1 
ATOM   372  C  CA    . LEU A 1 50  ? -31.735 -29.212 -30.311 1.00 158.24 ? 153  LEU A CA    1 
ATOM   373  C  C     . LEU A 1 50  ? -30.850 -28.060 -29.852 1.00 161.26 ? 153  LEU A C     1 
ATOM   374  O  O     . LEU A 1 50  ? -30.415 -27.249 -30.678 1.00 157.42 ? 153  LEU A O     1 
ATOM   375  C  CB    . LEU A 1 50  ? -33.203 -28.780 -30.330 1.00 144.32 ? 153  LEU A CB    1 
ATOM   376  C  CG    . LEU A 1 50  ? -33.600 -27.670 -31.305 1.00 157.42 ? 153  LEU A CG    1 
ATOM   377  C  CD1   . LEU A 1 50  ? -33.364 -28.107 -32.741 1.00 143.36 ? 153  LEU A CD1   1 
ATOM   378  C  CD2   . LEU A 1 50  ? -35.051 -27.268 -31.097 1.00 154.04 ? 153  LEU A CD2   1 
ATOM   379  N  N     . ARG A 1 51  ? -30.573 -27.975 -28.550 1.00 158.05 ? 154  ARG A N     1 
ATOM   380  C  CA    . ARG A 1 51  ? -29.662 -26.974 -28.013 1.00 146.83 ? 154  ARG A CA    1 
ATOM   381  C  C     . ARG A 1 51  ? -28.199 -27.311 -28.260 1.00 157.69 ? 154  ARG A C     1 
ATOM   382  O  O     . ARG A 1 51  ? -27.331 -26.487 -27.949 1.00 166.83 ? 154  ARG A O     1 
ATOM   383  C  CB    . ARG A 1 51  ? -29.884 -26.812 -26.507 1.00 148.76 ? 154  ARG A CB    1 
ATOM   384  C  CG    . ARG A 1 51  ? -31.301 -26.448 -26.112 1.00 138.87 ? 154  ARG A CG    1 
ATOM   385  C  CD    . ARG A 1 51  ? -31.620 -26.977 -24.723 1.00 156.23 ? 154  ARG A CD    1 
ATOM   386  N  NE    . ARG A 1 51  ? -30.683 -26.494 -23.716 1.00 137.87 ? 154  ARG A NE    1 
ATOM   387  C  CZ    . ARG A 1 51  ? -30.717 -26.837 -22.436 1.00 126.16 ? 154  ARG A CZ    1 
ATOM   388  N  NH1   . ARG A 1 51  ? -31.634 -27.668 -21.967 1.00 114.40 ? 154  ARG A NH1   1 
ATOM   389  N  NH2   . ARG A 1 51  ? -29.808 -26.335 -21.605 1.00 177.10 ? 154  ARG A NH2   1 
ATOM   390  N  N     . ASP A 1 52  ? -27.901 -28.497 -28.799 1.00 156.67 ? 155  ASP A N     1 
ATOM   391  C  CA    . ASP A 1 52  ? -26.524 -28.931 -28.998 1.00 162.70 ? 155  ASP A CA    1 
ATOM   392  C  C     . ASP A 1 52  ? -26.253 -29.353 -30.438 1.00 162.44 ? 155  ASP A C     1 
ATOM   393  O  O     . ASP A 1 52  ? -25.280 -30.071 -30.692 1.00 167.44 ? 155  ASP A O     1 
ATOM   394  C  CB    . ASP A 1 52  ? -26.174 -30.074 -28.041 1.00 184.26 ? 155  ASP A CB    1 
ATOM   395  C  CG    . ASP A 1 52  ? -26.256 -29.661 -26.583 1.00 178.24 ? 155  ASP A CG    1 
ATOM   396  O  OD1   . ASP A 1 52  ? -26.022 -28.470 -26.286 1.00 157.94 ? 155  ASP A OD1   1 
ATOM   397  O  OD2   . ASP A 1 52  ? -26.552 -30.528 -25.734 1.00 188.87 ? 155  ASP A OD2   1 
ATOM   398  N  N     . LEU A 1 53  ? -27.093 -28.932 -31.385 1.00 155.86 ? 156  LEU A N     1 
ATOM   399  C  CA    . LEU A 1 53  ? -26.822 -29.183 -32.796 1.00 155.63 ? 156  LEU A CA    1 
ATOM   400  C  C     . LEU A 1 53  ? -25.534 -28.479 -33.198 1.00 173.88 ? 156  LEU A C     1 
ATOM   401  O  O     . LEU A 1 53  ? -24.522 -29.130 -33.476 1.00 190.07 ? 156  LEU A O     1 
ATOM   402  C  CB    . LEU A 1 53  ? -27.988 -28.715 -33.669 1.00 150.62 ? 156  LEU A CB    1 
ATOM   403  C  CG    . LEU A 1 53  ? -29.277 -29.533 -33.580 1.00 169.44 ? 156  LEU A CG    1 
ATOM   404  C  CD1   . LEU A 1 53  ? -30.316 -28.996 -34.551 1.00 156.18 ? 156  LEU A CD1   1 
ATOM   405  C  CD2   . LEU A 1 53  ? -28.996 -31.004 -33.850 1.00 182.39 ? 156  LEU A CD2   1 
ATOM   406  N  N     . ASN A 1 54  ? -25.564 -27.150 -33.231 1.00 173.80 ? 157  ASN A N     1 
ATOM   407  C  CA    . ASN A 1 54  ? -24.342 -26.372 -33.363 1.00 185.51 ? 157  ASN A CA    1 
ATOM   408  C  C     . ASN A 1 54  ? -23.669 -26.267 -32.001 1.00 193.76 ? 157  ASN A C     1 
ATOM   409  O  O     . ASN A 1 54  ? -24.328 -26.037 -30.984 1.00 198.36 ? 157  ASN A O     1 
ATOM   410  C  CB    . ASN A 1 54  ? -24.649 -24.983 -33.923 1.00 170.12 ? 157  ASN A CB    1 
ATOM   411  C  CG    . ASN A 1 54  ? -23.397 -24.183 -34.214 1.00 184.76 ? 157  ASN A CG    1 
ATOM   412  O  OD1   . ASN A 1 54  ? -23.067 -23.244 -33.493 1.00 197.83 ? 157  ASN A OD1   1 
ATOM   413  N  ND2   . ASN A 1 54  ? -22.690 -24.555 -35.275 1.00 189.57 ? 157  ASN A ND2   1 
ATOM   414  N  N     . SER A 1 55  ? -22.344 -26.449 -31.983 1.00 190.65 ? 158  SER A N     1 
ATOM   415  C  CA    . SER A 1 55  ? -21.655 -26.606 -30.702 1.00 195.65 ? 158  SER A CA    1 
ATOM   416  C  C     . SER A 1 55  ? -21.684 -25.337 -29.857 1.00 189.57 ? 158  SER A C     1 
ATOM   417  O  O     . SER A 1 55  ? -22.111 -25.412 -28.691 1.00 205.74 ? 158  SER A O     1 
ATOM   418  C  CB    . SER A 1 55  ? -20.227 -27.111 -30.937 1.00 197.83 ? 158  SER A CB    1 
ATOM   419  O  OG    . SER A 1 55  ? -20.231 -28.356 -31.614 1.00 201.73 ? 158  SER A OG    1 
ATOM   420  N  N     . PRO A 1 56  ? -21.261 -24.155 -30.349 1.00 170.57 ? 159  PRO A N     1 
ATOM   421  C  CA    . PRO A 1 56  ? -21.241 -22.984 -29.462 1.00 166.25 ? 159  PRO A CA    1 
ATOM   422  C  C     . PRO A 1 56  ? -22.508 -22.138 -29.505 1.00 173.77 ? 159  PRO A C     1 
ATOM   423  O  O     . PRO A 1 56  ? -22.989 -21.687 -28.460 1.00 147.45 ? 159  PRO A O     1 
ATOM   424  C  CB    . PRO A 1 56  ? -20.029 -22.198 -29.971 1.00 146.60 ? 159  PRO A CB    1 
ATOM   425  C  CG    . PRO A 1 56  ? -20.010 -22.479 -31.434 1.00 160.62 ? 159  PRO A CG    1 
ATOM   426  C  CD    . PRO A 1 56  ? -20.591 -23.864 -31.633 1.00 172.06 ? 159  PRO A CD    1 
ATOM   427  N  N     . HIS A 1 57  ? -23.062 -21.917 -30.700 1.00 167.01 ? 160  HIS A N     1 
ATOM   428  C  CA    . HIS A 1 57  ? -24.132 -20.936 -30.854 1.00 150.94 ? 160  HIS A CA    1 
ATOM   429  C  C     . HIS A 1 57  ? -25.466 -21.447 -30.321 1.00 150.35 ? 160  HIS A C     1 
ATOM   430  O  O     . HIS A 1 57  ? -26.229 -20.680 -29.723 1.00 150.13 ? 160  HIS A O     1 
ATOM   431  C  CB    . HIS A 1 57  ? -24.268 -20.537 -32.324 1.00 164.22 ? 160  HIS A CB    1 
ATOM   432  C  CG    . HIS A 1 57  ? -25.208 -19.396 -32.558 1.00 156.66 ? 160  HIS A CG    1 
ATOM   433  N  ND1   . HIS A 1 57  ? -25.749 -19.120 -33.795 1.00 154.22 ? 160  HIS A ND1   1 
ATOM   434  C  CD2   . HIS A 1 57  ? -25.696 -18.454 -31.715 1.00 167.30 ? 160  HIS A CD2   1 
ATOM   435  C  CE1   . HIS A 1 57  ? -26.533 -18.061 -33.704 1.00 168.91 ? 160  HIS A CE1   1 
ATOM   436  N  NE2   . HIS A 1 57  ? -26.519 -17.638 -32.452 1.00 180.00 ? 160  HIS A NE2   1 
ATOM   437  N  N     . SER A 1 58  ? -25.768 -22.732 -30.531 1.00 166.21 ? 161  SER A N     1 
ATOM   438  C  CA    . SER A 1 58  ? -27.068 -23.259 -30.124 1.00 144.09 ? 161  SER A CA    1 
ATOM   439  C  C     . SER A 1 58  ? -27.279 -23.149 -28.620 1.00 144.25 ? 161  SER A C     1 
ATOM   440  O  O     . SER A 1 58  ? -28.408 -22.927 -28.168 1.00 142.65 ? 161  SER A O     1 
ATOM   441  C  CB    . SER A 1 58  ? -27.215 -24.710 -30.579 1.00 151.11 ? 161  SER A CB    1 
ATOM   442  O  OG    . SER A 1 58  ? -27.230 -24.803 -31.992 1.00 170.36 ? 161  SER A OG    1 
ATOM   443  N  N     . ARG A 1 59  ? -26.214 -23.297 -27.829 1.00 146.92 ? 162  ARG A N     1 
ATOM   444  C  CA    . ARG A 1 59  ? -26.344 -23.109 -26.389 1.00 119.93 ? 162  ARG A CA    1 
ATOM   445  C  C     . ARG A 1 59  ? -26.444 -21.632 -26.030 1.00 128.19 ? 162  ARG A C     1 
ATOM   446  O  O     . ARG A 1 59  ? -27.174 -21.263 -25.103 1.00 114.82 ? 162  ARG A O     1 
ATOM   447  C  CB    . ARG A 1 59  ? -25.165 -23.755 -25.659 1.00 137.59 ? 162  ARG A CB    1 
ATOM   448  C  CG    . ARG A 1 59  ? -24.918 -25.208 -26.029 1.00 135.91 ? 162  ARG A CG    1 
ATOM   449  C  CD    . ARG A 1 59  ? -24.083 -25.911 -24.970 1.00 148.98 ? 162  ARG A CD    1 
ATOM   450  N  NE    . ARG A 1 59  ? -22.926 -25.120 -24.567 1.00 189.91 ? 162  ARG A NE    1 
ATOM   451  C  CZ    . ARG A 1 59  ? -21.737 -25.179 -25.151 1.00 209.71 ? 162  ARG A CZ    1 
ATOM   452  N  NH1   . ARG A 1 59  ? -21.510 -25.980 -26.179 1.00 220.49 ? 162  ARG A NH1   1 
ATOM   453  N  NH2   . ARG A 1 59  ? -20.750 -24.414 -24.691 1.00 177.00 ? 162  ARG A NH2   1 
ATOM   454  N  N     . ALA A 1 60  ? -25.720 -20.774 -26.753 1.00 147.11 ? 163  ALA A N     1 
ATOM   455  C  CA    . ALA A 1 60  ? -25.787 -19.341 -26.485 1.00 130.28 ? 163  ALA A CA    1 
ATOM   456  C  C     . ALA A 1 60  ? -27.129 -18.762 -26.910 1.00 115.89 ? 163  ALA A C     1 
ATOM   457  O  O     . ALA A 1 60  ? -27.662 -17.864 -26.247 1.00 132.09 ? 163  ALA A O     1 
ATOM   458  C  CB    . ALA A 1 60  ? -24.641 -18.619 -27.192 1.00 139.49 ? 163  ALA A CB    1 
ATOM   459  N  N     . MET A 1 61  ? -27.689 -19.258 -28.016 1.00 131.92 ? 164  MET A N     1 
ATOM   460  C  CA    . MET A 1 61  ? -29.011 -18.811 -28.440 1.00 117.89 ? 164  MET A CA    1 
ATOM   461  C  C     . MET A 1 61  ? -30.079 -19.190 -27.423 1.00 135.47 ? 164  MET A C     1 
ATOM   462  O  O     . MET A 1 61  ? -31.053 -18.451 -27.240 1.00 123.12 ? 164  MET A O     1 
ATOM   463  C  CB    . MET A 1 61  ? -29.350 -19.402 -29.810 1.00 128.18 ? 164  MET A CB    1 
ATOM   464  C  CG    . MET A 1 61  ? -30.681 -18.935 -30.377 1.00 159.78 ? 164  MET A CG    1 
ATOM   465  S  SD    . MET A 1 61  ? -30.555 -17.377 -31.273 1.00 134.75 ? 164  MET A SD    1 
ATOM   466  C  CE    . MET A 1 61  ? -29.834 -17.938 -32.812 1.00 124.65 ? 164  MET A CE    1 
ATOM   467  N  N     . TYR A 1 62  ? -29.913 -20.331 -26.750 1.00 134.99 ? 165  TYR A N     1 
ATOM   468  C  CA    . TYR A 1 62  ? -30.883 -20.746 -25.742 1.00 127.67 ? 165  TYR A CA    1 
ATOM   469  C  C     . TYR A 1 62  ? -30.837 -19.833 -24.523 1.00 135.92 ? 165  TYR A C     1 
ATOM   470  O  O     . TYR A 1 62  ? -31.867 -19.299 -24.096 1.00 124.90 ? 165  TYR A O     1 
ATOM   471  C  CB    . TYR A 1 62  ? -30.629 -22.199 -25.338 1.00 130.00 ? 165  TYR A CB    1 
ATOM   472  C  CG    . TYR A 1 62  ? -31.329 -22.612 -24.062 1.00 123.95 ? 165  TYR A CG    1 
ATOM   473  C  CD1   . TYR A 1 62  ? -32.714 -22.634 -23.984 1.00 138.17 ? 165  TYR A CD1   1 
ATOM   474  C  CD2   . TYR A 1 62  ? -30.604 -22.989 -22.939 1.00 122.64 ? 165  TYR A CD2   1 
ATOM   475  C  CE1   . TYR A 1 62  ? -33.360 -23.011 -22.822 1.00 140.91 ? 165  TYR A CE1   1 
ATOM   476  C  CE2   . TYR A 1 62  ? -31.241 -23.369 -21.771 1.00 130.92 ? 165  TYR A CE2   1 
ATOM   477  C  CZ    . TYR A 1 62  ? -32.620 -23.379 -21.720 1.00 139.24 ? 165  TYR A CZ    1 
ATOM   478  O  OH    . TYR A 1 62  ? -33.263 -23.756 -20.563 1.00 118.45 ? 165  TYR A OH    1 
ATOM   479  N  N     . VAL A 1 63  ? -29.646 -19.636 -23.953 1.00 131.16 ? 166  VAL A N     1 
ATOM   480  C  CA    . VAL A 1 63  ? -29.526 -18.831 -22.741 1.00 122.76 ? 166  VAL A CA    1 
ATOM   481  C  C     . VAL A 1 63  ? -29.801 -17.362 -23.030 1.00 123.23 ? 166  VAL A C     1 
ATOM   482  O  O     . VAL A 1 63  ? -30.359 -16.649 -22.186 1.00 136.47 ? 166  VAL A O     1 
ATOM   483  C  CB    . VAL A 1 63  ? -28.137 -19.034 -22.108 1.00 128.10 ? 166  VAL A CB    1 
ATOM   484  C  CG1   . VAL A 1 63  ? -28.025 -18.265 -20.800 1.00 123.45 ? 166  VAL A CG1   1 
ATOM   485  C  CG2   . VAL A 1 63  ? -27.876 -20.512 -21.883 1.00 135.15 ? 166  VAL A CG2   1 
ATOM   486  N  N     . TYR A 1 64  ? -29.430 -16.881 -24.219 1.00 126.43 ? 167  TYR A N     1 
ATOM   487  C  CA    . TYR A 1 64  ? -29.624 -15.486 -24.613 1.00 130.27 ? 167  TYR A CA    1 
ATOM   488  C  C     . TYR A 1 64  ? -30.409 -15.446 -25.920 1.00 137.92 ? 167  TYR A C     1 
ATOM   489  O  O     . TYR A 1 64  ? -29.837 -15.206 -26.994 1.00 123.93 ? 167  TYR A O     1 
ATOM   490  C  CB    . TYR A 1 64  ? -28.287 -14.759 -24.747 1.00 130.97 ? 167  TYR A CB    1 
ATOM   491  C  CG    . TYR A 1 64  ? -27.464 -14.775 -23.479 1.00 130.18 ? 167  TYR A CG    1 
ATOM   492  C  CD1   . TYR A 1 64  ? -27.795 -13.959 -22.406 1.00 142.67 ? 167  TYR A CD1   1 
ATOM   493  C  CD2   . TYR A 1 64  ? -26.358 -15.605 -23.354 1.00 122.20 ? 167  TYR A CD2   1 
ATOM   494  C  CE1   . TYR A 1 64  ? -27.049 -13.969 -21.244 1.00 129.21 ? 167  TYR A CE1   1 
ATOM   495  C  CE2   . TYR A 1 64  ? -25.605 -15.622 -22.195 1.00 120.91 ? 167  TYR A CE2   1 
ATOM   496  C  CZ    . TYR A 1 64  ? -25.955 -14.801 -21.143 1.00 117.54 ? 167  TYR A CZ    1 
ATOM   497  O  OH    . TYR A 1 64  ? -25.211 -14.813 -19.987 1.00 149.37 ? 167  TYR A OH    1 
ATOM   498  N  N     . PRO A 1 65  ? -31.719 -15.668 -25.868 1.00 127.47 ? 168  PRO A N     1 
ATOM   499  C  CA    . PRO A 1 65  ? -32.531 -15.601 -27.084 1.00 103.25 ? 168  PRO A CA    1 
ATOM   500  C  C     . PRO A 1 65  ? -32.763 -14.160 -27.497 1.00 110.10 ? 168  PRO A C     1 
ATOM   501  O  O     . PRO A 1 65  ? -32.909 -13.274 -26.642 1.00 128.41 ? 168  PRO A O     1 
ATOM   502  C  CB    . PRO A 1 65  ? -33.841 -16.282 -26.667 1.00 113.87 ? 168  PRO A CB    1 
ATOM   503  C  CG    . PRO A 1 65  ? -33.938 -16.009 -25.211 1.00 104.90 ? 168  PRO A CG    1 
ATOM   504  C  CD    . PRO A 1 65  ? -32.526 -16.017 -24.685 1.00 106.10 ? 168  PRO A CD    1 
ATOM   505  N  N     . PRO A 1 66  ? -32.806 -13.885 -28.800 1.00 104.34 ? 169  PRO A N     1 
ATOM   506  C  CA    . PRO A 1 66  ? -32.995 -12.502 -29.257 1.00 108.37 ? 169  PRO A CA    1 
ATOM   507  C  C     . PRO A 1 66  ? -34.375 -11.957 -28.926 1.00 110.80 ? 169  PRO A C     1 
ATOM   508  O  O     . PRO A 1 66  ? -35.356 -12.272 -29.607 1.00 121.71 ? 169  PRO A O     1 
ATOM   509  C  CB    . PRO A 1 66  ? -32.779 -12.603 -30.772 1.00 110.27 ? 169  PRO A CB    1 
ATOM   510  C  CG    . PRO A 1 66  ? -33.123 -14.017 -31.104 1.00 115.00 ? 169  PRO A CG    1 
ATOM   511  C  CD    . PRO A 1 66  ? -32.680 -14.830 -29.923 1.00 123.39 ? 169  PRO A CD    1 
ATOM   512  N  N     . ASN A 1 67  ? -34.461 -11.142 -27.878 1.00 126.49 ? 170  ASN A N     1 
ATOM   513  C  CA    . ASN A 1 67  ? -35.717 -10.499 -27.502 1.00 121.73 ? 170  ASN A CA    1 
ATOM   514  C  C     . ASN A 1 67  ? -36.090 -9.503  -28.592 1.00 122.24 ? 170  ASN A C     1 
ATOM   515  O  O     . ASN A 1 67  ? -35.619 -8.364  -28.600 1.00 132.96 ? 170  ASN A O     1 
ATOM   516  C  CB    . ASN A 1 67  ? -35.583 -9.816  -26.146 1.00 107.42 ? 170  ASN A CB    1 
ATOM   517  C  CG    . ASN A 1 67  ? -36.909 -9.306  -25.617 1.00 119.57 ? 170  ASN A CG    1 
ATOM   518  O  OD1   . ASN A 1 67  ? -37.974 -9.712  -26.082 1.00 130.01 ? 170  ASN A OD1   1 
ATOM   519  N  ND2   . ASN A 1 67  ? -36.851 -8.412  -24.636 1.00 116.26 ? 170  ASN A ND2   1 
ATOM   520  N  N     . VAL A 1 68  ? -36.939 -9.934  -29.526 1.00 121.40 ? 171  VAL A N     1 
ATOM   521  C  CA    . VAL A 1 68  ? -37.291 -9.139  -30.693 1.00 92.97  ? 171  VAL A CA    1 
ATOM   522  C  C     . VAL A 1 68  ? -38.804 -9.006  -30.777 1.00 113.66 ? 171  VAL A C     1 
ATOM   523  O  O     . VAL A 1 68  ? -39.557 -9.734  -30.126 1.00 137.19 ? 171  VAL A O     1 
ATOM   524  C  CB    . VAL A 1 68  ? -36.738 -9.749  -31.999 1.00 87.18  ? 171  VAL A CB    1 
ATOM   525  C  CG1   . VAL A 1 68  ? -35.221 -9.803  -31.960 1.00 106.78 ? 171  VAL A CG1   1 
ATOM   526  C  CG2   . VAL A 1 68  ? -37.319 -11.135 -32.219 1.00 76.42  ? 171  VAL A CG2   1 
ATOM   527  N  N     . GLU A 1 69  ? -39.243 -8.054  -31.598 1.00 115.30 ? 172  GLU A N     1 
ATOM   528  C  CA    . GLU A 1 69  ? -40.661 -7.872  -31.853 1.00 96.30  ? 172  GLU A CA    1 
ATOM   529  C  C     . GLU A 1 69  ? -41.193 -9.012  -32.721 1.00 109.80 ? 172  GLU A C     1 
ATOM   530  O  O     . GLU A 1 69  ? -40.444 -9.859  -33.218 1.00 99.81  ? 172  GLU A O     1 
ATOM   531  C  CB    . GLU A 1 69  ? -40.915 -6.522  -32.525 1.00 102.69 ? 172  GLU A CB    1 
ATOM   532  C  CG    . GLU A 1 69  ? -40.579 -5.313  -31.661 1.00 87.97  ? 172  GLU A CG    1 
ATOM   533  C  CD    . GLU A 1 69  ? -41.574 -5.096  -30.534 1.00 131.75 ? 172  GLU A CD    1 
ATOM   534  O  OE1   . GLU A 1 69  ? -42.686 -5.662  -30.599 1.00 148.52 ? 172  GLU A OE1   1 
ATOM   535  O  OE2   . GLU A 1 69  ? -41.245 -4.355  -29.584 1.00 110.85 ? 172  GLU A OE2   1 
ATOM   536  N  N     . SER A 1 70  ? -42.513 -9.024  -32.908 1.00 115.42 ? 173  SER A N     1 
ATOM   537  C  CA    . SER A 1 70  ? -43.140 -10.107 -33.657 1.00 93.68  ? 173  SER A CA    1 
ATOM   538  C  C     . SER A 1 70  ? -43.079 -9.886  -35.163 1.00 95.02  ? 173  SER A C     1 
ATOM   539  O  O     . SER A 1 70  ? -43.113 -10.858 -35.925 1.00 119.74 ? 173  SER A O     1 
ATOM   540  C  CB    . SER A 1 70  ? -44.592 -10.279 -33.211 1.00 93.42  ? 173  SER A CB    1 
ATOM   541  O  OG    . SER A 1 70  ? -44.662 -10.629 -31.840 1.00 114.09 ? 173  SER A OG    1 
ATOM   542  N  N     . SER A 1 71  ? -42.990 -8.634  -35.613 1.00 100.61 ? 174  SER A N     1 
ATOM   543  C  CA    . SER A 1 71  ? -42.952 -8.333  -37.035 1.00 106.95 ? 174  SER A CA    1 
ATOM   544  C  C     . SER A 1 71  ? -41.870 -7.303  -37.329 1.00 115.43 ? 174  SER A C     1 
ATOM   545  O  O     . SER A 1 71  ? -41.742 -6.309  -36.598 1.00 138.55 ? 174  SER A O     1 
ATOM   546  C  CB    . SER A 1 71  ? -44.304 -7.810  -37.538 1.00 139.25 ? 174  SER A CB    1 
ATOM   547  O  OG    . SER A 1 71  ? -44.248 -7.507  -38.922 1.00 102.77 ? 174  SER A OG    1 
ATOM   548  N  N     . PRO A 1 72  ? -41.081 -7.510  -38.386 1.00 99.70  ? 175  PRO A N     1 
ATOM   549  C  CA    . PRO A 1 72  ? -40.074 -6.504  -38.755 1.00 116.39 ? 175  PRO A CA    1 
ATOM   550  C  C     . PRO A 1 72  ? -40.669 -5.250  -39.365 1.00 137.74 ? 175  PRO A C     1 
ATOM   551  O  O     . PRO A 1 72  ? -39.985 -4.219  -39.406 1.00 107.19 ? 175  PRO A O     1 
ATOM   552  C  CB    . PRO A 1 72  ? -39.190 -7.246  -39.763 1.00 109.27 ? 175  PRO A CB    1 
ATOM   553  C  CG    . PRO A 1 72  ? -40.104 -8.258  -40.370 1.00 99.29  ? 175  PRO A CG    1 
ATOM   554  C  CD    . PRO A 1 72  ? -41.039 -8.688  -39.270 1.00 133.24 ? 175  PRO A CD    1 
ATOM   555  N  N     . GLU A 1 73  ? -41.910 -5.305  -39.843 1.00 153.82 ? 176  GLU A N     1 
ATOM   556  C  CA    . GLU A 1 73  ? -42.532 -4.142  -40.462 1.00 100.50 ? 176  GLU A CA    1 
ATOM   557  C  C     . GLU A 1 73  ? -42.728 -3.042  -39.426 1.00 95.36  ? 176  GLU A C     1 
ATOM   558  O  O     . GLU A 1 73  ? -43.334 -3.263  -38.374 1.00 98.96  ? 176  GLU A O     1 
ATOM   559  C  CB    . GLU A 1 73  ? -43.870 -4.528  -41.091 1.00 105.29 ? 176  GLU A CB    1 
ATOM   560  C  CG    . GLU A 1 73  ? -44.375 -3.545  -42.137 1.00 146.09 ? 176  GLU A CG    1 
ATOM   561  C  CD    . GLU A 1 73  ? -43.556 -3.578  -43.417 1.00 177.99 ? 176  GLU A CD    1 
ATOM   562  O  OE1   . GLU A 1 73  ? -42.828 -4.570  -43.637 1.00 156.77 ? 176  GLU A OE1   1 
ATOM   563  O  OE2   . GLU A 1 73  ? -43.641 -2.612  -44.204 1.00 164.33 ? 176  GLU A OE2   1 
ATOM   564  N  N     . LEU A 1 74  ? -42.206 -1.858  -39.726 1.00 129.16 ? 177  LEU A N     1 
ATOM   565  C  CA    . LEU A 1 74  ? -42.258 -0.733  -38.802 1.00 113.35 ? 177  LEU A CA    1 
ATOM   566  C  C     . LEU A 1 74  ? -43.472 0.142   -39.103 1.00 118.29 ? 177  LEU A C     1 
ATOM   567  O  O     . LEU A 1 74  ? -43.754 0.430   -40.271 1.00 129.01 ? 177  LEU A O     1 
ATOM   568  C  CB    . LEU A 1 74  ? -40.985 0.102   -38.906 1.00 120.25 ? 177  LEU A CB    1 
ATOM   569  C  CG    . LEU A 1 74  ? -40.535 0.865   -37.660 1.00 121.19 ? 177  LEU A CG    1 
ATOM   570  C  CD1   . LEU A 1 74  ? -40.296 -0.095  -36.509 1.00 106.00 ? 177  LEU A CD1   1 
ATOM   571  C  CD2   . LEU A 1 74  ? -39.279 1.667   -37.955 1.00 110.85 ? 177  LEU A CD2   1 
ATOM   572  N  N     . PRO A 1 75  ? -44.211 0.562   -38.075 1.00 125.23 ? 178  PRO A N     1 
ATOM   573  C  CA    . PRO A 1 75  ? -45.350 1.457   -38.303 1.00 113.93 ? 178  PRO A CA    1 
ATOM   574  C  C     . PRO A 1 75  ? -44.908 2.765   -38.943 1.00 118.64 ? 178  PRO A C     1 
ATOM   575  O  O     . PRO A 1 75  ? -43.749 3.176   -38.852 1.00 123.05 ? 178  PRO A O     1 
ATOM   576  C  CB    . PRO A 1 75  ? -45.913 1.685   -36.895 1.00 99.89  ? 178  PRO A CB    1 
ATOM   577  C  CG    . PRO A 1 75  ? -45.460 0.498   -36.113 1.00 85.74  ? 178  PRO A CG    1 
ATOM   578  C  CD    . PRO A 1 75  ? -44.107 0.148   -36.666 1.00 122.60 ? 178  PRO A CD    1 
ATOM   579  N  N     . LYS A 1 76  ? -45.863 3.423   -39.606 1.00 124.97 ? 179  LYS A N     1 
ATOM   580  C  CA    . LYS A 1 76  ? -45.544 4.631   -40.360 1.00 109.95 ? 179  LYS A CA    1 
ATOM   581  C  C     . LYS A 1 76  ? -45.017 5.734   -39.450 1.00 106.89 ? 179  LYS A C     1 
ATOM   582  O  O     . LYS A 1 76  ? -44.043 6.416   -39.790 1.00 106.03 ? 179  LYS A O     1 
ATOM   583  C  CB    . LYS A 1 76  ? -46.775 5.110   -41.129 1.00 120.55 ? 179  LYS A CB    1 
ATOM   584  C  CG    . LYS A 1 76  ? -46.509 6.281   -42.062 1.00 140.46 ? 179  LYS A CG    1 
ATOM   585  C  CD    . LYS A 1 76  ? -45.525 5.903   -43.159 1.00 148.15 ? 179  LYS A CD    1 
ATOM   586  C  CE    . LYS A 1 76  ? -46.080 4.797   -44.044 1.00 165.23 ? 179  LYS A CE    1 
ATOM   587  N  NZ    . LYS A 1 76  ? -45.127 4.417   -45.124 1.00 170.57 ? 179  LYS A NZ    1 
ATOM   588  N  N     . HIS A 1 77  ? -45.641 5.922   -38.285 1.00 130.17 ? 180  HIS A N     1 
ATOM   589  C  CA    . HIS A 1 77  ? -45.203 6.966   -37.368 1.00 119.19 ? 180  HIS A CA    1 
ATOM   590  C  C     . HIS A 1 77  ? -43.929 6.597   -36.622 1.00 111.48 ? 180  HIS A C     1 
ATOM   591  O  O     . HIS A 1 77  ? -43.206 7.496   -36.178 1.00 124.49 ? 180  HIS A O     1 
ATOM   592  C  CB    . HIS A 1 77  ? -46.312 7.291   -36.365 1.00 107.92 ? 180  HIS A CB    1 
ATOM   593  C  CG    . HIS A 1 77  ? -46.499 6.247   -35.310 1.00 95.84  ? 180  HIS A CG    1 
ATOM   594  N  ND1   . HIS A 1 77  ? -47.035 5.006   -35.577 1.00 115.35 ? 180  HIS A ND1   1 
ATOM   595  C  CD2   . HIS A 1 77  ? -46.226 6.261   -33.984 1.00 101.47 ? 180  HIS A CD2   1 
ATOM   596  C  CE1   . HIS A 1 77  ? -47.081 4.299   -34.462 1.00 118.54 ? 180  HIS A CE1   1 
ATOM   597  N  NE2   . HIS A 1 77  ? -46.597 5.038   -33.480 1.00 114.90 ? 180  HIS A NE2   1 
ATOM   598  N  N     . ILE A 1 78  ? -43.639 5.304   -36.470 1.00 117.86 ? 181  ILE A N     1 
ATOM   599  C  CA    . ILE A 1 78  ? -42.383 4.897   -35.850 1.00 121.81 ? 181  ILE A CA    1 
ATOM   600  C  C     . ILE A 1 78  ? -41.224 5.079   -36.822 1.00 119.83 ? 181  ILE A C     1 
ATOM   601  O  O     . ILE A 1 78  ? -40.126 5.489   -36.428 1.00 110.68 ? 181  ILE A O     1 
ATOM   602  C  CB    . ILE A 1 78  ? -42.483 3.445   -35.347 1.00 91.83  ? 181  ILE A CB    1 
ATOM   603  C  CG1   . ILE A 1 78  ? -43.665 3.293   -34.390 1.00 90.86  ? 181  ILE A CG1   1 
ATOM   604  C  CG2   . ILE A 1 78  ? -41.193 3.027   -34.660 1.00 89.65  ? 181  ILE A CG2   1 
ATOM   605  N  N     . TYR A 1 79  ? -41.450 4.784   -38.105 1.00 133.57 ? 182  TYR A N     1 
ATOM   606  C  CA    . TYR A 1 79  ? -40.411 4.983   -39.110 1.00 106.69 ? 182  TYR A CA    1 
ATOM   607  C  C     . TYR A 1 79  ? -40.077 6.459   -39.289 1.00 120.98 ? 182  TYR A C     1 
ATOM   608  O  O     . TYR A 1 79  ? -38.932 6.798   -39.608 1.00 135.36 ? 182  TYR A O     1 
ATOM   609  C  CB    . TYR A 1 79  ? -40.849 4.368   -40.441 1.00 99.56  ? 182  TYR A CB    1 
ATOM   610  C  CG    . TYR A 1 79  ? -39.893 4.614   -41.590 1.00 105.82 ? 182  TYR A CG    1 
ATOM   611  C  CD1   . TYR A 1 79  ? -38.792 3.793   -41.791 1.00 124.76 ? 182  TYR A CD1   1 
ATOM   612  C  CD2   . TYR A 1 79  ? -40.099 5.663   -42.477 1.00 116.51 ? 182  TYR A CD2   1 
ATOM   613  C  CE1   . TYR A 1 79  ? -37.918 4.014   -42.840 1.00 115.13 ? 182  TYR A CE1   1 
ATOM   614  C  CE2   . TYR A 1 79  ? -39.230 5.892   -43.528 1.00 124.51 ? 182  TYR A CE2   1 
ATOM   615  C  CZ    . TYR A 1 79  ? -38.143 5.064   -43.705 1.00 123.06 ? 182  TYR A CZ    1 
ATOM   616  O  OH    . TYR A 1 79  ? -37.278 5.289   -44.752 1.00 137.87 ? 182  TYR A OH    1 
ATOM   617  N  N     . ASN A 1 80  ? -41.054 7.346   -39.087 1.00 107.23 ? 183  ASN A N     1 
ATOM   618  C  CA    . ASN A 1 80  ? -40.803 8.775   -39.235 1.00 113.45 ? 183  ASN A CA    1 
ATOM   619  C  C     . ASN A 1 80  ? -39.920 9.328   -38.125 1.00 121.24 ? 183  ASN A C     1 
ATOM   620  O  O     . ASN A 1 80  ? -39.383 10.431  -38.271 1.00 138.76 ? 183  ASN A O     1 
ATOM   621  C  CB    . ASN A 1 80  ? -42.126 9.542   -39.281 1.00 107.37 ? 183  ASN A CB    1 
ATOM   622  C  CG    . ASN A 1 80  ? -42.959 9.194   -40.500 1.00 126.55 ? 183  ASN A CG    1 
ATOM   623  O  OD1   . ASN A 1 80  ? -42.431 8.754   -41.522 1.00 108.43 ? 183  ASN A OD1   1 
ATOM   624  N  ND2   . ASN A 1 80  ? -44.269 9.390   -40.397 1.00 116.27 ? 183  ASN A ND2   1 
ATOM   625  N  N     . LYS A 1 81  ? -39.758 8.594   -37.023 1.00 105.97 ? 184  LYS A N     1 
ATOM   626  C  CA    . LYS A 1 81  ? -38.854 9.020   -35.962 1.00 106.45 ? 184  LYS A CA    1 
ATOM   627  C  C     . LYS A 1 81  ? -37.388 8.876   -36.346 1.00 119.24 ? 184  LYS A C     1 
ATOM   628  O  O     . LYS A 1 81  ? -36.526 9.411   -35.641 1.00 134.68 ? 184  LYS A O     1 
ATOM   629  C  CB    . LYS A 1 81  ? -39.127 8.224   -34.683 1.00 108.10 ? 184  LYS A CB    1 
ATOM   630  C  CG    . LYS A 1 81  ? -40.482 8.494   -34.051 1.00 119.31 ? 184  LYS A CG    1 
ATOM   631  C  CD    . LYS A 1 81  ? -40.333 9.117   -32.670 1.00 130.59 ? 184  LYS A CD    1 
ATOM   632  C  CE    . LYS A 1 81  ? -39.626 10.463  -32.740 1.00 134.84 ? 184  LYS A CE    1 
ATOM   633  N  NZ    . LYS A 1 81  ? -39.441 11.071  -31.394 1.00 145.41 ? 184  LYS A NZ    1 
ATOM   634  N  N     . LEU A 1 82  ? -37.089 8.177   -37.437 1.00 121.19 ? 185  LEU A N     1 
ATOM   635  C  CA    . LEU A 1 82  ? -35.717 7.947   -37.860 1.00 131.37 ? 185  LEU A CA    1 
ATOM   636  C  C     . LEU A 1 82  ? -35.244 9.073   -38.770 1.00 135.25 ? 185  LEU A C     1 
ATOM   637  O  O     . LEU A 1 82  ? -36.015 9.608   -39.571 1.00 129.02 ? 185  LEU A O     1 
ATOM   638  C  CB    . LEU A 1 82  ? -35.602 6.607   -38.588 1.00 133.80 ? 185  LEU A CB    1 
ATOM   639  C  CG    . LEU A 1 82  ? -36.113 5.387   -37.822 1.00 116.85 ? 185  LEU A CG    1 
ATOM   640  C  CD1   . LEU A 1 82  ? -36.211 4.185   -38.743 1.00 122.98 ? 185  LEU A CD1   1 
ATOM   641  C  CD2   . LEU A 1 82  ? -35.210 5.086   -36.636 1.00 118.60 ? 185  LEU A CD2   1 
ATOM   642  N  N     . ASP A 1 83  ? -33.969 9.428   -38.638 1.00 141.31 ? 186  ASP A N     1 
ATOM   643  C  CA    . ASP A 1 83  ? -33.355 10.437  -39.498 1.00 126.45 ? 186  ASP A CA    1 
ATOM   644  C  C     . ASP A 1 83  ? -33.191 9.847   -40.892 1.00 122.95 ? 186  ASP A C     1 
ATOM   645  O  O     . ASP A 1 83  ? -32.271 9.065   -41.144 1.00 153.96 ? 186  ASP A O     1 
ATOM   646  C  CB    . ASP A 1 83  ? -32.014 10.882  -38.925 1.00 144.92 ? 186  ASP A CB    1 
ATOM   647  C  CG    . ASP A 1 83  ? -31.374 11.998  -39.732 1.00 155.91 ? 186  ASP A CG    1 
ATOM   648  O  OD1   . ASP A 1 83  ? -32.075 12.619  -40.558 1.00 137.47 ? 186  ASP A OD1   1 
ATOM   649  O  OD2   . ASP A 1 83  ? -30.166 12.252  -39.541 1.00 166.25 ? 186  ASP A OD2   1 
ATOM   650  N  N     . LYS A 1 84  ? -34.094 10.219  -41.802 1.00 106.61 ? 187  LYS A N     1 
ATOM   651  C  CA    . LYS A 1 84  ? -34.078 9.739   -43.185 1.00 128.49 ? 187  LYS A CA    1 
ATOM   652  C  C     . LYS A 1 84  ? -34.162 8.217   -43.255 1.00 117.25 ? 187  LYS A C     1 
ATOM   653  O  O     . LYS A 1 84  ? -33.574 7.591   -44.141 1.00 132.59 ? 187  LYS A O     1 
ATOM   654  C  CB    . LYS A 1 84  ? -32.838 10.240  -43.934 1.00 167.37 ? 187  LYS A CB    1 
ATOM   655  C  CG    . LYS A 1 84  ? -32.560 11.725  -43.756 1.00 147.48 ? 187  LYS A CG    1 
ATOM   656  C  CD    . LYS A 1 84  ? -31.230 12.116  -44.379 1.00 131.82 ? 187  LYS A CD    1 
ATOM   657  C  CE    . LYS A 1 84  ? -30.871 13.556  -44.054 1.00 155.90 ? 187  LYS A CE    1 
ATOM   658  N  NZ    . LYS A 1 84  ? -31.912 14.509  -44.529 1.00 153.64 ? 187  LYS A NZ    1 
ATOM   659  N  N     . GLY A 1 85  ? -34.894 7.610   -42.324 1.00 116.88 ? 188  GLY A N     1 
ATOM   660  C  CA    . GLY A 1 85  ? -34.979 6.165   -42.277 1.00 115.34 ? 188  GLY A CA    1 
ATOM   661  C  C     . GLY A 1 85  ? -33.741 5.480   -41.750 1.00 112.76 ? 188  GLY A C     1 
ATOM   662  O  O     . GLY A 1 85  ? -33.537 4.294   -42.021 1.00 122.09 ? 188  GLY A O     1 
ATOM   663  N  N     . GLN A 1 86  ? -32.903 6.195   -41.003 1.00 110.95 ? 189  GLN A N     1 
ATOM   664  C  CA    . GLN A 1 86  ? -31.669 5.649   -40.460 1.00 118.85 ? 189  GLN A CA    1 
ATOM   665  C  C     . GLN A 1 86  ? -31.611 5.912   -38.962 1.00 111.17 ? 189  GLN A C     1 
ATOM   666  O  O     . GLN A 1 86  ? -32.266 6.819   -38.442 1.00 107.30 ? 189  GLN A O     1 
ATOM   667  C  CB    . GLN A 1 86  ? -30.439 6.247   -41.158 1.00 101.51 ? 189  GLN A CB    1 
ATOM   668  C  CG    . GLN A 1 86  ? -30.351 5.908   -42.638 1.00 105.49 ? 189  GLN A CG    1 
ATOM   669  C  CD    . GLN A 1 86  ? -29.213 6.623   -43.338 1.00 140.07 ? 189  GLN A CD    1 
ATOM   670  O  OE1   . GLN A 1 86  ? -28.759 7.677   -42.893 1.00 160.96 ? 189  GLN A OE1   1 
ATOM   671  N  NE2   . GLN A 1 86  ? -28.745 6.051   -44.441 1.00 136.33 ? 189  GLN A NE2   1 
ATOM   672  N  N     . ILE A 1 87  ? -30.813 5.103   -38.270 1.00 102.87 ? 190  ILE A N     1 
ATOM   673  C  CA    . ILE A 1 87  ? -30.707 5.145   -36.817 1.00 102.30 ? 190  ILE A CA    1 
ATOM   674  C  C     . ILE A 1 87  ? -29.274 5.493   -36.440 1.00 109.30 ? 190  ILE A C     1 
ATOM   675  O  O     . ILE A 1 87  ? -28.325 5.090   -37.122 1.00 110.64 ? 190  ILE A O     1 
ATOM   676  C  CB    . ILE A 1 87  ? -31.142 3.803   -36.186 1.00 104.08 ? 190  ILE A CB    1 
ATOM   677  C  CG1   . ILE A 1 87  ? -31.086 3.868   -34.657 1.00 108.72 ? 190  ILE A CG1   1 
ATOM   678  C  CG2   . ILE A 1 87  ? -30.294 2.653   -36.716 1.00 103.40 ? 190  ILE A CG2   1 
ATOM   679  C  CD1   . ILE A 1 87  ? -32.000 4.913   -34.055 1.00 121.78 ? 190  ILE A CD1   1 
ATOM   680  N  N     . ILE A 1 88  ? -29.121 6.260   -35.363 1.00 101.12 ? 191  ILE A N     1 
ATOM   681  C  CA    . ILE A 1 88  ? -27.816 6.636   -34.831 1.00 112.78 ? 191  ILE A CA    1 
ATOM   682  C  C     . ILE A 1 88  ? -27.532 5.707   -33.657 1.00 106.13 ? 191  ILE A C     1 
ATOM   683  O  O     . ILE A 1 88  ? -28.050 5.903   -32.554 1.00 93.75  ? 191  ILE A O     1 
ATOM   684  C  CB    . ILE A 1 88  ? -27.775 8.107   -34.408 1.00 127.46 ? 191  ILE A CB    1 
ATOM   685  C  CG1   . ILE A 1 88  ? -28.070 9.023   -35.597 1.00 111.02 ? 191  ILE A CG1   1 
ATOM   686  C  CG2   . ILE A 1 88  ? -26.422 8.447   -33.795 1.00 94.84  ? 191  ILE A CG2   1 
ATOM   687  C  CD1   . ILE A 1 88  ? -26.927 9.142   -36.572 1.00 108.08 ? 191  ILE A CD1   1 
ATOM   688  N  N     . VAL A 1 89  ? -26.705 4.691   -33.886 1.00 123.52 ? 192  VAL A N     1 
ATOM   689  C  CA    . VAL A 1 89  ? -26.335 3.737   -32.848 1.00 110.65 ? 192  VAL A CA    1 
ATOM   690  C  C     . VAL A 1 89  ? -24.912 4.030   -32.395 1.00 100.35 ? 192  VAL A C     1 
ATOM   691  O  O     . VAL A 1 89  ? -24.097 4.580   -33.145 1.00 106.28 ? 192  VAL A O     1 
ATOM   692  C  CB    . VAL A 1 89  ? -26.472 2.277   -33.330 1.00 83.22  ? 192  VAL A CB    1 
ATOM   693  C  CG1   . VAL A 1 89  ? -27.909 1.987   -33.732 1.00 106.85 ? 192  VAL A CG1   1 
ATOM   694  C  CG2   . VAL A 1 89  ? -25.525 2.005   -34.486 1.00 94.54  ? 192  VAL A CG2   1 
ATOM   695  N  N     . VAL A 1 90  ? -24.619 3.660   -31.152 1.00 110.75 ? 193  VAL A N     1 
ATOM   696  C  CA    . VAL A 1 90  ? -23.315 3.889   -30.539 1.00 125.20 ? 193  VAL A CA    1 
ATOM   697  C  C     . VAL A 1 90  ? -22.686 2.533   -30.252 1.00 144.92 ? 193  VAL A C     1 
ATOM   698  O  O     . VAL A 1 90  ? -23.254 1.725   -29.507 1.00 122.58 ? 193  VAL A O     1 
ATOM   699  C  CB    . VAL A 1 90  ? -23.426 4.723   -29.254 1.00 112.32 ? 193  VAL A CB    1 
ATOM   700  C  CG1   . VAL A 1 90  ? -22.043 5.088   -28.736 1.00 88.15  ? 193  VAL A CG1   1 
ATOM   701  C  CG2   . VAL A 1 90  ? -24.264 5.970   -29.499 1.00 100.67 ? 193  VAL A CG2   1 
ATOM   702  N  N     . ILE A 1 91  ? -21.519 2.287   -30.839 1.00 131.02 ? 194  ILE A N     1 
ATOM   703  C  CA    . ILE A 1 91  ? -20.786 1.040   -30.652 1.00 119.72 ? 194  ILE A CA    1 
ATOM   704  C  C     . ILE A 1 91  ? -19.674 1.289   -29.642 1.00 127.96 ? 194  ILE A C     1 
ATOM   705  O  O     . ILE A 1 91  ? -18.842 2.185   -29.831 1.00 145.53 ? 194  ILE A O     1 
ATOM   706  C  CB    . ILE A 1 91  ? -20.221 0.515   -31.981 1.00 127.58 ? 194  ILE A CB    1 
ATOM   707  C  CG1   . ILE A 1 91  ? -21.351 0.278   -32.986 1.00 130.20 ? 194  ILE A CG1   1 
ATOM   708  C  CG2   . ILE A 1 91  ? -19.426 -0.763  -31.756 1.00 98.04  ? 194  ILE A CG2   1 
ATOM   709  C  CD1   . ILE A 1 91  ? -22.368 -0.746  -32.531 1.00 120.18 ? 194  ILE A CD1   1 
ATOM   710  N  N     . TRP A 1 92  ? -19.658 0.501   -28.571 1.00 117.69 ? 195  TRP A N     1 
ATOM   711  C  CA    . TRP A 1 92  ? -18.647 0.601   -27.527 1.00 129.22 ? 195  TRP A CA    1 
ATOM   712  C  C     . TRP A 1 92  ? -17.701 -0.588  -27.618 1.00 131.74 ? 195  TRP A C     1 
ATOM   713  O  O     . TRP A 1 92  ? -18.147 -1.736  -27.715 1.00 125.10 ? 195  TRP A O     1 
ATOM   714  C  CB    . TRP A 1 92  ? -19.293 0.660   -26.141 1.00 126.54 ? 195  TRP A CB    1 
ATOM   715  C  CG    . TRP A 1 92  ? -19.975 1.961   -25.850 1.00 130.75 ? 195  TRP A CG    1 
ATOM   716  C  CD1   . TRP A 1 92  ? -21.257 2.306   -26.168 1.00 149.45 ? 195  TRP A CD1   1 
ATOM   717  C  CD2   . TRP A 1 92  ? -19.410 3.093   -25.179 1.00 148.92 ? 195  TRP A CD2   1 
ATOM   718  N  NE1   . TRP A 1 92  ? -21.525 3.583   -25.737 1.00 130.88 ? 195  TRP A NE1   1 
ATOM   719  C  CE2   . TRP A 1 92  ? -20.407 4.088   -25.127 1.00 158.55 ? 195  TRP A CE2   1 
ATOM   720  C  CE3   . TRP A 1 92  ? -18.158 3.362   -24.617 1.00 142.54 ? 195  TRP A CE3   1 
ATOM   721  C  CZ2   . TRP A 1 92  ? -20.190 5.331   -24.536 1.00 170.08 ? 195  TRP A CZ2   1 
ATOM   722  C  CZ3   . TRP A 1 92  ? -17.945 4.597   -24.031 1.00 152.18 ? 195  TRP A CZ3   1 
ATOM   723  C  CH2   . TRP A 1 92  ? -18.956 5.566   -23.995 1.00 170.41 ? 195  TRP A CH2   1 
ATOM   724  N  N     . VAL A 1 93  ? -16.399 -0.309  -27.588 1.00 152.03 ? 196  VAL A N     1 
ATOM   725  C  CA    . VAL A 1 93  ? -15.361 -1.328  -27.690 1.00 118.23 ? 196  VAL A CA    1 
ATOM   726  C  C     . VAL A 1 93  ? -14.348 -1.099  -26.578 1.00 129.13 ? 196  VAL A C     1 
ATOM   727  O  O     . VAL A 1 93  ? -13.907 0.035   -26.359 1.00 125.74 ? 196  VAL A O     1 
ATOM   728  C  CB    . VAL A 1 93  ? -14.665 -1.303  -29.066 1.00 114.88 ? 196  VAL A CB    1 
ATOM   729  C  CG1   . VAL A 1 93  ? -13.530 -2.315  -29.110 1.00 149.46 ? 196  VAL A CG1   1 
ATOM   730  C  CG2   . VAL A 1 93  ? -15.666 -1.575  -30.180 1.00 143.28 ? 196  VAL A CG2   1 
ATOM   731  N  N     . ILE A 1 94  ? -13.985 -2.170  -25.878 1.00 145.99 ? 197  ILE A N     1 
ATOM   732  C  CA    . ILE A 1 94  ? -12.961 -2.116  -24.840 1.00 165.12 ? 197  ILE A CA    1 
ATOM   733  C  C     . ILE A 1 94  ? -11.630 -2.515  -25.464 1.00 172.53 ? 197  ILE A C     1 
ATOM   734  O  O     . ILE A 1 94  ? -11.507 -3.595  -26.052 1.00 175.74 ? 197  ILE A O     1 
ATOM   735  C  CB    . ILE A 1 94  ? -13.314 -3.033  -23.659 1.00 157.95 ? 197  ILE A CB    1 
ATOM   736  C  CG1   . ILE A 1 94  ? -14.688 -2.668  -23.092 1.00 148.90 ? 197  ILE A CG1   1 
ATOM   737  C  CG2   . ILE A 1 94  ? -12.247 -2.941  -22.577 1.00 165.17 ? 197  ILE A CG2   1 
ATOM   738  C  CD1   . ILE A 1 94  ? -14.780 -1.255  -22.563 1.00 155.52 ? 197  ILE A CD1   1 
ATOM   739  N  N     . VAL A 1 95  ? -10.630 -1.645  -25.338 1.00 170.64 ? 198  VAL A N     1 
ATOM   740  C  CA    . VAL A 1 95  ? -9.343  -1.863  -25.988 1.00 191.60 ? 198  VAL A CA    1 
ATOM   741  C  C     . VAL A 1 95  ? -8.293  -2.267  -24.961 1.00 209.93 ? 198  VAL A C     1 
ATOM   742  O  O     . VAL A 1 95  ? -7.762  -3.383  -25.007 1.00 214.71 ? 198  VAL A O     1 
ATOM   743  C  CB    . VAL A 1 95  ? -8.897  -0.610  -26.764 1.00 201.48 ? 198  VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 95  ? -7.537  -0.838  -27.406 1.00 217.03 ? 198  VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 95  ? -9.932  -0.243  -27.816 1.00 173.29 ? 198  VAL A CG2   1 
ATOM   746  N  N     . SER A 1 96  ? -7.985  -1.366  -24.034 1.00 218.51 ? 199  SER A N     1 
ATOM   747  C  CA    . SER A 1 96  ? -6.945  -1.630  -23.056 1.00 223.92 ? 199  SER A CA    1 
ATOM   748  C  C     . SER A 1 96  ? -7.416  -2.665  -22.035 1.00 233.69 ? 199  SER A C     1 
ATOM   749  O  O     . SER A 1 96  ? -8.598  -2.710  -21.683 1.00 211.00 ? 199  SER A O     1 
ATOM   750  C  CB    . SER A 1 96  ? -6.548  -0.342  -22.340 1.00 232.82 ? 199  SER A CB    1 
ATOM   751  O  OG    . SER A 1 96  ? -5.537  -0.582  -21.378 1.00 211.80 ? 199  SER A OG    1 
ATOM   752  N  N     . PRO A 1 97  ? -6.507  -3.516  -21.548 1.00 247.44 ? 200  PRO A N     1 
ATOM   753  C  CA    . PRO A 1 97  ? -6.888  -4.481  -20.504 1.00 239.17 ? 200  PRO A CA    1 
ATOM   754  C  C     . PRO A 1 97  ? -7.239  -3.836  -19.174 1.00 246.25 ? 200  PRO A C     1 
ATOM   755  O  O     . PRO A 1 97  ? -7.797  -4.521  -18.306 1.00 234.35 ? 200  PRO A O     1 
ATOM   756  C  CB    . PRO A 1 97  ? -5.644  -5.371  -20.378 1.00 212.47 ? 200  PRO A CB    1 
ATOM   757  C  CG    . PRO A 1 97  ? -4.521  -4.518  -20.864 1.00 204.09 ? 200  PRO A CG    1 
ATOM   758  C  CD    . PRO A 1 97  ? -5.103  -3.675  -21.962 1.00 221.16 ? 200  PRO A CD    1 
ATOM   759  N  N     . ASN A 1 98  ? -6.933  -2.552  -18.983 1.00 249.17 ? 201  ASN A N     1 
ATOM   760  C  CA    . ASN A 1 98  ? -7.285  -1.827  -17.770 1.00 235.11 ? 201  ASN A CA    1 
ATOM   761  C  C     . ASN A 1 98  ? -8.708  -1.279  -17.799 1.00 231.85 ? 201  ASN A C     1 
ATOM   762  O  O     . ASN A 1 98  ? -9.003  -0.323  -17.070 1.00 229.06 ? 201  ASN A O     1 
ATOM   763  C  CB    . ASN A 1 98  ? -6.290  -0.688  -17.531 1.00 225.61 ? 201  ASN A CB    1 
ATOM   764  C  CG    . ASN A 1 98  ? -4.861  -1.178  -17.406 1.00 235.23 ? 201  ASN A CG    1 
ATOM   765  O  OD1   . ASN A 1 98  ? -4.615  -2.304  -16.974 1.00 243.66 ? 201  ASN A OD1   1 
ATOM   766  N  ND2   . ASN A 1 98  ? -3.910  -0.333  -17.784 1.00 245.01 ? 201  ASN A ND2   1 
ATOM   767  N  N     . ASN A 1 99  ? -9.579  -1.858  -18.627 1.00 215.92 ? 202  ASN A N     1 
ATOM   768  C  CA    . ASN A 1 99  ? -10.981 -1.456  -18.739 1.00 213.30 ? 202  ASN A CA    1 
ATOM   769  C  C     . ASN A 1 99  ? -11.105 0.011   -19.160 1.00 215.98 ? 202  ASN A C     1 
ATOM   770  O  O     . ASN A 1 99  ? -11.603 0.864   -18.421 1.00 213.63 ? 202  ASN A O     1 
ATOM   771  C  CB    . ASN A 1 99  ? -11.735 -1.726  -17.432 1.00 208.29 ? 202  ASN A CB    1 
ATOM   772  C  CG    . ASN A 1 99  ? -11.788 -3.201  -17.085 1.00 201.77 ? 202  ASN A CG    1 
ATOM   773  O  OD1   . ASN A 1 99  ? -10.870 -3.738  -16.465 1.00 213.51 ? 202  ASN A OD1   1 
ATOM   774  N  ND2   . ASN A 1 99  ? -12.867 -3.865  -17.485 1.00 180.96 ? 202  ASN A ND2   1 
ATOM   775  N  N     . ASP A 1 100 ? -10.637 0.290   -20.372 1.00 205.76 ? 203  ASP A N     1 
ATOM   776  C  CA    . ASP A 1 100 ? -10.778 1.600   -20.988 1.00 183.64 ? 203  ASP A CA    1 
ATOM   777  C  C     . ASP A 1 100 ? -11.862 1.556   -22.057 1.00 185.40 ? 203  ASP A C     1 
ATOM   778  O  O     . ASP A 1 100 ? -12.042 0.547   -22.744 1.00 177.73 ? 203  ASP A O     1 
ATOM   779  C  CB    . ASP A 1 100 ? -9.454  2.069   -21.597 1.00 174.99 ? 203  ASP A CB    1 
ATOM   780  C  CG    . ASP A 1 100 ? -8.426  2.436   -20.543 1.00 178.94 ? 203  ASP A CG    1 
ATOM   781  O  OD1   . ASP A 1 100 ? -8.747  2.339   -19.340 1.00 183.53 ? 203  ASP A OD1   1 
ATOM   782  O  OD2   . ASP A 1 100 ? -7.299  2.823   -20.918 1.00 166.83 ? 203  ASP A OD2   1 
ATOM   783  N  N     . LYS A 1 101 ? -12.584 2.665   -22.194 1.00 179.59 ? 204  LYS A N     1 
ATOM   784  C  CA    . LYS A 1 101 ? -13.764 2.738   -23.043 1.00 152.83 ? 204  LYS A CA    1 
ATOM   785  C  C     . LYS A 1 101 ? -13.485 3.585   -24.277 1.00 155.18 ? 204  LYS A C     1 
ATOM   786  O  O     . LYS A 1 101 ? -12.773 4.591   -24.205 1.00 149.68 ? 204  LYS A O     1 
ATOM   787  C  CB    . LYS A 1 101 ? -14.959 3.320   -22.276 1.00 154.61 ? 204  LYS A CB    1 
ATOM   788  C  CG    . LYS A 1 101 ? -15.611 2.370   -21.273 1.00 155.75 ? 204  LYS A CG    1 
ATOM   789  C  CD    . LYS A 1 101 ? -14.782 2.205   -20.005 1.00 176.93 ? 204  LYS A CD    1 
ATOM   790  C  CE    . LYS A 1 101 ? -14.499 3.546   -19.347 1.00 193.24 ? 204  LYS A CE    1 
ATOM   791  N  NZ    . LYS A 1 101 ? -13.641 3.402   -18.138 1.00 177.17 ? 204  LYS A NZ    1 
ATOM   792  N  N     . GLN A 1 102 ? -14.055 3.170   -25.408 1.00 150.61 ? 205  GLN A N     1 
ATOM   793  C  CA    . GLN A 1 102 ? -13.958 3.909   -26.663 1.00 163.85 ? 205  GLN A CA    1 
ATOM   794  C  C     . GLN A 1 102 ? -15.274 3.765   -27.411 1.00 146.96 ? 205  GLN A C     1 
ATOM   795  O  O     . GLN A 1 102 ? -15.635 2.657   -27.821 1.00 140.11 ? 205  GLN A O     1 
ATOM   796  C  CB    . GLN A 1 102 ? -12.797 3.404   -27.526 1.00 141.54 ? 205  GLN A CB    1 
ATOM   797  C  CG    . GLN A 1 102 ? -11.415 3.770   -27.013 1.00 141.29 ? 205  GLN A CG    1 
ATOM   798  C  CD    . GLN A 1 102 ? -10.316 3.368   -27.976 1.00 167.82 ? 205  GLN A CD    1 
ATOM   799  O  OE1   . GLN A 1 102 ? -10.580 2.792   -29.032 1.00 166.30 ? 205  GLN A OE1   1 
ATOM   800  N  NE2   . GLN A 1 102 ? -9.074  3.673   -27.618 1.00 166.10 ? 205  GLN A NE2   1 
ATOM   801  N  N     . LYS A 1 103 ? -15.986 4.873   -27.589 1.00 126.23 ? 206  LYS A N     1 
ATOM   802  C  CA    . LYS A 1 103 ? -17.252 4.860   -28.306 1.00 141.27 ? 206  LYS A CA    1 
ATOM   803  C  C     . LYS A 1 103 ? -17.022 5.111   -29.791 1.00 129.45 ? 206  LYS A C     1 
ATOM   804  O  O     . LYS A 1 103 ? -16.025 5.718   -30.193 1.00 129.67 ? 206  LYS A O     1 
ATOM   805  C  CB    . LYS A 1 103 ? -18.214 5.908   -27.741 1.00 124.52 ? 206  LYS A CB    1 
ATOM   806  C  CG    . LYS A 1 103 ? -18.036 7.305   -28.318 1.00 135.97 ? 206  LYS A CG    1 
ATOM   807  C  CD    . LYS A 1 103 ? -18.970 8.307   -27.659 1.00 129.20 ? 206  LYS A CD    1 
ATOM   808  C  CE    . LYS A 1 103 ? -18.662 8.457   -26.178 1.00 148.84 ? 206  LYS A CE    1 
ATOM   809  N  NZ    . LYS A 1 103 ? -19.534 9.473   -25.528 1.00 133.94 ? 206  LYS A NZ    1 
ATOM   810  N  N     . TYR A 1 104 ? -17.958 4.626   -30.610 1.00 122.46 ? 207  TYR A N     1 
ATOM   811  C  CA    . TYR A 1 104 ? -17.872 4.789   -32.064 1.00 125.07 ? 207  TYR A CA    1 
ATOM   812  C  C     . TYR A 1 104 ? -19.299 4.917   -32.600 1.00 127.64 ? 207  TYR A C     1 
ATOM   813  O  O     . TYR A 1 104 ? -19.951 3.918   -32.914 1.00 131.94 ? 207  TYR A O     1 
ATOM   814  C  CB    . TYR A 1 104 ? -17.128 3.632   -32.717 1.00 129.75 ? 207  TYR A CB    1 
ATOM   815  C  CG    . TYR A 1 104 ? -15.658 3.568   -32.368 1.00 155.91 ? 207  TYR A CG    1 
ATOM   816  C  CD1   . TYR A 1 104 ? -14.724 4.311   -33.079 1.00 163.17 ? 207  TYR A CD1   1 
ATOM   817  C  CD2   . TYR A 1 104 ? -15.204 2.765   -31.331 1.00 141.46 ? 207  TYR A CD2   1 
ATOM   818  C  CE1   . TYR A 1 104 ? -13.378 4.256   -32.765 1.00 154.87 ? 207  TYR A CE1   1 
ATOM   819  C  CE2   . TYR A 1 104 ? -13.862 2.704   -31.009 1.00 142.94 ? 207  TYR A CE2   1 
ATOM   820  C  CZ    . TYR A 1 104 ? -12.954 3.451   -31.729 1.00 150.65 ? 207  TYR A CZ    1 
ATOM   821  O  OH    . TYR A 1 104 ? -11.616 3.391   -31.412 1.00 157.47 ? 207  TYR A OH    1 
ATOM   822  N  N     . THR A 1 105 ? -19.771 6.156   -32.697 1.00 117.60 ? 208  THR A N     1 
ATOM   823  C  CA    . THR A 1 105 ? -21.089 6.425   -33.248 1.00 120.66 ? 208  THR A CA    1 
ATOM   824  C  C     . THR A 1 105 ? -21.072 6.282   -34.765 1.00 132.36 ? 208  THR A C     1 
ATOM   825  O  O     . THR A 1 105 ? -20.070 6.570   -35.427 1.00 133.17 ? 208  THR A O     1 
ATOM   826  C  CB    . THR A 1 105 ? -21.559 7.829   -32.866 1.00 103.75 ? 208  THR A CB    1 
ATOM   827  O  OG1   . THR A 1 105 ? -20.569 8.787   -33.259 1.00 127.85 ? 208  THR A OG1   1 
ATOM   828  C  CG2   . THR A 1 105 ? -21.783 7.928   -31.366 1.00 102.14 ? 208  THR A CG2   1 
ATOM   829  N  N     . LEU A 1 106 ? -22.197 5.832   -35.314 1.00 119.60 ? 209  LEU A N     1 
ATOM   830  C  CA    . LEU A 1 106 ? -22.313 5.645   -36.752 1.00 126.71 ? 209  LEU A CA    1 
ATOM   831  C  C     . LEU A 1 106 ? -23.784 5.654   -37.139 1.00 123.71 ? 209  LEU A C     1 
ATOM   832  O  O     . LEU A 1 106 ? -24.625 5.115   -36.415 1.00 99.56  ? 209  LEU A O     1 
ATOM   833  C  CB    . LEU A 1 106 ? -21.644 4.337   -37.198 1.00 133.88 ? 209  LEU A CB    1 
ATOM   834  C  CG    . LEU A 1 106 ? -22.093 3.033   -36.529 1.00 113.04 ? 209  LEU A CG    1 
ATOM   835  C  CD1   . LEU A 1 106 ? -23.164 2.328   -37.352 1.00 140.93 ? 209  LEU A CD1   1 
ATOM   836  C  CD2   . LEU A 1 106 ? -20.905 2.115   -36.290 1.00 107.99 ? 209  LEU A CD2   1 
ATOM   837  N  N     . LYS A 1 107 ? -24.085 6.277   -38.275 1.00 122.72 ? 210  LYS A N     1 
ATOM   838  C  CA    . LYS A 1 107 ? -25.433 6.269   -38.825 1.00 100.58 ? 210  LYS A CA    1 
ATOM   839  C  C     . LYS A 1 107 ? -25.576 5.091   -39.778 1.00 105.87 ? 210  LYS A C     1 
ATOM   840  O  O     . LYS A 1 107 ? -24.713 4.867   -40.633 1.00 133.61 ? 210  LYS A O     1 
ATOM   841  C  CB    . LYS A 1 107 ? -25.743 7.582   -39.546 1.00 100.60 ? 210  LYS A CB    1 
ATOM   842  C  CG    . LYS A 1 107 ? -27.182 7.682   -40.034 1.00 113.06 ? 210  LYS A CG    1 
ATOM   843  C  CD    . LYS A 1 107 ? -27.643 9.127   -40.171 1.00 97.43  ? 210  LYS A CD    1 
ATOM   844  C  CE    . LYS A 1 107 ? -26.874 9.867   -41.251 1.00 147.49 ? 210  LYS A CE    1 
ATOM   845  N  NZ    . LYS A 1 107 ? -27.367 11.263  -41.414 1.00 151.44 ? 210  LYS A NZ    1 
ATOM   846  N  N     . ILE A 1 108 ? -26.664 4.337   -39.624 1.00 96.10  ? 211  ILE A N     1 
ATOM   847  C  CA    . ILE A 1 108 ? -26.886 3.121   -40.395 1.00 95.30  ? 211  ILE A CA    1 
ATOM   848  C  C     . ILE A 1 108 ? -28.387 2.937   -40.570 1.00 115.14 ? 211  ILE A C     1 
ATOM   849  O  O     . ILE A 1 108 ? -29.193 3.486   -39.814 1.00 90.89  ? 211  ILE A O     1 
ATOM   850  C  CB    . ILE A 1 108 ? -26.242 1.890   -39.707 1.00 103.87 ? 211  ILE A CB    1 
ATOM   851  C  CG1   . ILE A 1 108 ? -25.947 0.788   -40.725 1.00 124.18 ? 211  ILE A CG1   1 
ATOM   852  C  CG2   . ILE A 1 108 ? -27.128 1.367   -38.586 1.00 97.09  ? 211  ILE A CG2   1 
ATOM   853  N  N     . ASN A 1 109 ? -28.763 2.172   -41.593 1.00 110.31 ? 212  ASN A N     1 
ATOM   854  C  CA    . ASN A 1 109 ? -30.172 1.886   -41.828 1.00 87.35  ? 212  ASN A CA    1 
ATOM   855  C  C     . ASN A 1 109 ? -30.760 1.118   -40.650 1.00 108.18 ? 212  ASN A C     1 
ATOM   856  O  O     . ASN A 1 109 ? -30.064 0.378   -39.949 1.00 126.93 ? 212  ASN A O     1 
ATOM   857  C  CB    . ASN A 1 109 ? -30.352 1.086   -43.120 1.00 81.75  ? 212  ASN A CB    1 
ATOM   858  C  CG    . ASN A 1 109 ? -30.064 1.908   -44.360 1.00 97.03  ? 212  ASN A CG    1 
ATOM   859  O  OD1   . ASN A 1 109 ? -30.164 3.134   -44.344 1.00 104.39 ? 212  ASN A OD1   1 
ATOM   860  N  ND2   . ASN A 1 109 ? -29.711 1.233   -45.448 1.00 101.54 ? 212  ASN A ND2   1 
ATOM   861  N  N     . HIS A 1 110 ? -32.063 1.303   -40.433 1.00 105.73 ? 213  HIS A N     1 
ATOM   862  C  CA    . HIS A 1 110 ? -32.707 0.680   -39.282 1.00 99.42  ? 213  HIS A CA    1 
ATOM   863  C  C     . HIS A 1 110 ? -32.867 -0.823  -39.467 1.00 100.74 ? 213  HIS A C     1 
ATOM   864  O  O     . HIS A 1 110 ? -32.841 -1.572  -38.484 1.00 122.38 ? 213  HIS A O     1 
ATOM   865  C  CB    . HIS A 1 110 ? -34.065 1.333   -39.024 1.00 117.46 ? 213  HIS A CB    1 
ATOM   866  C  CG    . HIS A 1 110 ? -35.108 0.987   -40.042 1.00 105.44 ? 213  HIS A CG    1 
ATOM   867  N  ND1   . HIS A 1 110 ? -35.918 -0.123  -39.930 1.00 85.64  ? 213  HIS A ND1   1 
ATOM   868  C  CD2   . HIS A 1 110 ? -35.472 1.604   -41.191 1.00 115.79 ? 213  HIS A CD2   1 
ATOM   869  C  CE1   . HIS A 1 110 ? -36.736 -0.175  -40.965 1.00 107.84 ? 213  HIS A CE1   1 
ATOM   870  N  NE2   . HIS A 1 110 ? -36.487 0.861   -41.745 1.00 107.29 ? 213  HIS A NE2   1 
ATOM   871  N  N     . ASP A 1 111 ? -33.028 -1.283  -40.706 1.00 97.44  ? 214  ASP A N     1 
ATOM   872  C  CA    . ASP A 1 111 ? -33.230 -2.703  -40.996 1.00 101.31 ? 214  ASP A CA    1 
ATOM   873  C  C     . ASP A 1 111 ? -31.927 -3.425  -41.309 1.00 116.30 ? 214  ASP A C     1 
ATOM   874  O  O     . ASP A 1 111 ? -31.872 -4.252  -42.223 1.00 148.61 ? 214  ASP A O     1 
ATOM   875  C  CB    . ASP A 1 111 ? -34.224 -2.857  -42.142 1.00 96.42  ? 214  ASP A CB    1 
ATOM   876  C  CG    . ASP A 1 111 ? -33.761 -2.172  -43.413 1.00 114.51 ? 214  ASP A CG    1 
ATOM   877  O  OD1   . ASP A 1 111 ? -32.988 -1.195  -43.317 1.00 148.48 ? 214  ASP A OD1   1 
ATOM   878  O  OD2   . ASP A 1 111 ? -34.170 -2.611  -44.509 1.00 87.93  ? 214  ASP A OD2   1 
ATOM   879  N  N     . CYS A 1 112 ? -30.863 -3.137  -40.566 1.00 116.26 ? 215  CYS A N     1 
ATOM   880  C  CA    . CYS A 1 112 ? -29.571 -3.777  -40.770 1.00 112.41 ? 215  CYS A CA    1 
ATOM   881  C  C     . CYS A 1 112 ? -29.399 -4.941  -39.805 1.00 130.52 ? 215  CYS A C     1 
ATOM   882  O  O     . CYS A 1 112 ? -29.742 -4.841  -38.623 1.00 111.68 ? 215  CYS A O     1 
ATOM   883  C  CB    . CYS A 1 112 ? -28.428 -2.778  -40.584 1.00 117.63 ? 215  CYS A CB    1 
ATOM   884  S  SG    . CYS A 1 112 ? -28.279 -1.570  -41.912 1.00 139.25 ? 215  CYS A SG    1 
ATOM   885  N  N     . VAL A 1 113 ? -28.866 -6.045  -40.319 1.00 136.60 ? 216  VAL A N     1 
ATOM   886  C  CA    . VAL A 1 113 ? -28.578 -7.224  -39.507 1.00 113.87 ? 216  VAL A CA    1 
ATOM   887  C  C     . VAL A 1 113 ? -27.370 -6.916  -38.630 1.00 121.23 ? 216  VAL A C     1 
ATOM   888  O  O     . VAL A 1 113 ? -26.572 -6.029  -38.971 1.00 122.42 ? 216  VAL A O     1 
ATOM   889  C  CB    . VAL A 1 113 ? -28.339 -8.461  -40.389 1.00 108.18 ? 216  VAL A CB    1 
ATOM   890  C  CG1   . VAL A 1 113 ? -29.580 -8.772  -41.209 1.00 110.12 ? 216  VAL A CG1   1 
ATOM   891  C  CG2   . VAL A 1 113 ? -27.138 -8.244  -41.295 1.00 122.56 ? 216  VAL A CG2   1 
ATOM   892  N  N     . PRO A 1 114 ? -27.198 -7.600  -37.495 1.00 106.36 ? 217  PRO A N     1 
ATOM   893  C  CA    . PRO A 1 114 ? -26.031 -7.320  -36.641 1.00 96.64  ? 217  PRO A CA    1 
ATOM   894  C  C     . PRO A 1 114 ? -24.695 -7.537  -37.331 1.00 113.28 ? 217  PRO A C     1 
ATOM   895  O  O     . PRO A 1 114 ? -23.688 -6.983  -36.876 1.00 116.66 ? 217  PRO A O     1 
ATOM   896  C  CB    . PRO A 1 114 ? -26.218 -8.290  -35.467 1.00 96.06  ? 217  PRO A CB    1 
ATOM   897  C  CG    . PRO A 1 114 ? -27.687 -8.530  -35.416 1.00 93.23  ? 217  PRO A CG    1 
ATOM   898  C  CD    . PRO A 1 114 ? -28.143 -8.526  -36.848 1.00 117.15 ? 217  PRO A CD    1 
ATOM   899  N  N     . GLU A 1 115 ? -24.646 -8.320  -38.411 1.00 128.16 ? 218  GLU A N     1 
ATOM   900  C  CA    . GLU A 1 115 ? -23.386 -8.500  -39.124 1.00 107.58 ? 218  GLU A CA    1 
ATOM   901  C  C     . GLU A 1 115 ? -22.990 -7.241  -39.885 1.00 114.03 ? 218  GLU A C     1 
ATOM   902  O  O     . GLU A 1 115 ? -21.796 -6.991  -40.089 1.00 124.40 ? 218  GLU A O     1 
ATOM   903  C  CB    . GLU A 1 115 ? -23.484 -9.692  -40.078 1.00 128.16 ? 218  GLU A CB    1 
ATOM   904  C  CG    . GLU A 1 115 ? -22.164 -10.077 -40.732 1.00 152.03 ? 218  GLU A CG    1 
ATOM   905  C  CD    . GLU A 1 115 ? -22.288 -11.289 -41.635 1.00 148.18 ? 218  GLU A CD    1 
ATOM   906  O  OE1   . GLU A 1 115 ? -23.421 -11.781 -41.823 1.00 132.87 ? 218  GLU A OE1   1 
ATOM   907  O  OE2   . GLU A 1 115 ? -21.251 -11.752 -42.156 1.00 147.81 ? 218  GLU A OE2   1 
ATOM   908  N  N     . GLN A 1 116 ? -23.969 -6.435  -40.302 1.00 115.16 ? 219  GLN A N     1 
ATOM   909  C  CA    . GLN A 1 116 ? -23.665 -5.219  -41.049 1.00 115.89 ? 219  GLN A CA    1 
ATOM   910  C  C     . GLN A 1 116 ? -23.183 -4.098  -40.136 1.00 111.13 ? 219  GLN A C     1 
ATOM   911  O  O     . GLN A 1 116 ? -22.305 -3.318  -40.521 1.00 115.78 ? 219  GLN A O     1 
ATOM   912  C  CB    . GLN A 1 116 ? -24.892 -4.772  -41.843 1.00 111.65 ? 219  GLN A CB    1 
ATOM   913  C  CG    . GLN A 1 116 ? -25.199 -5.647  -43.047 1.00 124.36 ? 219  GLN A CG    1 
ATOM   914  C  CD    . GLN A 1 116 ? -26.523 -5.301  -43.696 1.00 120.42 ? 219  GLN A CD    1 
ATOM   915  O  OE1   . GLN A 1 116 ? -27.510 -5.030  -43.013 1.00 127.01 ? 219  GLN A OE1   1 
ATOM   916  N  NE2   . GLN A 1 116 ? -26.550 -5.306  -45.024 1.00 135.09 ? 219  GLN A NE2   1 
ATOM   917  N  N     . VAL A 1 117 ? -23.743 -3.997  -38.927 1.00 108.29 ? 220  VAL A N     1 
ATOM   918  C  CA    . VAL A 1 117 ? -23.286 -2.968  -37.998 1.00 112.53 ? 220  VAL A CA    1 
ATOM   919  C  C     . VAL A 1 117 ? -21.913 -3.324  -37.439 1.00 126.72 ? 220  VAL A C     1 
ATOM   920  O  O     . VAL A 1 117 ? -21.124 -2.434  -37.097 1.00 141.46 ? 220  VAL A O     1 
ATOM   921  C  CB    . VAL A 1 117 ? -24.328 -2.752  -36.881 1.00 108.98 ? 220  VAL A CB    1 
ATOM   922  C  CG1   . VAL A 1 117 ? -24.520 -4.018  -36.067 1.00 120.03 ? 220  VAL A CG1   1 
ATOM   923  C  CG2   . VAL A 1 117 ? -23.927 -1.586  -35.985 1.00 101.91 ? 220  VAL A CG2   1 
ATOM   924  N  N     . ILE A 1 118 ? -21.596 -4.618  -37.347 1.00 121.55 ? 221  ILE A N     1 
ATOM   925  C  CA    . ILE A 1 118 ? -20.253 -5.022  -36.945 1.00 115.26 ? 221  ILE A CA    1 
ATOM   926  C  C     . ILE A 1 118 ? -19.237 -4.610  -38.003 1.00 110.34 ? 221  ILE A C     1 
ATOM   927  O  O     . ILE A 1 118 ? -18.167 -4.081  -37.682 1.00 127.14 ? 221  ILE A O     1 
ATOM   928  C  CB    . ILE A 1 118 ? -20.206 -6.538  -36.672 1.00 137.09 ? 221  ILE A CB    1 
ATOM   929  C  CG1   . ILE A 1 118 ? -20.935 -6.874  -35.368 1.00 124.90 ? 221  ILE A CG1   1 
ATOM   930  C  CG2   . ILE A 1 118 ? -18.767 -7.033  -36.620 1.00 117.75 ? 221  ILE A CG2   1 
ATOM   931  C  CD1   . ILE A 1 118 ? -20.309 -6.254  -34.141 1.00 139.83 ? 221  ILE A CD1   1 
ATOM   932  N  N     . ALA A 1 119 ? -19.561 -4.834  -39.280 1.00 116.35 ? 222  ALA A N     1 
ATOM   933  C  CA    . ALA A 1 119 ? -18.646 -4.461  -40.354 1.00 116.90 ? 222  ALA A CA    1 
ATOM   934  C  C     . ALA A 1 119 ? -18.453 -2.953  -40.434 1.00 127.18 ? 222  ALA A C     1 
ATOM   935  O  O     . ALA A 1 119 ? -17.384 -2.489  -40.845 1.00 162.23 ? 222  ALA A O     1 
ATOM   936  C  CB    . ALA A 1 119 ? -19.155 -5.002  -41.690 1.00 141.95 ? 222  ALA A CB    1 
ATOM   937  N  N     . GLU A 1 120 ? -19.468 -2.174  -40.053 1.00 134.54 ? 223  GLU A N     1 
ATOM   938  C  CA    . GLU A 1 120 ? -19.308 -0.725  -40.025 1.00 103.53 ? 223  GLU A CA    1 
ATOM   939  C  C     . GLU A 1 120 ? -18.425 -0.295  -38.861 1.00 122.99 ? 223  GLU A C     1 
ATOM   940  O  O     . GLU A 1 120 ? -17.626 0.640   -38.992 1.00 145.66 ? 223  GLU A O     1 
ATOM   941  C  CB    . GLU A 1 120 ? -20.674 -0.043  -39.950 1.00 96.17  ? 223  GLU A CB    1 
ATOM   942  C  CG    . GLU A 1 120 ? -20.614 1.478   -39.939 1.00 111.17 ? 223  GLU A CG    1 
ATOM   943  C  CD    . GLU A 1 120 ? -20.087 2.064   -41.239 1.00 130.12 ? 223  GLU A CD    1 
ATOM   944  O  OE1   . GLU A 1 120 ? -20.083 1.351   -42.265 1.00 92.83  ? 223  GLU A OE1   1 
ATOM   945  O  OE2   . GLU A 1 120 ? -19.677 3.243   -41.233 1.00 147.51 ? 223  GLU A OE2   1 
ATOM   946  N  N     . ALA A 1 121 ? -18.553 -0.967  -37.714 1.00 99.14  ? 224  ALA A N     1 
ATOM   947  C  CA    . ALA A 1 121 ? -17.647 -0.701  -36.602 1.00 107.79 ? 224  ALA A CA    1 
ATOM   948  C  C     . ALA A 1 121 ? -16.218 -1.103  -36.941 1.00 114.08 ? 224  ALA A C     1 
ATOM   949  O  O     . ALA A 1 121 ? -15.269 -0.534  -36.392 1.00 117.73 ? 224  ALA A O     1 
ATOM   950  C  CB    . ALA A 1 121 ? -18.124 -1.428  -35.345 1.00 103.18 ? 224  ALA A CB    1 
ATOM   951  N  N     . ILE A 1 122 ? -16.047 -2.079  -37.836 1.00 143.07 ? 225  ILE A N     1 
ATOM   952  C  CA    . ILE A 1 122 ? -14.712 -2.420  -38.317 1.00 132.41 ? 225  ILE A CA    1 
ATOM   953  C  C     . ILE A 1 122 ? -14.116 -1.254  -39.095 1.00 125.91 ? 225  ILE A C     1 
ATOM   954  O  O     . ILE A 1 122 ? -12.929 -0.937  -38.954 1.00 139.24 ? 225  ILE A O     1 
ATOM   955  C  CB    . ILE A 1 122 ? -14.761 -3.706  -39.163 1.00 130.54 ? 225  ILE A CB    1 
ATOM   956  C  CG1   . ILE A 1 122 ? -15.145 -4.905  -38.294 1.00 129.00 ? 225  ILE A CG1   1 
ATOM   957  C  CG2   . ILE A 1 122 ? -13.426 -3.952  -39.849 1.00 145.61 ? 225  ILE A CG2   1 
ATOM   958  C  CD1   . ILE A 1 122 ? -15.257 -6.204  -39.060 1.00 141.48 ? 225  ILE A CD1   1 
ATOM   959  N  N     . ARG A 1 123 ? -14.930 -0.591  -39.921 1.00 113.96 ? 226  ARG A N     1 
ATOM   960  C  CA    . ARG A 1 123 ? -14.452 0.588   -40.633 1.00 134.33 ? 226  ARG A CA    1 
ATOM   961  C  C     . ARG A 1 123 ? -14.148 1.731   -39.672 1.00 145.32 ? 226  ARG A C     1 
ATOM   962  O  O     . ARG A 1 123 ? -13.262 2.549   -39.943 1.00 139.51 ? 226  ARG A O     1 
ATOM   963  C  CB    . ARG A 1 123 ? -15.479 1.020   -41.682 1.00 117.89 ? 226  ARG A CB    1 
ATOM   964  C  CG    . ARG A 1 123 ? -14.967 2.059   -42.671 1.00 151.75 ? 226  ARG A CG    1 
ATOM   965  C  CD    . ARG A 1 123 ? -15.459 3.457   -42.328 1.00 145.61 ? 226  ARG A CD    1 
ATOM   966  N  NE    . ARG A 1 123 ? -16.891 3.604   -42.560 1.00 127.77 ? 226  ARG A NE    1 
ATOM   967  C  CZ    . ARG A 1 123 ? -17.427 3.963   -43.719 1.00 153.53 ? 226  ARG A CZ    1 
ATOM   968  N  NH1   . ARG A 1 123 ? -16.677 4.220   -44.778 1.00 125.69 ? 226  ARG A NH1   1 
ATOM   969  N  NH2   . ARG A 1 123 ? -18.750 4.065   -43.817 1.00 155.40 ? 226  ARG A NH2   1 
ATOM   970  N  N     . LYS A 1 124 ? -14.863 1.800   -38.546 1.00 142.99 ? 227  LYS A N     1 
ATOM   971  C  CA    . LYS A 1 124 ? -14.579 2.798   -37.521 1.00 157.79 ? 227  LYS A CA    1 
ATOM   972  C  C     . LYS A 1 124 ? -13.322 2.481   -36.722 1.00 140.42 ? 227  LYS A C     1 
ATOM   973  O  O     . LYS A 1 124 ? -12.898 3.314   -35.913 1.00 161.74 ? 227  LYS A O     1 
ATOM   974  C  CB    . LYS A 1 124 ? -15.772 2.931   -36.572 1.00 128.05 ? 227  LYS A CB    1 
ATOM   975  C  CG    . LYS A 1 124 ? -16.848 3.890   -37.052 1.00 120.81 ? 227  LYS A CG    1 
ATOM   976  C  CD    . LYS A 1 124 ? -16.351 5.326   -37.023 1.00 126.42 ? 227  LYS A CD    1 
ATOM   977  C  CE    . LYS A 1 124 ? -17.447 6.301   -37.420 1.00 150.55 ? 227  LYS A CE    1 
ATOM   978  N  NZ    . LYS A 1 124 ? -17.001 7.718   -37.306 1.00 144.43 ? 227  LYS A NZ    1 
ATOM   979  N  N     . LYS A 1 125 ? -12.723 1.307   -36.922 1.00 128.17 ? 228  LYS A N     1 
ATOM   980  C  CA    . LYS A 1 125 ? -11.494 0.931   -36.241 1.00 144.18 ? 228  LYS A CA    1 
ATOM   981  C  C     . LYS A 1 125 ? -10.293 0.839   -37.170 1.00 134.59 ? 228  LYS A C     1 
ATOM   982  O  O     . LYS A 1 125 ? -9.175  0.634   -36.686 1.00 115.07 ? 228  LYS A O     1 
ATOM   983  C  CB    . LYS A 1 125 ? -11.673 -0.416  -35.523 1.00 148.49 ? 228  LYS A CB    1 
ATOM   984  C  CG    . LYS A 1 125 ? -12.702 -0.397  -34.407 1.00 165.66 ? 228  LYS A CG    1 
ATOM   985  C  CD    . LYS A 1 125 ? -12.236 0.455   -33.241 1.00 187.48 ? 228  LYS A CD    1 
ATOM   986  C  CE    . LYS A 1 125 ? -10.971 -0.109  -32.614 1.00 186.99 ? 228  LYS A CE    1 
ATOM   987  N  NZ    . LYS A 1 125 ? -10.526 0.694   -31.442 1.00 156.86 ? 228  LYS A NZ    1 
ATOM   988  N  N     . THR A 1 126 ? -10.488 0.985   -38.479 1.00 157.30 ? 229  THR A N     1 
ATOM   989  C  CA    . THR A 1 126 ? -9.414  0.822   -39.451 1.00 146.80 ? 229  THR A CA    1 
ATOM   990  C  C     . THR A 1 126 ? -9.202  2.059   -40.309 1.00 162.32 ? 229  THR A C     1 
ATOM   991  O  O     . THR A 1 126 ? -8.055  2.485   -40.494 1.00 182.58 ? 229  THR A O     1 
ATOM   992  C  CB    . THR A 1 126 ? -9.699  -0.393  -40.351 1.00 158.46 ? 229  THR A CB    1 
ATOM   993  O  OG1   . THR A 1 126 ? -10.941 -0.201  -41.038 1.00 167.72 ? 229  THR A OG1   1 
ATOM   994  C  CG2   . THR A 1 126 ? -9.773  -1.668  -39.523 1.00 115.94 ? 229  THR A CG2   1 
ATOM   995  N  N     . ARG A 1 127 ? -10.277 2.646   -40.839 1.00 190.19 ? 230  ARG A N     1 
ATOM   996  C  CA    . ARG A 1 127 ? -10.218 3.807   -41.735 1.00 189.94 ? 230  ARG A CA    1 
ATOM   997  C  C     . ARG A 1 127 ? -9.403  3.405   -42.959 1.00 181.62 ? 230  ARG A C     1 
ATOM   998  O  O     . ARG A 1 127 ? -9.856  2.526   -43.711 1.00 212.38 ? 230  ARG A O     1 
ATOM   999  C  CB    . ARG A 1 127 ? -9.704  5.022   -40.959 1.00 172.67 ? 230  ARG A CB    1 
ATOM   1000 C  CG    . ARG A 1 127 ? -10.469 5.310   -39.680 1.00 179.46 ? 230  ARG A CG    1 
ATOM   1001 C  CD    . ARG A 1 127 ? -10.162 6.705   -39.169 1.00 183.87 ? 230  ARG A CD    1 
ATOM   1002 N  NE    . ARG A 1 127 ? -10.648 7.731   -40.085 1.00 165.35 ? 230  ARG A NE    1 
ATOM   1003 C  CZ    . ARG A 1 127 ? -10.455 9.032   -39.922 1.00 179.01 ? 230  ARG A CZ    1 
ATOM   1004 N  NH1   . ARG A 1 127 ? -9.775  9.506   -38.891 1.00 194.15 ? 230  ARG A NH1   1 
ATOM   1005 N  NH2   . ARG A 1 127 ? -10.955 9.880   -40.817 1.00 155.19 ? 230  ARG A NH2   1 
ATOM   1006 N  N     . SER A 1 128 ? -8.239  3.999   -43.209 1.00 144.32 ? 231  SER A N     1 
ATOM   1007 C  CA    . SER A 1 128 ? -7.337  3.584   -44.283 1.00 163.54 ? 231  SER A CA    1 
ATOM   1008 C  C     . SER A 1 128 ? -6.010  3.226   -43.619 1.00 173.45 ? 231  SER A C     1 
ATOM   1009 O  O     . SER A 1 128 ? -5.132  4.077   -43.460 1.00 147.03 ? 231  SER A O     1 
ATOM   1010 C  CB    . SER A 1 128 ? -7.173  4.679   -45.338 1.00 144.94 ? 231  SER A CB    1 
ATOM   1011 O  OG    . SER A 1 128 ? -6.582  5.840   -44.784 1.00 157.01 ? 231  SER A OG    1 
ATOM   1012 N  N     . MET A 1 129 ? -5.871  1.959   -43.231 1.00 163.65 ? 232  MET A N     1 
ATOM   1013 C  CA    . MET A 1 129 ? -4.788  1.482   -42.390 1.00 155.76 ? 232  MET A CA    1 
ATOM   1014 C  C     . MET A 1 129 ? -3.820  0.634   -43.225 1.00 186.41 ? 232  MET A C     1 
ATOM   1015 O  O     . MET A 1 129 ? -3.676  0.870   -44.438 1.00 167.37 ? 232  MET A O     1 
ATOM   1016 C  CB    . MET A 1 129 ? -5.390  0.743   -41.195 1.00 148.87 ? 232  MET A CB    1 
ATOM   1017 C  CG    . MET A 1 129 ? -4.484  0.660   -39.972 1.00 182.80 ? 232  MET A CG    1 
ATOM   1018 S  SD    . MET A 1 129 ? -5.253  -0.196  -38.585 1.00 175.13 ? 232  MET A SD    1 
ATOM   1019 C  CE    . MET A 1 129 ? -6.164  1.144   -37.827 1.00 129.70 ? 232  MET A CE    1 
ATOM   1020 N  N     . LEU A 1 130 ? -3.168  -0.336  -42.589 1.00 212.52 ? 233  LEU A N     1 
ATOM   1021 C  CA    . LEU A 1 130 ? -2.104  -1.122  -43.198 1.00 194.42 ? 233  LEU A CA    1 
ATOM   1022 C  C     . LEU A 1 130 ? -2.658  -2.421  -43.762 1.00 200.48 ? 233  LEU A C     1 
ATOM   1023 O  O     . LEU A 1 130 ? -3.410  -3.129  -43.084 1.00 197.74 ? 233  LEU A O     1 
ATOM   1024 C  CB    . LEU A 1 130 ? -1.009  -1.422  -42.173 1.00 193.25 ? 233  LEU A CB    1 
ATOM   1025 C  CG    . LEU A 1 130 ? 0.072   -2.450  -42.520 1.00 210.00 ? 233  LEU A CG    1 
ATOM   1026 C  CD1   . LEU A 1 130 ? 0.736   -2.146  -43.855 1.00 203.09 ? 233  LEU A CD1   1 
ATOM   1027 C  CD2   . LEU A 1 130 ? 1.108   -2.495  -41.411 1.00 177.37 ? 233  LEU A CD2   1 
ATOM   1028 N  N     . LEU A 1 131 ? -2.271  -2.733  -44.997 1.00 220.34 ? 234  LEU A N     1 
ATOM   1029 C  CA    . LEU A 1 131 ? -2.655  -3.987  -45.639 1.00 223.10 ? 234  LEU A CA    1 
ATOM   1030 C  C     . LEU A 1 131 ? -1.609  -4.318  -46.693 1.00 231.50 ? 234  LEU A C     1 
ATOM   1031 O  O     . LEU A 1 131 ? -1.501  -3.615  -47.702 1.00 228.49 ? 234  LEU A O     1 
ATOM   1032 C  CB    . LEU A 1 131 ? -4.044  -3.888  -46.261 1.00 207.84 ? 234  LEU A CB    1 
ATOM   1033 C  CG    . LEU A 1 131 ? -5.246  -4.254  -45.393 1.00 224.01 ? 234  LEU A CG    1 
ATOM   1034 C  CD1   . LEU A 1 131 ? -6.534  -4.065  -46.167 1.00 226.45 ? 234  LEU A CD1   1 
ATOM   1035 C  CD2   . LEU A 1 131 ? -5.116  -5.684  -44.914 1.00 209.06 ? 234  LEU A CD2   1 
ATOM   1036 N  N     . SER A 1 132 ? -0.836  -5.372  -46.455 1.00 208.88 ? 235  SER A N     1 
ATOM   1037 C  CA    . SER A 1 132 ? 0.047   -5.914  -47.474 1.00 182.87 ? 235  SER A CA    1 
ATOM   1038 C  C     . SER A 1 132 ? -0.685  -6.995  -48.262 1.00 190.27 ? 235  SER A C     1 
ATOM   1039 O  O     . SER A 1 132 ? -1.728  -7.503  -47.845 1.00 201.01 ? 235  SER A O     1 
ATOM   1040 C  CB    . SER A 1 132 ? 1.321   -6.485  -46.849 1.00 191.48 ? 235  SER A CB    1 
ATOM   1041 O  OG    . SER A 1 132 ? 2.068   -5.475  -46.193 1.00 158.91 ? 235  SER A OG    1 
ATOM   1042 N  N     . SER A 1 133 ? -0.118  -7.351  -49.415 1.00 190.50 ? 236  SER A N     1 
ATOM   1043 C  CA    . SER A 1 133 ? -0.758  -8.339  -50.277 1.00 182.48 ? 236  SER A CA    1 
ATOM   1044 C  C     . SER A 1 133 ? -0.743  -9.746  -49.691 1.00 183.61 ? 236  SER A C     1 
ATOM   1045 O  O     . SER A 1 133 ? -1.201  -10.678 -50.361 1.00 205.56 ? 236  SER A O     1 
ATOM   1046 C  CB    . SER A 1 133 ? -0.098  -8.342  -51.654 1.00 173.29 ? 236  SER A CB    1 
ATOM   1047 O  OG    . SER A 1 133 ? -0.714  -9.291  -52.505 1.00 202.17 ? 236  SER A OG    1 
ATOM   1048 N  N     . GLU A 1 134 ? -0.222  -9.927  -48.478 1.00 174.04 ? 237  GLU A N     1 
ATOM   1049 C  CA    . GLU A 1 134 ? -0.352  -11.177 -47.743 1.00 179.00 ? 237  GLU A CA    1 
ATOM   1050 C  C     . GLU A 1 134 ? -1.176  -11.010 -46.473 1.00 170.35 ? 237  GLU A C     1 
ATOM   1051 O  O     . GLU A 1 134 ? -1.251  -11.941 -45.666 1.00 169.55 ? 237  GLU A O     1 
ATOM   1052 C  CB    . GLU A 1 134 ? 1.027   -11.748 -47.399 1.00 166.18 ? 237  GLU A CB    1 
ATOM   1053 C  CG    . GLU A 1 134 ? 1.840   -12.217 -48.596 1.00 174.97 ? 237  GLU A CG    1 
ATOM   1054 C  CD    . GLU A 1 134 ? 2.659   -11.105 -49.223 1.00 213.98 ? 237  GLU A CD    1 
ATOM   1055 O  OE1   . GLU A 1 134 ? 2.530   -9.944  -48.782 1.00 209.08 ? 237  GLU A OE1   1 
ATOM   1056 O  OE2   . GLU A 1 134 ? 3.439   -11.396 -50.154 1.00 185.59 ? 237  GLU A OE2   1 
ATOM   1057 N  N     . GLN A 1 135 ? -1.796  -9.846  -46.277 1.00 185.11 ? 238  GLN A N     1 
ATOM   1058 C  CA    . GLN A 1 135 ? -2.561  -9.555  -45.072 1.00 184.90 ? 238  GLN A CA    1 
ATOM   1059 C  C     . GLN A 1 135 ? -4.058  -9.450  -45.343 1.00 198.61 ? 238  GLN A C     1 
ATOM   1060 O  O     . GLN A 1 135 ? -4.784  -8.838  -44.554 1.00 185.66 ? 238  GLN A O     1 
ATOM   1061 C  CB    . GLN A 1 135 ? -2.052  -8.269  -44.420 1.00 169.94 ? 238  GLN A CB    1 
ATOM   1062 C  CG    . GLN A 1 135 ? -0.596  -8.326  -43.990 1.00 132.77 ? 238  GLN A CG    1 
ATOM   1063 C  CD    . GLN A 1 135 ? -0.124  -7.029  -43.363 1.00 162.32 ? 238  GLN A CD    1 
ATOM   1064 O  OE1   . GLN A 1 135 ? -0.104  -5.982  -44.010 1.00 166.16 ? 238  GLN A OE1   1 
ATOM   1065 N  NE2   . GLN A 1 135 ? 0.255   -7.091  -42.093 1.00 147.35 ? 238  GLN A NE2   1 
ATOM   1066 N  N     . LEU A 1 136 ? -4.536  -10.032 -46.443 1.00 212.27 ? 239  LEU A N     1 
ATOM   1067 C  CA    . LEU A 1 136 ? -5.959  -9.998  -46.758 1.00 197.16 ? 239  LEU A CA    1 
ATOM   1068 C  C     . LEU A 1 136 ? -6.753  -10.765 -45.709 1.00 217.92 ? 239  LEU A C     1 
ATOM   1069 O  O     . LEU A 1 136 ? -7.483  -10.164 -44.915 1.00 221.55 ? 239  LEU A O     1 
ATOM   1070 C  CB    . LEU A 1 136 ? -6.229  -10.571 -48.152 1.00 197.40 ? 239  LEU A CB    1 
ATOM   1071 C  CG    . LEU A 1 136 ? -5.694  -9.790  -49.355 1.00 196.12 ? 239  LEU A CG    1 
ATOM   1072 C  CD1   . LEU A 1 136 ? -4.263  -10.185 -49.671 1.00 215.94 ? 239  LEU A CD1   1 
ATOM   1073 C  CD2   . LEU A 1 136 ? -6.586  -9.986  -50.571 1.00 187.49 ? 239  LEU A CD2   1 
ATOM   1074 N  N     . LYS A 1 137 ? -6.599  -12.093 -45.687 1.00 222.14 ? 240  LYS A N     1 
ATOM   1075 C  CA    . LYS A 1 137 ? -7.319  -12.917 -44.722 1.00 223.50 ? 240  LYS A CA    1 
ATOM   1076 C  C     . LYS A 1 137 ? -6.983  -12.553 -43.281 1.00 208.33 ? 240  LYS A C     1 
ATOM   1077 O  O     . LYS A 1 137 ? -7.730  -12.925 -42.370 1.00 220.85 ? 240  LYS A O     1 
ATOM   1078 C  CB    . LYS A 1 137 ? -7.027  -14.400 -44.968 1.00 224.91 ? 240  LYS A CB    1 
ATOM   1079 C  CG    . LYS A 1 137 ? -7.986  -15.083 -45.938 1.00 226.27 ? 240  LYS A CG    1 
ATOM   1080 C  CD    . LYS A 1 137 ? -7.887  -14.505 -47.342 1.00 234.38 ? 240  LYS A CD    1 
ATOM   1081 C  CE    . LYS A 1 137 ? -8.886  -15.161 -48.282 1.00 230.39 ? 240  LYS A CE    1 
ATOM   1082 N  NZ    . LYS A 1 137 ? -8.821  -14.581 -49.652 1.00 205.74 ? 240  LYS A NZ    1 
ATOM   1083 N  N     . LEU A 1 138 ? -5.876  -11.840 -43.055 1.00 168.59 ? 241  LEU A N     1 
ATOM   1084 C  CA    . LEU A 1 138 ? -5.587  -11.326 -41.721 1.00 158.22 ? 241  LEU A CA    1 
ATOM   1085 C  C     . LEU A 1 138 ? -6.637  -10.315 -41.281 1.00 175.12 ? 241  LEU A C     1 
ATOM   1086 O  O     . LEU A 1 138 ? -6.963  -10.236 -40.091 1.00 169.98 ? 241  LEU A O     1 
ATOM   1087 C  CB    . LEU A 1 138 ? -4.187  -10.703 -41.698 1.00 192.49 ? 241  LEU A CB    1 
ATOM   1088 C  CG    . LEU A 1 138 ? -3.555  -10.273 -40.368 1.00 178.24 ? 241  LEU A CG    1 
ATOM   1089 C  CD1   . LEU A 1 138 ? -3.936  -8.845  -39.987 1.00 176.66 ? 241  LEU A CD1   1 
ATOM   1090 C  CD2   . LEU A 1 138 ? -3.924  -11.244 -39.258 1.00 134.28 ? 241  LEU A CD2   1 
ATOM   1091 N  N     . CYS A 1 139 ? -7.179  -9.538  -42.221 1.00 190.43 ? 242  CYS A N     1 
ATOM   1092 C  CA    . CYS A 1 139 ? -8.215  -8.561  -41.920 1.00 170.50 ? 242  CYS A CA    1 
ATOM   1093 C  C     . CYS A 1 139 ? -9.591  -8.944  -42.445 1.00 170.15 ? 242  CYS A C     1 
ATOM   1094 O  O     . CYS A 1 139 ? -10.589 -8.410  -41.952 1.00 191.24 ? 242  CYS A O     1 
ATOM   1095 C  CB    . CYS A 1 139 ? -7.832  -7.184  -42.483 1.00 173.48 ? 242  CYS A CB    1 
ATOM   1096 S  SG    . CYS A 1 139 ? -6.368  -6.455  -41.711 1.00 152.05 ? 242  CYS A SG    1 
ATOM   1097 N  N     . VAL A 1 140 ? -9.671  -9.844  -43.429 1.00 158.63 ? 243  VAL A N     1 
ATOM   1098 C  CA    . VAL A 1 140 ? -10.973 -10.333 -43.870 1.00 167.79 ? 243  VAL A CA    1 
ATOM   1099 C  C     . VAL A 1 140 ? -11.597 -11.216 -42.798 1.00 171.09 ? 243  VAL A C     1 
ATOM   1100 O  O     . VAL A 1 140 ? -12.827 -11.289 -42.678 1.00 181.84 ? 243  VAL A O     1 
ATOM   1101 C  CB    . VAL A 1 140 ? -10.839 -11.072 -45.215 1.00 162.07 ? 243  VAL A CB    1 
ATOM   1102 C  CG1   . VAL A 1 140 ? -12.182 -11.628 -45.668 1.00 181.74 ? 243  VAL A CG1   1 
ATOM   1103 C  CG2   . VAL A 1 140 ? -10.284 -10.137 -46.265 1.00 133.63 ? 243  VAL A CG2   1 
ATOM   1104 N  N     . LEU A 1 141 ? -10.768 -11.883 -41.990 1.00 160.72 ? 244  LEU A N     1 
ATOM   1105 C  CA    . LEU A 1 141 ? -11.280 -12.682 -40.883 1.00 178.06 ? 244  LEU A CA    1 
ATOM   1106 C  C     . LEU A 1 141 ? -12.055 -11.838 -39.879 1.00 165.25 ? 244  LEU A C     1 
ATOM   1107 O  O     . LEU A 1 141 ? -12.870 -12.381 -39.126 1.00 169.47 ? 244  LEU A O     1 
ATOM   1108 C  CB    . LEU A 1 141 ? -10.127 -13.409 -40.188 1.00 158.22 ? 244  LEU A CB    1 
ATOM   1109 C  CG    . LEU A 1 141 ? -10.489 -14.569 -39.260 1.00 145.79 ? 244  LEU A CG    1 
ATOM   1110 C  CD1   . LEU A 1 141 ? -11.241 -15.648 -40.023 1.00 169.28 ? 244  LEU A CD1   1 
ATOM   1111 C  CD2   . LEU A 1 141 ? -9.240  -15.141 -38.608 1.00 138.09 ? 244  LEU A CD2   1 
ATOM   1112 N  N     . GLU A 1 142 ? -11.819 -10.523 -39.854 1.00 155.72 ? 245  GLU A N     1 
ATOM   1113 C  CA    . GLU A 1 142 ? -12.622 -9.641  -39.014 1.00 166.28 ? 245  GLU A CA    1 
ATOM   1114 C  C     . GLU A 1 142 ? -14.069 -9.599  -39.489 1.00 153.57 ? 245  GLU A C     1 
ATOM   1115 O  O     . GLU A 1 142 ? -14.995 -9.520  -38.673 1.00 136.24 ? 245  GLU A O     1 
ATOM   1116 C  CB    . GLU A 1 142 ? -12.022 -8.235  -39.007 1.00 167.52 ? 245  GLU A CB    1 
ATOM   1117 C  CG    . GLU A 1 142 ? -10.542 -8.184  -38.663 1.00 154.32 ? 245  GLU A CG    1 
ATOM   1118 C  CD    . GLU A 1 142 ? -10.270 -8.462  -37.199 1.00 165.41 ? 245  GLU A CD    1 
ATOM   1119 O  OE1   . GLU A 1 142 ? -11.169 -8.215  -36.369 1.00 166.08 ? 245  GLU A OE1   1 
ATOM   1120 O  OE2   . GLU A 1 142 ? -9.157  -8.929  -36.878 1.00 185.01 ? 245  GLU A OE2   1 
ATOM   1121 N  N     . TYR A 1 143 ? -14.283 -9.651  -40.805 1.00 172.28 ? 246  TYR A N     1 
ATOM   1122 C  CA    . TYR A 1 143 ? -15.625 -9.617  -41.370 1.00 167.83 ? 246  TYR A CA    1 
ATOM   1123 C  C     . TYR A 1 143 ? -16.340 -10.959 -41.288 1.00 172.60 ? 246  TYR A C     1 
ATOM   1124 O  O     . TYR A 1 143 ? -17.529 -11.028 -41.617 1.00 193.37 ? 246  TYR A O     1 
ATOM   1125 C  CB    . TYR A 1 143 ? -15.571 -9.158  -42.830 1.00 173.70 ? 246  TYR A CB    1 
ATOM   1126 C  CG    . TYR A 1 143 ? -14.942 -7.797  -43.026 1.00 167.83 ? 246  TYR A CG    1 
ATOM   1127 C  CD1   . TYR A 1 143 ? -15.683 -6.636  -42.846 1.00 160.44 ? 246  TYR A CD1   1 
ATOM   1128 C  CD2   . TYR A 1 143 ? -13.609 -7.673  -43.395 1.00 167.84 ? 246  TYR A CD2   1 
ATOM   1129 C  CE1   . TYR A 1 143 ? -15.112 -5.389  -43.026 1.00 169.39 ? 246  TYR A CE1   1 
ATOM   1130 C  CE2   . TYR A 1 143 ? -13.030 -6.431  -43.577 1.00 164.02 ? 246  TYR A CE2   1 
ATOM   1131 C  CZ    . TYR A 1 143 ? -13.786 -5.293  -43.392 1.00 167.27 ? 246  TYR A CZ    1 
ATOM   1132 O  OH    . TYR A 1 143 ? -13.214 -4.054  -43.572 1.00 165.42 ? 246  TYR A OH    1 
ATOM   1133 N  N     . GLN A 1 144 ? -15.654 -12.018 -40.867 1.00 157.00 ? 247  GLN A N     1 
ATOM   1134 C  CA    . GLN A 1 144 ? -16.273 -13.329 -40.729 1.00 159.40 ? 247  GLN A CA    1 
ATOM   1135 C  C     . GLN A 1 144 ? -16.996 -13.405 -39.385 1.00 153.55 ? 247  GLN A C     1 
ATOM   1136 O  O     . GLN A 1 144 ? -17.184 -12.401 -38.693 1.00 177.06 ? 247  GLN A O     1 
ATOM   1137 C  CB    . GLN A 1 144 ? -15.222 -14.427 -40.880 1.00 167.92 ? 247  GLN A CB    1 
ATOM   1138 C  CG    . GLN A 1 144 ? -14.338 -14.284 -42.111 1.00 170.84 ? 247  GLN A CG    1 
ATOM   1139 C  CD    . GLN A 1 144 ? -15.099 -14.463 -43.411 1.00 192.70 ? 247  GLN A CD    1 
ATOM   1140 O  OE1   . GLN A 1 144 ? -14.757 -13.863 -44.430 1.00 186.38 ? 247  GLN A OE1   1 
ATOM   1141 N  NE2   . GLN A 1 144 ? -16.130 -15.299 -43.384 1.00 194.13 ? 247  GLN A NE2   1 
ATOM   1142 N  N     . GLY A 1 145 ? -17.416 -14.607 -38.998 1.00 128.82 ? 248  GLY A N     1 
ATOM   1143 C  CA    . GLY A 1 145 ? -18.053 -14.793 -37.710 1.00 137.95 ? 248  GLY A CA    1 
ATOM   1144 C  C     . GLY A 1 145 ? -17.059 -14.726 -36.570 1.00 156.90 ? 248  GLY A C     1 
ATOM   1145 O  O     . GLY A 1 145 ? -16.482 -15.746 -36.181 1.00 203.83 ? 248  GLY A O     1 
ATOM   1146 N  N     . LYS A 1 146 ? -16.851 -13.529 -36.022 1.00 125.19 ? 249  LYS A N     1 
ATOM   1147 C  CA    . LYS A 1 146 ? -15.815 -13.336 -35.016 1.00 152.91 ? 249  LYS A CA    1 
ATOM   1148 C  C     . LYS A 1 146 ? -16.320 -12.526 -33.828 1.00 153.92 ? 249  LYS A C     1 
ATOM   1149 O  O     . LYS A 1 146 ? -15.898 -12.761 -32.690 1.00 135.27 ? 249  LYS A O     1 
ATOM   1150 C  CB    . LYS A 1 146 ? -14.595 -12.655 -35.642 1.00 138.65 ? 249  LYS A CB    1 
ATOM   1151 C  CG    . LYS A 1 146 ? -13.415 -12.490 -34.698 1.00 141.97 ? 249  LYS A CG    1 
ATOM   1152 C  CD    . LYS A 1 146 ? -12.237 -11.831 -35.398 1.00 133.30 ? 249  LYS A CD    1 
ATOM   1153 C  CE    . LYS A 1 146 ? -11.067 -11.645 -34.446 1.00 139.08 ? 249  LYS A CE    1 
ATOM   1154 N  NZ    . LYS A 1 146 ? -9.907  -10.995 -35.116 1.00 113.65 ? 249  LYS A NZ    1 
ATOM   1155 N  N     . TYR A 1 147 ? -17.220 -11.578 -34.072 1.00 144.67 ? 250  TYR A N     1 
ATOM   1156 C  CA    . TYR A 1 147 ? -17.703 -10.679 -33.036 1.00 127.91 ? 250  TYR A CA    1 
ATOM   1157 C  C     . TYR A 1 147 ? -19.219 -10.761 -32.916 1.00 117.20 ? 250  TYR A C     1 
ATOM   1158 O  O     . TYR A 1 147 ? -19.919 -11.107 -33.872 1.00 136.73 ? 250  TYR A O     1 
ATOM   1159 C  CB    . TYR A 1 147 ? -17.291 -9.229  -33.321 1.00 132.67 ? 250  TYR A CB    1 
ATOM   1160 C  CG    . TYR A 1 147 ? -15.796 -9.019  -33.410 1.00 142.52 ? 250  TYR A CG    1 
ATOM   1161 C  CD1   . TYR A 1 147 ? -15.018 -8.932  -32.262 1.00 127.98 ? 250  TYR A CD1   1 
ATOM   1162 C  CD2   . TYR A 1 147 ? -15.165 -8.899  -34.640 1.00 154.45 ? 250  TYR A CD2   1 
ATOM   1163 C  CE1   . TYR A 1 147 ? -13.652 -8.736  -32.339 1.00 133.30 ? 250  TYR A CE1   1 
ATOM   1164 C  CE2   . TYR A 1 147 ? -13.801 -8.703  -34.727 1.00 161.27 ? 250  TYR A CE2   1 
ATOM   1165 C  CZ    . TYR A 1 147 ? -13.049 -8.623  -33.574 1.00 151.79 ? 250  TYR A CZ    1 
ATOM   1166 O  OH    . TYR A 1 147 ? -11.690 -8.428  -33.657 1.00 168.68 ? 250  TYR A OH    1 
ATOM   1167 N  N     . ILE A 1 148 ? -19.717 -10.434 -31.724 1.00 107.85 ? 251  ILE A N     1 
ATOM   1168 C  CA    . ILE A 1 148 ? -21.150 -10.373 -31.465 1.00 124.40 ? 251  ILE A CA    1 
ATOM   1169 C  C     . ILE A 1 148 ? -21.513 -8.956  -31.042 1.00 132.50 ? 251  ILE A C     1 
ATOM   1170 O  O     . ILE A 1 148 ? -20.710 -8.028  -31.189 1.00 157.05 ? 251  ILE A O     1 
ATOM   1171 C  CB    . ILE A 1 148 ? -21.574 -11.395 -30.393 1.00 109.81 ? 251  ILE A CB    1 
ATOM   1172 C  CG1   . ILE A 1 148 ? -20.866 -11.104 -29.069 1.00 111.57 ? 251  ILE A CG1   1 
ATOM   1173 C  CG2   . ILE A 1 148 ? -21.284 -12.812 -30.862 1.00 124.61 ? 251  ILE A CG2   1 
ATOM   1174 C  CD1   . ILE A 1 148 ? -21.315 -11.991 -27.931 1.00 99.27  ? 251  ILE A CD1   1 
ATOM   1175 N  N     . LEU A 1 149 ? -22.722 -8.780  -30.511 1.00 140.91 ? 252  LEU A N     1 
ATOM   1176 C  CA    . LEU A 1 149 ? -23.185 -7.476  -30.063 1.00 126.12 ? 252  LEU A CA    1 
ATOM   1177 C  C     . LEU A 1 149 ? -24.015 -7.647  -28.799 1.00 112.28 ? 252  LEU A C     1 
ATOM   1178 O  O     . LEU A 1 149 ? -24.707 -8.653  -28.625 1.00 140.71 ? 252  LEU A O     1 
ATOM   1179 C  CB    . LEU A 1 149 ? -24.001 -6.768  -31.152 1.00 100.25 ? 252  LEU A CB    1 
ATOM   1180 C  CG    . LEU A 1 149 ? -23.842 -5.250  -31.224 1.00 102.74 ? 252  LEU A CG    1 
ATOM   1181 C  CD1   . LEU A 1 149 ? -22.370 -4.873  -31.244 1.00 123.13 ? 252  LEU A CD1   1 
ATOM   1182 C  CD2   . LEU A 1 149 ? -24.546 -4.709  -32.453 1.00 109.90 ? 252  LEU A CD2   1 
ATOM   1183 N  N     . LYS A 1 150 ? -23.940 -6.652  -27.917 1.00 107.49 ? 253  LYS A N     1 
ATOM   1184 C  CA    . LYS A 1 150 ? -24.568 -6.744  -26.606 1.00 103.93 ? 253  LYS A CA    1 
ATOM   1185 C  C     . LYS A 1 150 ? -25.083 -5.375  -26.186 1.00 110.30 ? 253  LYS A C     1 
ATOM   1186 O  O     . LYS A 1 150 ? -24.443 -4.354  -26.453 1.00 129.31 ? 253  LYS A O     1 
ATOM   1187 C  CB    . LYS A 1 150 ? -23.580 -7.281  -25.562 1.00 115.27 ? 253  LYS A CB    1 
ATOM   1188 C  CG    . LYS A 1 150 ? -24.101 -7.282  -24.134 1.00 95.30  ? 253  LYS A CG    1 
ATOM   1189 C  CD    . LYS A 1 150 ? -23.010 -7.677  -23.154 1.00 91.23  ? 253  LYS A CD    1 
ATOM   1190 C  CE    . LYS A 1 150 ? -23.492 -7.569  -21.717 1.00 127.96 ? 253  LYS A CE    1 
ATOM   1191 N  NZ    . LYS A 1 150 ? -23.948 -6.190  -21.386 1.00 126.59 ? 253  LYS A NZ    1 
ATOM   1192 N  N     . VAL A 1 151 ? -26.244 -5.363  -25.527 1.00 101.16 ? 254  VAL A N     1 
ATOM   1193 C  CA    . VAL A 1 151 ? -26.797 -4.126  -24.992 1.00 118.36 ? 254  VAL A CA    1 
ATOM   1194 C  C     . VAL A 1 151 ? -25.974 -3.679  -23.790 1.00 106.68 ? 254  VAL A C     1 
ATOM   1195 O  O     . VAL A 1 151 ? -25.588 -4.492  -22.939 1.00 115.17 ? 254  VAL A O     1 
ATOM   1196 C  CB    . VAL A 1 151 ? -28.276 -4.319  -24.612 1.00 111.53 ? 254  VAL A CB    1 
ATOM   1197 C  CG1   . VAL A 1 151 ? -28.874 -3.017  -24.100 1.00 123.89 ? 254  VAL A CG1   1 
ATOM   1198 C  CG2   . VAL A 1 151 ? -29.067 -4.842  -25.799 1.00 87.99  ? 254  VAL A CG2   1 
ATOM   1199 N  N     . CYS A 1 152 ? -25.697 -2.380  -23.716 1.00 113.22 ? 255  CYS A N     1 
ATOM   1200 C  CA    . CYS A 1 152 ? -24.934 -1.824  -22.606 1.00 124.95 ? 255  CYS A CA    1 
ATOM   1201 C  C     . CYS A 1 152 ? -25.829 -1.707  -21.378 1.00 119.51 ? 255  CYS A C     1 
ATOM   1202 O  O     . CYS A 1 152 ? -26.795 -0.937  -21.380 1.00 134.07 ? 255  CYS A O     1 
ATOM   1203 C  CB    . CYS A 1 152 ? -24.362 -0.460  -22.986 1.00 123.67 ? 255  CYS A CB    1 
ATOM   1204 S  SG    . CYS A 1 152 ? -23.192 -0.490  -24.366 1.00 105.04 ? 255  CYS A SG    1 
ATOM   1205 N  N     . GLY A 1 153 ? -25.513 -2.469  -20.335 1.00 121.13 ? 256  GLY A N     1 
ATOM   1206 C  CA    . GLY A 1 153 ? -26.281 -2.414  -19.107 1.00 128.00 ? 256  GLY A CA    1 
ATOM   1207 C  C     . GLY A 1 153 ? -27.066 -3.680  -18.834 1.00 147.23 ? 256  GLY A C     1 
ATOM   1208 O  O     . GLY A 1 153 ? -27.180 -4.104  -17.681 1.00 143.33 ? 256  GLY A O     1 
ATOM   1209 N  N     . CYS A 1 154 ? -27.609 -4.294  -19.883 1.00 130.22 ? 257  CYS A N     1 
ATOM   1210 C  CA    . CYS A 1 154 ? -28.395 -5.511  -19.762 1.00 125.78 ? 257  CYS A CA    1 
ATOM   1211 C  C     . CYS A 1 154 ? -27.581 -6.713  -20.233 1.00 140.77 ? 257  CYS A C     1 
ATOM   1212 O  O     . CYS A 1 154 ? -26.414 -6.602  -20.616 1.00 111.86 ? 257  CYS A O     1 
ATOM   1213 C  CB    . CYS A 1 154 ? -29.699 -5.390  -20.554 1.00 120.59 ? 257  CYS A CB    1 
ATOM   1214 S  SG    . CYS A 1 154 ? -31.041 -4.570  -19.668 1.00 169.65 ? 257  CYS A SG    1 
ATOM   1215 N  N     . ASP A 1 155 ? -28.219 -7.884  -20.202 1.00 149.67 ? 258  ASP A N     1 
ATOM   1216 C  CA    . ASP A 1 155 ? -27.607 -9.131  -20.638 1.00 144.55 ? 258  ASP A CA    1 
ATOM   1217 C  C     . ASP A 1 155 ? -28.192 -9.632  -21.953 1.00 144.78 ? 258  ASP A C     1 
ATOM   1218 O  O     . ASP A 1 155 ? -28.111 -10.829 -22.246 1.00 132.38 ? 258  ASP A O     1 
ATOM   1219 C  CB    . ASP A 1 155 ? -27.754 -10.200 -19.554 1.00 153.85 ? 258  ASP A CB    1 
ATOM   1220 C  CG    . ASP A 1 155 ? -27.029 -9.837  -18.274 1.00 158.83 ? 258  ASP A CG    1 
ATOM   1221 O  OD1   . ASP A 1 155 ? -25.969 -9.181  -18.353 1.00 154.03 ? 258  ASP A OD1   1 
ATOM   1222 O  OD2   . ASP A 1 155 ? -27.520 -10.210 -17.187 1.00 159.20 ? 258  ASP A OD2   1 
ATOM   1223 N  N     . GLU A 1 156 ? -28.784 -8.745  -22.749 1.00 138.95 ? 259  GLU A N     1 
ATOM   1224 C  CA    . GLU A 1 156 ? -29.358 -9.125  -24.031 1.00 135.07 ? 259  GLU A CA    1 
ATOM   1225 C  C     . GLU A 1 156 ? -28.295 -9.076  -25.120 1.00 111.09 ? 259  GLU A C     1 
ATOM   1226 O  O     . GLU A 1 156 ? -27.437 -8.189  -25.129 1.00 116.73 ? 259  GLU A O     1 
ATOM   1227 C  CB    . GLU A 1 156 ? -30.529 -8.210  -24.393 1.00 110.48 ? 259  GLU A CB    1 
ATOM   1228 C  CG    . GLU A 1 156 ? -31.734 -8.365  -23.480 1.00 112.09 ? 259  GLU A CG    1 
ATOM   1229 C  CD    . GLU A 1 156 ? -32.921 -7.539  -23.932 1.00 124.17 ? 259  GLU A CD    1 
ATOM   1230 O  OE1   . GLU A 1 156 ? -32.729 -6.616  -24.750 1.00 161.00 ? 259  GLU A OE1   1 
ATOM   1231 O  OE2   . GLU A 1 156 ? -34.048 -7.817  -23.471 1.00 140.66 ? 259  GLU A OE2   1 
ATOM   1232 N  N     . TYR A 1 157 ? -28.356 -10.040 -26.037 1.00 122.79 ? 260  TYR A N     1 
ATOM   1233 C  CA    . TYR A 1 157 ? -27.375 -10.172 -27.104 1.00 105.45 ? 260  TYR A CA    1 
ATOM   1234 C  C     . TYR A 1 157 ? -28.078 -10.239 -28.451 1.00 102.12 ? 260  TYR A C     1 
ATOM   1235 O  O     . TYR A 1 157 ? -29.161 -10.819 -28.571 1.00 111.07 ? 260  TYR A O     1 
ATOM   1236 C  CB    . TYR A 1 157 ? -26.504 -11.421 -26.908 1.00 117.61 ? 260  TYR A CB    1 
ATOM   1237 C  CG    . TYR A 1 157 ? -25.553 -11.332 -25.736 1.00 116.35 ? 260  TYR A CG    1 
ATOM   1238 C  CD1   . TYR A 1 157 ? -26.002 -11.524 -24.436 1.00 108.91 ? 260  TYR A CD1   1 
ATOM   1239 C  CD2   . TYR A 1 157 ? -24.204 -11.064 -25.930 1.00 123.15 ? 260  TYR A CD2   1 
ATOM   1240 C  CE1   . TYR A 1 157 ? -25.136 -11.445 -23.362 1.00 113.15 ? 260  TYR A CE1   1 
ATOM   1241 C  CE2   . TYR A 1 157 ? -23.330 -10.985 -24.862 1.00 120.75 ? 260  TYR A CE2   1 
ATOM   1242 C  CZ    . TYR A 1 157 ? -23.802 -11.176 -23.580 1.00 106.26 ? 260  TYR A CZ    1 
ATOM   1243 O  OH    . TYR A 1 157 ? -22.938 -11.098 -22.513 1.00 123.76 ? 260  TYR A OH    1 
ATOM   1244 N  N     . PHE A 1 158 ? -27.448 -9.643  -29.463 1.00 104.16 ? 261  PHE A N     1 
ATOM   1245 C  CA    . PHE A 1 158 ? -27.973 -9.651  -30.830 1.00 112.70 ? 261  PHE A CA    1 
ATOM   1246 C  C     . PHE A 1 158 ? -27.385 -10.846 -31.583 1.00 117.34 ? 261  PHE A C     1 
ATOM   1247 O  O     . PHE A 1 158 ? -26.610 -10.717 -32.533 1.00 110.14 ? 261  PHE A O     1 
ATOM   1248 C  CB    . PHE A 1 158 ? -27.656 -8.335  -31.530 1.00 106.53 ? 261  PHE A CB    1 
ATOM   1249 C  CG    . PHE A 1 158 ? -28.232 -7.124  -30.846 1.00 98.34  ? 261  PHE A CG    1 
ATOM   1250 C  CD1   . PHE A 1 158 ? -27.599 -6.559  -29.751 1.00 119.05 ? 261  PHE A CD1   1 
ATOM   1251 C  CD2   . PHE A 1 158 ? -29.398 -6.540  -31.310 1.00 102.92 ? 261  PHE A CD2   1 
ATOM   1252 C  CE1   . PHE A 1 158 ? -28.125 -5.445  -29.126 1.00 115.07 ? 261  PHE A CE1   1 
ATOM   1253 C  CE2   . PHE A 1 158 ? -29.928 -5.424  -30.688 1.00 108.99 ? 261  PHE A CE2   1 
ATOM   1254 C  CZ    . PHE A 1 158 ? -29.291 -4.876  -29.595 1.00 91.05  ? 261  PHE A CZ    1 
ATOM   1255 N  N     . LEU A 1 159 ? -27.779 -12.039 -31.130 1.00 97.61  ? 262  LEU A N     1 
ATOM   1256 C  CA    . LEU A 1 159 ? -27.200 -13.266 -31.667 1.00 110.68 ? 262  LEU A CA    1 
ATOM   1257 C  C     . LEU A 1 159 ? -27.807 -13.663 -33.007 1.00 129.95 ? 262  LEU A C     1 
ATOM   1258 O  O     . LEU A 1 159 ? -27.100 -14.209 -33.861 1.00 114.21 ? 262  LEU A O     1 
ATOM   1259 C  CB    . LEU A 1 159 ? -27.364 -14.406 -30.661 1.00 121.39 ? 262  LEU A CB    1 
ATOM   1260 C  CG    . LEU A 1 159 ? -26.521 -14.300 -29.389 1.00 118.81 ? 262  LEU A CG    1 
ATOM   1261 C  CD1   . LEU A 1 159 ? -26.850 -15.429 -28.426 1.00 124.70 ? 262  LEU A CD1   1 
ATOM   1262 C  CD2   . LEU A 1 159 ? -25.040 -14.305 -29.733 1.00 98.84  ? 262  LEU A CD2   1 
ATOM   1263 N  N     . GLU A 1 160 ? -29.094 -13.404 -33.214 1.00 113.42 ? 263  GLU A N     1 
ATOM   1264 C  CA    . GLU A 1 160 ? -29.767 -13.802 -34.440 1.00 112.02 ? 263  GLU A CA    1 
ATOM   1265 C  C     . GLU A 1 160 ? -29.673 -12.696 -35.490 1.00 112.71 ? 263  GLU A C     1 
ATOM   1266 O  O     . GLU A 1 160 ? -29.482 -11.519 -35.177 1.00 110.62 ? 263  GLU A O     1 
ATOM   1267 C  CB    . GLU A 1 160 ? -31.230 -14.152 -34.158 1.00 128.49 ? 263  GLU A CB    1 
ATOM   1268 C  CG    . GLU A 1 160 ? -31.977 -14.828 -35.306 1.00 137.86 ? 263  GLU A CG    1 
ATOM   1269 C  CD    . GLU A 1 160 ? -31.292 -16.090 -35.805 1.00 140.80 ? 263  GLU A CD    1 
ATOM   1270 O  OE1   . GLU A 1 160 ? -30.337 -15.981 -36.604 1.00 119.05 ? 263  GLU A OE1   1 
ATOM   1271 O  OE2   . GLU A 1 160 ? -31.710 -17.193 -35.397 1.00 151.29 ? 263  GLU A OE2   1 
ATOM   1272 N  N     . LYS A 1 161 ? -29.806 -13.097 -36.755 1.00 108.11 ? 264  LYS A N     1 
ATOM   1273 C  CA    . LYS A 1 161 ? -29.694 -12.185 -37.893 1.00 94.48  ? 264  LYS A CA    1 
ATOM   1274 C  C     . LYS A 1 161 ? -30.982 -11.422 -38.185 1.00 99.45  ? 264  LYS A C     1 
ATOM   1275 O  O     . LYS A 1 161 ? -31.310 -11.176 -39.349 1.00 116.45 ? 264  LYS A O     1 
ATOM   1276 C  CB    . LYS A 1 161 ? -29.242 -12.973 -39.121 1.00 141.23 ? 264  LYS A CB    1 
ATOM   1277 C  CG    . LYS A 1 161 ? -30.120 -14.169 -39.451 1.00 111.52 ? 264  LYS A CG    1 
ATOM   1278 C  CD    . LYS A 1 161 ? -29.619 -14.899 -40.687 1.00 141.99 ? 264  LYS A CD    1 
ATOM   1279 C  CE    . LYS A 1 161 ? -30.501 -16.094 -41.018 1.00 153.53 ? 264  LYS A CE    1 
ATOM   1280 N  NZ    . LYS A 1 161 ? -30.023 -16.821 -42.226 1.00 133.08 ? 264  LYS A NZ    1 
ATOM   1281 N  N     . TYR A 1 162 ? -31.728 -11.036 -37.152 1.00 117.44 ? 265  TYR A N     1 
ATOM   1282 C  CA    . TYR A 1 162 ? -32.925 -10.238 -37.353 1.00 110.78 ? 265  TYR A CA    1 
ATOM   1283 C  C     . TYR A 1 162 ? -32.555 -8.777  -37.606 1.00 108.58 ? 265  TYR A C     1 
ATOM   1284 O  O     . TYR A 1 162 ? -31.485 -8.322  -37.193 1.00 123.95 ? 265  TYR A O     1 
ATOM   1285 C  CB    . TYR A 1 162 ? -33.841 -10.333 -36.136 1.00 110.23 ? 265  TYR A CB    1 
ATOM   1286 C  CG    . TYR A 1 162 ? -34.486 -11.688 -35.950 1.00 147.41 ? 265  TYR A CG    1 
ATOM   1287 C  CD1   . TYR A 1 162 ? -34.705 -12.529 -37.033 1.00 152.76 ? 265  TYR A CD1   1 
ATOM   1288 C  CD2   . TYR A 1 162 ? -34.879 -12.124 -34.692 1.00 141.26 ? 265  TYR A CD2   1 
ATOM   1289 C  CE1   . TYR A 1 162 ? -35.295 -13.768 -36.867 1.00 159.82 ? 265  TYR A CE1   1 
ATOM   1290 C  CE2   . TYR A 1 162 ? -35.470 -13.361 -34.515 1.00 123.58 ? 265  TYR A CE2   1 
ATOM   1291 C  CZ    . TYR A 1 162 ? -35.676 -14.178 -35.606 1.00 145.93 ? 265  TYR A CZ    1 
ATOM   1292 O  OH    . TYR A 1 162 ? -36.264 -15.411 -35.436 1.00 156.26 ? 265  TYR A OH    1 
ATOM   1293 N  N     . PRO A 1 163 ? -33.415 -8.029  -38.300 1.00 119.28 ? 266  PRO A N     1 
ATOM   1294 C  CA    . PRO A 1 163 ? -33.167 -6.592  -38.467 1.00 124.54 ? 266  PRO A CA    1 
ATOM   1295 C  C     . PRO A 1 163 ? -33.056 -5.892  -37.121 1.00 107.17 ? 266  PRO A C     1 
ATOM   1296 O  O     . PRO A 1 163 ? -33.688 -6.283  -36.137 1.00 108.21 ? 266  PRO A O     1 
ATOM   1297 C  CB    . PRO A 1 163 ? -34.391 -6.108  -39.252 1.00 101.16 ? 266  PRO A CB    1 
ATOM   1298 C  CG    . PRO A 1 163 ? -34.856 -7.316  -39.991 1.00 102.17 ? 266  PRO A CG    1 
ATOM   1299 C  CD    . PRO A 1 163 ? -34.579 -8.482  -39.082 1.00 126.68 ? 266  PRO A CD    1 
ATOM   1300 N  N     . LEU A 1 164 ? -32.230 -4.843  -37.089 1.00 97.10  ? 267  LEU A N     1 
ATOM   1301 C  CA    . LEU A 1 164 ? -31.956 -4.155  -35.831 1.00 100.75 ? 267  LEU A CA    1 
ATOM   1302 C  C     . LEU A 1 164 ? -33.219 -3.559  -35.225 1.00 100.48 ? 267  LEU A C     1 
ATOM   1303 O  O     . LEU A 1 164 ? -33.327 -3.453  -33.998 1.00 123.24 ? 267  LEU A O     1 
ATOM   1304 C  CB    . LEU A 1 164 ? -30.904 -3.066  -36.048 1.00 111.86 ? 267  LEU A CB    1 
ATOM   1305 C  CG    . LEU A 1 164 ? -30.329 -2.409  -34.791 1.00 103.81 ? 267  LEU A CG    1 
ATOM   1306 C  CD1   . LEU A 1 164 ? -29.536 -3.417  -33.971 1.00 80.48  ? 267  LEU A CD1   1 
ATOM   1307 C  CD2   . LEU A 1 164 ? -29.467 -1.208  -35.153 1.00 86.14  ? 267  LEU A CD2   1 
ATOM   1308 N  N     . SER A 1 165 ? -34.189 -3.177  -36.060 1.00 120.85 ? 268  SER A N     1 
ATOM   1309 C  CA    . SER A 1 165 ? -35.420 -2.590  -35.542 1.00 109.18 ? 268  SER A CA    1 
ATOM   1310 C  C     . SER A 1 165 ? -36.270 -3.614  -34.799 1.00 114.06 ? 268  SER A C     1 
ATOM   1311 O  O     . SER A 1 165 ? -37.056 -3.239  -33.921 1.00 93.92  ? 268  SER A O     1 
ATOM   1312 C  CB    . SER A 1 165 ? -36.226 -1.967  -36.680 1.00 95.57  ? 268  SER A CB    1 
ATOM   1313 O  OG    . SER A 1 165 ? -35.507 -0.914  -37.294 1.00 111.61 ? 268  SER A OG    1 
ATOM   1314 N  N     . GLN A 1 166 ? -36.130 -4.901  -35.130 1.00 100.30 ? 269  GLN A N     1 
ATOM   1315 C  CA    . GLN A 1 166 ? -36.949 -5.921  -34.483 1.00 98.62  ? 269  GLN A CA    1 
ATOM   1316 C  C     . GLN A 1 166 ? -36.645 -6.036  -32.995 1.00 100.70 ? 269  GLN A C     1 
ATOM   1317 O  O     . GLN A 1 166 ? -37.548 -6.329  -32.204 1.00 123.54 ? 269  GLN A O     1 
ATOM   1318 C  CB    . GLN A 1 166 ? -36.752 -7.277  -35.159 1.00 102.56 ? 269  GLN A CB    1 
ATOM   1319 C  CG    . GLN A 1 166 ? -37.317 -7.371  -36.565 1.00 113.92 ? 269  GLN A CG    1 
ATOM   1320 C  CD    . GLN A 1 166 ? -37.812 -8.767  -36.897 1.00 124.96 ? 269  GLN A CD    1 
ATOM   1321 O  OE1   . GLN A 1 166 ? -37.512 -9.310  -37.961 1.00 118.13 ? 269  GLN A OE1   1 
ATOM   1322 N  NE2   . GLN A 1 166 ? -38.582 -9.353  -35.987 1.00 103.70 ? 269  GLN A NE2   1 
ATOM   1323 N  N     . TYR A 1 167 ? -35.394 -5.816  -32.597 1.00 95.70  ? 270  TYR A N     1 
ATOM   1324 C  CA    . TYR A 1 167 ? -35.027 -5.936  -31.193 1.00 111.84 ? 270  TYR A CA    1 
ATOM   1325 C  C     . TYR A 1 167 ? -35.744 -4.881  -30.361 1.00 98.06  ? 270  TYR A C     1 
ATOM   1326 O  O     . TYR A 1 167 ? -35.773 -3.700  -30.721 1.00 101.62 ? 270  TYR A O     1 
ATOM   1327 C  CB    . TYR A 1 167 ? -33.513 -5.814  -31.032 1.00 86.97  ? 270  TYR A CB    1 
ATOM   1328 C  CG    . TYR A 1 167 ? -32.759 -7.037  -31.503 1.00 98.06  ? 270  TYR A CG    1 
ATOM   1329 C  CD1   . TYR A 1 167 ? -32.395 -7.183  -32.836 1.00 93.07  ? 270  TYR A CD1   1 
ATOM   1330 C  CD2   . TYR A 1 167 ? -32.416 -8.048  -30.615 1.00 102.50 ? 270  TYR A CD2   1 
ATOM   1331 C  CE1   . TYR A 1 167 ? -31.706 -8.301  -33.270 1.00 85.56  ? 270  TYR A CE1   1 
ATOM   1332 C  CE2   . TYR A 1 167 ? -31.729 -9.169  -31.039 1.00 89.93  ? 270  TYR A CE2   1 
ATOM   1333 C  CZ    . TYR A 1 167 ? -31.377 -9.291  -32.367 1.00 100.88 ? 270  TYR A CZ    1 
ATOM   1334 O  OH    . TYR A 1 167 ? -30.692 -10.407 -32.790 1.00 95.21  ? 270  TYR A OH    1 
ATOM   1335 N  N     . LYS A 1 168 ? -36.327 -5.318  -29.241 1.00 125.57 ? 271  LYS A N     1 
ATOM   1336 C  CA    . LYS A 1 168 ? -37.149 -4.426  -28.429 1.00 126.66 ? 271  LYS A CA    1 
ATOM   1337 C  C     . LYS A 1 168 ? -36.347 -3.260  -27.868 1.00 134.41 ? 271  LYS A C     1 
ATOM   1338 O  O     . LYS A 1 168 ? -36.879 -2.153  -27.735 1.00 123.19 ? 271  LYS A O     1 
ATOM   1339 C  CB    . LYS A 1 168 ? -37.810 -5.207  -27.293 1.00 136.38 ? 271  LYS A CB    1 
ATOM   1340 C  CG    . LYS A 1 168 ? -38.973 -6.078  -27.734 1.00 135.61 ? 271  LYS A CG    1 
ATOM   1341 C  CD    . LYS A 1 168 ? -39.658 -6.723  -26.542 1.00 155.99 ? 271  LYS A CD    1 
ATOM   1342 C  CE    . LYS A 1 168 ? -40.965 -7.380  -26.949 1.00 154.07 ? 271  LYS A CE    1 
ATOM   1343 N  NZ    . LYS A 1 168 ? -40.766 -8.410  -28.005 1.00 154.54 ? 271  LYS A NZ    1 
ATOM   1344 N  N     . TYR A 1 169 ? -35.075 -3.483  -27.529 1.00 132.93 ? 272  TYR A N     1 
ATOM   1345 C  CA    . TYR A 1 169 ? -34.251 -2.392  -27.018 1.00 120.03 ? 272  TYR A CA    1 
ATOM   1346 C  C     . TYR A 1 169 ? -34.065 -1.310  -28.073 1.00 127.47 ? 272  TYR A C     1 
ATOM   1347 O  O     . TYR A 1 169 ? -34.236 -0.117  -27.794 1.00 140.60 ? 272  TYR A O     1 
ATOM   1348 C  CB    . TYR A 1 169 ? -32.897 -2.922  -26.547 1.00 136.06 ? 272  TYR A CB    1 
ATOM   1349 C  CG    . TYR A 1 169 ? -31.905 -1.824  -26.236 1.00 131.36 ? 272  TYR A CG    1 
ATOM   1350 C  CD1   . TYR A 1 169 ? -31.989 -1.101  -25.053 1.00 137.99 ? 272  TYR A CD1   1 
ATOM   1351 C  CD2   . TYR A 1 169 ? -30.888 -1.506  -27.127 1.00 115.94 ? 272  TYR A CD2   1 
ATOM   1352 C  CE1   . TYR A 1 169 ? -31.087 -0.093  -24.766 1.00 128.25 ? 272  TYR A CE1   1 
ATOM   1353 C  CE2   . TYR A 1 169 ? -29.983 -0.500  -26.849 1.00 122.92 ? 272  TYR A CE2   1 
ATOM   1354 C  CZ    . TYR A 1 169 ? -30.086 0.203   -25.667 1.00 134.71 ? 272  TYR A CZ    1 
ATOM   1355 O  OH    . TYR A 1 169 ? -29.186 1.205   -25.385 1.00 132.51 ? 272  TYR A OH    1 
ATOM   1356 N  N     . ILE A 1 170 ? -33.712 -1.708  -29.297 1.00 114.91 ? 273  ILE A N     1 
ATOM   1357 C  CA    . ILE A 1 170 ? -33.563 -0.738  -30.376 1.00 103.19 ? 273  ILE A CA    1 
ATOM   1358 C  C     . ILE A 1 170 ? -34.909 -0.112  -30.715 1.00 112.82 ? 273  ILE A C     1 
ATOM   1359 O  O     . ILE A 1 170 ? -35.002 1.094   -30.973 1.00 106.72 ? 273  ILE A O     1 
ATOM   1360 C  CB    . ILE A 1 170 ? -32.924 -1.403  -31.608 1.00 106.62 ? 273  ILE A CB    1 
ATOM   1361 C  CG1   . ILE A 1 170 ? -31.651 -2.154  -31.213 1.00 117.43 ? 273  ILE A CG1   1 
ATOM   1362 C  CG2   . ILE A 1 170 ? -32.625 -0.365  -32.679 1.00 107.58 ? 273  ILE A CG2   1 
ATOM   1363 C  CD1   . ILE A 1 170 ? -30.551 -1.263  -30.693 1.00 102.14 ? 273  ILE A CD1   1 
ATOM   1364 N  N     . ARG A 1 171 ? -35.973 -0.920  -30.717 1.00 126.20 ? 274  ARG A N     1 
ATOM   1365 C  CA    . ARG A 1 171 ? -37.306 -0.395  -30.996 1.00 103.53 ? 274  ARG A CA    1 
ATOM   1366 C  C     . ARG A 1 171 ? -37.736 0.609   -29.934 1.00 104.90 ? 274  ARG A C     1 
ATOM   1367 O  O     . ARG A 1 171 ? -38.330 1.645   -30.254 1.00 103.06 ? 274  ARG A O     1 
ATOM   1368 C  CB    . ARG A 1 171 ? -38.311 -1.543  -31.087 1.00 105.60 ? 274  ARG A CB    1 
ATOM   1369 C  CG    . ARG A 1 171 ? -39.729 -1.111  -31.420 1.00 97.75  ? 274  ARG A CG    1 
ATOM   1370 C  CD    . ARG A 1 171 ? -39.874 -0.779  -32.894 1.00 89.04  ? 274  ARG A CD    1 
ATOM   1371 N  NE    . ARG A 1 171 ? -39.740 -1.964  -33.733 1.00 90.57  ? 274  ARG A NE    1 
ATOM   1372 C  CZ    . ARG A 1 171 ? -40.755 -2.725  -34.122 1.00 105.91 ? 274  ARG A CZ    1 
ATOM   1373 N  NH1   . ARG A 1 171 ? -41.999 -2.453  -33.765 1.00 126.39 ? 274  ARG A NH1   1 
ATOM   1374 N  NH2   . ARG A 1 171 ? -40.514 -3.784  -34.890 1.00 93.88  ? 274  ARG A NH2   1 
ATOM   1375 N  N     . SER A 1 172 ? -37.442 0.322   -28.663 1.00 108.44 ? 275  SER A N     1 
ATOM   1376 C  CA    . SER A 1 172 ? -37.809 1.244   -27.593 1.00 100.00 ? 275  SER A CA    1 
ATOM   1377 C  C     . SER A 1 172 ? -36.994 2.530   -27.654 1.00 123.45 ? 275  SER A C     1 
ATOM   1378 O  O     . SER A 1 172 ? -37.488 3.592   -27.261 1.00 120.10 ? 275  SER A O     1 
ATOM   1379 C  CB    . SER A 1 172 ? -37.635 0.572   -26.232 1.00 109.32 ? 275  SER A CB    1 
ATOM   1380 O  OG    . SER A 1 172 ? -36.290 0.174   -26.028 1.00 160.72 ? 275  SER A OG    1 
ATOM   1381 N  N     . CYS A 1 173 ? -35.751 2.456   -28.136 1.00 141.37 ? 276  CYS A N     1 
ATOM   1382 C  CA    . CYS A 1 173 ? -34.953 3.668   -28.290 1.00 128.16 ? 276  CYS A CA    1 
ATOM   1383 C  C     . CYS A 1 173 ? -35.500 4.560   -29.396 1.00 118.64 ? 276  CYS A C     1 
ATOM   1384 O  O     . CYS A 1 173 ? -35.350 5.785   -29.332 1.00 130.50 ? 276  CYS A O     1 
ATOM   1385 C  CB    . CYS A 1 173 ? -33.493 3.309   -28.569 1.00 126.60 ? 276  CYS A CB    1 
ATOM   1386 S  SG    . CYS A 1 173 ? -32.627 2.561   -27.169 1.00 119.38 ? 276  CYS A SG    1 
ATOM   1387 N  N     . ILE A 1 174 ? -36.133 3.971   -30.413 1.00 97.25  ? 277  ILE A N     1 
ATOM   1388 C  CA    . ILE A 1 174 ? -36.765 4.773   -31.455 1.00 94.44  ? 277  ILE A CA    1 
ATOM   1389 C  C     . ILE A 1 174 ? -37.993 5.486   -30.905 1.00 107.22 ? 277  ILE A C     1 
ATOM   1390 O  O     . ILE A 1 174 ? -38.227 6.666   -31.197 1.00 137.11 ? 277  ILE A O     1 
ATOM   1391 C  CB    . ILE A 1 174 ? -37.115 3.893   -32.669 1.00 113.74 ? 277  ILE A CB    1 
ATOM   1392 C  CG1   . ILE A 1 174 ? -35.856 3.232   -33.231 1.00 110.89 ? 277  ILE A CG1   1 
ATOM   1393 C  CG2   . ILE A 1 174 ? -37.808 4.715   -33.745 1.00 93.21  ? 277  ILE A CG2   1 
ATOM   1394 C  CD1   . ILE A 1 174 ? -36.127 2.290   -34.384 1.00 86.58  ? 277  ILE A CD1   1 
ATOM   1395 N  N     . MET A 1 175 ? -38.796 4.787   -30.099 1.00 107.56 ? 278  MET A N     1 
ATOM   1396 C  CA    . MET A 1 175 ? -39.973 5.401   -29.494 1.00 102.88 ? 278  MET A CA    1 
ATOM   1397 C  C     . MET A 1 175 ? -39.573 6.534   -28.556 1.00 112.16 ? 278  MET A C     1 
ATOM   1398 O  O     . MET A 1 175 ? -40.014 7.678   -28.713 1.00 131.39 ? 278  MET A O     1 
ATOM   1399 C  CB    . MET A 1 175 ? -40.785 4.346   -28.738 1.00 131.88 ? 278  MET A CB    1 
ATOM   1400 C  CG    . MET A 1 175 ? -41.090 3.082   -29.525 1.00 113.82 ? 278  MET A CG    1 
ATOM   1401 S  SD    . MET A 1 175 ? -42.265 3.325   -30.868 1.00 133.97 ? 278  MET A SD    1 
ATOM   1402 C  CE    . MET A 1 175 ? -42.609 1.623   -31.311 1.00 125.53 ? 278  MET A CE    1 
ATOM   1403 N  N     . LEU A 1 176 ? -38.729 6.227   -27.568 1.00 116.53 ? 279  LEU A N     1 
ATOM   1404 C  CA    . LEU A 1 176 ? -38.332 7.222   -26.579 1.00 142.86 ? 279  LEU A CA    1 
ATOM   1405 C  C     . LEU A 1 176 ? -37.381 8.266   -27.148 1.00 134.94 ? 279  LEU A C     1 
ATOM   1406 O  O     . LEU A 1 176 ? -37.197 9.320   -26.528 1.00 119.80 ? 279  LEU A O     1 
ATOM   1407 C  CB    . LEU A 1 176 ? -37.680 6.539   -25.373 1.00 127.46 ? 279  LEU A CB    1 
ATOM   1408 C  CG    . LEU A 1 176 ? -38.572 5.913   -24.295 1.00 122.22 ? 279  LEU A CG    1 
ATOM   1409 C  CD1   . LEU A 1 176 ? -39.344 4.708   -24.816 1.00 125.10 ? 279  LEU A CD1   1 
ATOM   1410 C  CD2   . LEU A 1 176 ? -37.738 5.530   -23.080 1.00 135.05 ? 279  LEU A CD2   1 
ATOM   1411 N  N     . GLY A 1 177 ? -36.778 8.006   -28.305 1.00 115.75 ? 280  GLY A N     1 
ATOM   1412 C  CA    . GLY A 1 177 ? -35.798 8.918   -28.859 1.00 107.12 ? 280  GLY A CA    1 
ATOM   1413 C  C     . GLY A 1 177 ? -34.526 8.947   -28.037 1.00 108.08 ? 280  GLY A C     1 
ATOM   1414 O  O     . GLY A 1 177 ? -34.186 9.972   -27.440 1.00 105.02 ? 280  GLY A O     1 
ATOM   1415 N  N     . ARG A 1 178 ? -33.817 7.821   -27.995 1.00 129.01 ? 281  ARG A N     1 
ATOM   1416 C  CA    . ARG A 1 178 ? -32.615 7.682   -27.189 1.00 124.11 ? 281  ARG A CA    1 
ATOM   1417 C  C     . ARG A 1 178 ? -31.526 7.009   -28.013 1.00 129.58 ? 281  ARG A C     1 
ATOM   1418 O  O     . ARG A 1 178 ? -31.790 6.412   -29.060 1.00 121.00 ? 281  ARG A O     1 
ATOM   1419 C  CB    . ARG A 1 178 ? -32.895 6.877   -25.911 1.00 114.19 ? 281  ARG A CB    1 
ATOM   1420 C  CG    . ARG A 1 178 ? -32.016 7.253   -24.730 1.00 153.82 ? 281  ARG A CG    1 
ATOM   1421 C  CD    . ARG A 1 178 ? -32.605 6.732   -23.431 1.00 174.33 ? 281  ARG A CD    1 
ATOM   1422 N  NE    . ARG A 1 178 ? -34.005 7.115   -23.286 1.00 154.74 ? 281  ARG A NE    1 
ATOM   1423 C  CZ    . ARG A 1 178 ? -34.418 8.280   -22.806 1.00 175.87 ? 281  ARG A CZ    1 
ATOM   1424 N  NH1   . ARG A 1 178 ? -33.562 9.207   -22.408 1.00 192.69 ? 281  ARG A NH1   1 
ATOM   1425 N  NH2   . ARG A 1 178 ? -35.724 8.523   -22.727 1.00 168.29 ? 281  ARG A NH2   1 
ATOM   1426 N  N     . MET A 1 179 ? -30.294 7.116   -27.528 1.00 118.11 ? 282  MET A N     1 
ATOM   1427 C  CA    . MET A 1 179 ? -29.150 6.551   -28.234 1.00 120.21 ? 282  MET A CA    1 
ATOM   1428 C  C     . MET A 1 179 ? -29.018 5.065   -27.923 1.00 140.10 ? 282  MET A C     1 
ATOM   1429 O  O     . MET A 1 179 ? -28.806 4.703   -26.760 1.00 111.82 ? 282  MET A O     1 
ATOM   1430 C  CB    . MET A 1 179 ? -27.869 7.279   -27.845 1.00 145.91 ? 282  MET A CB    1 
ATOM   1431 C  CG    . MET A 1 179 ? -27.711 8.665   -28.456 1.00 136.48 ? 282  MET A CG    1 
ATOM   1432 S  SD    . MET A 1 179 ? -27.301 8.632   -30.215 1.00 139.10 ? 282  MET A SD    1 
ATOM   1433 C  CE    . MET A 1 179 ? -28.920 8.820   -30.963 1.00 171.26 ? 282  MET A CE    1 
ATOM   1434 N  N     . PRO A 1 180 ? -29.142 4.180   -28.914 1.00 134.60 ? 283  PRO A N     1 
ATOM   1435 C  CA    . PRO A 1 180 ? -28.903 2.754   -28.661 1.00 119.41 ? 283  PRO A CA    1 
ATOM   1436 C  C     . PRO A 1 180 ? -27.426 2.453   -28.466 1.00 116.03 ? 283  PRO A C     1 
ATOM   1437 O  O     . PRO A 1 180 ? -26.688 2.279   -29.441 1.00 124.04 ? 283  PRO A O     1 
ATOM   1438 C  CB    . PRO A 1 180 ? -29.450 2.073   -29.925 1.00 109.57 ? 283  PRO A CB    1 
ATOM   1439 C  CG    . PRO A 1 180 ? -30.294 3.111   -30.605 1.00 111.94 ? 283  PRO A CG    1 
ATOM   1440 C  CD    . PRO A 1 180 ? -29.657 4.418   -30.270 1.00 120.03 ? 283  PRO A CD    1 
ATOM   1441 N  N     . ASN A 1 181 ? -26.983 2.393   -27.213 1.00 111.24 ? 284  ASN A N     1 
ATOM   1442 C  CA    . ASN A 1 181 ? -25.592 2.098   -26.895 1.00 113.31 ? 284  ASN A CA    1 
ATOM   1443 C  C     . ASN A 1 181 ? -25.403 0.587   -26.826 1.00 114.97 ? 284  ASN A C     1 
ATOM   1444 O  O     . ASN A 1 181 ? -26.027 -0.085  -25.997 1.00 114.22 ? 284  ASN A O     1 
ATOM   1445 C  CB    . ASN A 1 181 ? -25.190 2.757   -25.577 1.00 121.37 ? 284  ASN A CB    1 
ATOM   1446 C  CG    . ASN A 1 181 ? -25.307 4.268   -25.622 1.00 139.22 ? 284  ASN A CG    1 
ATOM   1447 O  OD1   . ASN A 1 181 ? -24.363 4.965   -25.994 1.00 141.58 ? 284  ASN A OD1   1 
ATOM   1448 N  ND2   . ASN A 1 181 ? -26.471 4.783   -25.242 1.00 149.31 ? 284  ASN A ND2   1 
ATOM   1449 N  N     . LEU A 1 182 ? -24.542 0.057   -27.694 1.00 115.98 ? 285  LEU A N     1 
ATOM   1450 C  CA    . LEU A 1 182 ? -24.309 -1.379  -27.796 1.00 116.57 ? 285  LEU A CA    1 
ATOM   1451 C  C     . LEU A 1 182 ? -22.822 -1.654  -27.637 1.00 130.30 ? 285  LEU A C     1 
ATOM   1452 O  O     . LEU A 1 182 ? -22.004 -1.100  -28.379 1.00 133.14 ? 285  LEU A O     1 
ATOM   1453 C  CB    . LEU A 1 182 ? -24.814 -1.925  -29.135 1.00 84.76  ? 285  LEU A CB    1 
ATOM   1454 C  CG    . LEU A 1 182 ? -26.260 -1.582  -29.497 1.00 83.11  ? 285  LEU A CG    1 
ATOM   1455 C  CD1   . LEU A 1 182 ? -26.636 -2.177  -30.844 1.00 82.44  ? 285  LEU A CD1   1 
ATOM   1456 C  CD2   . LEU A 1 182 ? -27.209 -2.058  -28.412 1.00 85.27  ? 285  LEU A CD2   1 
ATOM   1457 N  N     . MET A 1 183 ? -22.476 -2.506  -26.676 1.00 123.92 ? 286  MET A N     1 
ATOM   1458 C  CA    . MET A 1 183 ? -21.092 -2.898  -26.451 1.00 125.61 ? 286  MET A CA    1 
ATOM   1459 C  C     . MET A 1 183 ? -20.729 -4.070  -27.353 1.00 120.08 ? 286  MET A C     1 
ATOM   1460 O  O     . MET A 1 183 ? -21.521 -4.999  -27.536 1.00 131.69 ? 286  MET A O     1 
ATOM   1461 C  CB    . MET A 1 183 ? -20.868 -3.270  -24.983 1.00 135.42 ? 286  MET A CB    1 
ATOM   1462 C  CG    . MET A 1 183 ? -19.453 -3.729  -24.665 1.00 129.76 ? 286  MET A CG    1 
ATOM   1463 S  SD    . MET A 1 183 ? -19.170 -3.957  -22.899 1.00 176.14 ? 286  MET A SD    1 
ATOM   1464 C  CE    . MET A 1 183 ? -20.511 -5.066  -22.479 1.00 161.02 ? 286  MET A CE    1 
ATOM   1465 N  N     . LEU A 1 184 ? -19.526 -4.019  -27.916 1.00 117.29 ? 287  LEU A N     1 
ATOM   1466 C  CA    . LEU A 1 184 ? -19.052 -5.029  -28.852 1.00 117.17 ? 287  LEU A CA    1 
ATOM   1467 C  C     . LEU A 1 184 ? -18.218 -6.065  -28.110 1.00 115.81 ? 287  LEU A C     1 
ATOM   1468 O  O     . LEU A 1 184 ? -17.329 -5.711  -27.329 1.00 135.86 ? 287  LEU A O     1 
ATOM   1469 C  CB    . LEU A 1 184 ? -18.235 -4.382  -29.973 1.00 113.62 ? 287  LEU A CB    1 
ATOM   1470 C  CG    . LEU A 1 184 ? -18.105 -5.122  -31.308 1.00 94.97  ? 287  LEU A CG    1 
ATOM   1471 C  CD1   . LEU A 1 184 ? -17.761 -4.142  -32.416 1.00 134.27 ? 287  LEU A CD1   1 
ATOM   1472 C  CD2   . LEU A 1 184 ? -17.056 -6.217  -31.237 1.00 137.00 ? 287  LEU A CD2   1 
ATOM   1473 N  N     . MET A 1 185 ? -18.510 -7.339  -28.356 1.00 139.96 ? 288  MET A N     1 
ATOM   1474 C  CA    . MET A 1 185 ? -17.780 -8.457  -27.775 1.00 128.73 ? 288  MET A CA    1 
ATOM   1475 C  C     . MET A 1 185 ? -17.339 -9.398  -28.888 1.00 150.06 ? 288  MET A C     1 
ATOM   1476 O  O     . MET A 1 185 ? -17.676 -9.215  -30.061 1.00 152.97 ? 288  MET A O     1 
ATOM   1477 C  CB    . MET A 1 185 ? -18.633 -9.214  -26.749 1.00 138.85 ? 288  MET A CB    1 
ATOM   1478 C  CG    . MET A 1 185 ? -18.788 -8.525  -25.408 1.00 161.68 ? 288  MET A CG    1 
ATOM   1479 S  SD    . MET A 1 185 ? -19.683 -9.566  -24.239 1.00 145.21 ? 288  MET A SD    1 
ATOM   1480 C  CE    . MET A 1 185 ? -19.500 -8.620  -22.730 1.00 178.68 ? 288  MET A CE    1 
ATOM   1481 N  N     . ALA A 1 186 ? -16.578 -10.417 -28.509 1.00 147.77 ? 289  ALA A N     1 
ATOM   1482 C  CA    . ALA A 1 186 ? -16.200 -11.495 -29.408 1.00 118.98 ? 289  ALA A CA    1 
ATOM   1483 C  C     . ALA A 1 186 ? -17.025 -12.738 -29.098 1.00 143.65 ? 289  ALA A C     1 
ATOM   1484 O  O     . ALA A 1 186 ? -17.643 -12.853 -28.037 1.00 152.95 ? 289  ALA A O     1 
ATOM   1485 C  CB    . ALA A 1 186 ? -14.707 -11.808 -29.290 1.00 107.25 ? 289  ALA A CB    1 
ATOM   1486 N  N     . LYS A 1 187 ? -17.033 -13.673 -30.051 1.00 152.49 ? 290  LYS A N     1 
ATOM   1487 C  CA    . LYS A 1 187 ? -17.774 -14.913 -29.850 1.00 122.46 ? 290  LYS A CA    1 
ATOM   1488 C  C     . LYS A 1 187 ? -17.195 -15.720 -28.695 1.00 137.84 ? 290  LYS A C     1 
ATOM   1489 O  O     . LYS A 1 187 ? -17.938 -16.351 -27.935 1.00 161.97 ? 290  LYS A O     1 
ATOM   1490 C  CB    . LYS A 1 187 ? -17.779 -15.740 -31.136 1.00 131.16 ? 290  LYS A CB    1 
ATOM   1491 C  CG    . LYS A 1 187 ? -18.688 -15.193 -32.224 1.00 132.27 ? 290  LYS A CG    1 
ATOM   1492 C  CD    . LYS A 1 187 ? -18.706 -16.109 -33.437 1.00 136.54 ? 290  LYS A CD    1 
ATOM   1493 C  CE    . LYS A 1 187 ? -19.704 -15.628 -34.478 1.00 154.15 ? 290  LYS A CE    1 
ATOM   1494 N  NZ    . LYS A 1 187 ? -21.097 -15.622 -33.952 1.00 171.50 ? 290  LYS A NZ    1 
ATOM   1495 N  N     . GLU A 1 188 ? -15.869 -15.704 -28.541 1.00 150.64 ? 291  GLU A N     1 
ATOM   1496 C  CA    . GLU A 1 188 ? -15.243 -16.465 -27.465 1.00 146.56 ? 291  GLU A CA    1 
ATOM   1497 C  C     . GLU A 1 188 ? -15.526 -15.853 -26.099 1.00 143.91 ? 291  GLU A C     1 
ATOM   1498 O  O     . GLU A 1 188 ? -15.551 -16.573 -25.095 1.00 141.44 ? 291  GLU A O     1 
ATOM   1499 C  CB    . GLU A 1 188 ? -13.735 -16.563 -27.699 1.00 158.69 ? 291  GLU A CB    1 
ATOM   1500 C  CG    . GLU A 1 188 ? -13.349 -17.251 -28.999 1.00 166.85 ? 291  GLU A CG    1 
ATOM   1501 C  CD    . GLU A 1 188 ? -13.729 -18.720 -29.023 1.00 175.49 ? 291  GLU A CD    1 
ATOM   1502 O  OE1   . GLU A 1 188 ? -13.885 -19.317 -27.938 1.00 183.19 ? 291  GLU A OE1   1 
ATOM   1503 O  OE2   . GLU A 1 188 ? -13.873 -19.278 -30.131 1.00 208.26 ? 291  GLU A OE2   1 
ATOM   1504 N  N     . SER A 1 189 ? -15.740 -14.536 -26.039 1.00 145.11 ? 292  SER A N     1 
ATOM   1505 C  CA    . SER A 1 189 ? -16.007 -13.889 -24.759 1.00 152.83 ? 292  SER A CA    1 
ATOM   1506 C  C     . SER A 1 189 ? -17.325 -14.356 -24.154 1.00 150.91 ? 292  SER A C     1 
ATOM   1507 O  O     . SER A 1 189 ? -17.475 -14.361 -22.927 1.00 149.36 ? 292  SER A O     1 
ATOM   1508 C  CB    . SER A 1 189 ? -16.011 -12.369 -24.929 1.00 179.37 ? 292  SER A CB    1 
ATOM   1509 O  OG    . SER A 1 189 ? -14.766 -11.908 -25.425 1.00 190.57 ? 292  SER A OG    1 
ATOM   1510 N  N     . LEU A 1 190 ? -18.283 -14.750 -24.990 1.00 136.37 ? 293  LEU A N     1 
ATOM   1511 C  CA    . LEU A 1 190 ? -19.578 -15.235 -24.529 1.00 127.42 ? 293  LEU A CA    1 
ATOM   1512 C  C     . LEU A 1 190 ? -19.658 -16.754 -24.477 1.00 134.67 ? 293  LEU A C     1 
ATOM   1513 O  O     . LEU A 1 190 ? -20.222 -17.307 -23.529 1.00 140.77 ? 293  LEU A O     1 
ATOM   1514 C  CB    . LEU A 1 190 ? -20.694 -14.700 -25.432 1.00 134.58 ? 293  LEU A CB    1 
ATOM   1515 C  CG    . LEU A 1 190 ? -22.122 -15.115 -25.074 1.00 141.06 ? 293  LEU A CG    1 
ATOM   1516 C  CD1   . LEU A 1 190 ? -22.530 -14.530 -23.731 1.00 139.84 ? 293  LEU A CD1   1 
ATOM   1517 C  CD2   . LEU A 1 190 ? -23.097 -14.701 -26.165 1.00 124.79 ? 293  LEU A CD2   1 
ATOM   1518 N  N     . TYR A 1 191 ? -19.098 -17.442 -25.475 1.00 134.80 ? 294  TYR A N     1 
ATOM   1519 C  CA    . TYR A 1 191 ? -19.209 -18.896 -25.530 1.00 118.34 ? 294  TYR A CA    1 
ATOM   1520 C  C     . TYR A 1 191 ? -18.426 -19.571 -24.410 1.00 137.07 ? 294  TYR A C     1 
ATOM   1521 O  O     . TYR A 1 191 ? -18.777 -20.683 -23.997 1.00 149.19 ? 294  TYR A O     1 
ATOM   1522 C  CB    . TYR A 1 191 ? -18.732 -19.410 -26.888 1.00 148.76 ? 294  TYR A CB    1 
ATOM   1523 C  CG    . TYR A 1 191 ? -19.569 -18.949 -28.062 1.00 118.55 ? 294  TYR A CG    1 
ATOM   1524 C  CD1   . TYR A 1 191 ? -20.874 -18.511 -27.883 1.00 112.47 ? 294  TYR A CD1   1 
ATOM   1525 C  CD2   . TYR A 1 191 ? -19.052 -18.955 -29.351 1.00 134.03 ? 294  TYR A CD2   1 
ATOM   1526 C  CE1   . TYR A 1 191 ? -21.640 -18.091 -28.955 1.00 119.26 ? 294  TYR A CE1   1 
ATOM   1527 C  CE2   . TYR A 1 191 ? -19.811 -18.540 -30.428 1.00 144.89 ? 294  TYR A CE2   1 
ATOM   1528 C  CZ    . TYR A 1 191 ? -21.103 -18.107 -30.224 1.00 145.67 ? 294  TYR A CZ    1 
ATOM   1529 O  OH    . TYR A 1 191 ? -21.861 -17.690 -31.294 1.00 169.99 ? 294  TYR A OH    1 
ATOM   1530 N  N     . SER A 1 192 ? -17.374 -18.924 -23.907 1.00 152.93 ? 295  SER A N     1 
ATOM   1531 C  CA    . SER A 1 192 ? -16.545 -19.521 -22.865 1.00 164.33 ? 295  SER A CA    1 
ATOM   1532 C  C     . SER A 1 192 ? -17.218 -19.538 -21.499 1.00 177.85 ? 295  SER A C     1 
ATOM   1533 O  O     . SER A 1 192 ? -16.603 -20.012 -20.537 1.00 172.00 ? 295  SER A O     1 
ATOM   1534 C  CB    . SER A 1 192 ? -15.210 -18.781 -22.771 1.00 157.93 ? 295  SER A CB    1 
ATOM   1535 O  OG    . SER A 1 192 ? -14.492 -18.872 -23.989 1.00 185.05 ? 295  SER A OG    1 
ATOM   1536 N  N     . GLN A 1 193 ? -18.449 -19.040 -21.385 1.00 168.70 ? 296  GLN A N     1 
ATOM   1537 C  CA    . GLN A 1 193 ? -19.185 -19.053 -20.128 1.00 160.72 ? 296  GLN A CA    1 
ATOM   1538 C  C     . GLN A 1 193 ? -20.334 -20.054 -20.137 1.00 174.78 ? 296  GLN A C     1 
ATOM   1539 O  O     . GLN A 1 193 ? -21.170 -20.033 -19.228 1.00 185.49 ? 296  GLN A O     1 
ATOM   1540 C  CB    . GLN A 1 193 ? -19.710 -17.652 -19.810 1.00 163.85 ? 296  GLN A CB    1 
ATOM   1541 C  CG    . GLN A 1 193 ? -18.623 -16.595 -19.690 1.00 165.34 ? 296  GLN A CG    1 
ATOM   1542 C  CD    . GLN A 1 193 ? -17.677 -16.858 -18.534 1.00 189.16 ? 296  GLN A CD    1 
ATOM   1543 O  OE1   . GLN A 1 193 ? -18.050 -17.480 -17.539 1.00 208.41 ? 296  GLN A OE1   1 
ATOM   1544 N  NE2   . GLN A 1 193 ? -16.442 -16.385 -18.661 1.00 177.44 ? 296  GLN A NE2   1 
ATOM   1545 N  N     . LEU A 1 194 ? -20.397 -20.924 -21.138 1.00 162.93 ? 297  LEU A N     1 
ATOM   1546 C  CA    . LEU A 1 194 ? -21.464 -21.917 -21.257 1.00 165.93 ? 297  LEU A CA    1 
ATOM   1547 C  C     . LEU A 1 194 ? -20.847 -23.295 -21.440 1.00 167.11 ? 297  LEU A C     1 
ATOM   1548 O  O     . LEU A 1 194 ? -20.227 -23.557 -22.492 1.00 152.77 ? 297  LEU A O     1 
ATOM   1549 C  CB    . LEU A 1 194 ? -22.398 -21.589 -22.419 1.00 157.98 ? 297  LEU A CB    1 
ATOM   1550 C  CG    . LEU A 1 194 ? -23.391 -20.433 -22.266 1.00 141.36 ? 297  LEU A CG    1 
ATOM   1551 C  CD1   . LEU A 1 194 ? -22.719 -19.077 -22.424 1.00 151.52 ? 297  LEU A CD1   1 
ATOM   1552 C  CD2   . LEU A 1 194 ? -24.521 -20.585 -23.264 1.00 143.39 ? 297  LEU A CD2   1 
ATOM   1553 N  N     . PRO A 1 195 ? -20.981 -24.193 -20.472 1.00 191.35 ? 298  PRO A N     1 
ATOM   1554 C  CA    . PRO A 1 195 ? -20.432 -25.544 -20.611 1.00 210.73 ? 298  PRO A CA    1 
ATOM   1555 C  C     . PRO A 1 195 ? -21.338 -26.411 -21.481 1.00 206.99 ? 298  PRO A C     1 
ATOM   1556 O  O     . PRO A 1 195 ? -22.394 -25.987 -21.945 1.00 196.63 ? 298  PRO A O     1 
ATOM   1557 C  CB    . PRO A 1 195 ? -20.386 -26.047 -19.168 1.00 216.11 ? 298  PRO A CB    1 
ATOM   1558 C  CG    . PRO A 1 195 ? -21.517 -25.339 -18.505 1.00 206.98 ? 298  PRO A CG    1 
ATOM   1559 C  CD    . PRO A 1 195 ? -21.591 -23.976 -19.148 1.00 196.45 ? 298  PRO A CD    1 
ATOM   1560 N  N     . MET A 1 196 ? -20.900 -27.650 -21.694 1.00 191.22 ? 299  MET A N     1 
ATOM   1561 C  CA    . MET A 1 196 ? -21.646 -28.631 -22.482 1.00 203.59 ? 299  MET A CA    1 
ATOM   1562 C  C     . MET A 1 196 ? -22.331 -29.585 -21.509 1.00 210.81 ? 299  MET A C     1 
ATOM   1563 O  O     . MET A 1 196 ? -21.744 -30.567 -21.053 1.00 200.69 ? 299  MET A O     1 
ATOM   1564 C  CB    . MET A 1 196 ? -20.727 -29.371 -23.446 1.00 205.47 ? 299  MET A CB    1 
ATOM   1565 C  CG    . MET A 1 196 ? -20.066 -28.483 -24.486 1.00 204.96 ? 299  MET A CG    1 
ATOM   1566 S  SD    . MET A 1 196 ? -19.005 -29.408 -25.612 1.00 257.99 ? 299  MET A SD    1 
ATOM   1567 C  CE    . MET A 1 196 ? -20.175 -30.575 -26.301 1.00 214.24 ? 299  MET A CE    1 
ATOM   1568 N  N     . ASP A 1 197 ? -23.589 -29.290 -21.190 1.00 207.26 ? 300  ASP A N     1 
ATOM   1569 C  CA    . ASP A 1 197 ? -24.361 -30.109 -20.262 1.00 189.93 ? 300  ASP A CA    1 
ATOM   1570 C  C     . ASP A 1 197 ? -24.879 -31.342 -20.991 1.00 194.79 ? 300  ASP A C     1 
ATOM   1571 O  O     . ASP A 1 197 ? -25.811 -31.251 -21.797 1.00 189.46 ? 300  ASP A O     1 
ATOM   1572 C  CB    . ASP A 1 197 ? -25.512 -29.306 -19.664 1.00 184.86 ? 300  ASP A CB    1 
ATOM   1573 C  CG    . ASP A 1 197 ? -25.039 -28.224 -18.717 1.00 197.44 ? 300  ASP A CG    1 
ATOM   1574 O  OD1   . ASP A 1 197 ? -23.824 -27.935 -18.699 1.00 230.90 ? 300  ASP A OD1   1 
ATOM   1575 O  OD2   . ASP A 1 197 ? -25.883 -27.668 -17.983 1.00 181.83 ? 300  ASP A OD2   1 
ATOM   1576 N  N     . CYS A 1 198 ? -24.276 -32.494 -20.713 1.00 213.92 ? 301  CYS A N     1 
ATOM   1577 C  CA    . CYS A 1 198 ? -24.768 -33.745 -21.271 1.00 216.52 ? 301  CYS A CA    1 
ATOM   1578 C  C     . CYS A 1 198 ? -26.072 -34.141 -20.590 1.00 219.39 ? 301  CYS A C     1 
ATOM   1579 O  O     . CYS A 1 198 ? -26.241 -33.957 -19.381 1.00 220.87 ? 301  CYS A O     1 
ATOM   1580 C  CB    . CYS A 1 198 ? -23.725 -34.849 -21.104 1.00 205.76 ? 301  CYS A CB    1 
ATOM   1581 S  SG    . CYS A 1 198 ? -24.209 -36.448 -21.795 1.00 234.09 ? 301  CYS A SG    1 
ATOM   1582 N  N     . PHE A 1 199 ? -27.002 -34.682 -21.377 1.00 200.98 ? 302  PHE A N     1 
ATOM   1583 C  CA    . PHE A 1 199 ? -28.307 -35.066 -20.854 1.00 186.17 ? 302  PHE A CA    1 
ATOM   1584 C  C     . PHE A 1 199 ? -28.169 -36.182 -19.825 1.00 206.86 ? 302  PHE A C     1 
ATOM   1585 O  O     . PHE A 1 199 ? -27.795 -37.309 -20.166 1.00 195.14 ? 302  PHE A O     1 
ATOM   1586 C  CB    . PHE A 1 199 ? -29.237 -35.503 -21.989 1.00 166.62 ? 302  PHE A CB    1 
ATOM   1587 C  CG    . PHE A 1 199 ? -30.679 -35.620 -21.580 1.00 168.85 ? 302  PHE A CG    1 
ATOM   1588 C  CD1   . PHE A 1 199 ? -31.157 -34.944 -20.468 1.00 157.78 ? 302  PHE A CD1   1 
ATOM   1589 C  CD2   . PHE A 1 199 ? -31.556 -36.412 -22.302 1.00 164.30 ? 302  PHE A CD2   1 
ATOM   1590 C  CE1   . PHE A 1 199 ? -32.481 -35.051 -20.088 1.00 138.24 ? 302  PHE A CE1   1 
ATOM   1591 C  CE2   . PHE A 1 199 ? -32.881 -36.524 -21.926 1.00 156.66 ? 302  PHE A CE2   1 
ATOM   1592 C  CZ    . PHE A 1 199 ? -33.344 -35.843 -20.818 1.00 146.70 ? 302  PHE A CZ    1 
ATOM   1593 N  N     . THR A 1 200 ? -28.468 -35.875 -18.566 1.00 214.13 ? 303  THR A N     1 
ATOM   1594 C  CA    . THR A 1 200 ? -28.376 -36.839 -17.472 1.00 216.85 ? 303  THR A CA    1 
ATOM   1595 C  C     . THR A 1 200 ? -29.785 -37.330 -17.156 1.00 203.74 ? 303  THR A C     1 
ATOM   1596 O  O     . THR A 1 200 ? -30.545 -36.660 -16.451 1.00 190.51 ? 303  THR A O     1 
ATOM   1597 C  CB    . THR A 1 200 ? -27.715 -36.214 -16.247 1.00 213.82 ? 303  THR A CB    1 
ATOM   1598 O  OG1   . THR A 1 200 ? -26.430 -35.692 -16.609 1.00 213.66 ? 303  THR A OG1   1 
ATOM   1599 C  CG2   . THR A 1 200 ? -27.543 -37.252 -15.147 1.00 183.92 ? 303  THR A CG2   1 
ATOM   1600 N  N     . MET A 1 201 ? -30.133 -38.499 -17.683 1.00 193.15 ? 304  MET A N     1 
ATOM   1601 C  CA    . MET A 1 201 ? -31.440 -39.070 -17.407 1.00 194.17 ? 304  MET A CA    1 
ATOM   1602 C  C     . MET A 1 201 ? -31.475 -39.631 -15.986 1.00 202.68 ? 304  MET A C     1 
ATOM   1603 O  O     . MET A 1 201 ? -30.487 -40.209 -15.521 1.00 196.26 ? 304  MET A O     1 
ATOM   1604 C  CB    . MET A 1 201 ? -31.774 -40.170 -18.414 1.00 197.03 ? 304  MET A CB    1 
ATOM   1605 C  CG    . MET A 1 201 ? -31.910 -39.679 -19.847 1.00 203.83 ? 304  MET A CG    1 
ATOM   1606 S  SD    . MET A 1 201 ? -32.419 -40.980 -20.988 1.00 190.52 ? 304  MET A SD    1 
ATOM   1607 C  CE    . MET A 1 201 ? -32.489 -40.073 -22.530 1.00 158.44 ? 304  MET A CE    1 
ATOM   1608 N  N     . PRO A 1 202 ? -32.592 -39.475 -15.272 1.00 207.94 ? 305  PRO A N     1 
ATOM   1609 C  CA    . PRO A 1 202 ? -32.657 -39.958 -13.885 1.00 211.50 ? 305  PRO A CA    1 
ATOM   1610 C  C     . PRO A 1 202 ? -32.713 -41.475 -13.786 1.00 209.04 ? 305  PRO A C     1 
ATOM   1611 O  O     . PRO A 1 202 ? -32.604 -42.178 -14.795 1.00 205.50 ? 305  PRO A O     1 
ATOM   1612 C  CB    . PRO A 1 202 ? -33.942 -39.312 -13.353 1.00 198.25 ? 305  PRO A CB    1 
ATOM   1613 C  CG    . PRO A 1 202 ? -34.786 -39.119 -14.567 1.00 195.20 ? 305  PRO A CG    1 
ATOM   1614 C  CD    . PRO A 1 202 ? -33.833 -38.797 -15.684 1.00 184.75 ? 305  PRO A CD    1 
ATOM   1615 N  N     . SER A 1 203 ? -32.886 -41.987 -12.566 1.00 207.00 ? 306  SER A N     1 
ATOM   1616 C  CA    . SER A 1 203 ? -32.913 -43.431 -12.359 1.00 207.21 ? 306  SER A CA    1 
ATOM   1617 C  C     . SER A 1 203 ? -34.221 -44.057 -12.822 1.00 214.55 ? 306  SER A C     1 
ATOM   1618 O  O     . SER A 1 203 ? -34.228 -45.218 -13.247 1.00 217.96 ? 306  SER A O     1 
ATOM   1619 C  CB    . SER A 1 203 ? -32.673 -43.757 -10.884 1.00 204.95 ? 306  SER A CB    1 
ATOM   1620 O  OG    . SER A 1 203 ? -33.669 -43.172 -10.063 1.00 204.48 ? 306  SER A OG    1 
ATOM   1621 N  N     . TYR A 1 204 ? -35.329 -43.319 -12.751 1.00 215.58 ? 307  TYR A N     1 
ATOM   1622 C  CA    . TYR A 1 204 ? -36.632 -43.838 -13.149 1.00 217.61 ? 307  TYR A CA    1 
ATOM   1623 C  C     . TYR A 1 204 ? -36.889 -43.722 -14.650 1.00 225.83 ? 307  TYR A C     1 
ATOM   1624 O  O     . TYR A 1 204 ? -38.052 -43.731 -15.069 1.00 228.44 ? 307  TYR A O     1 
ATOM   1625 C  CB    . TYR A 1 204 ? -37.744 -43.130 -12.369 1.00 206.94 ? 307  TYR A CB    1 
ATOM   1626 C  CG    . TYR A 1 204 ? -37.708 -41.620 -12.452 1.00 205.54 ? 307  TYR A CG    1 
ATOM   1627 C  CD1   . TYR A 1 204 ? -38.323 -40.946 -13.500 1.00 195.13 ? 307  TYR A CD1   1 
ATOM   1628 C  CD2   . TYR A 1 204 ? -37.070 -40.867 -11.475 1.00 197.25 ? 307  TYR A CD2   1 
ATOM   1629 C  CE1   . TYR A 1 204 ? -38.296 -39.566 -13.577 1.00 188.63 ? 307  TYR A CE1   1 
ATOM   1630 C  CE2   . TYR A 1 204 ? -37.038 -39.486 -11.543 1.00 211.28 ? 307  TYR A CE2   1 
ATOM   1631 C  CZ    . TYR A 1 204 ? -37.653 -38.841 -12.596 1.00 198.79 ? 307  TYR A CZ    1 
ATOM   1632 O  OH    . TYR A 1 204 ? -37.625 -37.467 -12.670 1.00 186.35 ? 307  TYR A OH    1 
ATOM   1633 N  N     . SER A 1 205 ? -35.839 -43.617 -15.462 1.00 206.81 ? 308  SER A N     1 
ATOM   1634 C  CA    . SER A 1 205 ? -35.960 -43.553 -16.917 1.00 196.81 ? 308  SER A CA    1 
ATOM   1635 C  C     . SER A 1 205 ? -35.694 -44.906 -17.564 1.00 213.19 ? 308  SER A C     1 
ATOM   1636 O  O     . SER A 1 205 ? -35.101 -44.985 -18.643 1.00 227.16 ? 308  SER A O     1 
ATOM   1637 C  CB    . SER A 1 205 ? -35.016 -42.495 -17.480 1.00 191.59 ? 308  SER A CB    1 
ATOM   1638 O  OG    . SER A 1 205 ? -33.669 -42.784 -17.149 1.00 191.30 ? 308  SER A OG    1 
ATOM   1639 N  N     . ARG A 1 206 ? -36.126 -45.985 -16.921 1.00 212.37 ? 309  ARG A N     1 
ATOM   1640 C  CA    . ARG A 1 206 ? -35.870 -47.332 -17.402 1.00 218.22 ? 309  ARG A CA    1 
ATOM   1641 C  C     . ARG A 1 206 ? -36.938 -47.761 -18.404 1.00 226.59 ? 309  ARG A C     1 
ATOM   1642 O  O     . ARG A 1 206 ? -38.039 -47.207 -18.456 1.00 224.33 ? 309  ARG A O     1 
ATOM   1643 C  CB    . ARG A 1 206 ? -35.821 -48.315 -16.232 1.00 214.78 ? 309  ARG A CB    1 
ATOM   1644 C  CG    . ARG A 1 206 ? -35.053 -47.792 -15.030 1.00 202.63 ? 309  ARG A CG    1 
ATOM   1645 C  CD    . ARG A 1 206 ? -35.105 -48.760 -13.861 1.00 198.31 ? 309  ARG A CD    1 
ATOM   1646 N  NE    . ARG A 1 206 ? -34.650 -48.137 -12.624 1.00 218.65 ? 309  ARG A NE    1 
ATOM   1647 C  CZ    . ARG A 1 206 ? -33.382 -48.059 -12.244 1.00 228.18 ? 309  ARG A CZ    1 
ATOM   1648 N  NH1   . ARG A 1 206 ? -32.406 -48.560 -12.984 1.00 224.47 ? 309  ARG A NH1   1 
ATOM   1649 N  NH2   . ARG A 1 206 ? -33.085 -47.462 -11.093 1.00 202.76 ? 309  ARG A NH2   1 
ATOM   1650 N  N     . ARG A 1 207 ? -36.594 -48.764 -19.206 1.00 219.28 ? 310  ARG A N     1 
ATOM   1651 C  CA    . ARG A 1 207 ? -37.510 -49.293 -20.210 1.00 220.86 ? 310  ARG A CA    1 
ATOM   1652 C  C     . ARG A 1 207 ? -38.547 -50.212 -19.570 1.00 220.08 ? 310  ARG A C     1 
ATOM   1653 O  O     . ARG A 1 207 ? -39.726 -49.869 -19.486 1.00 203.28 ? 310  ARG A O     1 
ATOM   1654 C  CB    . ARG A 1 207 ? -36.734 -50.040 -21.299 1.00 214.28 ? 310  ARG A CB    1 
ATOM   1655 C  CG    . ARG A 1 207 ? -37.606 -50.707 -22.354 1.00 204.58 ? 310  ARG A CG    1 
ATOM   1656 C  CD    . ARG A 1 207 ? -37.653 -52.216 -22.163 1.00 206.62 ? 310  ARG A CD    1 
ATOM   1657 N  NE    . ARG A 1 207 ? -38.484 -52.871 -23.165 1.00 217.73 ? 310  ARG A NE    1 
ATOM   1658 C  CZ    . ARG A 1 207 ? -38.679 -54.181 -23.237 1.00 220.56 ? 310  ARG A CZ    1 
ATOM   1659 N  NH1   . ARG A 1 207 ? -38.113 -55.012 -22.376 1.00 190.16 ? 310  ARG A NH1   1 
ATOM   1660 N  NH2   . ARG A 1 207 ? -39.461 -54.669 -24.195 1.00 215.17 ? 310  ARG A NH2   1 
ATOM   1661 N  N     . SER A 1 220 ? -59.025 -59.062 -24.219 1.00 190.62 ? 323  SER A N     1 
ATOM   1662 C  CA    . SER A 1 220 ? -59.864 -58.782 -25.378 1.00 198.68 ? 323  SER A CA    1 
ATOM   1663 C  C     . SER A 1 220 ? -59.683 -57.341 -25.843 1.00 199.45 ? 323  SER A C     1 
ATOM   1664 O  O     . SER A 1 220 ? -59.296 -57.093 -26.985 1.00 217.96 ? 323  SER A O     1 
ATOM   1665 C  CB    . SER A 1 220 ? -61.335 -59.055 -25.054 1.00 192.31 ? 323  SER A CB    1 
ATOM   1666 O  OG    . SER A 1 220 ? -62.155 -58.853 -26.191 1.00 184.91 ? 323  SER A OG    1 
ATOM   1667 N  N     . THR A 1 221 ? -59.964 -56.400 -24.941 1.00 175.96 ? 324  THR A N     1 
ATOM   1668 C  CA    . THR A 1 221 ? -59.832 -54.964 -25.191 1.00 183.02 ? 324  THR A CA    1 
ATOM   1669 C  C     . THR A 1 221 ? -60.622 -54.546 -26.435 1.00 193.53 ? 324  THR A C     1 
ATOM   1670 O  O     . THR A 1 221 ? -60.072 -54.207 -27.483 1.00 201.36 ? 324  THR A O     1 
ATOM   1671 C  CB    . THR A 1 221 ? -58.359 -54.559 -25.314 1.00 187.33 ? 324  THR A CB    1 
ATOM   1672 O  OG1   . THR A 1 221 ? -57.804 -55.106 -26.517 1.00 220.30 ? 324  THR A OG1   1 
ATOM   1673 C  CG2   . THR A 1 221 ? -57.564 -55.067 -24.119 1.00 193.88 ? 324  THR A CG2   1 
ATOM   1674 N  N     . LYS A 1 222 ? -61.944 -54.579 -26.282 1.00 168.58 ? 325  LYS A N     1 
ATOM   1675 C  CA    . LYS A 1 222 ? -62.841 -54.177 -27.353 1.00 155.73 ? 325  LYS A CA    1 
ATOM   1676 C  C     . LYS A 1 222 ? -63.007 -52.659 -27.358 1.00 144.43 ? 325  LYS A C     1 
ATOM   1677 O  O     . LYS A 1 222 ? -62.437 -51.938 -26.534 1.00 161.63 ? 325  LYS A O     1 
ATOM   1678 C  CB    . LYS A 1 222 ? -64.188 -54.883 -27.212 1.00 160.31 ? 325  LYS A CB    1 
ATOM   1679 C  CG    . LYS A 1 222 ? -64.102 -56.400 -27.275 1.00 194.36 ? 325  LYS A CG    1 
ATOM   1680 C  CD    . LYS A 1 222 ? -63.441 -56.868 -28.564 1.00 208.41 ? 325  LYS A CD    1 
ATOM   1681 C  CE    . LYS A 1 222 ? -64.260 -56.483 -29.786 1.00 197.94 ? 325  LYS A CE    1 
ATOM   1682 N  NZ    . LYS A 1 222 ? -63.595 -56.898 -31.052 1.00 189.47 ? 325  LYS A NZ    1 
ATOM   1683 N  N     . SER A 1 223 ? -63.801 -52.163 -28.301 1.00 138.57 ? 326  SER A N     1 
ATOM   1684 C  CA    . SER A 1 223 ? -64.004 -50.732 -28.456 1.00 129.89 ? 326  SER A CA    1 
ATOM   1685 C  C     . SER A 1 223 ? -65.228 -50.269 -27.671 1.00 136.36 ? 326  SER A C     1 
ATOM   1686 O  O     . SER A 1 223 ? -65.974 -51.063 -27.094 1.00 162.12 ? 326  SER A O     1 
ATOM   1687 C  CB    . SER A 1 223 ? -64.149 -50.368 -29.934 1.00 150.45 ? 326  SER A CB    1 
ATOM   1688 O  OG    . SER A 1 223 ? -65.289 -50.989 -30.502 1.00 171.17 ? 326  SER A OG    1 
ATOM   1689 N  N     . LEU A 1 224 ? -65.428 -48.950 -27.655 1.00 142.80 ? 327  LEU A N     1 
ATOM   1690 C  CA    . LEU A 1 224 ? -66.563 -48.370 -26.946 1.00 129.91 ? 327  LEU A CA    1 
ATOM   1691 C  C     . LEU A 1 224 ? -67.841 -48.425 -27.772 1.00 125.42 ? 327  LEU A C     1 
ATOM   1692 O  O     . LEU A 1 224 ? -68.931 -48.577 -27.209 1.00 144.32 ? 327  LEU A O     1 
ATOM   1693 C  CB    . LEU A 1 224 ? -66.253 -46.923 -26.559 1.00 121.02 ? 327  LEU A CB    1 
ATOM   1694 C  CG    . LEU A 1 224 ? -67.332 -46.156 -25.791 1.00 134.02 ? 327  LEU A CG    1 
ATOM   1695 C  CD1   . LEU A 1 224 ? -67.451 -46.672 -24.366 1.00 127.30 ? 327  LEU A CD1   1 
ATOM   1696 C  CD2   . LEU A 1 224 ? -67.047 -44.662 -25.807 1.00 117.31 ? 327  LEU A CD2   1 
ATOM   1697 N  N     . TRP A 1 225 ? -67.730 -48.312 -29.095 1.00 127.36 ? 328  TRP A N     1 
ATOM   1698 C  CA    . TRP A 1 225 ? -68.885 -48.264 -29.982 1.00 144.59 ? 328  TRP A CA    1 
ATOM   1699 C  C     . TRP A 1 225 ? -69.429 -49.646 -30.338 1.00 170.47 ? 328  TRP A C     1 
ATOM   1700 O  O     . TRP A 1 225 ? -70.089 -49.789 -31.375 1.00 146.92 ? 328  TRP A O     1 
ATOM   1701 C  CB    . TRP A 1 225 ? -68.531 -47.492 -31.256 1.00 140.95 ? 328  TRP A CB    1 
ATOM   1702 C  CG    . TRP A 1 225 ? -68.291 -46.032 -31.014 1.00 136.73 ? 328  TRP A CG    1 
ATOM   1703 C  CD1   . TRP A 1 225 ? -68.493 -45.353 -29.848 1.00 154.89 ? 328  TRP A CD1   1 
ATOM   1704 C  CD2   . TRP A 1 225 ? -67.802 -45.071 -31.957 1.00 146.71 ? 328  TRP A CD2   1 
ATOM   1705 N  NE1   . TRP A 1 225 ? -68.164 -44.029 -30.007 1.00 161.50 ? 328  TRP A NE1   1 
ATOM   1706 C  CE2   . TRP A 1 225 ? -67.736 -43.830 -31.292 1.00 145.37 ? 328  TRP A CE2   1 
ATOM   1707 C  CE3   . TRP A 1 225 ? -67.414 -45.138 -33.299 1.00 139.69 ? 328  TRP A CE3   1 
ATOM   1708 C  CZ2   . TRP A 1 225 ? -67.298 -42.667 -31.923 1.00 138.45 ? 328  TRP A CZ2   1 
ATOM   1709 C  CZ3   . TRP A 1 225 ? -66.979 -43.981 -33.922 1.00 144.62 ? 328  TRP A CZ3   1 
ATOM   1710 C  CH2   . TRP A 1 225 ? -66.926 -42.763 -33.235 1.00 134.14 ? 328  TRP A CH2   1 
ATOM   1711 N  N     . VAL A 1 226 ? -69.173 -50.660 -29.512 1.00 169.34 ? 329  VAL A N     1 
ATOM   1712 C  CA    . VAL A 1 226 ? -69.716 -51.996 -29.735 1.00 161.48 ? 329  VAL A CA    1 
ATOM   1713 C  C     . VAL A 1 226 ? -70.376 -52.484 -28.452 1.00 177.07 ? 329  VAL A C     1 
ATOM   1714 O  O     . VAL A 1 226 ? -70.764 -53.653 -28.346 1.00 181.95 ? 329  VAL A O     1 
ATOM   1715 C  CB    . VAL A 1 226 ? -68.627 -52.979 -30.203 1.00 157.84 ? 329  VAL A CB    1 
ATOM   1716 C  CG1   . VAL A 1 226 ? -68.068 -52.555 -31.554 1.00 166.48 ? 329  VAL A CG1   1 
ATOM   1717 C  CG2   . VAL A 1 226 ? -67.520 -53.079 -29.166 1.00 163.17 ? 329  VAL A CG2   1 
ATOM   1718 N  N     . ILE A 1 227 ? -70.506 -51.591 -27.471 1.00 163.72 ? 330  ILE A N     1 
ATOM   1719 C  CA    . ILE A 1 227 ? -71.114 -51.962 -26.198 1.00 127.83 ? 330  ILE A CA    1 
ATOM   1720 C  C     . ILE A 1 227 ? -72.631 -52.004 -26.315 1.00 177.72 ? 330  ILE A C     1 
ATOM   1721 O  O     . ILE A 1 227 ? -73.263 -53.018 -25.998 1.00 212.54 ? 330  ILE A O     1 
ATOM   1722 C  CB    . ILE A 1 227 ? -70.659 -50.995 -25.089 1.00 113.50 ? 330  ILE A CB    1 
ATOM   1723 C  CG1   . ILE A 1 227 ? -69.158 -51.146 -24.836 1.00 148.65 ? 330  ILE A CG1   1 
ATOM   1724 C  CG2   . ILE A 1 227 ? -71.449 -51.238 -23.814 1.00 128.79 ? 330  ILE A CG2   1 
ATOM   1725 C  CD1   . ILE A 1 227 ? -68.749 -52.541 -24.417 1.00 122.27 ? 330  ILE A CD1   1 
ATOM   1726 N  N     . ASN A 1 228 ? -73.234 -50.902 -26.767 1.00 165.97 ? 331  ASN A N     1 
ATOM   1727 C  CA    . ASN A 1 228 ? -74.681 -50.797 -26.964 1.00 178.45 ? 331  ASN A CA    1 
ATOM   1728 C  C     . ASN A 1 228 ? -75.434 -51.059 -25.657 1.00 177.25 ? 331  ASN A C     1 
ATOM   1729 O  O     . ASN A 1 228 ? -76.237 -51.986 -25.539 1.00 187.90 ? 331  ASN A O     1 
ATOM   1730 C  CB    . ASN A 1 228 ? -75.153 -51.739 -28.077 1.00 179.45 ? 331  ASN A CB    1 
ATOM   1731 C  CG    . ASN A 1 228 ? -74.440 -51.488 -29.392 1.00 200.54 ? 331  ASN A CG    1 
ATOM   1732 O  OD1   . ASN A 1 228 ? -74.101 -50.351 -29.721 1.00 200.66 ? 331  ASN A OD1   1 
ATOM   1733 N  ND2   . ASN A 1 228 ? -74.205 -52.552 -30.150 1.00 201.11 ? 331  ASN A ND2   1 
ATOM   1734 N  N     . SER A 1 229 ? -75.156 -50.212 -24.669 1.00 165.30 ? 332  SER A N     1 
ATOM   1735 C  CA    . SER A 1 229 ? -75.796 -50.302 -23.365 1.00 158.05 ? 332  SER A CA    1 
ATOM   1736 C  C     . SER A 1 229 ? -75.963 -48.894 -22.809 1.00 165.29 ? 332  SER A C     1 
ATOM   1737 O  O     . SER A 1 229 ? -75.545 -47.908 -23.424 1.00 158.08 ? 332  SER A O     1 
ATOM   1738 C  CB    . SER A 1 229 ? -74.989 -51.192 -22.414 1.00 150.83 ? 332  SER A CB    1 
ATOM   1739 O  OG    . SER A 1 229 ? -75.565 -51.212 -21.120 1.00 161.14 ? 332  SER A OG    1 
ATOM   1740 N  N     . ALA A 1 230 ? -76.582 -48.805 -21.637 1.00 160.54 ? 333  ALA A N     1 
ATOM   1741 C  CA    . ALA A 1 230 ? -76.806 -47.535 -20.963 1.00 113.70 ? 333  ALA A CA    1 
ATOM   1742 C  C     . ALA A 1 230 ? -75.780 -47.348 -19.854 1.00 117.85 ? 333  ALA A C     1 
ATOM   1743 O  O     . ALA A 1 230 ? -75.400 -48.307 -19.176 1.00 121.04 ? 333  ALA A O     1 
ATOM   1744 C  CB    . ALA A 1 230 ? -78.220 -47.462 -20.385 1.00 167.53 ? 333  ALA A CB    1 
ATOM   1745 N  N     . LEU A 1 231 ? -75.329 -46.108 -19.679 1.00 118.77 ? 334  LEU A N     1 
ATOM   1746 C  CA    . LEU A 1 231 ? -74.337 -45.804 -18.655 1.00 112.29 ? 334  LEU A CA    1 
ATOM   1747 C  C     . LEU A 1 231 ? -74.961 -45.949 -17.272 1.00 123.62 ? 334  LEU A C     1 
ATOM   1748 O  O     . LEU A 1 231 ? -75.970 -45.305 -16.966 1.00 140.62 ? 334  LEU A O     1 
ATOM   1749 C  CB    . LEU A 1 231 ? -73.784 -44.396 -18.851 1.00 106.41 ? 334  LEU A CB    1 
ATOM   1750 C  CG    . LEU A 1 231 ? -72.724 -43.965 -17.835 1.00 111.18 ? 334  LEU A CG    1 
ATOM   1751 C  CD1   . LEU A 1 231 ? -71.537 -44.914 -17.868 1.00 135.27 ? 334  LEU A CD1   1 
ATOM   1752 C  CD2   . LEU A 1 231 ? -72.278 -42.535 -18.089 1.00 115.51 ? 334  LEU A CD2   1 
ATOM   1753 N  N     . ARG A 1 232 ? -74.360 -46.795 -16.438 1.00 112.30 ? 335  ARG A N     1 
ATOM   1754 C  CA    . ARG A 1 232 ? -74.870 -47.062 -15.099 1.00 132.60 ? 335  ARG A CA    1 
ATOM   1755 C  C     . ARG A 1 232 ? -73.704 -47.078 -14.124 1.00 139.53 ? 335  ARG A C     1 
ATOM   1756 O  O     . ARG A 1 232 ? -72.811 -47.923 -14.235 1.00 169.05 ? 335  ARG A O     1 
ATOM   1757 C  CB    . ARG A 1 232 ? -75.638 -48.388 -15.056 1.00 141.39 ? 335  ARG A CB    1 
ATOM   1758 C  CG    . ARG A 1 232 ? -74.996 -49.508 -15.863 1.00 154.41 ? 335  ARG A CG    1 
ATOM   1759 C  CD    . ARG A 1 232 ? -75.895 -50.731 -15.933 1.00 149.23 ? 335  ARG A CD    1 
ATOM   1760 N  NE    . ARG A 1 232 ? -76.109 -51.335 -14.624 1.00 165.19 ? 335  ARG A NE    1 
ATOM   1761 C  CZ    . ARG A 1 232 ? -75.359 -52.303 -14.115 1.00 161.98 ? 335  ARG A CZ    1 
ATOM   1762 N  NH1   . ARG A 1 232 ? -74.324 -52.795 -14.775 1.00 176.98 ? 335  ARG A NH1   1 
ATOM   1763 N  NH2   . ARG A 1 232 ? -75.656 -52.791 -12.914 1.00 143.52 ? 335  ARG A NH2   1 
ATOM   1764 N  N     . ILE A 1 233 ? -73.710 -46.141 -13.179 1.00 118.47 ? 336  ILE A N     1 
ATOM   1765 C  CA    . ILE A 1 233 ? -72.678 -46.035 -12.157 1.00 125.14 ? 336  ILE A CA    1 
ATOM   1766 C  C     . ILE A 1 233 ? -73.338 -46.184 -10.794 1.00 132.44 ? 336  ILE A C     1 
ATOM   1767 O  O     . ILE A 1 233 ? -74.388 -45.584 -10.535 1.00 149.88 ? 336  ILE A O     1 
ATOM   1768 C  CB    . ILE A 1 233 ? -71.914 -44.697 -12.250 1.00 136.03 ? 336  ILE A CB    1 
ATOM   1769 C  CG1   . ILE A 1 233 ? -71.493 -44.416 -13.695 1.00 156.37 ? 336  ILE A CG1   1 
ATOM   1770 C  CG2   . ILE A 1 233 ? -70.701 -44.709 -11.333 1.00 142.28 ? 336  ILE A CG2   1 
ATOM   1771 C  CD1   . ILE A 1 233 ? -70.628 -45.494 -14.309 1.00 165.21 ? 336  ILE A CD1   1 
ATOM   1772 N  N     . LYS A 1 234 ? -72.726 -46.983 -9.927  1.00 136.58 ? 337  LYS A N     1 
ATOM   1773 C  CA    . LYS A 1 234 ? -73.254 -47.250 -8.597  1.00 148.83 ? 337  LYS A CA    1 
ATOM   1774 C  C     . LYS A 1 234 ? -72.388 -46.582 -7.538  1.00 152.12 ? 337  LYS A C     1 
ATOM   1775 O  O     . LYS A 1 234 ? -71.156 -46.640 -7.602  1.00 159.22 ? 337  LYS A O     1 
ATOM   1776 C  CB    . LYS A 1 234 ? -73.332 -48.755 -8.323  1.00 165.11 ? 337  LYS A CB    1 
ATOM   1777 C  CG    . LYS A 1 234 ? -73.697 -49.102 -6.885  1.00 156.78 ? 337  LYS A CG    1 
ATOM   1778 C  CD    . LYS A 1 234 ? -73.816 -50.602 -6.679  1.00 171.85 ? 337  LYS A CD    1 
ATOM   1779 C  CE    . LYS A 1 234 ? -72.547 -51.323 -7.101  1.00 185.18 ? 337  LYS A CE    1 
ATOM   1780 N  NZ    . LYS A 1 234 ? -72.661 -52.797 -6.927  1.00 174.41 ? 337  LYS A NZ    1 
ATOM   1781 N  N     . ILE A 1 235 ? -73.041 -45.948 -6.569  1.00 151.58 ? 338  ILE A N     1 
ATOM   1782 C  CA    . ILE A 1 235 ? -72.378 -45.400 -5.392  1.00 148.04 ? 338  ILE A CA    1 
ATOM   1783 C  C     . ILE A 1 235 ? -72.551 -46.403 -4.260  1.00 147.80 ? 338  ILE A C     1 
ATOM   1784 O  O     . ILE A 1 235 ? -73.681 -46.742 -3.886  1.00 146.15 ? 338  ILE A O     1 
ATOM   1785 C  CB    . ILE A 1 235 ? -72.942 -44.021 -5.011  1.00 144.25 ? 338  ILE A CB    1 
ATOM   1786 C  CG1   . ILE A 1 235 ? -72.313 -42.917 -5.869  1.00 142.58 ? 338  ILE A CG1   1 
ATOM   1787 C  CG2   . ILE A 1 235 ? -72.704 -43.732 -3.537  1.00 146.45 ? 338  ILE A CG2   1 
ATOM   1788 C  CD1   . ILE A 1 235 ? -72.828 -42.850 -7.291  1.00 128.63 ? 338  ILE A CD1   1 
ATOM   1789 N  N     . LEU A 1 236 ? -71.433 -46.892 -3.722  1.00 171.77 ? 339  LEU A N     1 
ATOM   1790 C  CA    . LEU A 1 236 ? -71.488 -47.910 -2.673  1.00 177.16 ? 339  LEU A CA    1 
ATOM   1791 C  C     . LEU A 1 236 ? -71.756 -47.284 -1.308  1.00 167.17 ? 339  LEU A C     1 
ATOM   1792 O  O     . LEU A 1 236 ? -72.858 -47.401 -0.763  1.00 168.10 ? 339  LEU A O     1 
ATOM   1793 C  CB    . LEU A 1 236 ? -70.187 -48.721 -2.661  1.00 164.99 ? 339  LEU A CB    1 
ATOM   1794 C  CG    . LEU A 1 236 ? -70.002 -49.714 -3.811  1.00 179.83 ? 339  LEU A CG    1 
ATOM   1795 C  CD1   . LEU A 1 236 ? -68.632 -50.369 -3.742  1.00 178.05 ? 339  LEU A CD1   1 
ATOM   1796 C  CD2   . LEU A 1 236 ? -71.102 -50.764 -3.785  1.00 190.91 ? 339  LEU A CD2   1 
ATOM   1797 N  N     . CYS A 1 237 ? -70.756 -46.616 -0.742  1.00 166.69 ? 340  CYS A N     1 
ATOM   1798 C  CA    . CYS A 1 237 ? -70.882 -46.016 0.579   1.00 166.23 ? 340  CYS A CA    1 
ATOM   1799 C  C     . CYS A 1 237 ? -70.051 -44.738 0.613   1.00 167.07 ? 340  CYS A C     1 
ATOM   1800 O  O     . CYS A 1 237 ? -69.636 -44.217 -0.427  1.00 180.43 ? 340  CYS A O     1 
ATOM   1801 C  CB    . CYS A 1 237 ? -70.459 -47.011 1.667   1.00 180.19 ? 340  CYS A CB    1 
ATOM   1802 S  SG    . CYS A 1 237 ? -68.753 -47.591 1.528   1.00 193.29 ? 340  CYS A SG    1 
ATOM   1803 N  N     . ALA A 1 238 ? -69.809 -44.232 1.820   1.00 161.58 ? 341  ALA A N     1 
ATOM   1804 C  CA    . ALA A 1 238 ? -69.027 -43.017 2.005   1.00 159.17 ? 341  ALA A CA    1 
ATOM   1805 C  C     . ALA A 1 238 ? -68.476 -43.005 3.424   1.00 162.49 ? 341  ALA A C     1 
ATOM   1806 O  O     . ALA A 1 238 ? -68.864 -43.813 4.270   1.00 196.19 ? 341  ALA A O     1 
ATOM   1807 C  CB    . ALA A 1 238 ? -69.863 -41.764 1.730   1.00 140.80 ? 341  ALA A CB    1 
ATOM   1808 N  N     . THR A 1 239 ? -67.558 -42.074 3.670   1.00 132.50 ? 342  THR A N     1 
ATOM   1809 C  CA    . THR A 1 239 ? -66.955 -41.884 4.981   1.00 151.04 ? 342  THR A CA    1 
ATOM   1810 C  C     . THR A 1 239 ? -67.108 -40.427 5.397   1.00 169.11 ? 342  THR A C     1 
ATOM   1811 O  O     . THR A 1 239 ? -67.438 -39.557 4.586   1.00 145.58 ? 342  THR A O     1 
ATOM   1812 C  CB    . THR A 1 239 ? -65.472 -42.286 4.988   1.00 150.86 ? 342  THR A CB    1 
ATOM   1813 O  OG1   . THR A 1 239 ? -64.744 -41.453 4.078   1.00 171.03 ? 342  THR A OG1   1 
ATOM   1814 C  CG2   . THR A 1 239 ? -65.308 -43.743 4.579   1.00 133.61 ? 342  THR A CG2   1 
ATOM   1815 N  N     . TYR A 1 240 ? -66.861 -40.173 6.681   1.00 178.87 ? 343  TYR A N     1 
ATOM   1816 C  CA    . TYR A 1 240 ? -66.965 -38.834 7.263   1.00 179.01 ? 343  TYR A CA    1 
ATOM   1817 C  C     . TYR A 1 240 ? -68.337 -38.211 7.018   1.00 171.73 ? 343  TYR A C     1 
ATOM   1818 O  O     . TYR A 1 240 ? -68.440 -37.082 6.539   1.00 144.60 ? 343  TYR A O     1 
ATOM   1819 C  CB    . TYR A 1 240 ? -65.869 -37.918 6.710   1.00 169.88 ? 343  TYR A CB    1 
ATOM   1820 C  CG    . TYR A 1 240 ? -64.472 -38.282 7.160   1.00 177.14 ? 343  TYR A CG    1 
ATOM   1821 C  CD1   . TYR A 1 240 ? -63.753 -39.284 6.520   1.00 175.72 ? 343  TYR A CD1   1 
ATOM   1822 C  CD2   . TYR A 1 240 ? -63.869 -37.618 8.221   1.00 182.35 ? 343  TYR A CD2   1 
ATOM   1823 C  CE1   . TYR A 1 240 ? -62.475 -39.618 6.928   1.00 186.67 ? 343  TYR A CE1   1 
ATOM   1824 C  CE2   . TYR A 1 240 ? -62.592 -37.945 8.635   1.00 188.22 ? 343  TYR A CE2   1 
ATOM   1825 C  CZ    . TYR A 1 240 ? -61.899 -38.945 7.986   1.00 188.70 ? 343  TYR A CZ    1 
ATOM   1826 O  OH    . TYR A 1 240 ? -60.627 -39.273 8.395   1.00 176.38 ? 343  TYR A OH    1 
ATOM   1827 N  N     . LYS A 1 250 ? -80.779 -35.301 6.568   1.00 139.45 ? 353  LYS A N     1 
ATOM   1828 C  CA    . LYS A 1 250 ? -81.042 -35.920 5.274   1.00 174.75 ? 353  LYS A CA    1 
ATOM   1829 C  C     . LYS A 1 250 ? -80.122 -35.352 4.198   1.00 185.18 ? 353  LYS A C     1 
ATOM   1830 O  O     . LYS A 1 250 ? -80.096 -34.143 3.966   1.00 163.74 ? 353  LYS A O     1 
ATOM   1831 C  CB    . LYS A 1 250 ? -82.506 -35.722 4.873   1.00 164.54 ? 353  LYS A CB    1 
ATOM   1832 N  N     . ILE A 1 251 ? -79.362 -36.233 3.545   1.00 195.68 ? 354  ILE A N     1 
ATOM   1833 C  CA    . ILE A 1 251 ? -78.431 -35.851 2.490   1.00 178.85 ? 354  ILE A CA    1 
ATOM   1834 C  C     . ILE A 1 251 ? -78.577 -36.825 1.328   1.00 181.20 ? 354  ILE A C     1 
ATOM   1835 O  O     . ILE A 1 251 ? -79.225 -37.867 1.434   1.00 163.17 ? 354  ILE A O     1 
ATOM   1836 C  CB    . ILE A 1 251 ? -76.966 -35.819 2.978   1.00 155.34 ? 354  ILE A CB    1 
ATOM   1837 C  CG1   . ILE A 1 251 ? -76.561 -37.181 3.545   1.00 150.76 ? 354  ILE A CG1   1 
ATOM   1838 C  CG2   . ILE A 1 251 ? -76.763 -34.717 4.009   1.00 165.51 ? 354  ILE A CG2   1 
ATOM   1839 C  CD1   . ILE A 1 251 ? -75.125 -37.243 4.016   1.00 129.23 ? 354  ILE A CD1   1 
ATOM   1840 N  N     . TYR A 1 252 ? -77.961 -36.467 0.205   1.00 161.69 ? 355  TYR A N     1 
ATOM   1841 C  CA    . TYR A 1 252 ? -77.946 -37.312 -0.982  1.00 153.38 ? 355  TYR A CA    1 
ATOM   1842 C  C     . TYR A 1 252 ? -76.770 -36.882 -1.851  1.00 146.70 ? 355  TYR A C     1 
ATOM   1843 O  O     . TYR A 1 252 ? -76.025 -35.960 -1.508  1.00 153.95 ? 355  TYR A O     1 
ATOM   1844 C  CB    . TYR A 1 252 ? -79.278 -37.237 -1.737  1.00 158.48 ? 355  TYR A CB    1 
ATOM   1845 C  CG    . TYR A 1 252 ? -79.572 -35.890 -2.357  1.00 174.34 ? 355  TYR A CG    1 
ATOM   1846 C  CD1   . TYR A 1 252 ? -80.041 -34.834 -1.587  1.00 181.09 ? 355  TYR A CD1   1 
ATOM   1847 C  CD2   . TYR A 1 252 ? -79.392 -35.679 -3.717  1.00 180.20 ? 355  TYR A CD2   1 
ATOM   1848 C  CE1   . TYR A 1 252 ? -80.313 -33.602 -2.153  1.00 183.26 ? 355  TYR A CE1   1 
ATOM   1849 C  CE2   . TYR A 1 252 ? -79.664 -34.453 -4.290  1.00 175.37 ? 355  TYR A CE2   1 
ATOM   1850 C  CZ    . TYR A 1 252 ? -80.123 -33.418 -3.505  1.00 182.94 ? 355  TYR A CZ    1 
ATOM   1851 O  OH    . TYR A 1 252 ? -80.393 -32.195 -4.076  1.00 167.02 ? 355  TYR A OH    1 
ATOM   1852 N  N     . VAL A 1 253 ? -76.606 -37.561 -2.984  1.00 143.86 ? 356  VAL A N     1 
ATOM   1853 C  CA    . VAL A 1 253 ? -75.473 -37.348 -3.878  1.00 156.28 ? 356  VAL A CA    1 
ATOM   1854 C  C     . VAL A 1 253 ? -76.003 -36.916 -5.238  1.00 151.13 ? 356  VAL A C     1 
ATOM   1855 O  O     . VAL A 1 253 ? -76.830 -37.614 -5.838  1.00 129.89 ? 356  VAL A O     1 
ATOM   1856 C  CB    . VAL A 1 253 ? -74.604 -38.610 -4.006  1.00 119.12 ? 356  VAL A CB    1 
ATOM   1857 C  CG1   . VAL A 1 253 ? -73.471 -38.375 -4.992  1.00 163.53 ? 356  VAL A CG1   1 
ATOM   1858 C  CG2   . VAL A 1 253 ? -74.056 -39.020 -2.648  1.00 121.13 ? 356  VAL A CG2   1 
ATOM   1859 N  N     . ARG A 1 254 ? -75.525 -35.772 -5.722  1.00 149.62 ? 357  ARG A N     1 
ATOM   1860 C  CA    . ARG A 1 254 ? -75.849 -35.291 -7.059  1.00 150.78 ? 357  ARG A CA    1 
ATOM   1861 C  C     . ARG A 1 254 ? -74.790 -35.790 -8.035  1.00 158.99 ? 357  ARG A C     1 
ATOM   1862 O  O     . ARG A 1 254 ? -73.613 -35.434 -7.918  1.00 153.17 ? 357  ARG A O     1 
ATOM   1863 C  CB    . ARG A 1 254 ? -75.930 -33.765 -7.091  1.00 151.32 ? 357  ARG A CB    1 
ATOM   1864 C  CG    . ARG A 1 254 ? -77.225 -33.199 -6.539  1.00 181.77 ? 357  ARG A CG    1 
ATOM   1865 C  CD    . ARG A 1 254 ? -78.410 -33.618 -7.392  1.00 182.35 ? 357  ARG A CD    1 
ATOM   1866 N  NE    . ARG A 1 254 ? -78.562 -32.795 -8.584  1.00 162.04 ? 357  ARG A NE    1 
ATOM   1867 C  CZ    . ARG A 1 254 ? -79.470 -31.837 -8.719  1.00 164.72 ? 357  ARG A CZ    1 
ATOM   1868 N  NH1   . ARG A 1 254 ? -80.329 -31.559 -7.752  1.00 173.76 ? 357  ARG A NH1   1 
ATOM   1869 N  NH2   . ARG A 1 254 ? -79.520 -31.146 -9.854  1.00 175.70 ? 357  ARG A NH2   1 
ATOM   1870 N  N     . THR A 1 255 ? -75.208 -36.614 -8.990  1.00 154.39 ? 358  THR A N     1 
ATOM   1871 C  CA    . THR A 1 255 ? -74.318 -37.180 -9.993  1.00 118.90 ? 358  THR A CA    1 
ATOM   1872 C  C     . THR A 1 255 ? -74.694 -36.638 -11.365 1.00 132.82 ? 358  THR A C     1 
ATOM   1873 O  O     . THR A 1 255 ? -75.878 -36.589 -11.715 1.00 134.52 ? 358  THR A O     1 
ATOM   1874 C  CB    . THR A 1 255 ? -74.389 -38.709 -9.994  1.00 123.54 ? 358  THR A CB    1 
ATOM   1875 O  OG1   . THR A 1 255 ? -75.645 -39.129 -10.540 1.00 149.26 ? 358  THR A OG1   1 
ATOM   1876 C  CG2   . THR A 1 255 ? -74.261 -39.250 -8.578  1.00 152.23 ? 358  THR A CG2   1 
ATOM   1877 N  N     . GLY A 1 256 ? -73.694 -36.234 -12.133 1.00 138.10 ? 359  GLY A N     1 
ATOM   1878 C  CA    . GLY A 1 256 ? -73.937 -35.695 -13.459 1.00 134.66 ? 359  GLY A CA    1 
ATOM   1879 C  C     . GLY A 1 256 ? -72.787 -35.999 -14.389 1.00 129.81 ? 359  GLY A C     1 
ATOM   1880 O  O     . GLY A 1 256 ? -71.623 -36.036 -13.976 1.00 124.17 ? 359  GLY A O     1 
ATOM   1881 N  N     . ILE A 1 257 ? -73.119 -36.223 -15.657 1.00 109.70 ? 360  ILE A N     1 
ATOM   1882 C  CA    . ILE A 1 257 ? -72.132 -36.454 -16.705 1.00 133.62 ? 360  ILE A CA    1 
ATOM   1883 C  C     . ILE A 1 257 ? -72.022 -35.178 -17.528 1.00 132.36 ? 360  ILE A C     1 
ATOM   1884 O  O     . ILE A 1 257 ? -73.008 -34.725 -18.122 1.00 118.24 ? 360  ILE A O     1 
ATOM   1885 C  CB    . ILE A 1 257 ? -72.507 -37.659 -17.585 1.00 126.77 ? 360  ILE A CB    1 
ATOM   1886 C  CG1   . ILE A 1 257 ? -72.136 -38.975 -16.895 1.00 121.00 ? 360  ILE A CG1   1 
ATOM   1887 C  CG2   . ILE A 1 257 ? -71.813 -37.572 -18.938 1.00 138.53 ? 360  ILE A CG2   1 
ATOM   1888 C  CD1   . ILE A 1 257 ? -73.086 -39.401 -15.798 1.00 119.02 ? 360  ILE A CD1   1 
ATOM   1889 N  N     . TYR A 1 258 ? -70.828 -34.593 -17.557 1.00 131.27 ? 361  TYR A N     1 
ATOM   1890 C  CA    . TYR A 1 258 ? -70.603 -33.312 -18.207 1.00 135.62 ? 361  TYR A CA    1 
ATOM   1891 C  C     . TYR A 1 258 ? -69.450 -33.422 -19.194 1.00 135.40 ? 361  TYR A C     1 
ATOM   1892 O  O     . TYR A 1 258 ? -68.596 -34.307 -19.095 1.00 133.66 ? 361  TYR A O     1 
ATOM   1893 C  CB    . TYR A 1 258 ? -70.307 -32.206 -17.181 1.00 131.53 ? 361  TYR A CB    1 
ATOM   1894 C  CG    . TYR A 1 258 ? -71.514 -31.753 -16.391 1.00 133.29 ? 361  TYR A CG    1 
ATOM   1895 C  CD1   . TYR A 1 258 ? -72.051 -32.547 -15.386 1.00 125.54 ? 361  TYR A CD1   1 
ATOM   1896 C  CD2   . TYR A 1 258 ? -72.111 -30.525 -16.643 1.00 138.82 ? 361  TYR A CD2   1 
ATOM   1897 C  CE1   . TYR A 1 258 ? -73.151 -32.134 -14.660 1.00 127.53 ? 361  TYR A CE1   1 
ATOM   1898 C  CE2   . TYR A 1 258 ? -73.211 -30.103 -15.921 1.00 135.92 ? 361  TYR A CE2   1 
ATOM   1899 C  CZ    . TYR A 1 258 ? -73.727 -30.912 -14.932 1.00 133.07 ? 361  TYR A CZ    1 
ATOM   1900 O  OH    . TYR A 1 258 ? -74.823 -30.497 -14.210 1.00 159.59 ? 361  TYR A OH    1 
ATOM   1901 N  N     . HIS A 1 259 ? -69.443 -32.502 -20.157 1.00 126.98 ? 362  HIS A N     1 
ATOM   1902 C  CA    . HIS A 1 259 ? -68.371 -32.361 -21.141 1.00 119.23 ? 362  HIS A CA    1 
ATOM   1903 C  C     . HIS A 1 259 ? -67.865 -30.925 -21.040 1.00 141.43 ? 362  HIS A C     1 
ATOM   1904 O  O     . HIS A 1 259 ? -68.207 -30.068 -21.857 1.00 119.48 ? 362  HIS A O     1 
ATOM   1905 C  CB    . HIS A 1 259 ? -68.863 -32.699 -22.554 1.00 112.60 ? 362  HIS A CB    1 
ATOM   1906 C  CG    . HIS A 1 259 ? -67.780 -32.704 -23.587 1.00 120.43 ? 362  HIS A CG    1 
ATOM   1907 N  ND1   . HIS A 1 259 ? -67.702 -31.759 -24.588 1.00 100.38 ? 362  HIS A ND1   1 
ATOM   1908 C  CD2   . HIS A 1 259 ? -66.731 -33.539 -23.776 1.00 139.10 ? 362  HIS A CD2   1 
ATOM   1909 C  CE1   . HIS A 1 259 ? -66.652 -32.013 -25.348 1.00 122.12 ? 362  HIS A CE1   1 
ATOM   1910 N  NE2   . HIS A 1 259 ? -66.046 -33.087 -24.877 1.00 117.82 ? 362  HIS A NE2   1 
ATOM   1911 N  N     . GLY A 1 260 ? -67.049 -30.667 -20.020 1.00 136.59 ? 363  GLY A N     1 
ATOM   1912 C  CA    . GLY A 1 260 ? -66.590 -29.322 -19.739 1.00 134.71 ? 363  GLY A CA    1 
ATOM   1913 C  C     . GLY A 1 260 ? -67.526 -28.589 -18.799 1.00 147.05 ? 363  GLY A C     1 
ATOM   1914 O  O     . GLY A 1 260 ? -67.369 -28.656 -17.576 1.00 166.80 ? 363  GLY A O     1 
ATOM   1915 N  N     . GLY A 1 261 ? -68.507 -27.889 -19.361 1.00 117.01 ? 364  GLY A N     1 
ATOM   1916 C  CA    . GLY A 1 261 ? -69.500 -27.197 -18.564 1.00 127.34 ? 364  GLY A CA    1 
ATOM   1917 C  C     . GLY A 1 261 ? -70.913 -27.526 -18.997 1.00 146.78 ? 364  GLY A C     1 
ATOM   1918 O  O     . GLY A 1 261 ? -71.878 -27.242 -18.280 1.00 140.81 ? 364  GLY A O     1 
ATOM   1919 N  N     . GLU A 1 262 ? -71.041 -28.128 -20.176 1.00 155.23 ? 365  GLU A N     1 
ATOM   1920 C  CA    . GLU A 1 262 ? -72.326 -28.528 -20.739 1.00 143.72 ? 365  GLU A CA    1 
ATOM   1921 C  C     . GLU A 1 262 ? -72.689 -29.928 -20.260 1.00 156.43 ? 365  GLU A C     1 
ATOM   1922 O  O     . GLU A 1 262 ? -71.840 -30.827 -20.297 1.00 154.56 ? 365  GLU A O     1 
ATOM   1923 C  CB    . GLU A 1 262 ? -72.278 -28.501 -22.262 1.00 142.13 ? 365  GLU A CB    1 
ATOM   1924 C  CG    . GLU A 1 262 ? -73.545 -28.991 -22.947 1.00 168.81 ? 365  GLU A CG    1 
ATOM   1925 C  CD    . GLU A 1 262 ? -73.403 -29.062 -24.456 1.00 181.21 ? 365  GLU A CD    1 
ATOM   1926 O  OE1   . GLU A 1 262 ? -72.337 -28.665 -24.974 1.00 173.67 ? 365  GLU A OE1   1 
ATOM   1927 O  OE2   . GLU A 1 262 ? -74.356 -29.516 -25.124 1.00 155.91 ? 365  GLU A OE2   1 
ATOM   1928 N  N     . PRO A 1 263 ? -73.919 -30.153 -19.804 1.00 138.76 ? 366  PRO A N     1 
ATOM   1929 C  CA    . PRO A 1 263 ? -74.322 -31.496 -19.383 1.00 139.41 ? 366  PRO A CA    1 
ATOM   1930 C  C     . PRO A 1 263 ? -74.825 -32.338 -20.544 1.00 144.62 ? 366  PRO A C     1 
ATOM   1931 O  O     . PRO A 1 263 ? -75.457 -31.851 -21.484 1.00 135.38 ? 366  PRO A O     1 
ATOM   1932 C  CB    . PRO A 1 263 ? -75.449 -31.218 -18.377 1.00 146.28 ? 366  PRO A CB    1 
ATOM   1933 C  CG    . PRO A 1 263 ? -75.956 -29.829 -18.705 1.00 134.02 ? 366  PRO A CG    1 
ATOM   1934 C  CD    . PRO A 1 263 ? -75.029 -29.192 -19.709 1.00 130.53 ? 366  PRO A CD    1 
ATOM   1935 N  N     . LEU A 1 264 ? -74.525 -33.633 -20.463 1.00 136.09 ? 367  LEU A N     1 
ATOM   1936 C  CA    . LEU A 1 264 ? -74.943 -34.578 -21.491 1.00 143.09 ? 367  LEU A CA    1 
ATOM   1937 C  C     . LEU A 1 264 ? -76.355 -35.103 -21.270 1.00 152.11 ? 367  LEU A C     1 
ATOM   1938 O  O     . LEU A 1 264 ? -77.066 -35.377 -22.244 1.00 149.01 ? 367  LEU A O     1 
ATOM   1939 C  CB    . LEU A 1 264 ? -73.971 -35.761 -21.553 1.00 145.78 ? 367  LEU A CB    1 
ATOM   1940 C  CG    . LEU A 1 264 ? -72.649 -35.583 -22.303 1.00 136.94 ? 367  LEU A CG    1 
ATOM   1941 C  CD1   . LEU A 1 264 ? -71.692 -34.688 -21.539 1.00 141.91 ? 367  LEU A CD1   1 
ATOM   1942 C  CD2   . LEU A 1 264 ? -72.019 -36.937 -22.570 1.00 141.19 ? 367  LEU A CD2   1 
ATOM   1943 N  N     . CYS A 1 265 ? -76.774 -35.250 -20.016 1.00 165.25 ? 368  CYS A N     1 
ATOM   1944 C  CA    . CYS A 1 265 ? -78.092 -35.777 -19.696 1.00 134.49 ? 368  CYS A CA    1 
ATOM   1945 C  C     . CYS A 1 265 ? -78.607 -35.076 -18.446 1.00 140.20 ? 368  CYS A C     1 
ATOM   1946 O  O     . CYS A 1 265 ? -77.908 -34.267 -17.830 1.00 134.60 ? 368  CYS A O     1 
ATOM   1947 C  CB    . CYS A 1 265 ? -78.043 -37.295 -19.507 1.00 135.24 ? 368  CYS A CB    1 
ATOM   1948 S  SG    . CYS A 1 265 ? -76.794 -37.846 -18.322 1.00 159.60 ? 368  CYS A SG    1 
ATOM   1949 N  N     . ASP A 1 266 ? -79.844 -35.395 -18.074 1.00 151.69 ? 369  ASP A N     1 
ATOM   1950 C  CA    . ASP A 1 266 ? -80.439 -34.807 -16.883 1.00 138.02 ? 369  ASP A CA    1 
ATOM   1951 C  C     . ASP A 1 266 ? -79.719 -35.295 -15.632 1.00 134.09 ? 369  ASP A C     1 
ATOM   1952 O  O     . ASP A 1 266 ? -79.281 -36.446 -15.556 1.00 138.76 ? 369  ASP A O     1 
ATOM   1953 C  CB    . ASP A 1 266 ? -81.927 -35.148 -16.805 1.00 139.10 ? 369  ASP A CB    1 
ATOM   1954 C  CG    . ASP A 1 266 ? -82.712 -34.596 -17.980 1.00 152.97 ? 369  ASP A CG    1 
ATOM   1955 O  OD1   . ASP A 1 266 ? -82.092 -33.989 -18.878 1.00 157.72 ? 369  ASP A OD1   1 
ATOM   1956 O  OD2   . ASP A 1 266 ? -83.949 -34.768 -18.005 1.00 168.62 ? 369  ASP A OD2   1 
ATOM   1957 N  N     . ASN A 1 267 ? -79.595 -34.406 -14.649 1.00 163.28 ? 370  ASN A N     1 
ATOM   1958 C  CA    . ASN A 1 267 ? -78.864 -34.707 -13.422 1.00 164.30 ? 370  ASN A CA    1 
ATOM   1959 C  C     . ASN A 1 267 ? -79.601 -35.789 -12.641 1.00 175.36 ? 370  ASN A C     1 
ATOM   1960 O  O     . ASN A 1 267 ? -80.698 -35.555 -12.122 1.00 182.66 ? 370  ASN A O     1 
ATOM   1961 C  CB    . ASN A 1 267 ? -78.701 -33.437 -12.590 1.00 179.57 ? 370  ASN A CB    1 
ATOM   1962 C  CG    . ASN A 1 267 ? -77.638 -33.571 -11.516 1.00 188.40 ? 370  ASN A CG    1 
ATOM   1963 O  OD1   . ASN A 1 267 ? -77.591 -34.562 -10.788 1.00 199.05 ? 370  ASN A OD1   1 
ATOM   1964 N  ND2   . ASN A 1 267 ? -76.774 -32.567 -11.415 1.00 167.71 ? 370  ASN A ND2   1 
ATOM   1965 N  N     . VAL A 1 268 ? -79.002 -36.973 -12.558 1.00 149.98 ? 371  VAL A N     1 
ATOM   1966 C  CA    . VAL A 1 268 ? -79.581 -38.108 -11.848 1.00 138.57 ? 371  VAL A CA    1 
ATOM   1967 C  C     . VAL A 1 268 ? -78.936 -38.188 -10.472 1.00 164.20 ? 371  VAL A C     1 
ATOM   1968 O  O     . VAL A 1 268 ? -77.708 -38.272 -10.356 1.00 158.75 ? 371  VAL A O     1 
ATOM   1969 C  CB    . VAL A 1 268 ? -79.383 -39.418 -12.627 1.00 124.74 ? 371  VAL A CB    1 
ATOM   1970 C  CG1   . VAL A 1 268 ? -79.975 -40.587 -11.857 1.00 128.20 ? 371  VAL A CG1   1 
ATOM   1971 C  CG2   . VAL A 1 268 ? -80.006 -39.313 -14.010 1.00 140.83 ? 371  VAL A CG2   1 
ATOM   1972 N  N     . ASN A 1 269 ? -79.760 -38.164 -9.429  1.00 178.86 ? 372  ASN A N     1 
ATOM   1973 C  CA    . ASN A 1 269 ? -79.293 -38.220 -8.053  1.00 166.18 ? 372  ASN A CA    1 
ATOM   1974 C  C     . ASN A 1 269 ? -79.873 -39.444 -7.354  1.00 162.27 ? 372  ASN A C     1 
ATOM   1975 O  O     . ASN A 1 269 ? -80.811 -40.084 -7.837  1.00 152.29 ? 372  ASN A O     1 
ATOM   1976 C  CB    . ASN A 1 269 ? -79.665 -36.941 -7.292  1.00 156.21 ? 372  ASN A CB    1 
ATOM   1977 C  CG    . ASN A 1 269 ? -81.073 -36.470 -7.596  1.00 171.46 ? 372  ASN A CG    1 
ATOM   1978 O  OD1   . ASN A 1 269 ? -81.894 -37.223 -8.120  1.00 179.21 ? 372  ASN A OD1   1 
ATOM   1979 N  ND2   . ASN A 1 269 ? -81.360 -35.215 -7.269  1.00 163.96 ? 372  ASN A ND2   1 
ATOM   1980 N  N     . THR A 1 270 ? -79.298 -39.762 -6.197  1.00 158.83 ? 373  THR A N     1 
ATOM   1981 C  CA    . THR A 1 270 ? -79.710 -40.919 -5.420  1.00 153.49 ? 373  THR A CA    1 
ATOM   1982 C  C     . THR A 1 270 ? -80.757 -40.516 -4.382  1.00 171.71 ? 373  THR A C     1 
ATOM   1983 O  O     . THR A 1 270 ? -81.121 -39.345 -4.245  1.00 164.46 ? 373  THR A O     1 
ATOM   1984 C  CB    . THR A 1 270 ? -78.499 -41.570 -4.754  1.00 132.58 ? 373  THR A CB    1 
ATOM   1985 O  OG1   . THR A 1 270 ? -78.928 -42.684 -3.961  1.00 210.03 ? 373  THR A OG1   1 
ATOM   1986 C  CG2   . THR A 1 270 ? -77.779 -40.569 -3.867  1.00 124.95 ? 373  THR A CG2   1 
ATOM   1987 N  N     . GLN A 1 271 ? -81.248 -41.504 -3.639  1.00 178.22 ? 374  GLN A N     1 
ATOM   1988 C  CA    . GLN A 1 271 ? -82.269 -41.255 -2.632  1.00 165.65 ? 374  GLN A CA    1 
ATOM   1989 C  C     . GLN A 1 271 ? -81.702 -40.444 -1.473  1.00 179.94 ? 374  GLN A C     1 
ATOM   1990 O  O     . GLN A 1 271 ? -80.510 -40.512 -1.158  1.00 183.27 ? 374  GLN A O     1 
ATOM   1991 C  CB    . GLN A 1 271 ? -82.842 -42.575 -2.115  1.00 161.46 ? 374  GLN A CB    1 
ATOM   1992 N  N     . ARG A 1 272 ? -82.575 -39.667 -0.835  1.00 192.43 ? 375  ARG A N     1 
ATOM   1993 C  CA    . ARG A 1 272 ? -82.186 -38.808 0.282   1.00 184.74 ? 375  ARG A CA    1 
ATOM   1994 C  C     . ARG A 1 272 ? -82.095 -39.663 1.540   1.00 170.62 ? 375  ARG A C     1 
ATOM   1995 O  O     . ARG A 1 272 ? -83.065 -39.828 2.281   1.00 183.51 ? 375  ARG A O     1 
ATOM   1996 C  CB    . ARG A 1 272 ? -83.178 -37.664 0.456   1.00 177.94 ? 375  ARG A CB    1 
ATOM   1997 C  CG    . ARG A 1 272 ? -83.386 -36.823 -0.792  1.00 180.85 ? 375  ARG A CG    1 
ATOM   1998 C  CD    . ARG A 1 272 ? -84.294 -35.636 -0.511  1.00 157.58 ? 375  ARG A CD    1 
ATOM   1999 N  NE    . ARG A 1 272 ? -85.565 -36.046 0.075   1.00 182.14 ? 375  ARG A NE    1 
ATOM   2000 C  CZ    . ARG A 1 272 ? -86.656 -36.331 -0.624  1.00 171.54 ? 375  ARG A CZ    1 
ATOM   2001 N  NH1   . ARG A 1 272 ? -86.669 -36.261 -1.945  1.00 157.05 ? 375  ARG A NH1   1 
ATOM   2002 N  NH2   . ARG A 1 272 ? -87.761 -36.696 0.020   1.00 177.51 ? 375  ARG A NH2   1 
ATOM   2003 N  N     . VAL A 1 273 ? -80.911 -40.215 1.784   1.00 168.32 ? 376  VAL A N     1 
ATOM   2004 C  CA    . VAL A 1 273 ? -80.666 -41.019 2.978   1.00 177.85 ? 376  VAL A CA    1 
ATOM   2005 C  C     . VAL A 1 273 ? -80.359 -40.076 4.136   1.00 187.27 ? 376  VAL A C     1 
ATOM   2006 O  O     . VAL A 1 273 ? -79.843 -38.972 3.913   1.00 189.61 ? 376  VAL A O     1 
ATOM   2007 C  CB    . VAL A 1 273 ? -79.526 -42.026 2.752   1.00 173.43 ? 376  VAL A CB    1 
ATOM   2008 C  CG1   . VAL A 1 273 ? -79.846 -42.932 1.571   1.00 199.51 ? 376  VAL A CG1   1 
ATOM   2009 C  CG2   . VAL A 1 273 ? -78.205 -41.304 2.538   1.00 169.92 ? 376  VAL A CG2   1 
ATOM   2010 N  N     . PRO A 1 274 ? -80.669 -40.450 5.375   1.00 184.11 ? 377  PRO A N     1 
ATOM   2011 C  CA    . PRO A 1 274 ? -80.372 -39.567 6.508   1.00 186.00 ? 377  PRO A CA    1 
ATOM   2012 C  C     . PRO A 1 274 ? -78.875 -39.482 6.766   1.00 186.56 ? 377  PRO A C     1 
ATOM   2013 O  O     . PRO A 1 274 ? -78.071 -40.258 6.245   1.00 183.81 ? 377  PRO A O     1 
ATOM   2014 C  CB    . PRO A 1 274 ? -81.107 -40.228 7.677   1.00 202.90 ? 377  PRO A CB    1 
ATOM   2015 C  CG    . PRO A 1 274 ? -81.197 -41.667 7.292   1.00 173.72 ? 377  PRO A CG    1 
ATOM   2016 C  CD    . PRO A 1 274 ? -81.365 -41.678 5.798   1.00 175.17 ? 377  PRO A CD    1 
ATOM   2017 N  N     . CYS A 1 275 ? -78.505 -38.505 7.591   1.00 197.04 ? 378  CYS A N     1 
ATOM   2018 C  CA    . CYS A 1 275 ? -77.112 -38.330 7.967   1.00 190.54 ? 378  CYS A CA    1 
ATOM   2019 C  C     . CYS A 1 275 ? -76.653 -39.486 8.855   1.00 215.39 ? 378  CYS A C     1 
ATOM   2020 O  O     . CYS A 1 275 ? -77.455 -40.269 9.374   1.00 218.34 ? 378  CYS A O     1 
ATOM   2021 C  CB    . CYS A 1 275 ? -76.914 -36.994 8.682   1.00 179.40 ? 378  CYS A CB    1 
ATOM   2022 S  SG    . CYS A 1 275 ? -77.295 -35.543 7.673   1.00 163.79 ? 378  CYS A SG    1 
ATOM   2023 N  N     . SER A 1 276 ? -75.334 -39.592 9.014   1.00 202.19 ? 379  SER A N     1 
ATOM   2024 C  CA    . SER A 1 276 ? -74.669 -40.646 9.776   1.00 211.31 ? 379  SER A CA    1 
ATOM   2025 C  C     . SER A 1 276 ? -74.933 -42.040 9.216   1.00 200.73 ? 379  SER A C     1 
ATOM   2026 O  O     . SER A 1 276 ? -74.567 -43.037 9.850   1.00 177.10 ? 379  SER A O     1 
ATOM   2027 C  CB    . SER A 1 276 ? -75.055 -40.600 11.262  1.00 177.02 ? 379  SER A CB    1 
ATOM   2028 O  OG    . SER A 1 276 ? -74.401 -41.625 11.990  1.00 161.60 ? 379  SER A OG    1 
ATOM   2029 N  N     . ASN A 1 277 ? -75.558 -42.137 8.044   1.00 205.81 ? 380  ASN A N     1 
ATOM   2030 C  CA    . ASN A 1 277 ? -75.804 -43.410 7.368   1.00 209.26 ? 380  ASN A CA    1 
ATOM   2031 C  C     . ASN A 1 277 ? -75.337 -43.269 5.926   1.00 231.18 ? 380  ASN A C     1 
ATOM   2032 O  O     . ASN A 1 277 ? -76.154 -43.141 5.004   1.00 214.92 ? 380  ASN A O     1 
ATOM   2033 C  CB    . ASN A 1 277 ? -77.279 -43.806 7.442   1.00 198.99 ? 380  ASN A CB    1 
ATOM   2034 N  N     . PRO A 1 278 ? -74.022 -43.284 5.693   1.00 248.28 ? 381  PRO A N     1 
ATOM   2035 C  CA    . PRO A 1 278 ? -73.489 -43.096 4.332   1.00 220.25 ? 381  PRO A CA    1 
ATOM   2036 C  C     . PRO A 1 278 ? -73.565 -44.369 3.495   1.00 224.86 ? 381  PRO A C     1 
ATOM   2037 O  O     . PRO A 1 278 ? -72.554 -44.918 3.051   1.00 232.19 ? 381  PRO A O     1 
ATOM   2038 C  CB    . PRO A 1 278 ? -72.046 -42.657 4.610   1.00 217.61 ? 381  PRO A CB    1 
ATOM   2039 C  CG    . PRO A 1 278 ? -71.688 -43.389 5.858   1.00 216.87 ? 381  PRO A CG    1 
ATOM   2040 C  CD    . PRO A 1 278 ? -72.947 -43.455 6.687   1.00 232.43 ? 381  PRO A CD    1 
ATOM   2041 N  N     . ARG A 1 279 ? -74.786 -44.852 3.277   1.00 191.16 ? 382  ARG A N     1 
ATOM   2042 C  CA    . ARG A 1 279 ? -75.027 -46.057 2.498   1.00 187.85 ? 382  ARG A CA    1 
ATOM   2043 C  C     . ARG A 1 279 ? -76.092 -45.776 1.450   1.00 182.31 ? 382  ARG A C     1 
ATOM   2044 O  O     . ARG A 1 279 ? -77.089 -45.103 1.731   1.00 187.95 ? 382  ARG A O     1 
ATOM   2045 C  CB    . ARG A 1 279 ? -75.467 -47.225 3.393   1.00 193.55 ? 382  ARG A CB    1 
ATOM   2046 C  CG    . ARG A 1 279 ? -74.547 -47.488 4.578   1.00 195.94 ? 382  ARG A CG    1 
ATOM   2047 C  CD    . ARG A 1 279 ? -73.162 -47.944 4.139   1.00 184.05 ? 382  ARG A CD    1 
ATOM   2048 N  NE    . ARG A 1 279 ? -73.153 -49.329 3.682   1.00 183.88 ? 382  ARG A NE    1 
ATOM   2049 C  CZ    . ARG A 1 279 ? -73.199 -49.702 2.410   1.00 192.30 ? 382  ARG A CZ    1 
ATOM   2050 N  NH1   . ARG A 1 279 ? -73.255 -48.814 1.431   1.00 211.78 ? 382  ARG A NH1   1 
ATOM   2051 N  NH2   . ARG A 1 279 ? -73.186 -50.998 2.114   1.00 200.14 ? 382  ARG A NH2   1 
ATOM   2052 N  N     . TRP A 1 280 ? -75.877 -46.292 0.241   1.00 170.38 ? 383  TRP A N     1 
ATOM   2053 C  CA    . TRP A 1 280 ? -76.826 -46.100 -0.849  1.00 156.36 ? 383  TRP A CA    1 
ATOM   2054 C  C     . TRP A 1 280 ? -77.050 -47.397 -1.616  1.00 170.13 ? 383  TRP A C     1 
ATOM   2055 O  O     . TRP A 1 280 ? -78.170 -47.918 -1.649  1.00 190.74 ? 383  TRP A O     1 
ATOM   2056 C  CB    . TRP A 1 280 ? -76.342 -45.001 -1.797  1.00 181.68 ? 383  TRP A CB    1 
ATOM   2057 C  CG    . TRP A 1 280 ? -76.353 -43.628 -1.193  1.00 183.56 ? 383  TRP A CG    1 
ATOM   2058 C  CD1   . TRP A 1 280 ? -77.394 -42.746 -1.185  1.00 172.45 ? 383  TRP A CD1   1 
ATOM   2059 C  CD2   . TRP A 1 280 ? -75.271 -42.979 -0.515  1.00 158.66 ? 383  TRP A CD2   1 
ATOM   2060 N  NE1   . TRP A 1 280 ? -77.028 -41.588 -0.543  1.00 142.89 ? 383  TRP A NE1   1 
ATOM   2061 C  CE2   . TRP A 1 280 ? -75.729 -41.706 -0.121  1.00 146.54 ? 383  TRP A CE2   1 
ATOM   2062 C  CE3   . TRP A 1 280 ? -73.960 -43.351 -0.201  1.00 153.21 ? 383  TRP A CE3   1 
ATOM   2063 C  CZ2   . TRP A 1 280 ? -74.924 -40.803 0.570   1.00 146.79 ? 383  TRP A CZ2   1 
ATOM   2064 C  CZ3   . TRP A 1 280 ? -73.162 -42.453 0.485   1.00 177.88 ? 383  TRP A CZ3   1 
ATOM   2065 C  CH2   . TRP A 1 280 ? -73.646 -41.194 0.863   1.00 161.37 ? 383  TRP A CH2   1 
ATOM   2066 N  N     . ASN A 1 281 ? -75.988 -47.920 -2.234  1.00 176.75 ? 384  ASN A N     1 
ATOM   2067 C  CA    . ASN A 1 281 ? -76.047 -49.138 -3.043  1.00 160.28 ? 384  ASN A CA    1 
ATOM   2068 C  C     . ASN A 1 281 ? -77.102 -49.008 -4.143  1.00 163.37 ? 384  ASN A C     1 
ATOM   2069 O  O     . ASN A 1 281 ? -78.058 -49.782 -4.227  1.00 186.46 ? 384  ASN A O     1 
ATOM   2070 C  CB    . ASN A 1 281 ? -76.308 -50.369 -2.167  1.00 164.47 ? 384  ASN A CB    1 
ATOM   2071 C  CG    . ASN A 1 281 ? -75.322 -50.490 -1.023  1.00 198.21 ? 384  ASN A CG    1 
ATOM   2072 O  OD1   . ASN A 1 281 ? -74.225 -51.025 -1.187  1.00 203.86 ? 384  ASN A OD1   1 
ATOM   2073 N  ND2   . ASN A 1 281 ? -75.710 -49.995 0.147   1.00 202.31 ? 384  ASN A ND2   1 
ATOM   2074 N  N     . GLU A 1 282 ? -76.908 -48.003 -4.994  1.00 166.43 ? 385  GLU A N     1 
ATOM   2075 C  CA    . GLU A 1 282 ? -77.854 -47.674 -6.053  1.00 176.85 ? 385  GLU A CA    1 
ATOM   2076 C  C     . GLU A 1 282 ? -77.095 -47.433 -7.348  1.00 156.68 ? 385  GLU A C     1 
ATOM   2077 O  O     . GLU A 1 282 ? -76.217 -46.565 -7.403  1.00 158.84 ? 385  GLU A O     1 
ATOM   2078 C  CB    . GLU A 1 282 ? -78.686 -46.442 -5.681  1.00 169.52 ? 385  GLU A CB    1 
ATOM   2079 C  CG    . GLU A 1 282 ? -79.342 -45.741 -6.864  1.00 179.32 ? 385  GLU A CG    1 
ATOM   2080 C  CD    . GLU A 1 282 ? -80.398 -46.589 -7.547  1.00 204.96 ? 385  GLU A CD    1 
ATOM   2081 O  OE1   . GLU A 1 282 ? -80.939 -47.511 -6.901  1.00 216.89 ? 385  GLU A OE1   1 
ATOM   2082 O  OE2   . GLU A 1 282 ? -80.688 -46.331 -8.734  1.00 208.43 ? 385  GLU A OE2   1 
ATOM   2083 N  N     . TRP A 1 283 ? -77.430 -48.200 -8.383  1.00 136.78 ? 386  TRP A N     1 
ATOM   2084 C  CA    . TRP A 1 283 ? -76.879 -47.987 -9.719  1.00 150.88 ? 386  TRP A CA    1 
ATOM   2085 C  C     . TRP A 1 283 ? -77.622 -46.820 -10.357 1.00 147.96 ? 386  TRP A C     1 
ATOM   2086 O  O     . TRP A 1 283 ? -78.753 -46.969 -10.825 1.00 182.99 ? 386  TRP A O     1 
ATOM   2087 C  CB    . TRP A 1 283 ? -77.006 -49.248 -10.567 1.00 169.29 ? 386  TRP A CB    1 
ATOM   2088 C  CG    . TRP A 1 283 ? -76.020 -50.326 -10.229 1.00 160.39 ? 386  TRP A CG    1 
ATOM   2089 C  CD1   . TRP A 1 283 ? -76.147 -51.283 -9.264  1.00 162.53 ? 386  TRP A CD1   1 
ATOM   2090 C  CD2   . TRP A 1 283 ? -74.760 -50.568 -10.868 1.00 163.45 ? 386  TRP A CD2   1 
ATOM   2091 N  NE1   . TRP A 1 283 ? -75.044 -52.101 -9.260  1.00 152.71 ? 386  TRP A NE1   1 
ATOM   2092 C  CE2   . TRP A 1 283 ? -74.176 -51.682 -10.234 1.00 165.25 ? 386  TRP A CE2   1 
ATOM   2093 C  CE3   . TRP A 1 283 ? -74.067 -49.947 -11.913 1.00 149.76 ? 386  TRP A CE3   1 
ATOM   2094 C  CZ2   . TRP A 1 283 ? -72.933 -52.189 -10.609 1.00 171.55 ? 386  TRP A CZ2   1 
ATOM   2095 C  CZ3   . TRP A 1 283 ? -72.833 -50.452 -12.283 1.00 152.05 ? 386  TRP A CZ3   1 
ATOM   2096 C  CH2   . TRP A 1 283 ? -72.279 -51.561 -11.633 1.00 160.55 ? 386  TRP A CH2   1 
ATOM   2097 N  N     . LEU A 1 284 ? -76.991 -45.648 -10.372 1.00 138.58 ? 387  LEU A N     1 
ATOM   2098 C  CA    . LEU A 1 284 ? -77.595 -44.465 -10.976 1.00 152.47 ? 387  LEU A CA    1 
ATOM   2099 C  C     . LEU A 1 284 ? -77.679 -44.656 -12.486 1.00 147.15 ? 387  LEU A C     1 
ATOM   2100 O  O     . LEU A 1 284 ? -76.653 -44.699 -13.173 1.00 150.50 ? 387  LEU A O     1 
ATOM   2101 C  CB    . LEU A 1 284 ? -76.791 -43.215 -10.627 1.00 164.16 ? 387  LEU A CB    1 
ATOM   2102 C  CG    . LEU A 1 284 ? -77.003 -42.575 -9.251  1.00 134.44 ? 387  LEU A CG    1 
ATOM   2103 C  CD1   . LEU A 1 284 ? -78.486 -42.376 -8.971  1.00 148.05 ? 387  LEU A CD1   1 
ATOM   2104 C  CD2   . LEU A 1 284 ? -76.345 -43.381 -8.141  1.00 136.52 ? 387  LEU A CD2   1 
ATOM   2105 N  N     . ASN A 1 285 ? -78.898 -44.772 -13.005 1.00 137.79 ? 388  ASN A N     1 
ATOM   2106 C  CA    . ASN A 1 285 ? -79.122 -44.963 -14.432 1.00 133.10 ? 388  ASN A CA    1 
ATOM   2107 C  C     . ASN A 1 285 ? -79.185 -43.604 -15.118 1.00 135.82 ? 388  ASN A C     1 
ATOM   2108 O  O     . ASN A 1 285 ? -80.053 -42.783 -14.803 1.00 135.95 ? 388  ASN A O     1 
ATOM   2109 C  CB    . ASN A 1 285 ? -80.409 -45.750 -14.676 1.00 154.54 ? 388  ASN A CB    1 
ATOM   2110 C  CG    . ASN A 1 285 ? -80.421 -47.086 -13.959 1.00 165.20 ? 388  ASN A CG    1 
ATOM   2111 O  OD1   . ASN A 1 285 ? -80.908 -47.195 -12.833 1.00 173.01 ? 388  ASN A OD1   1 
ATOM   2112 N  ND2   . ASN A 1 285 ? -79.884 -48.112 -14.609 1.00 166.71 ? 388  ASN A ND2   1 
ATOM   2113 N  N     . TYR A 1 286 ? -78.269 -43.369 -16.050 1.00 150.28 ? 389  TYR A N     1 
ATOM   2114 C  CA    . TYR A 1 286 ? -78.197 -42.112 -16.779 1.00 123.69 ? 389  TYR A CA    1 
ATOM   2115 C  C     . TYR A 1 286 ? -78.816 -42.260 -18.164 1.00 129.76 ? 389  TYR A C     1 
ATOM   2116 O  O     . TYR A 1 286 ? -78.908 -43.357 -18.720 1.00 150.00 ? 389  TYR A O     1 
ATOM   2117 C  CB    . TYR A 1 286 ? -76.747 -41.636 -16.898 1.00 120.01 ? 389  TYR A CB    1 
ATOM   2118 C  CG    . TYR A 1 286 ? -76.024 -41.553 -15.574 1.00 132.59 ? 389  TYR A CG    1 
ATOM   2119 C  CD1   . TYR A 1 286 ? -76.281 -40.519 -14.683 1.00 123.85 ? 389  TYR A CD1   1 
ATOM   2120 C  CD2   . TYR A 1 286 ? -75.082 -42.508 -15.215 1.00 135.21 ? 389  TYR A CD2   1 
ATOM   2121 C  CE1   . TYR A 1 286 ? -75.621 -40.439 -13.471 1.00 122.92 ? 389  TYR A CE1   1 
ATOM   2122 C  CE2   . TYR A 1 286 ? -74.417 -42.436 -14.006 1.00 141.59 ? 389  TYR A CE2   1 
ATOM   2123 C  CZ    . TYR A 1 286 ? -74.690 -41.400 -13.139 1.00 134.43 ? 389  TYR A CZ    1 
ATOM   2124 O  OH    . TYR A 1 286 ? -74.029 -41.328 -11.934 1.00 141.22 ? 389  TYR A OH    1 
ATOM   2125 N  N     . ASP A 1 287 ? -79.240 -41.126 -18.719 1.00 125.17 ? 390  ASP A N     1 
ATOM   2126 C  CA    . ASP A 1 287 ? -79.903 -41.099 -20.016 1.00 135.07 ? 390  ASP A CA    1 
ATOM   2127 C  C     . ASP A 1 287 ? -78.925 -41.120 -21.185 1.00 144.88 ? 390  ASP A C     1 
ATOM   2128 O  O     . ASP A 1 287 ? -79.362 -41.039 -22.338 1.00 169.82 ? 390  ASP A O     1 
ATOM   2129 C  CB    . ASP A 1 287 ? -80.802 -39.862 -20.114 1.00 144.22 ? 390  ASP A CB    1 
ATOM   2130 C  CG    . ASP A 1 287 ? -81.903 -40.018 -21.144 1.00 180.64 ? 390  ASP A CG    1 
ATOM   2131 O  OD1   . ASP A 1 287 ? -82.112 -41.150 -21.630 1.00 190.84 ? 390  ASP A OD1   1 
ATOM   2132 O  OD2   . ASP A 1 287 ? -82.560 -39.007 -21.471 1.00 202.01 ? 390  ASP A OD2   1 
ATOM   2133 N  N     . ILE A 1 288 ? -77.629 -41.229 -20.926 1.00 139.01 ? 391  ILE A N     1 
ATOM   2134 C  CA    . ILE A 1 288 ? -76.622 -41.215 -21.979 1.00 143.07 ? 391  ILE A CA    1 
ATOM   2135 C  C     . ILE A 1 288 ? -76.357 -42.637 -22.449 1.00 139.53 ? 391  ILE A C     1 
ATOM   2136 O  O     . ILE A 1 288 ? -76.289 -43.575 -21.646 1.00 144.33 ? 391  ILE A O     1 
ATOM   2137 C  CB    . ILE A 1 288 ? -75.325 -40.541 -21.493 1.00 144.23 ? 391  ILE A CB    1 
ATOM   2138 C  CG1   . ILE A 1 288 ? -74.937 -41.062 -20.108 1.00 144.72 ? 391  ILE A CG1   1 
ATOM   2139 C  CG2   . ILE A 1 288 ? -75.482 -39.032 -21.485 1.00 159.84 ? 391  ILE A CG2   1 
ATOM   2140 N  N     . TYR A 1 289 ? -76.209 -42.794 -23.760 1.00 138.19 ? 392  TYR A N     1 
ATOM   2141 C  CA    . TYR A 1 289 ? -75.840 -44.076 -24.341 1.00 136.57 ? 392  TYR A CA    1 
ATOM   2142 C  C     . TYR A 1 289 ? -74.330 -44.257 -24.255 1.00 147.75 ? 392  TYR A C     1 
ATOM   2143 O  O     . TYR A 1 289 ? -73.566 -43.314 -24.480 1.00 173.08 ? 392  TYR A O     1 
ATOM   2144 C  CB    . TYR A 1 289 ? -76.312 -44.148 -25.794 1.00 137.65 ? 392  TYR A CB    1 
ATOM   2145 C  CG    . TYR A 1 289 ? -76.642 -45.540 -26.283 1.00 149.04 ? 392  TYR A CG    1 
ATOM   2146 C  CD1   . TYR A 1 289 ? -77.462 -46.381 -25.543 1.00 163.62 ? 392  TYR A CD1   1 
ATOM   2147 C  CD2   . TYR A 1 289 ? -76.156 -46.002 -27.499 1.00 161.16 ? 392  TYR A CD2   1 
ATOM   2148 C  CE1   . TYR A 1 289 ? -77.773 -47.652 -25.991 1.00 194.00 ? 392  TYR A CE1   1 
ATOM   2149 C  CE2   . TYR A 1 289 ? -76.461 -47.270 -27.955 1.00 162.10 ? 392  TYR A CE2   1 
ATOM   2150 C  CZ    . TYR A 1 289 ? -77.270 -48.091 -27.198 1.00 193.85 ? 392  TYR A CZ    1 
ATOM   2151 O  OH    . TYR A 1 289 ? -77.578 -49.354 -27.649 1.00 212.64 ? 392  TYR A OH    1 
ATOM   2152 N  N     . ILE A 1 290 ? -73.902 -45.476 -23.915 1.00 128.44 ? 393  ILE A N     1 
ATOM   2153 C  CA    . ILE A 1 290 ? -72.475 -45.723 -23.688 1.00 134.02 ? 393  ILE A CA    1 
ATOM   2154 C  C     . ILE A 1 290 ? -71.633 -45.450 -24.930 1.00 141.17 ? 393  ILE A C     1 
ATOM   2155 O  O     . ILE A 1 290 ? -70.585 -44.795 -24.805 1.00 132.02 ? 393  ILE A O     1 
ATOM   2156 C  CB    . ILE A 1 290 ? -72.268 -47.140 -23.123 1.00 123.62 ? 393  ILE A CB    1 
ATOM   2157 C  CG1   . ILE A 1 290 ? -72.868 -47.242 -21.721 1.00 139.29 ? 393  ILE A CG1   1 
ATOM   2158 C  CG2   . ILE A 1 290 ? -70.791 -47.497 -23.093 1.00 135.46 ? 393  ILE A CG2   1 
ATOM   2159 C  CD1   . ILE A 1 290 ? -72.747 -48.612 -21.107 1.00 163.25 ? 393  ILE A CD1   1 
ATOM   2160 N  N     . PRO A 1 291 ? -72.008 -45.901 -26.134 1.00 127.19 ? 394  PRO A N     1 
ATOM   2161 C  CA    . PRO A 1 291 ? -71.234 -45.518 -27.326 1.00 129.75 ? 394  PRO A CA    1 
ATOM   2162 C  C     . PRO A 1 291 ? -71.289 -44.035 -27.660 1.00 130.28 ? 394  PRO A C     1 
ATOM   2163 O  O     . PRO A 1 291 ? -70.599 -43.607 -28.593 1.00 140.76 ? 394  PRO A O     1 
ATOM   2164 C  CB    . PRO A 1 291 ? -71.879 -46.353 -28.444 1.00 123.17 ? 394  PRO A CB    1 
ATOM   2165 C  CG    . PRO A 1 291 ? -72.493 -47.505 -27.747 1.00 115.49 ? 394  PRO A CG    1 
ATOM   2166 C  CD    . PRO A 1 291 ? -72.999 -46.945 -26.456 1.00 140.05 ? 394  PRO A CD    1 
ATOM   2167 N  N     . ASP A 1 292 ? -72.075 -43.233 -26.943 1.00 129.84 ? 395  ASP A N     1 
ATOM   2168 C  CA    . ASP A 1 292 ? -72.189 -41.808 -27.219 1.00 147.86 ? 395  ASP A CA    1 
ATOM   2169 C  C     . ASP A 1 292 ? -71.379 -40.943 -26.262 1.00 138.63 ? 395  ASP A C     1 
ATOM   2170 O  O     . ASP A 1 292 ? -71.437 -39.713 -26.362 1.00 120.34 ? 395  ASP A O     1 
ATOM   2171 C  CB    . ASP A 1 292 ? -73.660 -41.379 -27.180 1.00 130.96 ? 395  ASP A CB    1 
ATOM   2172 C  CG    . ASP A 1 292 ? -74.450 -41.909 -28.359 1.00 141.14 ? 395  ASP A CG    1 
ATOM   2173 O  OD1   . ASP A 1 292 ? -74.694 -43.133 -28.411 1.00 179.10 ? 395  ASP A OD1   1 
ATOM   2174 O  OD2   . ASP A 1 292 ? -74.825 -41.102 -29.235 1.00 165.59 ? 395  ASP A OD2   1 
ATOM   2175 N  N     . LEU A 1 293 ? -70.633 -41.543 -25.346 1.00 124.12 ? 396  LEU A N     1 
ATOM   2176 C  CA    . LEU A 1 293 ? -69.796 -40.768 -24.437 1.00 132.01 ? 396  LEU A CA    1 
ATOM   2177 C  C     . LEU A 1 293 ? -68.596 -40.208 -25.190 1.00 133.06 ? 396  LEU A C     1 
ATOM   2178 O  O     . LEU A 1 293 ? -67.815 -40.985 -25.756 1.00 125.74 ? 396  LEU A O     1 
ATOM   2179 C  CB    . LEU A 1 293 ? -69.331 -41.634 -23.270 1.00 123.61 ? 396  LEU A CB    1 
ATOM   2180 C  CG    . LEU A 1 293 ? -70.402 -42.077 -22.272 1.00 117.17 ? 396  LEU A CG    1 
ATOM   2181 C  CD1   . LEU A 1 293 ? -69.802 -42.998 -21.221 1.00 114.18 ? 396  LEU A CD1   1 
ATOM   2182 C  CD2   . LEU A 1 293 ? -71.055 -40.870 -21.619 1.00 123.62 ? 396  LEU A CD2   1 
ATOM   2183 N  N     . PRO A 1 294 ? -68.409 -38.891 -25.230 1.00 124.96 ? 397  PRO A N     1 
ATOM   2184 C  CA    . PRO A 1 294 ? -67.249 -38.329 -25.928 1.00 134.12 ? 397  PRO A CA    1 
ATOM   2185 C  C     . PRO A 1 294 ? -65.956 -38.666 -25.200 1.00 134.37 ? 397  PRO A C     1 
ATOM   2186 O  O     . PRO A 1 294 ? -65.946 -39.197 -24.088 1.00 122.03 ? 397  PRO A O     1 
ATOM   2187 C  CB    . PRO A 1 294 ? -67.524 -36.823 -25.922 1.00 131.04 ? 397  PRO A CB    1 
ATOM   2188 C  CG    . PRO A 1 294 ? -68.397 -36.613 -24.731 1.00 113.99 ? 397  PRO A CG    1 
ATOM   2189 C  CD    . PRO A 1 294 ? -69.252 -37.845 -24.627 1.00 123.70 ? 397  PRO A CD    1 
ATOM   2190 N  N     . ARG A 1 295 ? -64.842 -38.341 -25.859 1.00 139.58 ? 398  ARG A N     1 
ATOM   2191 C  CA    . ARG A 1 295 ? -63.536 -38.665 -25.295 1.00 130.09 ? 398  ARG A CA    1 
ATOM   2192 C  C     . ARG A 1 295 ? -63.264 -37.884 -24.015 1.00 107.77 ? 398  ARG A C     1 
ATOM   2193 O  O     . ARG A 1 295 ? -62.577 -38.387 -23.119 1.00 99.62  ? 398  ARG A O     1 
ATOM   2194 C  CB    . ARG A 1 295 ? -62.442 -38.404 -26.331 1.00 124.06 ? 398  ARG A CB    1 
ATOM   2195 C  CG    . ARG A 1 295 ? -61.059 -38.846 -25.892 1.00 105.76 ? 398  ARG A CG    1 
ATOM   2196 C  CD    . ARG A 1 295 ? -61.075 -40.278 -25.388 1.00 114.56 ? 398  ARG A CD    1 
ATOM   2197 N  NE    . ARG A 1 295 ? -59.831 -40.625 -24.713 1.00 128.43 ? 398  ARG A NE    1 
ATOM   2198 C  CZ    . ARG A 1 295 ? -59.538 -40.281 -23.466 1.00 123.84 ? 398  ARG A CZ    1 
ATOM   2199 N  NH1   . ARG A 1 295 ? -60.374 -39.565 -22.732 1.00 117.40 ? 398  ARG A NH1   1 
ATOM   2200 N  NH2   . ARG A 1 295 ? -58.374 -40.660 -22.945 1.00 135.20 ? 398  ARG A NH2   1 
ATOM   2201 N  N     . ALA A 1 296 ? -63.799 -36.668 -23.903 1.00 124.94 ? 399  ALA A N     1 
ATOM   2202 C  CA    . ALA A 1 296 ? -63.619 -35.834 -22.721 1.00 123.05 ? 399  ALA A CA    1 
ATOM   2203 C  C     . ALA A 1 296 ? -64.818 -35.896 -21.780 1.00 121.81 ? 399  ALA A C     1 
ATOM   2204 O  O     . ALA A 1 296 ? -65.121 -34.913 -21.095 1.00 126.67 ? 399  ALA A O     1 
ATOM   2205 C  CB    . ALA A 1 296 ? -63.339 -34.388 -23.130 1.00 111.00 ? 399  ALA A CB    1 
ATOM   2206 N  N     . ALA A 1 297 ? -65.507 -37.034 -21.733 1.00 130.33 ? 400  ALA A N     1 
ATOM   2207 C  CA    . ALA A 1 297 ? -66.656 -37.179 -20.850 1.00 123.70 ? 400  ALA A CA    1 
ATOM   2208 C  C     . ALA A 1 297 ? -66.203 -37.200 -19.396 1.00 118.49 ? 400  ALA A C     1 
ATOM   2209 O  O     . ALA A 1 297 ? -65.233 -37.880 -19.046 1.00 113.74 ? 400  ALA A O     1 
ATOM   2210 C  CB    . ALA A 1 297 ? -67.428 -38.453 -21.187 1.00 126.15 ? 400  ALA A CB    1 
ATOM   2211 N  N     . ARG A 1 298 ? -66.907 -36.454 -18.549 1.00 111.75 ? 401  ARG A N     1 
ATOM   2212 C  CA    . ARG A 1 298 ? -66.548 -36.310 -17.147 1.00 114.25 ? 401  ARG A CA    1 
ATOM   2213 C  C     . ARG A 1 298 ? -67.744 -36.639 -16.267 1.00 133.41 ? 401  ARG A C     1 
ATOM   2214 O  O     . ARG A 1 298 ? -68.896 -36.407 -16.643 1.00 131.89 ? 401  ARG A O     1 
ATOM   2215 C  CB    . ARG A 1 298 ? -66.062 -34.888 -16.837 1.00 134.68 ? 401  ARG A CB    1 
ATOM   2216 C  CG    . ARG A 1 298 ? -64.831 -34.456 -17.615 1.00 145.76 ? 401  ARG A CG    1 
ATOM   2217 C  CD    . ARG A 1 298 ? -64.587 -32.966 -17.447 1.00 151.56 ? 401  ARG A CD    1 
ATOM   2218 N  NE    . ARG A 1 298 ? -64.643 -32.566 -16.046 1.00 167.95 ? 401  ARG A NE    1 
ATOM   2219 C  CZ    . ARG A 1 298 ? -64.526 -31.317 -15.617 1.00 168.85 ? 401  ARG A CZ    1 
ATOM   2220 N  NH1   . ARG A 1 298 ? -64.345 -30.311 -16.457 1.00 195.21 ? 401  ARG A NH1   1 
ATOM   2221 N  NH2   . ARG A 1 298 ? -64.593 -31.071 -14.311 1.00 149.71 ? 401  ARG A NH2   1 
ATOM   2222 N  N     . LEU A 1 299 ? -67.455 -37.179 -15.087 1.00 128.94 ? 402  LEU A N     1 
ATOM   2223 C  CA    . LEU A 1 299 ? -68.461 -37.451 -14.069 1.00 104.73 ? 402  LEU A CA    1 
ATOM   2224 C  C     . LEU A 1 299 ? -68.329 -36.418 -12.960 1.00 109.97 ? 402  LEU A C     1 
ATOM   2225 O  O     . LEU A 1 299 ? -67.228 -36.188 -12.449 1.00 123.08 ? 402  LEU A O     1 
ATOM   2226 C  CB    . LEU A 1 299 ? -68.305 -38.864 -13.501 1.00 110.28 ? 402  LEU A CB    1 
ATOM   2227 C  CG    . LEU A 1 299 ? -69.254 -39.246 -12.363 1.00 108.77 ? 402  LEU A CG    1 
ATOM   2228 C  CD1   . LEU A 1 299 ? -70.697 -39.258 -12.845 1.00 118.14 ? 402  LEU A CD1   1 
ATOM   2229 C  CD2   . LEU A 1 299 ? -68.871 -40.592 -11.766 1.00 105.49 ? 402  LEU A CD2   1 
ATOM   2230 N  N     . CYS A 1 300 ? -69.447 -35.796 -12.595 1.00 105.73 ? 403  CYS A N     1 
ATOM   2231 C  CA    . CYS A 1 300 ? -69.469 -34.741 -11.590 1.00 146.93 ? 403  CYS A CA    1 
ATOM   2232 C  C     . CYS A 1 300 ? -70.297 -35.209 -10.403 1.00 141.92 ? 403  CYS A C     1 
ATOM   2233 O  O     . CYS A 1 300 ? -71.484 -35.517 -10.554 1.00 126.33 ? 403  CYS A O     1 
ATOM   2234 C  CB    . CYS A 1 300 ? -70.035 -33.444 -12.171 1.00 152.72 ? 403  CYS A CB    1 
ATOM   2235 S  SG    . CYS A 1 300 ? -69.145 -32.828 -13.619 1.00 121.37 ? 403  CYS A SG    1 
ATOM   2236 N  N     . LEU A 1 301 ? -69.673 -35.256 -9.228  1.00 132.19 ? 404  LEU A N     1 
ATOM   2237 C  CA    . LEU A 1 301 ? -70.320 -35.712 -8.008  1.00 142.97 ? 404  LEU A CA    1 
ATOM   2238 C  C     . LEU A 1 301 ? -70.329 -34.596 -6.973  1.00 154.80 ? 404  LEU A C     1 
ATOM   2239 O  O     . LEU A 1 301 ? -69.413 -33.771 -6.918  1.00 173.68 ? 404  LEU A O     1 
ATOM   2240 C  CB    . LEU A 1 301 ? -69.611 -36.943 -7.428  1.00 166.37 ? 404  LEU A CB    1 
ATOM   2241 C  CG    . LEU A 1 301 ? -69.393 -38.129 -8.368  1.00 155.91 ? 404  LEU A CG    1 
ATOM   2242 C  CD1   . LEU A 1 301 ? -68.697 -39.261 -7.634  1.00 135.77 ? 404  LEU A CD1   1 
ATOM   2243 C  CD2   . LEU A 1 301 ? -70.709 -38.600 -8.960  1.00 132.05 ? 404  LEU A CD2   1 
ATOM   2244 N  N     . SER A 1 302 ? -71.376 -34.581 -6.151  1.00 175.13 ? 405  SER A N     1 
ATOM   2245 C  CA    . SER A 1 302 ? -71.492 -33.615 -5.069  1.00 167.55 ? 405  SER A CA    1 
ATOM   2246 C  C     . SER A 1 302 ? -72.504 -34.132 -4.058  1.00 166.36 ? 405  SER A C     1 
ATOM   2247 O  O     . SER A 1 302 ? -73.405 -34.901 -4.403  1.00 172.96 ? 405  SER A O     1 
ATOM   2248 C  CB    . SER A 1 302 ? -71.911 -32.232 -5.580  1.00 175.01 ? 405  SER A CB    1 
ATOM   2249 O  OG    . SER A 1 302 ? -73.200 -32.273 -6.167  1.00 179.50 ? 405  SER A OG    1 
ATOM   2250 N  N     . ILE A 1 303 ? -72.344 -33.702 -2.809  1.00 160.89 ? 406  ILE A N     1 
ATOM   2251 C  CA    . ILE A 1 303 ? -73.222 -34.093 -1.712  1.00 161.03 ? 406  ILE A CA    1 
ATOM   2252 C  C     . ILE A 1 303 ? -74.025 -32.875 -1.281  1.00 160.43 ? 406  ILE A C     1 
ATOM   2253 O  O     . ILE A 1 303 ? -73.453 -31.819 -0.984  1.00 155.37 ? 406  ILE A O     1 
ATOM   2254 C  CB    . ILE A 1 303 ? -72.427 -34.675 -0.530  1.00 153.38 ? 406  ILE A CB    1 
ATOM   2255 C  CG1   . ILE A 1 303 ? -71.679 -35.939 -0.960  1.00 150.93 ? 406  ILE A CG1   1 
ATOM   2256 C  CG2   . ILE A 1 303 ? -73.354 -34.973 0.638   1.00 151.41 ? 406  ILE A CG2   1 
ATOM   2257 C  CD1   . ILE A 1 303 ? -70.939 -36.621 0.170   1.00 105.28 ? 406  ILE A CD1   1 
ATOM   2258 N  N     . CYS A 1 304 ? -75.346 -33.023 -1.244  1.00 164.76 ? 407  CYS A N     1 
ATOM   2259 C  CA    . CYS A 1 304 ? -76.251 -31.948 -0.872  1.00 180.57 ? 407  CYS A CA    1 
ATOM   2260 C  C     . CYS A 1 304 ? -77.040 -32.340 0.369   1.00 186.86 ? 407  CYS A C     1 
ATOM   2261 O  O     . CYS A 1 304 ? -77.358 -33.515 0.575   1.00 177.73 ? 407  CYS A O     1 
ATOM   2262 C  CB    . CYS A 1 304 ? -77.212 -31.614 -2.017  1.00 171.91 ? 407  CYS A CB    1 
ATOM   2263 S  SG    . CYS A 1 304 ? -76.390 -31.292 -3.592  1.00 195.89 ? 407  CYS A SG    1 
ATOM   2264 N  N     . SER A 1 305 ? -77.353 -31.345 1.193   1.00 175.95 ? 408  SER A N     1 
ATOM   2265 C  CA    . SER A 1 305 ? -78.090 -31.555 2.430   1.00 179.11 ? 408  SER A CA    1 
ATOM   2266 C  C     . SER A 1 305 ? -79.531 -31.088 2.270   1.00 199.97 ? 408  SER A C     1 
ATOM   2267 O  O     . SER A 1 305 ? -79.801 -30.087 1.599   1.00 198.78 ? 408  SER A O     1 
ATOM   2268 C  CB    . SER A 1 305 ? -77.427 -30.812 3.593   1.00 187.40 ? 408  SER A CB    1 
ATOM   2269 O  OG    . SER A 1 305 ? -77.386 -29.417 3.349   1.00 203.91 ? 408  SER A OG    1 
ATOM   2270 N  N     . VAL A 1 306 ? -80.453 -31.819 2.891   1.00 204.14 ? 409  VAL A N     1 
ATOM   2271 C  CA    . VAL A 1 306 ? -81.877 -31.507 2.854   1.00 202.63 ? 409  VAL A CA    1 
ATOM   2272 C  C     . VAL A 1 306 ? -82.338 -31.250 4.281   1.00 218.30 ? 409  VAL A C     1 
ATOM   2273 O  O     . VAL A 1 306 ? -82.227 -32.132 5.143   1.00 230.85 ? 409  VAL A O     1 
ATOM   2274 C  CB    . VAL A 1 306 ? -82.695 -32.636 2.208   1.00 199.35 ? 409  VAL A CB    1 
ATOM   2275 C  CG1   . VAL A 1 306 ? -84.173 -32.276 2.188   1.00 200.66 ? 409  VAL A CG1   1 
ATOM   2276 C  CG2   . VAL A 1 306 ? -82.191 -32.918 0.803   1.00 184.75 ? 409  VAL A CG2   1 
ATOM   2277 N  N     . LYS A 1 307 ? -82.852 -30.050 4.529   1.00 212.31 ? 410  LYS A N     1 
ATOM   2278 C  CA    . LYS A 1 307 ? -83.325 -29.679 5.857   1.00 215.20 ? 410  LYS A CA    1 
ATOM   2279 C  C     . LYS A 1 307 ? -84.828 -29.418 5.852   1.00 204.93 ? 410  LYS A C     1 
ATOM   2280 O  O     . LYS A 1 307 ? -85.621 -30.302 5.526   1.00 188.79 ? 410  LYS A O     1 
ATOM   2281 C  CB    . LYS A 1 307 ? -82.578 -28.444 6.366   1.00 198.06 ? 410  LYS A CB    1 
ATOM   2282 C  CG    . LYS A 1 307 ? -81.069 -28.621 6.448   1.00 182.43 ? 410  LYS A CG    1 
ATOM   2283 C  CD    . LYS A 1 307 ? -80.692 -29.720 7.428   1.00 188.37 ? 410  LYS A CD    1 
ATOM   2284 C  CE    . LYS A 1 307 ? -81.141 -29.380 8.840   1.00 179.02 ? 410  LYS A CE    1 
ATOM   2285 N  NZ    . LYS A 1 307 ? -80.790 -30.455 9.808   1.00 176.90 ? 410  LYS A NZ    1 
ATOM   2286 N  N     . LYS A 1 313 ? -91.670 -25.090 0.461   1.00 176.49 ? 416  LYS A N     1 
ATOM   2287 C  CA    . LYS A 1 313 ? -90.289 -24.654 0.633   1.00 198.69 ? 416  LYS A CA    1 
ATOM   2288 C  C     . LYS A 1 313 ? -89.316 -25.710 0.118   1.00 202.22 ? 416  LYS A C     1 
ATOM   2289 O  O     . LYS A 1 313 ? -89.725 -26.798 -0.289  1.00 194.37 ? 416  LYS A O     1 
ATOM   2290 C  CB    . LYS A 1 313 ? -90.005 -24.343 2.103   1.00 192.19 ? 416  LYS A CB    1 
ATOM   2291 C  CG    . LYS A 1 313 ? -90.245 -25.513 3.043   1.00 180.84 ? 416  LYS A CG    1 
ATOM   2292 C  CD    . LYS A 1 313 ? -89.968 -25.127 4.486   1.00 179.71 ? 416  LYS A CD    1 
ATOM   2293 C  CE    . LYS A 1 313 ? -90.154 -26.313 5.418   1.00 204.25 ? 416  LYS A CE    1 
ATOM   2294 N  NZ    . LYS A 1 313 ? -89.823 -25.969 6.828   1.00 207.20 ? 416  LYS A NZ    1 
ATOM   2295 N  N     . GLU A 1 314 ? -88.025 -25.384 0.139   1.00 204.44 ? 417  GLU A N     1 
ATOM   2296 C  CA    . GLU A 1 314 ? -86.997 -26.293 -0.347  1.00 213.02 ? 417  GLU A CA    1 
ATOM   2297 C  C     . GLU A 1 314 ? -85.683 -25.977 0.351   1.00 212.47 ? 417  GLU A C     1 
ATOM   2298 O  O     . GLU A 1 314 ? -85.346 -24.807 0.552   1.00 223.80 ? 417  GLU A O     1 
ATOM   2299 C  CB    . GLU A 1 314 ? -86.830 -26.184 -1.867  1.00 220.10 ? 417  GLU A CB    1 
ATOM   2300 C  CG    . GLU A 1 314 ? -86.021 -27.312 -2.488  1.00 219.52 ? 417  GLU A CG    1 
ATOM   2301 C  CD    . GLU A 1 314 ? -86.765 -28.634 -2.482  1.00 224.47 ? 417  GLU A CD    1 
ATOM   2302 O  OE1   . GLU A 1 314 ? -88.009 -28.619 -2.376  1.00 230.79 ? 417  GLU A OE1   1 
ATOM   2303 O  OE2   . GLU A 1 314 ? -86.105 -29.689 -2.583  1.00 221.98 ? 417  GLU A OE2   1 
ATOM   2304 N  N     . GLU A 1 315 ? -84.947 -27.025 0.716   1.00 208.69 ? 418  GLU A N     1 
ATOM   2305 C  CA    . GLU A 1 315 ? -83.654 -26.893 1.388   1.00 205.21 ? 418  GLU A CA    1 
ATOM   2306 C  C     . GLU A 1 315 ? -82.641 -27.753 0.638   1.00 202.12 ? 418  GLU A C     1 
ATOM   2307 O  O     . GLU A 1 315 ? -82.596 -28.973 0.824   1.00 210.03 ? 418  GLU A O     1 
ATOM   2308 C  CB    . GLU A 1 315 ? -83.743 -27.302 2.857   1.00 206.26 ? 418  GLU A CB    1 
ATOM   2309 C  CG    . GLU A 1 315 ? -84.807 -26.570 3.662   1.00 219.38 ? 418  GLU A CG    1 
ATOM   2310 C  CD    . GLU A 1 315 ? -86.175 -27.217 3.549   1.00 217.23 ? 418  GLU A CD    1 
ATOM   2311 O  OE1   . GLU A 1 315 ? -86.273 -28.304 2.943   1.00 211.78 ? 418  GLU A OE1   1 
ATOM   2312 O  OE2   . GLU A 1 315 ? -87.151 -26.639 4.070   1.00 203.69 ? 418  GLU A OE2   1 
ATOM   2313 N  N     . HIS A 1 316 ? -81.830 -27.119 -0.207  1.00 186.91 ? 419  HIS A N     1 
ATOM   2314 C  CA    . HIS A 1 316 ? -80.795 -27.812 -0.971  1.00 182.83 ? 419  HIS A CA    1 
ATOM   2315 C  C     . HIS A 1 316 ? -79.528 -26.970 -0.933  1.00 189.60 ? 419  HIS A C     1 
ATOM   2316 O  O     . HIS A 1 316 ? -79.494 -25.871 -1.495  1.00 186.34 ? 419  HIS A O     1 
ATOM   2317 C  CB    . HIS A 1 316 ? -81.238 -28.064 -2.413  1.00 188.80 ? 419  HIS A CB    1 
ATOM   2318 C  CG    . HIS A 1 316 ? -82.169 -29.227 -2.567  1.00 177.54 ? 419  HIS A CG    1 
ATOM   2319 N  ND1   . HIS A 1 316 ? -82.521 -30.044 -1.514  1.00 198.66 ? 419  HIS A ND1   1 
ATOM   2320 C  CD2   . HIS A 1 316 ? -82.815 -29.714 -3.652  1.00 173.41 ? 419  HIS A CD2   1 
ATOM   2321 C  CE1   . HIS A 1 316 ? -83.347 -30.981 -1.943  1.00 195.10 ? 419  HIS A CE1   1 
ATOM   2322 N  NE2   . HIS A 1 316 ? -83.542 -30.804 -3.237  1.00 180.26 ? 419  HIS A NE2   1 
ATOM   2323 N  N     . CYS A 1 317 ? -78.487 -27.486 -0.274  1.00 203.63 ? 420  CYS A N     1 
ATOM   2324 C  CA    . CYS A 1 317 ? -77.212 -26.794 -0.162  1.00 194.52 ? 420  CYS A CA    1 
ATOM   2325 C  C     . CYS A 1 317 ? -76.091 -27.822 -0.276  1.00 178.67 ? 420  CYS A C     1 
ATOM   2326 O  O     . CYS A 1 317 ? -76.103 -28.831 0.454   1.00 185.43 ? 420  CYS A O     1 
ATOM   2327 C  CB    . CYS A 1 317 ? -77.099 -26.025 1.158   1.00 221.39 ? 420  CYS A CB    1 
ATOM   2328 S  SG    . CYS A 1 317 ? -78.340 -24.729 1.387   1.00 254.90 ? 420  CYS A SG    1 
ATOM   2329 N  N     . PRO A 1 318 ? -75.125 -27.611 -1.163  1.00 164.31 ? 421  PRO A N     1 
ATOM   2330 C  CA    . PRO A 1 318 ? -74.012 -28.554 -1.293  1.00 147.44 ? 421  PRO A CA    1 
ATOM   2331 C  C     . PRO A 1 318 ? -73.009 -28.388 -0.158  1.00 164.14 ? 421  PRO A C     1 
ATOM   2332 O  O     . PRO A 1 318 ? -73.043 -27.427 0.611   1.00 190.69 ? 421  PRO A O     1 
ATOM   2333 C  CB    . PRO A 1 318 ? -73.392 -28.178 -2.642  1.00 144.08 ? 421  PRO A CB    1 
ATOM   2334 C  CG    . PRO A 1 318 ? -73.683 -26.722 -2.777  1.00 151.31 ? 421  PRO A CG    1 
ATOM   2335 C  CD    . PRO A 1 318 ? -75.027 -26.501 -2.128  1.00 178.35 ? 421  PRO A CD    1 
ATOM   2336 N  N     . LEU A 1 319 ? -72.099 -29.358 -0.067  1.00 149.51 ? 422  LEU A N     1 
ATOM   2337 C  CA    . LEU A 1 319 ? -71.071 -29.338 0.967   1.00 155.41 ? 422  LEU A CA    1 
ATOM   2338 C  C     . LEU A 1 319 ? -69.727 -29.792 0.412   1.00 158.10 ? 422  LEU A C     1 
ATOM   2339 O  O     . LEU A 1 319 ? -68.717 -29.098 0.571   1.00 163.82 ? 422  LEU A O     1 
ATOM   2340 C  CB    . LEU A 1 319 ? -71.482 -30.219 2.148   1.00 160.91 ? 422  LEU A CB    1 
ATOM   2341 C  CG    . LEU A 1 319 ? -70.484 -30.287 3.307   1.00 177.74 ? 422  LEU A CG    1 
ATOM   2342 C  CD1   . LEU A 1 319 ? -70.230 -28.900 3.879   1.00 178.32 ? 422  LEU A CD1   1 
ATOM   2343 C  CD2   . LEU A 1 319 ? -70.978 -31.235 4.389   1.00 153.70 ? 422  LEU A CD2   1 
ATOM   2344 N  N     . ALA A 1 320 ? -69.703 -30.956 -0.233  1.00 176.60 ? 423  ALA A N     1 
ATOM   2345 C  CA    . ALA A 1 320 ? -68.491 -31.504 -0.819  1.00 181.44 ? 423  ALA A CA    1 
ATOM   2346 C  C     . ALA A 1 320 ? -68.777 -31.964 -2.241  1.00 169.82 ? 423  ALA A C     1 
ATOM   2347 O  O     . ALA A 1 320 ? -69.879 -32.424 -2.551  1.00 178.11 ? 423  ALA A O     1 
ATOM   2348 C  CB    . ALA A 1 320 ? -67.941 -32.671 0.012   1.00 161.71 ? 423  ALA A CB    1 
ATOM   2349 N  N     . TRP A 1 321 ? -67.771 -31.838 -3.104  1.00 147.65 ? 424  TRP A N     1 
ATOM   2350 C  CA    . TRP A 1 321 ? -67.920 -32.163 -4.515  1.00 150.31 ? 424  TRP A CA    1 
ATOM   2351 C  C     . TRP A 1 321 ? -66.688 -32.912 -5.003  1.00 151.16 ? 424  TRP A C     1 
ATOM   2352 O  O     . TRP A 1 321 ? -65.604 -32.816 -4.422  1.00 142.30 ? 424  TRP A O     1 
ATOM   2353 C  CB    . TRP A 1 321 ? -68.142 -30.902 -5.361  1.00 147.36 ? 424  TRP A CB    1 
ATOM   2354 C  CG    . TRP A 1 321 ? -67.047 -29.888 -5.224  1.00 149.46 ? 424  TRP A CG    1 
ATOM   2355 C  CD1   . TRP A 1 321 ? -66.929 -28.934 -4.255  1.00 162.71 ? 424  TRP A CD1   1 
ATOM   2356 C  CD2   . TRP A 1 321 ? -65.914 -29.725 -6.086  1.00 158.92 ? 424  TRP A CD2   1 
ATOM   2357 N  NE1   . TRP A 1 321 ? -65.793 -28.189 -4.459  1.00 173.88 ? 424  TRP A NE1   1 
ATOM   2358 C  CE2   . TRP A 1 321 ? -65.152 -28.655 -5.577  1.00 168.14 ? 424  TRP A CE2   1 
ATOM   2359 C  CE3   . TRP A 1 321 ? -65.470 -30.381 -7.237  1.00 153.00 ? 424  TRP A CE3   1 
ATOM   2360 C  CZ2   . TRP A 1 321 ? -63.972 -28.225 -6.180  1.00 161.08 ? 424  TRP A CZ2   1 
ATOM   2361 C  CZ3   . TRP A 1 321 ? -64.298 -29.954 -7.834  1.00 159.39 ? 424  TRP A CZ3   1 
ATOM   2362 C  CH2   . TRP A 1 321 ? -63.563 -28.886 -7.305  1.00 154.86 ? 424  TRP A CH2   1 
ATOM   2363 N  N     . GLY A 1 322 ? -66.869 -33.658 -6.083  1.00 154.13 ? 425  GLY A N     1 
ATOM   2364 C  CA    . GLY A 1 322 ? -65.779 -34.411 -6.679  1.00 139.98 ? 425  GLY A CA    1 
ATOM   2365 C  C     . GLY A 1 322 ? -66.013 -34.608 -8.159  1.00 143.89 ? 425  GLY A C     1 
ATOM   2366 O  O     . GLY A 1 322 ? -67.155 -34.626 -8.628  1.00 131.18 ? 425  GLY A O     1 
ATOM   2367 N  N     . ASN A 1 323 ? -64.917 -34.760 -8.900  1.00 140.28 ? 426  ASN A N     1 
ATOM   2368 C  CA    . ASN A 1 323 ? -64.974 -34.920 -10.348 1.00 123.65 ? 426  ASN A CA    1 
ATOM   2369 C  C     . ASN A 1 323 ? -64.034 -36.034 -10.779 1.00 114.26 ? 426  ASN A C     1 
ATOM   2370 O  O     . ASN A 1 323 ? -62.881 -36.082 -10.342 1.00 130.49 ? 426  ASN A O     1 
ATOM   2371 C  CB    . ASN A 1 323 ? -64.606 -33.616 -11.065 1.00 137.94 ? 426  ASN A CB    1 
ATOM   2372 C  CG    . ASN A 1 323 ? -65.745 -32.618 -11.079 1.00 136.07 ? 426  ASN A CG    1 
ATOM   2373 O  OD1   . ASN A 1 323 ? -66.441 -32.470 -12.083 1.00 140.07 ? 426  ASN A OD1   1 
ATOM   2374 N  ND2   . ASN A 1 323 ? -65.945 -31.930 -9.963  1.00 149.66 ? 426  ASN A ND2   1 
ATOM   2375 N  N     . ILE A 1 324 ? -64.534 -36.925 -11.633 1.00 118.29 ? 427  ILE A N     1 
ATOM   2376 C  CA    . ILE A 1 324 ? -63.747 -38.017 -12.198 1.00 107.45 ? 427  ILE A CA    1 
ATOM   2377 C  C     . ILE A 1 324 ? -64.060 -38.102 -13.685 1.00 113.45 ? 427  ILE A C     1 
ATOM   2378 O  O     . ILE A 1 324 ? -65.232 -38.096 -14.077 1.00 111.36 ? 427  ILE A O     1 
ATOM   2379 C  CB    . ILE A 1 324 ? -64.044 -39.365 -11.513 1.00 124.27 ? 427  ILE A CB    1 
ATOM   2380 C  CG1   . ILE A 1 324 ? -63.726 -39.300 -10.018 1.00 139.85 ? 427  ILE A CG1   1 
ATOM   2381 C  CG2   . ILE A 1 324 ? -63.254 -40.486 -12.171 1.00 154.21 ? 427  ILE A CG2   1 
ATOM   2382 C  CD1   . ILE A 1 324 ? -64.031 -40.582 -9.279  1.00 144.86 ? 427  ILE A CD1   1 
ATOM   2383 N  N     . ASN A 1 325 ? -63.021 -38.176 -14.511 1.00 129.00 ? 428  ASN A N     1 
ATOM   2384 C  CA    . ASN A 1 325 ? -63.214 -38.341 -15.945 1.00 145.15 ? 428  ASN A CA    1 
ATOM   2385 C  C     . ASN A 1 325 ? -63.531 -39.795 -16.271 1.00 134.18 ? 428  ASN A C     1 
ATOM   2386 O  O     . ASN A 1 325 ? -62.918 -40.718 -15.726 1.00 127.59 ? 428  ASN A O     1 
ATOM   2387 C  CB    . ASN A 1 325 ? -61.974 -37.879 -16.712 1.00 137.59 ? 428  ASN A CB    1 
ATOM   2388 C  CG    . ASN A 1 325 ? -60.681 -38.247 -16.012 1.00 145.73 ? 428  ASN A CG    1 
ATOM   2389 O  OD1   . ASN A 1 325 ? -60.658 -39.114 -15.138 1.00 158.56 ? 428  ASN A OD1   1 
ATOM   2390 N  ND2   . ASN A 1 325 ? -59.595 -37.584 -16.392 1.00 126.59 ? 428  ASN A ND2   1 
ATOM   2391 N  N     . LEU A 1 326 ? -64.503 -39.994 -17.165 1.00 114.26 ? 429  LEU A N     1 
ATOM   2392 C  CA    . LEU A 1 326 ? -64.968 -41.340 -17.482 1.00 110.56 ? 429  LEU A CA    1 
ATOM   2393 C  C     . LEU A 1 326 ? -63.915 -42.171 -18.204 1.00 115.65 ? 429  LEU A C     1 
ATOM   2394 O  O     . LEU A 1 326 ? -64.007 -43.403 -18.199 1.00 130.02 ? 429  LEU A O     1 
ATOM   2395 C  CB    . LEU A 1 326 ? -66.246 -41.270 -18.321 1.00 123.46 ? 429  LEU A CB    1 
ATOM   2396 C  CG    . LEU A 1 326 ? -67.442 -40.596 -17.644 1.00 127.92 ? 429  LEU A CG    1 
ATOM   2397 C  CD1   . LEU A 1 326 ? -68.682 -40.679 -18.522 1.00 123.63 ? 429  LEU A CD1   1 
ATOM   2398 C  CD2   . LEU A 1 326 ? -67.706 -41.211 -16.278 1.00 95.47  ? 429  LEU A CD2   1 
ATOM   2399 N  N     . PHE A 1 327 ? -62.926 -41.533 -18.823 1.00 125.63 ? 430  PHE A N     1 
ATOM   2400 C  CA    . PHE A 1 327 ? -61.812 -42.224 -19.456 1.00 110.25 ? 430  PHE A CA    1 
ATOM   2401 C  C     . PHE A 1 327 ? -60.510 -41.769 -18.813 1.00 117.15 ? 430  PHE A C     1 
ATOM   2402 O  O     . PHE A 1 327 ? -60.345 -40.585 -18.499 1.00 128.28 ? 430  PHE A O     1 
ATOM   2403 C  CB    . PHE A 1 327 ? -61.766 -41.955 -20.964 1.00 117.91 ? 430  PHE A CB    1 
ATOM   2404 C  CG    . PHE A 1 327 ? -62.994 -42.404 -21.703 1.00 118.23 ? 430  PHE A CG    1 
ATOM   2405 C  CD1   . PHE A 1 327 ? -63.087 -43.693 -22.201 1.00 111.51 ? 430  PHE A CD1   1 
ATOM   2406 C  CD2   . PHE A 1 327 ? -64.051 -41.533 -21.911 1.00 117.56 ? 430  PHE A CD2   1 
ATOM   2407 C  CE1   . PHE A 1 327 ? -64.214 -44.107 -22.885 1.00 114.27 ? 430  PHE A CE1   1 
ATOM   2408 C  CE2   . PHE A 1 327 ? -65.180 -41.941 -22.595 1.00 119.49 ? 430  PHE A CE2   1 
ATOM   2409 C  CZ    . PHE A 1 327 ? -65.262 -43.230 -23.082 1.00 100.43 ? 430  PHE A CZ    1 
ATOM   2410 N  N     . ASP A 1 328 ? -59.590 -42.708 -18.616 1.00 107.95 ? 431  ASP A N     1 
ATOM   2411 C  CA    . ASP A 1 328 ? -58.288 -42.386 -18.053 1.00 133.81 ? 431  ASP A CA    1 
ATOM   2412 C  C     . ASP A 1 328 ? -57.339 -41.967 -19.177 1.00 125.57 ? 431  ASP A C     1 
ATOM   2413 O  O     . ASP A 1 328 ? -57.752 -41.738 -20.316 1.00 131.15 ? 431  ASP A O     1 
ATOM   2414 C  CB    . ASP A 1 328 ? -57.751 -43.564 -17.241 1.00 107.64 ? 431  ASP A CB    1 
ATOM   2415 C  CG    . ASP A 1 328 ? -57.699 -44.852 -18.038 1.00 112.07 ? 431  ASP A CG    1 
ATOM   2416 O  OD1   . ASP A 1 328 ? -58.133 -44.853 -19.208 1.00 147.45 ? 431  ASP A OD1   1 
ATOM   2417 O  OD2   . ASP A 1 328 ? -57.221 -45.866 -17.488 1.00 97.03  ? 431  ASP A OD2   1 
ATOM   2418 N  N     . TYR A 1 329 ? -56.046 -41.862 -18.865 1.00 141.68 ? 432  TYR A N     1 
ATOM   2419 C  CA    . TYR A 1 329 ? -55.082 -41.344 -19.829 1.00 140.76 ? 432  TYR A CA    1 
ATOM   2420 C  C     . TYR A 1 329 ? -54.739 -42.340 -20.930 1.00 142.25 ? 432  TYR A C     1 
ATOM   2421 O  O     . TYR A 1 329 ? -54.085 -41.952 -21.903 1.00 142.85 ? 432  TYR A O     1 
ATOM   2422 C  CB    . TYR A 1 329 ? -53.805 -40.904 -19.109 1.00 146.35 ? 432  TYR A CB    1 
ATOM   2423 C  CG    . TYR A 1 329 ? -52.979 -42.038 -18.544 1.00 122.61 ? 432  TYR A CG    1 
ATOM   2424 C  CD1   . TYR A 1 329 ? -53.361 -42.690 -17.379 1.00 116.37 ? 432  TYR A CD1   1 
ATOM   2425 C  CD2   . TYR A 1 329 ? -51.807 -42.446 -19.168 1.00 133.48 ? 432  TYR A CD2   1 
ATOM   2426 C  CE1   . TYR A 1 329 ? -52.606 -43.725 -16.858 1.00 126.52 ? 432  TYR A CE1   1 
ATOM   2427 C  CE2   . TYR A 1 329 ? -51.045 -43.479 -18.655 1.00 122.28 ? 432  TYR A CE2   1 
ATOM   2428 C  CZ    . TYR A 1 329 ? -51.449 -44.114 -17.500 1.00 121.92 ? 432  TYR A CZ    1 
ATOM   2429 O  OH    . TYR A 1 329 ? -50.693 -45.142 -16.985 1.00 127.23 ? 432  TYR A OH    1 
ATOM   2430 N  N     . THR A 1 330 ? -55.160 -43.600 -20.809 1.00 119.29 ? 433  THR A N     1 
ATOM   2431 C  CA    . THR A 1 330 ? -54.910 -44.606 -21.832 1.00 123.96 ? 433  THR A CA    1 
ATOM   2432 C  C     . THR A 1 330 ? -56.144 -44.887 -22.686 1.00 134.95 ? 433  THR A C     1 
ATOM   2433 O  O     . THR A 1 330 ? -56.235 -45.958 -23.297 1.00 156.56 ? 433  THR A O     1 
ATOM   2434 C  CB    . THR A 1 330 ? -54.400 -45.899 -21.193 1.00 134.07 ? 433  THR A CB    1 
ATOM   2435 O  OG1   . THR A 1 330 ? -54.240 -46.903 -22.203 1.00 181.26 ? 433  THR A OG1   1 
ATOM   2436 C  CG2   . THR A 1 330 ? -55.372 -46.397 -20.138 1.00 140.98 ? 433  THR A CG2   1 
ATOM   2437 N  N     . ASP A 1 331 ? -57.092 -43.949 -22.732 1.00 132.96 ? 434  ASP A N     1 
ATOM   2438 C  CA    . ASP A 1 331 ? -58.285 -44.024 -23.576 1.00 139.12 ? 434  ASP A CA    1 
ATOM   2439 C  C     . ASP A 1 331 ? -59.169 -45.226 -23.253 1.00 143.33 ? 434  ASP A C     1 
ATOM   2440 O  O     . ASP A 1 331 ? -59.969 -45.651 -24.092 1.00 150.12 ? 434  ASP A O     1 
ATOM   2441 C  CB    . ASP A 1 331 ? -57.916 -44.032 -25.065 1.00 133.22 ? 434  ASP A CB    1 
ATOM   2442 C  CG    . ASP A 1 331 ? -57.317 -42.719 -25.526 1.00 135.13 ? 434  ASP A CG    1 
ATOM   2443 O  OD1   . ASP A 1 331 ? -57.085 -41.837 -24.673 1.00 156.03 ? 434  ASP A OD1   1 
ATOM   2444 O  OD2   . ASP A 1 331 ? -57.083 -42.566 -26.744 1.00 140.00 ? 434  ASP A OD2   1 
ATOM   2445 N  N     . THR A 1 332 ? -59.055 -45.783 -22.052 1.00 122.52 ? 435  THR A N     1 
ATOM   2446 C  CA    . THR A 1 332 ? -59.871 -46.917 -21.648 1.00 134.94 ? 435  THR A CA    1 
ATOM   2447 C  C     . THR A 1 332 ? -60.986 -46.463 -20.715 1.00 137.00 ? 435  THR A C     1 
ATOM   2448 O  O     . THR A 1 332 ? -60.818 -45.537 -19.918 1.00 135.00 ? 435  THR A O     1 
ATOM   2449 C  CB    . THR A 1 332 ? -59.025 -47.991 -20.960 1.00 136.50 ? 435  THR A CB    1 
ATOM   2450 O  OG1   . THR A 1 332 ? -58.441 -47.452 -19.768 1.00 148.80 ? 435  THR A OG1   1 
ATOM   2451 C  CG2   . THR A 1 332 ? -57.919 -48.474 -21.889 1.00 144.59 ? 435  THR A CG2   1 
ATOM   2452 N  N     . LEU A 1 333 ? -62.134 -47.127 -20.825 1.00 139.49 ? 436  LEU A N     1 
ATOM   2453 C  CA    . LEU A 1 333 ? -63.275 -46.792 -19.987 1.00 139.03 ? 436  LEU A CA    1 
ATOM   2454 C  C     . LEU A 1 333 ? -63.040 -47.254 -18.553 1.00 145.11 ? 436  LEU A C     1 
ATOM   2455 O  O     . LEU A 1 333 ? -62.379 -48.266 -18.301 1.00 172.07 ? 436  LEU A O     1 
ATOM   2456 C  CB    . LEU A 1 333 ? -64.550 -47.426 -20.544 1.00 140.58 ? 436  LEU A CB    1 
ATOM   2457 C  CG    . LEU A 1 333 ? -65.878 -47.006 -19.908 1.00 120.03 ? 436  LEU A CG    1 
ATOM   2458 C  CD1   . LEU A 1 333 ? -66.122 -45.519 -20.108 1.00 107.36 ? 436  LEU A CD1   1 
ATOM   2459 C  CD2   . LEU A 1 333 ? -67.029 -47.823 -20.473 1.00 135.36 ? 436  LEU A CD2   1 
ATOM   2460 N  N     . VAL A 1 334 ? -63.589 -46.494 -17.606 1.00 137.37 ? 437  VAL A N     1 
ATOM   2461 C  CA    . VAL A 1 334 ? -63.421 -46.813 -16.195 1.00 150.41 ? 437  VAL A CA    1 
ATOM   2462 C  C     . VAL A 1 334 ? -64.272 -48.025 -15.837 1.00 137.58 ? 437  VAL A C     1 
ATOM   2463 O  O     . VAL A 1 334 ? -65.388 -48.200 -16.347 1.00 142.27 ? 437  VAL A O     1 
ATOM   2464 C  CB    . VAL A 1 334 ? -63.775 -45.591 -15.328 1.00 142.86 ? 437  VAL A CB    1 
ATOM   2465 C  CG1   . VAL A 1 334 ? -65.219 -45.163 -15.559 1.00 121.63 ? 437  VAL A CG1   1 
ATOM   2466 C  CG2   . VAL A 1 334 ? -63.513 -45.875 -13.855 1.00 143.53 ? 437  VAL A CG2   1 
ATOM   2467 N  N     . SER A 1 335 ? -63.738 -48.883 -14.970 1.00 129.10 ? 438  SER A N     1 
ATOM   2468 C  CA    . SER A 1 335 ? -64.443 -50.079 -14.536 1.00 141.24 ? 438  SER A CA    1 
ATOM   2469 C  C     . SER A 1 335 ? -63.946 -50.479 -13.155 1.00 146.88 ? 438  SER A C     1 
ATOM   2470 O  O     . SER A 1 335 ? -62.802 -50.200 -12.786 1.00 133.63 ? 438  SER A O     1 
ATOM   2471 C  CB    . SER A 1 335 ? -64.254 -51.236 -15.525 1.00 170.08 ? 438  SER A CB    1 
ATOM   2472 O  OG    . SER A 1 335 ? -64.787 -50.914 -16.798 1.00 171.58 ? 438  SER A OG    1 
ATOM   2473 N  N     . GLY A 1 336 ? -64.819 -51.135 -12.396 1.00 169.84 ? 439  GLY A N     1 
ATOM   2474 C  CA    . GLY A 1 336 ? -64.475 -51.589 -11.065 1.00 147.61 ? 439  GLY A CA    1 
ATOM   2475 C  C     . GLY A 1 336 ? -64.850 -50.593 -9.987  1.00 130.01 ? 439  GLY A C     1 
ATOM   2476 O  O     . GLY A 1 336 ? -65.565 -49.610 -10.209 1.00 138.21 ? 439  GLY A O     1 
ATOM   2477 N  N     . LYS A 1 337 ? -64.351 -50.865 -8.785  1.00 144.99 ? 440  LYS A N     1 
ATOM   2478 C  CA    . LYS A 1 337 ? -64.587 -49.982 -7.655  1.00 147.28 ? 440  LYS A CA    1 
ATOM   2479 C  C     . LYS A 1 337 ? -63.559 -48.854 -7.636  1.00 153.61 ? 440  LYS A C     1 
ATOM   2480 O  O     . LYS A 1 337 ? -62.473 -48.954 -8.213  1.00 150.13 ? 440  LYS A O     1 
ATOM   2481 C  CB    . LYS A 1 337 ? -64.537 -50.759 -6.339  1.00 154.04 ? 440  LYS A CB    1 
ATOM   2482 C  CG    . LYS A 1 337 ? -65.562 -51.876 -6.233  1.00 181.73 ? 440  LYS A CG    1 
ATOM   2483 C  CD    . LYS A 1 337 ? -65.584 -52.474 -4.834  1.00 171.46 ? 440  LYS A CD    1 
ATOM   2484 C  CE    . LYS A 1 337 ? -64.208 -52.973 -4.422  1.00 182.31 ? 440  LYS A CE    1 
ATOM   2485 N  NZ    . LYS A 1 337 ? -63.694 -54.018 -5.350  1.00 192.69 ? 440  LYS A NZ    1 
ATOM   2486 N  N     . MET A 1 338 ? -63.918 -47.767 -6.957  1.00 143.71 ? 441  MET A N     1 
ATOM   2487 C  CA    . MET A 1 338 ? -63.058 -46.594 -6.898  1.00 131.13 ? 441  MET A CA    1 
ATOM   2488 C  C     . MET A 1 338 ? -63.401 -45.789 -5.653  1.00 126.13 ? 441  MET A C     1 
ATOM   2489 O  O     . MET A 1 338 ? -64.568 -45.710 -5.262  1.00 134.36 ? 441  MET A O     1 
ATOM   2490 C  CB    . MET A 1 338 ? -63.212 -45.733 -8.157  1.00 138.76 ? 441  MET A CB    1 
ATOM   2491 C  CG    . MET A 1 338 ? -62.180 -44.626 -8.292  1.00 148.72 ? 441  MET A CG    1 
ATOM   2492 S  SD    . MET A 1 338 ? -62.331 -43.735 -9.852  1.00 170.47 ? 441  MET A SD    1 
ATOM   2493 C  CE    . MET A 1 338 ? -60.942 -42.610 -9.734  1.00 176.27 ? 441  MET A CE    1 
ATOM   2494 N  N     . ALA A 1 339 ? -62.379 -45.197 -5.040  1.00 106.38 ? 442  ALA A N     1 
ATOM   2495 C  CA    . ALA A 1 339 ? -62.532 -44.372 -3.846  1.00 124.26 ? 442  ALA A CA    1 
ATOM   2496 C  C     . ALA A 1 339 ? -62.178 -42.934 -4.205  1.00 152.04 ? 442  ALA A C     1 
ATOM   2497 O  O     . ALA A 1 339 ? -61.011 -42.623 -4.468  1.00 143.88 ? 442  ALA A O     1 
ATOM   2498 C  CB    . ALA A 1 339 ? -61.654 -44.889 -2.708  1.00 137.66 ? 442  ALA A CB    1 
ATOM   2499 N  N     . LEU A 1 340 ? -63.182 -42.062 -4.215  1.00 147.35 ? 443  LEU A N     1 
ATOM   2500 C  CA    . LEU A 1 340 ? -63.010 -40.658 -4.559  1.00 145.59 ? 443  LEU A CA    1 
ATOM   2501 C  C     . LEU A 1 340 ? -63.069 -39.808 -3.298  1.00 156.05 ? 443  LEU A C     1 
ATOM   2502 O  O     . LEU A 1 340 ? -64.006 -39.934 -2.503  1.00 164.19 ? 443  LEU A O     1 
ATOM   2503 C  CB    . LEU A 1 340 ? -64.081 -40.198 -5.550  1.00 120.95 ? 443  LEU A CB    1 
ATOM   2504 C  CG    . LEU A 1 340 ? -64.086 -38.698 -5.857  1.00 120.83 ? 443  LEU A CG    1 
ATOM   2505 C  CD1   . LEU A 1 340 ? -62.793 -38.286 -6.545  1.00 127.38 ? 443  LEU A CD1   1 
ATOM   2506 C  CD2   . LEU A 1 340 ? -65.293 -38.316 -6.697  1.00 126.22 ? 443  LEU A CD2   1 
ATOM   2507 N  N     . ASN A 1 341 ? -62.074 -38.944 -3.123  1.00 152.67 ? 444  ASN A N     1 
ATOM   2508 C  CA    . ASN A 1 341 ? -62.029 -38.007 -2.010  1.00 145.18 ? 444  ASN A CA    1 
ATOM   2509 C  C     . ASN A 1 341 ? -62.519 -36.651 -2.504  1.00 141.64 ? 444  ASN A C     1 
ATOM   2510 O  O     . ASN A 1 341 ? -61.982 -36.111 -3.477  1.00 163.89 ? 444  ASN A O     1 
ATOM   2511 C  CB    . ASN A 1 341 ? -60.615 -37.905 -1.441  1.00 159.39 ? 444  ASN A CB    1 
ATOM   2512 C  CG    . ASN A 1 341 ? -60.598 -37.851 0.073   1.00 168.88 ? 444  ASN A CG    1 
ATOM   2513 O  OD1   . ASN A 1 341 ? -61.538 -38.296 0.732   1.00 176.70 ? 444  ASN A OD1   1 
ATOM   2514 N  ND2   . ASN A 1 341 ? -59.525 -37.305 0.634   1.00 174.00 ? 444  ASN A ND2   1 
ATOM   2515 N  N     . LEU A 1 342 ? -63.533 -36.108 -1.838  1.00 117.08 ? 445  LEU A N     1 
ATOM   2516 C  CA    . LEU A 1 342 ? -64.204 -34.906 -2.308  1.00 138.50 ? 445  LEU A CA    1 
ATOM   2517 C  C     . LEU A 1 342 ? -63.474 -33.647 -1.847  1.00 159.67 ? 445  LEU A C     1 
ATOM   2518 O  O     . LEU A 1 342 ? -62.633 -33.675 -0.946  1.00 146.19 ? 445  LEU A O     1 
ATOM   2519 C  CB    . LEU A 1 342 ? -65.654 -34.881 -1.824  1.00 144.85 ? 445  LEU A CB    1 
ATOM   2520 C  CG    . LEU A 1 342 ? -66.490 -36.113 -2.182  1.00 146.40 ? 445  LEU A CG    1 
ATOM   2521 C  CD1   . LEU A 1 342 ? -67.943 -35.912 -1.786  1.00 150.99 ? 445  LEU A CD1   1 
ATOM   2522 C  CD2   . LEU A 1 342 ? -66.375 -36.437 -3.664  1.00 126.60 ? 445  LEU A CD2   1 
ATOM   2523 N  N     . TRP A 1 343 ? -63.819 -32.522 -2.489  1.00 168.83 ? 446  TRP A N     1 
ATOM   2524 C  CA    . TRP A 1 343 ? -63.213 -31.221 -2.252  1.00 170.98 ? 446  TRP A CA    1 
ATOM   2525 C  C     . TRP A 1 343 ? -64.190 -30.286 -1.544  1.00 180.65 ? 446  TRP A C     1 
ATOM   2526 O  O     . TRP A 1 343 ? -65.408 -30.409 -1.709  1.00 189.21 ? 446  TRP A O     1 
ATOM   2527 C  CB    . TRP A 1 343 ? -62.772 -30.567 -3.568  1.00 154.11 ? 446  TRP A CB    1 
ATOM   2528 C  CG    . TRP A 1 343 ? -61.871 -31.419 -4.405  1.00 152.66 ? 446  TRP A CG    1 
ATOM   2529 C  CD1   . TRP A 1 343 ? -62.249 -32.352 -5.326  1.00 167.95 ? 446  TRP A CD1   1 
ATOM   2530 C  CD2   . TRP A 1 343 ? -60.439 -31.410 -4.407  1.00 147.74 ? 446  TRP A CD2   1 
ATOM   2531 N  NE1   . TRP A 1 343 ? -61.140 -32.928 -5.898  1.00 169.76 ? 446  TRP A NE1   1 
ATOM   2532 C  CE2   . TRP A 1 343 ? -60.017 -32.367 -5.351  1.00 153.18 ? 446  TRP A CE2   1 
ATOM   2533 C  CE3   . TRP A 1 343 ? -59.473 -30.688 -3.699  1.00 139.35 ? 446  TRP A CE3   1 
ATOM   2534 C  CZ2   . TRP A 1 343 ? -58.671 -32.620 -5.606  1.00 152.66 ? 446  TRP A CZ2   1 
ATOM   2535 C  CZ3   . TRP A 1 343 ? -58.137 -30.941 -3.954  1.00 139.45 ? 446  TRP A CZ3   1 
ATOM   2536 C  CH2   . TRP A 1 343 ? -57.749 -31.898 -4.899  1.00 148.41 ? 446  TRP A CH2   1 
ATOM   2537 N  N     . PRO A 1 344 ? -63.689 -29.343 -0.749  1.00 176.37 ? 447  PRO A N     1 
ATOM   2538 C  CA    . PRO A 1 344 ? -64.579 -28.344 -0.147  1.00 162.71 ? 447  PRO A CA    1 
ATOM   2539 C  C     . PRO A 1 344 ? -65.088 -27.361 -1.189  1.00 152.04 ? 447  PRO A C     1 
ATOM   2540 O  O     . PRO A 1 344 ? -64.383 -26.999 -2.134  1.00 155.75 ? 447  PRO A O     1 
ATOM   2541 C  CB    . PRO A 1 344 ? -63.686 -27.644 0.886   1.00 164.94 ? 447  PRO A CB    1 
ATOM   2542 C  CG    . PRO A 1 344 ? -62.510 -28.558 1.081   1.00 154.67 ? 447  PRO A CG    1 
ATOM   2543 C  CD    . PRO A 1 344 ? -62.314 -29.235 -0.237  1.00 148.90 ? 447  PRO A CD    1 
ATOM   2544 N  N     . VAL A 1 345 ? -66.332 -26.929 -1.005  1.00 160.12 ? 448  VAL A N     1 
ATOM   2545 C  CA    . VAL A 1 345 ? -66.968 -25.985 -1.922  1.00 173.32 ? 448  VAL A CA    1 
ATOM   2546 C  C     . VAL A 1 345 ? -66.322 -24.614 -1.755  1.00 179.20 ? 448  VAL A C     1 
ATOM   2547 O  O     . VAL A 1 345 ? -65.880 -24.268 -0.649  1.00 180.65 ? 448  VAL A O     1 
ATOM   2548 C  CB    . VAL A 1 345 ? -68.486 -25.916 -1.692  1.00 172.64 ? 448  VAL A CB    1 
ATOM   2549 C  CG1   . VAL A 1 345 ? -69.144 -27.225 -2.100  1.00 147.91 ? 448  VAL A CG1   1 
ATOM   2550 C  CG2   . VAL A 1 345 ? -68.791 -25.594 -0.236  1.00 184.50 ? 448  VAL A CG2   1 
ATOM   2551 N  N     . PRO A 1 346 ? -66.235 -23.807 -2.817  1.00 197.04 ? 449  PRO A N     1 
ATOM   2552 C  CA    . PRO A 1 346 ? -65.634 -22.472 -2.683  1.00 217.97 ? 449  PRO A CA    1 
ATOM   2553 C  C     . PRO A 1 346 ? -66.491 -21.521 -1.862  1.00 227.88 ? 449  PRO A C     1 
ATOM   2554 O  O     . PRO A 1 346 ? -67.524 -21.915 -1.310  1.00 218.20 ? 449  PRO A O     1 
ATOM   2555 C  CB    . PRO A 1 346 ? -65.509 -21.994 -4.138  1.00 203.59 ? 449  PRO A CB    1 
ATOM   2556 C  CG    . PRO A 1 346 ? -65.605 -23.238 -4.970  1.00 194.29 ? 449  PRO A CG    1 
ATOM   2557 C  CD    . PRO A 1 346 ? -66.527 -24.143 -4.219  1.00 188.02 ? 449  PRO A CD    1 
ATOM   2558 N  N     . HIS A 1 347 ? -66.066 -20.258 -1.778  1.00 220.30 ? 450  HIS A N     1 
ATOM   2559 C  CA    . HIS A 1 347 ? -66.824 -19.271 -1.017  1.00 214.04 ? 450  HIS A CA    1 
ATOM   2560 C  C     . HIS A 1 347 ? -68.159 -18.961 -1.683  1.00 217.94 ? 450  HIS A C     1 
ATOM   2561 O  O     . HIS A 1 347 ? -69.181 -18.817 -1.001  1.00 199.74 ? 450  HIS A O     1 
ATOM   2562 C  CB    . HIS A 1 347 ? -65.999 -17.995 -0.847  1.00 207.80 ? 450  HIS A CB    1 
ATOM   2563 C  CG    . HIS A 1 347 ? -66.762 -16.859 -0.239  1.00 208.61 ? 450  HIS A CG    1 
ATOM   2564 N  ND1   . HIS A 1 347 ? -67.325 -15.853 -0.994  1.00 199.93 ? 450  HIS A ND1   1 
ATOM   2565 C  CD2   . HIS A 1 347 ? -67.054 -16.569 1.051   1.00 210.08 ? 450  HIS A CD2   1 
ATOM   2566 C  CE1   . HIS A 1 347 ? -67.932 -14.993 -0.196  1.00 209.66 ? 450  HIS A CE1   1 
ATOM   2567 N  NE2   . HIS A 1 347 ? -67.782 -15.404 1.050   1.00 207.26 ? 450  HIS A NE2   1 
ATOM   2568 N  N     . GLY A 1 348 ? -68.172 -18.858 -3.009  1.00 216.21 ? 451  GLY A N     1 
ATOM   2569 C  CA    . GLY A 1 348 ? -69.393 -18.552 -3.729  1.00 196.41 ? 451  GLY A CA    1 
ATOM   2570 C  C     . GLY A 1 348 ? -69.742 -19.577 -4.787  1.00 187.48 ? 451  GLY A C     1 
ATOM   2571 O  O     . GLY A 1 348 ? -69.240 -19.513 -5.913  1.00 199.49 ? 451  GLY A O     1 
ATOM   2572 N  N     . LEU A 1 349 ? -70.603 -20.528 -4.437  1.00 198.51 ? 452  LEU A N     1 
ATOM   2573 C  CA    . LEU A 1 349 ? -71.064 -21.559 -5.356  1.00 196.66 ? 452  LEU A CA    1 
ATOM   2574 C  C     . LEU A 1 349 ? -72.581 -21.492 -5.454  1.00 208.70 ? 452  LEU A C     1 
ATOM   2575 O  O     . LEU A 1 349 ? -73.272 -21.466 -4.430  1.00 201.71 ? 452  LEU A O     1 
ATOM   2576 C  CB    . LEU A 1 349 ? -70.618 -22.950 -4.897  1.00 196.40 ? 452  LEU A CB    1 
ATOM   2577 C  CG    . LEU A 1 349 ? -70.988 -24.116 -5.816  1.00 199.38 ? 452  LEU A CG    1 
ATOM   2578 C  CD1   . LEU A 1 349 ? -70.391 -23.918 -7.201  1.00 196.04 ? 452  LEU A CD1   1 
ATOM   2579 C  CD2   . LEU A 1 349 ? -70.532 -25.438 -5.217  1.00 188.59 ? 452  LEU A CD2   1 
ATOM   2580 N  N     . GLU A 1 350 ? -73.094 -21.465 -6.684  1.00 222.12 ? 453  GLU A N     1 
ATOM   2581 C  CA    . GLU A 1 350 ? -74.538 -21.333 -6.914  1.00 221.26 ? 453  GLU A CA    1 
ATOM   2582 C  C     . GLU A 1 350 ? -75.197 -22.704 -7.036  1.00 216.79 ? 453  GLU A C     1 
ATOM   2583 O  O     . GLU A 1 350 ? -75.956 -23.118 -6.155  1.00 221.81 ? 453  GLU A O     1 
ATOM   2584 C  CB    . GLU A 1 350 ? -74.797 -20.480 -8.158  1.00 220.13 ? 453  GLU A CB    1 
ATOM   2585 C  CG    . GLU A 1 350 ? -76.262 -20.392 -8.559  1.00 237.26 ? 453  GLU A CG    1 
ATOM   2586 C  CD    . GLU A 1 350 ? -77.123 -19.730 -7.499  1.00 239.71 ? 453  GLU A CD    1 
ATOM   2587 O  OE1   . GLU A 1 350 ? -76.608 -18.860 -6.766  1.00 234.37 ? 453  GLU A OE1   1 
ATOM   2588 O  OE2   . GLU A 1 350 ? -78.317 -20.084 -7.398  1.00 238.30 ? 453  GLU A OE2   1 
ATOM   2589 N  N     . ASP A 1 351 ? -74.916 -23.412 -8.126  1.00 203.68 ? 454  ASP A N     1 
ATOM   2590 C  CA    . ASP A 1 351 ? -75.549 -24.700 -8.368  1.00 199.65 ? 454  ASP A CA    1 
ATOM   2591 C  C     . ASP A 1 351 ? -75.073 -25.735 -7.355  1.00 185.62 ? 454  ASP A C     1 
ATOM   2592 O  O     . ASP A 1 351 ? -73.974 -25.638 -6.800  1.00 183.23 ? 454  ASP A O     1 
ATOM   2593 C  CB    . ASP A 1 351 ? -75.255 -25.179 -9.790  1.00 208.23 ? 454  ASP A CB    1 
ATOM   2594 C  CG    . ASP A 1 351 ? -76.068 -26.402 -10.174 1.00 208.54 ? 454  ASP A CG    1 
ATOM   2595 O  OD1   . ASP A 1 351 ? -77.306 -26.282 -10.287 1.00 210.06 ? 454  ASP A OD1   1 
ATOM   2596 O  OD2   . ASP A 1 351 ? -75.470 -27.481 -10.365 1.00 199.38 ? 454  ASP A OD2   1 
ATOM   2597 N  N     . LEU A 1 352 ? -75.925 -26.734 -7.111  1.00 175.64 ? 455  LEU A N     1 
ATOM   2598 C  CA    . LEU A 1 352 ? -75.579 -27.798 -6.175  1.00 176.68 ? 455  LEU A CA    1 
ATOM   2599 C  C     . LEU A 1 352 ? -74.363 -28.579 -6.660  1.00 174.68 ? 455  LEU A C     1 
ATOM   2600 O  O     . LEU A 1 352 ? -73.430 -28.841 -5.891  1.00 161.10 ? 455  LEU A O     1 
ATOM   2601 C  CB    . LEU A 1 352 ? -76.775 -28.731 -5.982  1.00 153.94 ? 455  LEU A CB    1 
ATOM   2602 C  CG    . LEU A 1 352 ? -78.091 -28.090 -5.536  1.00 168.23 ? 455  LEU A CG    1 
ATOM   2603 C  CD1   . LEU A 1 352 ? -79.182 -29.143 -5.407  1.00 165.05 ? 455  LEU A CD1   1 
ATOM   2604 C  CD2   . LEU A 1 352 ? -77.910 -27.338 -4.227  1.00 170.94 ? 455  LEU A CD2   1 
ATOM   2605 N  N     . LEU A 1 353 ? -74.356 -28.955 -7.935  1.00 178.63 ? 456  LEU A N     1 
ATOM   2606 C  CA    . LEU A 1 353 ? -73.247 -29.692 -8.521  1.00 174.56 ? 456  LEU A CA    1 
ATOM   2607 C  C     . LEU A 1 353 ? -72.272 -28.729 -9.185  1.00 169.19 ? 456  LEU A C     1 
ATOM   2608 O  O     . LEU A 1 353 ? -72.678 -27.744 -9.807  1.00 168.31 ? 456  LEU A O     1 
ATOM   2609 C  CB    . LEU A 1 353 ? -73.762 -30.712 -9.538  1.00 161.10 ? 456  LEU A CB    1 
ATOM   2610 C  CG    . LEU A 1 353 ? -72.729 -31.600 -10.232 1.00 147.11 ? 456  LEU A CG    1 
ATOM   2611 C  CD1   . LEU A 1 353 ? -71.849 -32.296 -9.209  1.00 137.43 ? 456  LEU A CD1   1 
ATOM   2612 C  CD2   . LEU A 1 353 ? -73.425 -32.617 -11.120 1.00 145.32 ? 456  LEU A CD2   1 
ATOM   2613 N  N     . ASN A 1 354 ? -70.977 -29.019 -9.042  1.00 161.03 ? 457  ASN A N     1 
ATOM   2614 C  CA    . ASN A 1 354 ? -69.928 -28.176 -9.597  1.00 164.76 ? 457  ASN A CA    1 
ATOM   2615 C  C     . ASN A 1 354 ? -69.372 -28.820 -10.860 1.00 167.10 ? 457  ASN A C     1 
ATOM   2616 O  O     . ASN A 1 354 ? -68.544 -29.740 -10.768 1.00 171.66 ? 457  ASN A O     1 
ATOM   2617 C  CB    . ASN A 1 354 ? -68.815 -27.957 -8.569  1.00 171.61 ? 457  ASN A CB    1 
ATOM   2618 C  CG    . ASN A 1 354 ? -67.642 -27.182 -9.135  1.00 167.17 ? 457  ASN A CG    1 
ATOM   2619 O  OD1   . ASN A 1 354 ? -67.676 -25.955 -9.221  1.00 184.98 ? 457  ASN A OD1   1 
ATOM   2620 N  ND2   . ASN A 1 354 ? -66.592 -27.898 -9.521  1.00 157.45 ? 457  ASN A ND2   1 
ATOM   2621 N  N     . PRO A 1 355 ? -69.785 -28.386 -12.054 1.00 161.11 ? 458  PRO A N     1 
ATOM   2622 C  CA    . PRO A 1 355 ? -69.243 -29.003 -13.274 1.00 137.83 ? 458  PRO A CA    1 
ATOM   2623 C  C     . PRO A 1 355 ? -67.802 -28.618 -13.550 1.00 146.11 ? 458  PRO A C     1 
ATOM   2624 O  O     . PRO A 1 355 ? -67.043 -29.442 -14.075 1.00 144.68 ? 458  PRO A O     1 
ATOM   2625 C  CB    . PRO A 1 355 ? -70.187 -28.492 -14.370 1.00 155.31 ? 458  PRO A CB    1 
ATOM   2626 C  CG    . PRO A 1 355 ? -70.674 -27.181 -13.849 1.00 181.33 ? 458  PRO A CG    1 
ATOM   2627 C  CD    . PRO A 1 355 ? -70.774 -27.336 -12.353 1.00 180.91 ? 458  PRO A CD    1 
ATOM   2628 N  N     . ILE A 1 356 ? -67.400 -27.393 -13.215 1.00 188.82 ? 459  ILE A N     1 
ATOM   2629 C  CA    . ILE A 1 356 ? -66.030 -26.941 -13.428 1.00 200.60 ? 459  ILE A CA    1 
ATOM   2630 C  C     . ILE A 1 356 ? -65.141 -27.484 -12.317 1.00 195.18 ? 459  ILE A C     1 
ATOM   2631 O  O     . ILE A 1 356 ? -64.674 -26.734 -11.452 1.00 187.89 ? 459  ILE A O     1 
ATOM   2632 C  CB    . ILE A 1 356 ? -65.958 -25.404 -13.502 1.00 188.81 ? 459  ILE A CB    1 
ATOM   2633 C  CG1   . ILE A 1 356 ? -66.911 -24.773 -12.483 1.00 185.75 ? 459  ILE A CG1   1 
ATOM   2634 C  CG2   . ILE A 1 356 ? -66.279 -24.924 -14.910 1.00 171.45 ? 459  ILE A CG2   1 
ATOM   2635 C  CD1   . ILE A 1 356 ? -66.908 -23.260 -12.498 1.00 204.69 ? 459  ILE A CD1   1 
ATOM   2636 N  N     . GLY A 1 357 ? -64.898 -28.791 -12.336 1.00 180.63 ? 460  GLY A N     1 
ATOM   2637 C  CA    . GLY A 1 357 ? -64.106 -29.451 -11.320 1.00 166.36 ? 460  GLY A CA    1 
ATOM   2638 C  C     . GLY A 1 357 ? -62.646 -29.573 -11.700 1.00 141.82 ? 460  GLY A C     1 
ATOM   2639 O  O     . GLY A 1 357 ? -62.152 -28.912 -12.617 1.00 146.21 ? 460  GLY A O     1 
ATOM   2640 N  N     . VAL A 1 358 ? -61.946 -30.443 -10.974 1.00 154.28 ? 461  VAL A N     1 
ATOM   2641 C  CA    . VAL A 1 358 ? -60.519 -30.664 -11.187 1.00 158.82 ? 461  VAL A CA    1 
ATOM   2642 C  C     . VAL A 1 358 ? -60.211 -32.040 -11.755 1.00 173.30 ? 461  VAL A C     1 
ATOM   2643 O  O     . VAL A 1 358 ? -59.040 -32.310 -12.072 1.00 181.12 ? 461  VAL A O     1 
ATOM   2644 C  CB    . VAL A 1 358 ? -59.714 -30.444 -9.889  1.00 145.66 ? 461  VAL A CB    1 
ATOM   2645 C  CG1   . VAL A 1 358 ? -59.921 -29.029 -9.371  1.00 139.23 ? 461  VAL A CG1   1 
ATOM   2646 C  CG2   . VAL A 1 358 ? -60.114 -31.467 -8.838  1.00 164.63 ? 461  VAL A CG2   1 
ATOM   2647 N  N     . THR A 1 359 ? -61.210 -32.913 -11.896 1.00 170.00 ? 462  THR A N     1 
ATOM   2648 C  CA    . THR A 1 359 ? -61.032 -34.263 -12.437 1.00 166.44 ? 462  THR A CA    1 
ATOM   2649 C  C     . THR A 1 359 ? -59.956 -35.029 -11.669 1.00 168.55 ? 462  THR A C     1 
ATOM   2650 O  O     . THR A 1 359 ? -59.070 -35.661 -12.249 1.00 167.83 ? 462  THR A O     1 
ATOM   2651 C  CB    . THR A 1 359 ? -60.712 -34.223 -13.934 1.00 163.29 ? 462  THR A CB    1 
ATOM   2652 O  OG1   . THR A 1 359 ? -59.402 -33.678 -14.135 1.00 180.03 ? 462  THR A OG1   1 
ATOM   2653 C  CG2   . THR A 1 359 ? -61.728 -33.367 -14.672 1.00 175.81 ? 462  THR A CG2   1 
ATOM   2654 N  N     . GLY A 1 360 ? -60.043 -34.970 -10.344 1.00 144.54 ? 463  GLY A N     1 
ATOM   2655 C  CA    . GLY A 1 360 ? -59.085 -35.659 -9.501  1.00 149.35 ? 463  GLY A CA    1 
ATOM   2656 C  C     . GLY A 1 360 ? -59.611 -35.821 -8.095  1.00 123.89 ? 463  GLY A C     1 
ATOM   2657 O  O     . GLY A 1 360 ? -60.577 -35.166 -7.691  1.00 136.08 ? 463  GLY A O     1 
ATOM   2658 N  N     . SER A 1 361 ? -58.959 -36.707 -7.350  1.00 143.99 ? 464  SER A N     1 
ATOM   2659 C  CA    . SER A 1 361 ? -59.325 -36.972 -5.967  1.00 160.10 ? 464  SER A CA    1 
ATOM   2660 C  C     . SER A 1 361 ? -58.525 -36.082 -5.024  1.00 159.93 ? 464  SER A C     1 
ATOM   2661 O  O     . SER A 1 361 ? -57.412 -35.651 -5.337  1.00 166.31 ? 464  SER A O     1 
ATOM   2662 C  CB    . SER A 1 361 ? -59.098 -38.444 -5.617  1.00 152.75 ? 464  SER A CB    1 
ATOM   2663 O  OG    . SER A 1 361 ? -57.740 -38.809 -5.798  1.00 174.62 ? 464  SER A OG    1 
ATOM   2664 N  N     . ASN A 1 362 ? -59.107 -35.811 -3.862  1.00 156.66 ? 465  ASN A N     1 
ATOM   2665 C  CA    . ASN A 1 362 ? -58.470 -34.946 -2.876  1.00 159.96 ? 465  ASN A CA    1 
ATOM   2666 C  C     . ASN A 1 362 ? -57.340 -35.701 -2.184  1.00 172.17 ? 465  ASN A C     1 
ATOM   2667 O  O     . ASN A 1 362 ? -57.581 -36.776 -1.623  1.00 186.63 ? 465  ASN A O     1 
ATOM   2668 C  CB    . ASN A 1 362 ? -59.494 -34.468 -1.853  1.00 156.93 ? 465  ASN A CB    1 
ATOM   2669 C  CG    . ASN A 1 362 ? -59.040 -33.233 -1.095  1.00 158.71 ? 465  ASN A CG    1 
ATOM   2670 O  OD1   . ASN A 1 362 ? -57.859 -33.074 -0.787  1.00 160.49 ? 465  ASN A OD1   1 
ATOM   2671 N  ND2   . ASN A 1 362 ? -59.983 -32.349 -0.789  1.00 149.42 ? 465  ASN A ND2   1 
ATOM   2672 N  N     . PRO A 1 363 ? -56.106 -35.187 -2.199  1.00 177.95 ? 466  PRO A N     1 
ATOM   2673 C  CA    . PRO A 1 363 ? -55.009 -35.893 -1.525  1.00 177.27 ? 466  PRO A CA    1 
ATOM   2674 C  C     . PRO A 1 363 ? -54.863 -35.491 -0.066  1.00 171.14 ? 466  PRO A C     1 
ATOM   2675 O  O     . PRO A 1 363 ? -53.755 -35.493 0.479   1.00 164.71 ? 466  PRO A O     1 
ATOM   2676 C  CB    . PRO A 1 363 ? -53.779 -35.489 -2.349  1.00 179.16 ? 466  PRO A CB    1 
ATOM   2677 C  CG    . PRO A 1 363 ? -54.166 -34.191 -3.042  1.00 159.97 ? 466  PRO A CG    1 
ATOM   2678 C  CD    . PRO A 1 363 ? -55.643 -33.948 -2.845  1.00 164.62 ? 466  PRO A CD    1 
ATOM   2679 N  N     . ASN A 1 364 ? -55.979 -35.147 0.577   1.00 175.56 ? 467  ASN A N     1 
ATOM   2680 C  CA    . ASN A 1 364 ? -55.974 -34.780 1.986   1.00 198.95 ? 467  ASN A CA    1 
ATOM   2681 C  C     . ASN A 1 364 ? -56.144 -35.978 2.911   1.00 220.21 ? 467  ASN A C     1 
ATOM   2682 O  O     . ASN A 1 364 ? -55.833 -35.868 4.103   1.00 225.41 ? 467  ASN A O     1 
ATOM   2683 C  CB    . ASN A 1 364 ? -57.080 -33.754 2.263   1.00 189.18 ? 467  ASN A CB    1 
ATOM   2684 C  CG    . ASN A 1 364 ? -57.041 -33.217 3.681   1.00 196.81 ? 467  ASN A CG    1 
ATOM   2685 O  OD1   . ASN A 1 364 ? -57.812 -33.645 4.540   1.00 216.08 ? 467  ASN A OD1   1 
ATOM   2686 N  ND2   . ASN A 1 364 ? -56.139 -32.276 3.934   1.00 190.95 ? 467  ASN A ND2   1 
ATOM   2687 N  N     . LYS A 1 365 ? -56.636 -37.106 2.387   1.00 219.57 ? 468  LYS A N     1 
ATOM   2688 C  CA    . LYS A 1 365 ? -56.840 -38.367 3.115   1.00 235.53 ? 468  LYS A CA    1 
ATOM   2689 C  C     . LYS A 1 365 ? -57.545 -38.174 4.460   1.00 238.80 ? 468  LYS A C     1 
ATOM   2690 O  O     . LYS A 1 365 ? -57.489 -39.049 5.331   1.00 257.78 ? 468  LYS A O     1 
ATOM   2691 C  CB    . LYS A 1 365 ? -55.520 -39.134 3.297   1.00 248.43 ? 468  LYS A CB    1 
ATOM   2692 C  CG    . LYS A 1 365 ? -54.556 -38.585 4.341   1.00 239.45 ? 468  LYS A CG    1 
ATOM   2693 C  CD    . LYS A 1 365 ? -53.254 -39.370 4.356   1.00 250.11 ? 468  LYS A CD    1 
ATOM   2694 C  CE    . LYS A 1 365 ? -52.276 -38.797 5.367   1.00 240.92 ? 468  LYS A CE    1 
ATOM   2695 N  NZ    . LYS A 1 365 ? -50.983 -39.536 5.370   1.00 245.34 ? 468  LYS A NZ    1 
ATOM   2696 N  N     . GLU A 1 366 ? -58.230 -37.042 4.643   1.00 209.01 ? 469  GLU A N     1 
ATOM   2697 C  CA    . GLU A 1 366 ? -59.034 -36.811 5.834   1.00 202.27 ? 469  GLU A CA    1 
ATOM   2698 C  C     . GLU A 1 366 ? -60.397 -36.212 5.519   1.00 196.57 ? 469  GLU A C     1 
ATOM   2699 O  O     . GLU A 1 366 ? -61.202 -36.039 6.439   1.00 206.67 ? 469  GLU A O     1 
ATOM   2700 C  CB    . GLU A 1 366 ? -58.289 -35.897 6.823   1.00 201.40 ? 469  GLU A CB    1 
ATOM   2701 C  CG    . GLU A 1 366 ? -57.000 -36.490 7.374   1.00 203.56 ? 469  GLU A CG    1 
ATOM   2702 C  CD    . GLU A 1 366 ? -56.340 -35.599 8.409   1.00 211.65 ? 469  GLU A CD    1 
ATOM   2703 O  OE1   . GLU A 1 366 ? -56.958 -34.590 8.808   1.00 197.25 ? 469  GLU A OE1   1 
ATOM   2704 O  OE2   . GLU A 1 366 ? -55.202 -35.908 8.822   1.00 221.30 ? 469  GLU A OE2   1 
ATOM   2705 N  N     . THR A 1 367 ? -60.677 -35.893 4.262   1.00 189.01 ? 470  THR A N     1 
ATOM   2706 C  CA    . THR A 1 367 ? -61.971 -35.376 3.845   1.00 166.84 ? 470  THR A CA    1 
ATOM   2707 C  C     . THR A 1 367 ? -62.928 -36.536 3.588   1.00 151.77 ? 470  THR A C     1 
ATOM   2708 O  O     . THR A 1 367 ? -62.511 -37.695 3.515   1.00 148.70 ? 470  THR A O     1 
ATOM   2709 C  CB    . THR A 1 367 ? -61.793 -34.507 2.602   1.00 177.73 ? 470  THR A CB    1 
ATOM   2710 O  OG1   . THR A 1 367 ? -61.111 -35.255 1.588   1.00 185.79 ? 470  THR A OG1   1 
ATOM   2711 C  CG2   . THR A 1 367 ? -60.986 -33.261 2.936   1.00 178.32 ? 470  THR A CG2   1 
ATOM   2712 N  N     . PRO A 1 368 ? -64.229 -36.264 3.468   1.00 151.98 ? 471  PRO A N     1 
ATOM   2713 C  CA    . PRO A 1 368 ? -65.177 -37.346 3.161   1.00 162.03 ? 471  PRO A CA    1 
ATOM   2714 C  C     . PRO A 1 368 ? -64.830 -38.046 1.854   1.00 164.76 ? 471  PRO A C     1 
ATOM   2715 O  O     . PRO A 1 368 ? -64.648 -37.408 0.814   1.00 148.69 ? 471  PRO A O     1 
ATOM   2716 C  CB    . PRO A 1 368 ? -66.529 -36.624 3.080   1.00 156.93 ? 471  PRO A CB    1 
ATOM   2717 C  CG    . PRO A 1 368 ? -66.199 -35.165 2.973   1.00 147.03 ? 471  PRO A CG    1 
ATOM   2718 C  CD    . PRO A 1 368 ? -64.933 -35.000 3.743   1.00 161.94 ? 471  PRO A CD    1 
ATOM   2719 N  N     . CYS A 1 369 ? -64.744 -39.372 1.919   1.00 162.86 ? 472  CYS A N     1 
ATOM   2720 C  CA    . CYS A 1 369 ? -64.372 -40.210 0.786   1.00 144.16 ? 472  CYS A CA    1 
ATOM   2721 C  C     . CYS A 1 369 ? -65.596 -40.981 0.312   1.00 143.43 ? 472  CYS A C     1 
ATOM   2722 O  O     . CYS A 1 369 ? -66.146 -41.798 1.059   1.00 152.17 ? 472  CYS A O     1 
ATOM   2723 C  CB    . CYS A 1 369 ? -63.245 -41.170 1.168   1.00 142.75 ? 472  CYS A CB    1 
ATOM   2724 S  SG    . CYS A 1 369 ? -62.872 -42.428 -0.073  1.00 152.46 ? 472  CYS A SG    1 
ATOM   2725 N  N     . LEU A 1 370 ? -66.016 -40.724 -0.924  1.00 148.13 ? 473  LEU A N     1 
ATOM   2726 C  CA    . LEU A 1 370 ? -67.165 -41.389 -1.522  1.00 124.86 ? 473  LEU A CA    1 
ATOM   2727 C  C     . LEU A 1 370 ? -66.689 -42.567 -2.363  1.00 136.14 ? 473  LEU A C     1 
ATOM   2728 O  O     . LEU A 1 370 ? -65.838 -42.403 -3.243  1.00 146.92 ? 473  LEU A O     1 
ATOM   2729 C  CB    . LEU A 1 370 ? -67.970 -40.413 -2.382  1.00 111.04 ? 473  LEU A CB    1 
ATOM   2730 C  CG    . LEU A 1 370 ? -69.268 -40.933 -3.005  1.00 141.44 ? 473  LEU A CG    1 
ATOM   2731 C  CD1   . LEU A 1 370 ? -70.278 -41.293 -1.927  1.00 120.11 ? 473  LEU A CD1   1 
ATOM   2732 C  CD2   . LEU A 1 370 ? -69.849 -39.910 -3.969  1.00 138.09 ? 473  LEU A CD2   1 
ATOM   2733 N  N     . GLU A 1 371 ? -67.237 -43.747 -2.089  1.00 141.63 ? 474  GLU A N     1 
ATOM   2734 C  CA    . GLU A 1 371 ? -66.875 -44.963 -2.802  1.00 151.82 ? 474  GLU A CA    1 
ATOM   2735 C  C     . GLU A 1 371 ? -67.907 -45.264 -3.881  1.00 155.12 ? 474  GLU A C     1 
ATOM   2736 O  O     . GLU A 1 371 ? -69.112 -45.105 -3.665  1.00 143.48 ? 474  GLU A O     1 
ATOM   2737 C  CB    . GLU A 1 371 ? -66.763 -46.148 -1.840  1.00 142.96 ? 474  GLU A CB    1 
ATOM   2738 C  CG    . GLU A 1 371 ? -65.747 -45.947 -0.728  1.00 135.90 ? 474  GLU A CG    1 
ATOM   2739 C  CD    . GLU A 1 371 ? -65.597 -47.171 0.153   1.00 159.24 ? 474  GLU A CD    1 
ATOM   2740 O  OE1   . GLU A 1 371 ? -66.101 -48.247 -0.232  1.00 162.36 ? 474  GLU A OE1   1 
ATOM   2741 O  OE2   . GLU A 1 371 ? -64.977 -47.056 1.231   1.00 185.03 ? 474  GLU A OE2   1 
ATOM   2742 N  N     . LEU A 1 372 ? -67.427 -45.700 -5.043  1.00 145.78 ? 475  LEU A N     1 
ATOM   2743 C  CA    . LEU A 1 372 ? -68.279 -45.991 -6.185  1.00 137.51 ? 475  LEU A CA    1 
ATOM   2744 C  C     . LEU A 1 372 ? -67.915 -47.349 -6.770  1.00 143.49 ? 475  LEU A C     1 
ATOM   2745 O  O     . LEU A 1 372 ? -66.955 -48.000 -6.352  1.00 153.75 ? 475  LEU A O     1 
ATOM   2746 C  CB    . LEU A 1 372 ? -68.165 -44.911 -7.271  1.00 156.86 ? 475  LEU A CB    1 
ATOM   2747 C  CG    . LEU A 1 372 ? -68.690 -43.502 -6.984  1.00 156.76 ? 475  LEU A CG    1 
ATOM   2748 C  CD1   . LEU A 1 372 ? -67.666 -42.667 -6.229  1.00 133.99 ? 475  LEU A CD1   1 
ATOM   2749 C  CD2   . LEU A 1 372 ? -69.093 -42.819 -8.283  1.00 139.78 ? 475  LEU A CD2   1 
ATOM   2750 N  N     . GLU A 1 373 ? -68.707 -47.768 -7.754  1.00 141.95 ? 476  GLU A N     1 
ATOM   2751 C  CA    . GLU A 1 373 ? -68.442 -48.991 -8.504  1.00 146.03 ? 476  GLU A CA    1 
ATOM   2752 C  C     . GLU A 1 373 ? -68.995 -48.807 -9.908  1.00 155.40 ? 476  GLU A C     1 
ATOM   2753 O  O     . GLU A 1 373 ? -70.184 -48.517 -10.072 1.00 151.60 ? 476  GLU A O     1 
ATOM   2754 C  CB    . GLU A 1 373 ? -69.069 -50.212 -7.827  1.00 163.60 ? 476  GLU A CB    1 
ATOM   2755 C  CG    . GLU A 1 373 ? -68.887 -51.507 -8.605  1.00 177.40 ? 476  GLU A CG    1 
ATOM   2756 C  CD    . GLU A 1 373 ? -69.419 -52.717 -7.862  1.00 179.70 ? 476  GLU A CD    1 
ATOM   2757 O  OE1   . GLU A 1 373 ? -69.569 -52.639 -6.625  1.00 175.94 ? 476  GLU A OE1   1 
ATOM   2758 O  OE2   . GLU A 1 373 ? -69.691 -53.745 -8.517  1.00 193.54 ? 476  GLU A OE2   1 
ATOM   2759 N  N     . PHE A 1 374 ? -68.138 -48.970 -10.909 1.00 149.02 ? 477  PHE A N     1 
ATOM   2760 C  CA    . PHE A 1 374 ? -68.504 -48.749 -12.299 1.00 136.60 ? 477  PHE A CA    1 
ATOM   2761 C  C     . PHE A 1 374 ? -68.875 -50.067 -12.971 1.00 149.95 ? 477  PHE A C     1 
ATOM   2762 O  O     . PHE A 1 374 ? -68.653 -51.156 -12.437 1.00 178.41 ? 477  PHE A O     1 
ATOM   2763 C  CB    . PHE A 1 374 ? -67.357 -48.064 -13.049 1.00 140.70 ? 477  PHE A CB    1 
ATOM   2764 C  CG    . PHE A 1 374 ? -66.929 -46.758 -12.438 1.00 145.42 ? 477  PHE A CG    1 
ATOM   2765 C  CD1   . PHE A 1 374 ? -65.959 -46.723 -11.450 1.00 153.59 ? 477  PHE A CD1   1 
ATOM   2766 C  CD2   . PHE A 1 374 ? -67.497 -45.565 -12.852 1.00 129.13 ? 477  PHE A CD2   1 
ATOM   2767 C  CE1   . PHE A 1 374 ? -65.565 -45.524 -10.887 1.00 148.92 ? 477  PHE A CE1   1 
ATOM   2768 C  CE2   . PHE A 1 374 ? -67.109 -44.363 -12.293 1.00 122.85 ? 477  PHE A CE2   1 
ATOM   2769 C  CZ    . PHE A 1 374 ? -66.141 -44.342 -11.309 1.00 151.12 ? 477  PHE A CZ    1 
ATOM   2770 N  N     . ASP A 1 375 ? -69.454 -49.953 -14.164 1.00 151.21 ? 478  ASP A N     1 
ATOM   2771 C  CA    . ASP A 1 375 ? -69.871 -51.130 -14.911 1.00 157.76 ? 478  ASP A CA    1 
ATOM   2772 C  C     . ASP A 1 375 ? -68.655 -51.936 -15.357 1.00 169.97 ? 478  ASP A C     1 
ATOM   2773 O  O     . ASP A 1 375 ? -67.569 -51.395 -15.581 1.00 159.16 ? 478  ASP A O     1 
ATOM   2774 C  CB    . ASP A 1 375 ? -70.711 -50.722 -16.121 1.00 158.02 ? 478  ASP A CB    1 
ATOM   2775 C  CG    . ASP A 1 375 ? -71.657 -51.817 -16.571 1.00 173.43 ? 478  ASP A CG    1 
ATOM   2776 O  OD1   . ASP A 1 375 ? -71.382 -53.001 -16.283 1.00 177.48 ? 478  ASP A OD1   1 
ATOM   2777 O  OD2   . ASP A 1 375 ? -72.679 -51.494 -17.213 1.00 171.42 ? 478  ASP A OD2   1 
ATOM   2778 N  N     . TRP A 1 376 ? -68.849 -53.249 -15.485 1.00 181.32 ? 479  TRP A N     1 
ATOM   2779 C  CA    . TRP A 1 376 ? -67.741 -54.164 -15.748 1.00 190.40 ? 479  TRP A CA    1 
ATOM   2780 C  C     . TRP A 1 376 ? -67.542 -54.420 -17.240 1.00 195.73 ? 479  TRP A C     1 
ATOM   2781 O  O     . TRP A 1 376 ? -66.465 -54.151 -17.782 1.00 195.62 ? 479  TRP A O     1 
ATOM   2782 C  CB    . TRP A 1 376 ? -67.971 -55.488 -15.010 1.00 177.53 ? 479  TRP A CB    1 
ATOM   2783 C  CG    . TRP A 1 376 ? -66.786 -56.401 -15.050 1.00 185.94 ? 479  TRP A CG    1 
ATOM   2784 C  CD1   . TRP A 1 376 ? -65.472 -56.038 -15.009 1.00 204.85 ? 479  TRP A CD1   1 
ATOM   2785 C  CD2   . TRP A 1 376 ? -66.806 -57.829 -15.153 1.00 189.72 ? 479  TRP A CD2   1 
ATOM   2786 N  NE1   . TRP A 1 376 ? -64.671 -57.153 -15.072 1.00 208.27 ? 479  TRP A NE1   1 
ATOM   2787 C  CE2   . TRP A 1 376 ? -65.466 -58.265 -15.162 1.00 198.21 ? 479  TRP A CE2   1 
ATOM   2788 C  CE3   . TRP A 1 376 ? -67.825 -58.782 -15.236 1.00 192.00 ? 479  TRP A CE3   1 
ATOM   2789 C  CZ2   . TRP A 1 376 ? -65.119 -59.612 -15.250 1.00 223.62 ? 479  TRP A CZ2   1 
ATOM   2790 C  CZ3   . TRP A 1 376 ? -67.480 -60.118 -15.322 1.00 179.40 ? 479  TRP A CZ3   1 
ATOM   2791 C  CH2   . TRP A 1 376 ? -66.138 -60.521 -15.329 1.00 216.87 ? 479  TRP A CH2   1 
ATOM   2792 N  N     . PHE A 1 377 ? -68.567 -54.956 -17.905 1.00 167.46 ? 480  PHE A N     1 
ATOM   2793 C  CA    . PHE A 1 377 ? -68.575 -55.381 -19.305 1.00 151.21 ? 480  PHE A CA    1 
ATOM   2794 C  C     . PHE A 1 377 ? -67.690 -56.595 -19.563 1.00 163.71 ? 480  PHE A C     1 
ATOM   2795 O  O     . PHE A 1 377 ? -67.631 -57.064 -20.707 1.00 154.66 ? 480  PHE A O     1 
ATOM   2796 C  CB    . PHE A 1 377 ? -68.160 -54.260 -20.271 1.00 144.40 ? 480  PHE A CB    1 
ATOM   2797 C  CG    . PHE A 1 377 ? -68.896 -52.971 -20.058 1.00 154.87 ? 480  PHE A CG    1 
ATOM   2798 C  CD1   . PHE A 1 377 ? -70.195 -52.815 -20.512 1.00 136.86 ? 480  PHE A CD1   1 
ATOM   2799 C  CD2   . PHE A 1 377 ? -68.286 -51.911 -19.410 1.00 181.79 ? 480  PHE A CD2   1 
ATOM   2800 C  CE1   . PHE A 1 377 ? -70.873 -51.628 -20.317 1.00 145.68 ? 480  PHE A CE1   1 
ATOM   2801 C  CE2   . PHE A 1 377 ? -68.958 -50.721 -19.213 1.00 176.77 ? 480  PHE A CE2   1 
ATOM   2802 C  CZ    . PHE A 1 377 ? -70.253 -50.580 -19.667 1.00 141.75 ? 480  PHE A CZ    1 
ATOM   2803 N  N     . SER A 1 378 ? -67.001 -57.119 -18.545 1.00 171.39 ? 481  SER A N     1 
ATOM   2804 C  CA    . SER A 1 378 ? -66.143 -58.302 -18.669 1.00 173.01 ? 481  SER A CA    1 
ATOM   2805 C  C     . SER A 1 378 ? -65.068 -58.124 -19.738 1.00 173.75 ? 481  SER A C     1 
ATOM   2806 O  O     . SER A 1 378 ? -64.588 -59.102 -20.317 1.00 188.50 ? 481  SER A O     1 
ATOM   2807 C  CB    . SER A 1 378 ? -66.967 -59.564 -18.947 1.00 168.39 ? 481  SER A CB    1 
ATOM   2808 O  OG    . SER A 1 378 ? -67.531 -59.539 -20.247 1.00 145.33 ? 481  SER A OG    1 
ATOM   2809 N  N     . SER A 1 379 ? -64.675 -56.881 -20.004 1.00 176.82 ? 482  SER A N     1 
ATOM   2810 C  CA    . SER A 1 379 ? -63.655 -56.596 -21.003 1.00 159.40 ? 482  SER A CA    1 
ATOM   2811 C  C     . SER A 1 379 ? -63.124 -55.190 -20.771 1.00 158.18 ? 482  SER A C     1 
ATOM   2812 O  O     . SER A 1 379 ? -63.739 -54.382 -20.071 1.00 174.34 ? 482  SER A O     1 
ATOM   2813 C  CB    . SER A 1 379 ? -64.204 -56.739 -22.427 1.00 163.51 ? 482  SER A CB    1 
ATOM   2814 O  OG    . SER A 1 379 ? -63.188 -56.522 -23.390 1.00 187.70 ? 482  SER A OG    1 
ATOM   2815 N  N     . VAL A 1 380 ? -61.970 -54.910 -21.372 1.00 163.01 ? 483  VAL A N     1 
ATOM   2816 C  CA    . VAL A 1 380 ? -61.322 -53.608 -21.253 1.00 147.71 ? 483  VAL A CA    1 
ATOM   2817 C  C     . VAL A 1 380 ? -61.889 -52.718 -22.355 1.00 137.81 ? 483  VAL A C     1 
ATOM   2818 O  O     . VAL A 1 380 ? -61.417 -52.736 -23.492 1.00 171.04 ? 483  VAL A O     1 
ATOM   2819 C  CB    . VAL A 1 380 ? -59.800 -53.721 -21.341 1.00 107.37 ? 483  VAL A CB    1 
ATOM   2820 C  CG1   . VAL A 1 380 ? -59.155 -52.354 -21.175 1.00 125.29 ? 483  VAL A CG1   1 
ATOM   2821 C  CG2   . VAL A 1 380 ? -59.281 -54.691 -20.291 1.00 139.21 ? 483  VAL A CG2   1 
ATOM   2822 N  N     . VAL A 1 381 ? -62.910 -51.933 -22.014 1.00 157.83 ? 484  VAL A N     1 
ATOM   2823 C  CA    . VAL A 1 381 ? -63.535 -51.045 -22.987 1.00 156.29 ? 484  VAL A CA    1 
ATOM   2824 C  C     . VAL A 1 381 ? -62.613 -49.858 -23.231 1.00 151.00 ? 484  VAL A C     1 
ATOM   2825 O  O     . VAL A 1 381 ? -62.319 -49.083 -22.313 1.00 158.44 ? 484  VAL A O     1 
ATOM   2826 C  CB    . VAL A 1 381 ? -64.918 -50.588 -22.506 1.00 172.90 ? 484  VAL A CB    1 
ATOM   2827 C  CG1   . VAL A 1 381 ? -65.597 -49.747 -23.574 1.00 149.28 ? 484  VAL A CG1   1 
ATOM   2828 C  CG2   . VAL A 1 381 ? -65.774 -51.791 -22.139 1.00 174.98 ? 484  VAL A CG2   1 
ATOM   2829 N  N     . LYS A 1 382 ? -62.152 -49.712 -24.470 1.00 126.09 ? 485  LYS A N     1 
ATOM   2830 C  CA    . LYS A 1 382 ? -61.227 -48.655 -24.852 1.00 127.39 ? 485  LYS A CA    1 
ATOM   2831 C  C     . LYS A 1 382 ? -61.874 -47.761 -25.900 1.00 113.21 ? 485  LYS A C     1 
ATOM   2832 O  O     . LYS A 1 382 ? -62.584 -48.244 -26.788 1.00 125.05 ? 485  LYS A O     1 
ATOM   2833 C  CB    . LYS A 1 382 ? -59.917 -49.243 -25.393 1.00 111.33 ? 485  LYS A CB    1 
ATOM   2834 C  CG    . LYS A 1 382 ? -58.854 -48.211 -25.729 1.00 119.85 ? 485  LYS A CG    1 
ATOM   2835 C  CD    . LYS A 1 382 ? -57.588 -48.874 -26.247 1.00 149.26 ? 485  LYS A CD    1 
ATOM   2836 C  CE    . LYS A 1 382 ? -56.525 -47.842 -26.588 1.00 172.33 ? 485  LYS A CE    1 
ATOM   2837 N  NZ    . LYS A 1 382 ? -55.277 -48.477 -27.097 1.00 181.62 ? 485  LYS A NZ    1 
ATOM   2838 N  N     . PHE A 1 383 ? -61.631 -46.459 -25.788 1.00 115.49 ? 486  PHE A N     1 
ATOM   2839 C  CA    . PHE A 1 383 ? -62.182 -45.517 -26.749 1.00 115.60 ? 486  PHE A CA    1 
ATOM   2840 C  C     . PHE A 1 383 ? -61.592 -45.787 -28.132 1.00 124.02 ? 486  PHE A C     1 
ATOM   2841 O  O     . PHE A 1 383 ? -60.383 -46.019 -28.256 1.00 150.00 ? 486  PHE A O     1 
ATOM   2842 C  CB    . PHE A 1 383 ? -61.890 -44.078 -26.317 1.00 135.66 ? 486  PHE A CB    1 
ATOM   2843 C  CG    . PHE A 1 383 ? -62.687 -43.043 -27.061 1.00 126.80 ? 486  PHE A CG    1 
ATOM   2844 C  CD1   . PHE A 1 383 ? -63.958 -42.692 -26.637 1.00 119.99 ? 486  PHE A CD1   1 
ATOM   2845 C  CD2   . PHE A 1 383 ? -62.164 -42.416 -28.180 1.00 146.96 ? 486  PHE A CD2   1 
ATOM   2846 C  CE1   . PHE A 1 383 ? -64.694 -41.739 -27.318 1.00 129.59 ? 486  PHE A CE1   1 
ATOM   2847 C  CE2   . PHE A 1 383 ? -62.895 -41.462 -28.865 1.00 123.81 ? 486  PHE A CE2   1 
ATOM   2848 C  CZ    . PHE A 1 383 ? -64.161 -41.124 -28.433 1.00 105.89 ? 486  PHE A CZ    1 
ATOM   2849 N  N     . PRO A 1 384 ? -62.406 -45.770 -29.185 1.00 119.68 ? 487  PRO A N     1 
ATOM   2850 C  CA    . PRO A 1 384 ? -61.894 -46.117 -30.515 1.00 146.89 ? 487  PRO A CA    1 
ATOM   2851 C  C     . PRO A 1 384 ? -60.935 -45.065 -31.048 1.00 134.87 ? 487  PRO A C     1 
ATOM   2852 O  O     . PRO A 1 384 ? -61.028 -43.878 -30.725 1.00 129.08 ? 487  PRO A O     1 
ATOM   2853 C  CB    . PRO A 1 384 ? -63.162 -46.196 -31.372 1.00 140.53 ? 487  PRO A CB    1 
ATOM   2854 C  CG    . PRO A 1 384 ? -64.130 -45.296 -30.681 1.00 128.77 ? 487  PRO A CG    1 
ATOM   2855 C  CD    . PRO A 1 384 ? -63.842 -45.445 -29.212 1.00 112.31 ? 487  PRO A CD    1 
ATOM   2856 N  N     . ASP A 1 385 ? -60.002 -45.521 -31.880 1.00 137.10 ? 488  ASP A N     1 
ATOM   2857 C  CA    . ASP A 1 385 ? -59.034 -44.633 -32.503 1.00 159.22 ? 488  ASP A CA    1 
ATOM   2858 C  C     . ASP A 1 385 ? -59.696 -43.845 -33.633 1.00 140.73 ? 488  ASP A C     1 
ATOM   2859 O  O     . ASP A 1 385 ? -60.875 -44.027 -33.950 1.00 138.83 ? 488  ASP A O     1 
ATOM   2860 C  CB    . ASP A 1 385 ? -57.835 -45.429 -33.013 1.00 162.34 ? 488  ASP A CB    1 
ATOM   2861 C  CG    . ASP A 1 385 ? -58.231 -46.520 -33.989 1.00 156.15 ? 488  ASP A CG    1 
ATOM   2862 O  OD1   . ASP A 1 385 ? -59.342 -47.073 -33.844 1.00 156.20 ? 488  ASP A OD1   1 
ATOM   2863 O  OD2   . ASP A 1 385 ? -57.433 -46.825 -34.899 1.00 151.45 ? 488  ASP A OD2   1 
ATOM   2864 N  N     . MET A 1 386 ? -58.919 -42.954 -34.254 1.00 132.25 ? 489  MET A N     1 
ATOM   2865 C  CA    . MET A 1 386 ? -59.452 -42.131 -35.334 1.00 141.37 ? 489  MET A CA    1 
ATOM   2866 C  C     . MET A 1 386 ? -59.850 -42.972 -36.542 1.00 148.24 ? 489  MET A C     1 
ATOM   2867 O  O     . MET A 1 386 ? -60.743 -42.578 -37.300 1.00 145.24 ? 489  MET A O     1 
ATOM   2868 C  CB    . MET A 1 386 ? -58.428 -41.065 -35.731 1.00 164.12 ? 489  MET A CB    1 
ATOM   2869 C  CG    . MET A 1 386 ? -58.869 -40.148 -36.865 1.00 181.01 ? 489  MET A CG    1 
ATOM   2870 S  SD    . MET A 1 386 ? -60.436 -39.314 -36.541 1.00 123.98 ? 489  MET A SD    1 
ATOM   2871 C  CE    . MET A 1 386 ? -59.984 -38.255 -35.171 1.00 121.63 ? 489  MET A CE    1 
ATOM   2872 N  N     . SER A 1 387 ? -59.213 -44.132 -36.729 1.00 161.49 ? 490  SER A N     1 
ATOM   2873 C  CA    . SER A 1 387 ? -59.548 -44.988 -37.863 1.00 144.24 ? 490  SER A CA    1 
ATOM   2874 C  C     . SER A 1 387 ? -61.000 -45.448 -37.802 1.00 147.82 ? 490  SER A C     1 
ATOM   2875 O  O     . SER A 1 387 ? -61.707 -45.428 -38.816 1.00 149.18 ? 490  SER A O     1 
ATOM   2876 C  CB    . SER A 1 387 ? -58.606 -46.192 -37.907 1.00 146.54 ? 490  SER A CB    1 
ATOM   2877 O  OG    . SER A 1 387 ? -58.943 -47.066 -38.970 1.00 170.62 ? 490  SER A OG    1 
ATOM   2878 N  N     . VAL A 1 388 ? -61.461 -45.867 -36.623 1.00 140.91 ? 491  VAL A N     1 
ATOM   2879 C  CA    . VAL A 1 388 ? -62.853 -46.282 -36.485 1.00 122.64 ? 491  VAL A CA    1 
ATOM   2880 C  C     . VAL A 1 388 ? -63.781 -45.071 -36.450 1.00 147.79 ? 491  VAL A C     1 
ATOM   2881 O  O     . VAL A 1 388 ? -64.926 -45.150 -36.910 1.00 141.09 ? 491  VAL A O     1 
ATOM   2882 C  CB    . VAL A 1 388 ? -63.023 -47.160 -35.233 1.00 116.69 ? 491  VAL A CB    1 
ATOM   2883 C  CG1   . VAL A 1 388 ? -64.443 -47.701 -35.141 1.00 152.08 ? 491  VAL A CG1   1 
ATOM   2884 C  CG2   . VAL A 1 388 ? -62.018 -48.301 -35.248 1.00 134.03 ? 491  VAL A CG2   1 
ATOM   2885 N  N     . ILE A 1 389 ? -63.309 -43.940 -35.921 1.00 148.32 ? 492  ILE A N     1 
ATOM   2886 C  CA    . ILE A 1 389 ? -64.142 -42.743 -35.859 1.00 140.37 ? 492  ILE A CA    1 
ATOM   2887 C  C     . ILE A 1 389 ? -64.448 -42.229 -37.261 1.00 137.36 ? 492  ILE A C     1 
ATOM   2888 O  O     . ILE A 1 389 ? -65.591 -41.868 -37.567 1.00 145.09 ? 492  ILE A O     1 
ATOM   2889 C  CB    . ILE A 1 389 ? -63.466 -41.667 -34.989 1.00 137.61 ? 492  ILE A CB    1 
ATOM   2890 C  CG1   . ILE A 1 389 ? -63.432 -42.115 -33.526 1.00 117.56 ? 492  ILE A CG1   1 
ATOM   2891 C  CG2   . ILE A 1 389 ? -64.185 -40.334 -35.128 1.00 137.15 ? 492  ILE A CG2   1 
ATOM   2892 C  CD1   . ILE A 1 389 ? -62.819 -41.101 -32.587 1.00 130.63 ? 492  ILE A CD1   1 
ATOM   2893 N  N     . GLU A 1 390 ? -63.442 -42.192 -38.137 1.00 151.15 ? 493  GLU A N     1 
ATOM   2894 C  CA    . GLU A 1 390 ? -63.681 -41.804 -39.521 1.00 153.71 ? 493  GLU A CA    1 
ATOM   2895 C  C     . GLU A 1 390 ? -64.371 -42.902 -40.319 1.00 158.53 ? 493  GLU A C     1 
ATOM   2896 O  O     . GLU A 1 390 ? -65.006 -42.605 -41.335 1.00 162.70 ? 493  GLU A O     1 
ATOM   2897 C  CB    . GLU A 1 390 ? -62.365 -41.414 -40.201 1.00 169.37 ? 493  GLU A CB    1 
ATOM   2898 C  CG    . GLU A 1 390 ? -61.400 -42.566 -40.426 1.00 191.65 ? 493  GLU A CG    1 
ATOM   2899 C  CD    . GLU A 1 390 ? -60.060 -42.103 -40.964 1.00 193.89 ? 493  GLU A CD    1 
ATOM   2900 O  OE1   . GLU A 1 390 ? -59.825 -40.877 -40.999 1.00 161.09 ? 493  GLU A OE1   1 
ATOM   2901 O  OE2   . GLU A 1 390 ? -59.242 -42.964 -41.351 1.00 208.51 ? 493  GLU A OE2   1 
ATOM   2902 N  N     . GLU A 1 391 ? -64.261 -44.159 -39.882 1.00 165.34 ? 494  GLU A N     1 
ATOM   2903 C  CA    . GLU A 1 391 ? -65.006 -45.235 -40.527 1.00 175.57 ? 494  GLU A CA    1 
ATOM   2904 C  C     . GLU A 1 391 ? -66.489 -45.143 -40.193 1.00 174.70 ? 494  GLU A C     1 
ATOM   2905 O  O     . GLU A 1 391 ? -67.344 -45.241 -41.081 1.00 192.39 ? 494  GLU A O     1 
ATOM   2906 C  CB    . GLU A 1 391 ? -64.440 -46.593 -40.107 1.00 164.14 ? 494  GLU A CB    1 
ATOM   2907 C  CG    . GLU A 1 391 ? -65.269 -47.785 -40.562 1.00 166.22 ? 494  GLU A CG    1 
ATOM   2908 C  CD    . GLU A 1 391 ? -65.311 -47.932 -42.071 1.00 194.38 ? 494  GLU A CD    1 
ATOM   2909 O  OE1   . GLU A 1 391 ? -64.371 -47.461 -42.746 1.00 188.13 ? 494  GLU A OE1   1 
ATOM   2910 O  OE2   . GLU A 1 391 ? -66.287 -48.520 -42.582 1.00 217.70 ? 494  GLU A OE2   1 
ATOM   2911 N  N     . HIS A 1 392 ? -66.813 -44.956 -38.912 1.00 166.18 ? 495  HIS A N     1 
ATOM   2912 C  CA    . HIS A 1 392 ? -68.199 -44.745 -38.515 1.00 174.78 ? 495  HIS A CA    1 
ATOM   2913 C  C     . HIS A 1 392 ? -68.737 -43.409 -39.010 1.00 172.98 ? 495  HIS A C     1 
ATOM   2914 O  O     . HIS A 1 392 ? -69.957 -43.252 -39.129 1.00 191.51 ? 495  HIS A O     1 
ATOM   2915 C  CB    . HIS A 1 392 ? -68.328 -44.834 -36.994 1.00 185.96 ? 495  HIS A CB    1 
ATOM   2916 C  CG    . HIS A 1 392 ? -69.718 -44.602 -36.488 1.00 183.02 ? 495  HIS A CG    1 
ATOM   2917 N  ND1   . HIS A 1 392 ? -70.198 -43.346 -36.182 1.00 167.79 ? 495  HIS A ND1   1 
ATOM   2918 C  CD2   . HIS A 1 392 ? -70.731 -45.464 -36.235 1.00 176.67 ? 495  HIS A CD2   1 
ATOM   2919 C  CE1   . HIS A 1 392 ? -71.447 -43.445 -35.763 1.00 169.94 ? 495  HIS A CE1   1 
ATOM   2920 N  NE2   . HIS A 1 392 ? -71.795 -44.719 -35.786 1.00 185.59 ? 495  HIS A NE2   1 
ATOM   2921 N  N     . ALA A 1 393 ? -67.856 -42.447 -39.301 1.00 156.59 ? 496  ALA A N     1 
ATOM   2922 C  CA    . ALA A 1 393 ? -68.305 -41.184 -39.876 1.00 167.86 ? 496  ALA A CA    1 
ATOM   2923 C  C     . ALA A 1 393 ? -68.965 -41.394 -41.231 1.00 184.20 ? 496  ALA A C     1 
ATOM   2924 O  O     . ALA A 1 393 ? -69.835 -40.609 -41.627 1.00 197.87 ? 496  ALA A O     1 
ATOM   2925 C  CB    . ALA A 1 393 ? -67.129 -40.214 -39.999 1.00 162.58 ? 496  ALA A CB    1 
ATOM   2926 N  N     . ASN A 1 394 ? -68.566 -42.442 -41.956 1.00 188.12 ? 497  ASN A N     1 
ATOM   2927 C  CA    . ASN A 1 394 ? -69.239 -42.775 -43.207 1.00 188.26 ? 497  ASN A CA    1 
ATOM   2928 C  C     . ASN A 1 394 ? -70.642 -43.308 -42.951 1.00 185.90 ? 497  ASN A C     1 
ATOM   2929 O  O     . ASN A 1 394 ? -71.572 -43.016 -43.713 1.00 189.00 ? 497  ASN A O     1 
ATOM   2930 C  CB    . ASN A 1 394 ? -68.417 -43.797 -43.993 1.00 190.30 ? 497  ASN A CB    1 
ATOM   2931 C  CG    . ASN A 1 394 ? -67.051 -43.273 -44.387 1.00 187.49 ? 497  ASN A CG    1 
ATOM   2932 O  OD1   . ASN A 1 394 ? -66.556 -42.301 -43.816 1.00 188.73 ? 497  ASN A OD1   1 
ATOM   2933 N  ND2   . ASN A 1 394 ? -66.432 -43.918 -45.369 1.00 184.03 ? 497  ASN A ND2   1 
ATOM   2934 N  N     . TRP A 1 395 ? -70.815 -44.089 -41.879 1.00 198.31 ? 498  TRP A N     1 
ATOM   2935 C  CA    . TRP A 1 395 ? -72.115 -44.687 -41.593 1.00 210.67 ? 498  TRP A CA    1 
ATOM   2936 C  C     . TRP A 1 395 ? -73.178 -43.633 -41.312 1.00 204.16 ? 498  TRP A C     1 
ATOM   2937 O  O     . TRP A 1 395 ? -74.370 -43.887 -41.516 1.00 200.21 ? 498  TRP A O     1 
ATOM   2938 C  CB    . TRP A 1 395 ? -72.003 -45.654 -40.414 1.00 219.74 ? 498  TRP A CB    1 
ATOM   2939 C  CG    . TRP A 1 395 ? -71.398 -46.978 -40.771 1.00 226.84 ? 498  TRP A CG    1 
ATOM   2940 C  CD1   . TRP A 1 395 ? -70.937 -47.366 -41.995 1.00 229.48 ? 498  TRP A CD1   1 
ATOM   2941 C  CD2   . TRP A 1 395 ? -71.196 -48.093 -39.894 1.00 240.66 ? 498  TRP A CD2   1 
ATOM   2942 N  NE1   . TRP A 1 395 ? -70.457 -48.653 -41.934 1.00 246.24 ? 498  TRP A NE1   1 
ATOM   2943 C  CE2   . TRP A 1 395 ? -70.605 -49.121 -40.655 1.00 255.59 ? 498  TRP A CE2   1 
ATOM   2944 C  CE3   . TRP A 1 395 ? -71.456 -48.321 -38.539 1.00 229.92 ? 498  TRP A CE3   1 
ATOM   2945 C  CZ2   . TRP A 1 395 ? -70.270 -50.358 -40.107 1.00 261.41 ? 498  TRP A CZ2   1 
ATOM   2946 C  CZ3   . TRP A 1 395 ? -71.122 -49.549 -37.997 1.00 226.15 ? 498  TRP A CZ3   1 
ATOM   2947 C  CH2   . TRP A 1 395 ? -70.536 -50.552 -38.779 1.00 240.77 ? 498  TRP A CH2   1 
ATOM   2948 N  N     . SER A 1 396 ? -72.773 -42.450 -40.846 1.00 202.08 ? 499  SER A N     1 
ATOM   2949 C  CA    . SER A 1 396 ? -73.742 -41.387 -40.598 1.00 190.43 ? 499  SER A CA    1 
ATOM   2950 C  C     . SER A 1 396 ? -74.379 -40.908 -41.896 1.00 195.30 ? 499  SER A C     1 
ATOM   2951 O  O     . SER A 1 396 ? -75.589 -40.653 -41.944 1.00 206.30 ? 499  SER A O     1 
ATOM   2952 C  CB    . SER A 1 396 ? -73.070 -40.225 -39.870 1.00 202.07 ? 499  SER A CB    1 
ATOM   2953 O  OG    . SER A 1 396 ? -72.057 -39.647 -40.674 1.00 203.45 ? 499  SER A OG    1 
ATOM   2954 N  N     . VAL A 1 397 ? -73.582 -40.776 -42.957 1.00 181.01 ? 500  VAL A N     1 
ATOM   2955 C  CA    . VAL A 1 397 ? -74.117 -40.371 -44.253 1.00 185.10 ? 500  VAL A CA    1 
ATOM   2956 C  C     . VAL A 1 397 ? -74.694 -41.555 -45.023 1.00 201.98 ? 500  VAL A C     1 
ATOM   2957 O  O     . VAL A 1 397 ? -75.605 -41.370 -45.841 1.00 212.40 ? 500  VAL A O     1 
ATOM   2958 C  CB    . VAL A 1 397 ? -73.024 -39.649 -45.063 1.00 160.84 ? 500  VAL A CB    1 
ATOM   2959 C  CG1   . VAL A 1 397 ? -73.539 -39.224 -46.433 1.00 156.86 ? 500  VAL A CG1   1 
ATOM   2960 C  CG2   . VAL A 1 397 ? -72.518 -38.437 -44.291 1.00 140.45 ? 500  VAL A CG2   1 
ATOM   2961 N  N     . SER A 1 398 ? -74.216 -42.774 -44.763 1.00 213.53 ? 501  SER A N     1 
ATOM   2962 C  CA    . SER A 1 398 ? -74.734 -43.936 -45.476 1.00 215.65 ? 501  SER A CA    1 
ATOM   2963 C  C     . SER A 1 398 ? -76.063 -44.418 -44.906 1.00 212.69 ? 501  SER A C     1 
ATOM   2964 O  O     . SER A 1 398 ? -76.862 -45.015 -45.635 1.00 214.31 ? 501  SER A O     1 
ATOM   2965 C  CB    . SER A 1 398 ? -73.712 -45.073 -45.453 1.00 218.10 ? 501  SER A CB    1 
ATOM   2966 O  OG    . SER A 1 398 ? -73.614 -45.643 -44.162 1.00 251.70 ? 501  SER A OG    1 
ATOM   2967 N  N     . ARG A 1 399 ? -76.320 -44.175 -43.619 1.00 196.76 ? 502  ARG A N     1 
ATOM   2968 C  CA    . ARG A 1 399 ? -77.596 -44.551 -43.023 1.00 199.88 ? 502  ARG A CA    1 
ATOM   2969 C  C     . ARG A 1 399 ? -78.736 -43.630 -43.437 1.00 205.86 ? 502  ARG A C     1 
ATOM   2970 O  O     . ARG A 1 399 ? -79.896 -43.945 -43.147 1.00 217.95 ? 502  ARG A O     1 
ATOM   2971 C  CB    . ARG A 1 399 ? -77.486 -44.570 -41.496 1.00 187.06 ? 502  ARG A CB    1 
ATOM   2972 N  N     . GLU A 1 400 ? -78.432 -42.516 -44.099 1.00 196.98 ? 503  GLU A N     1 
ATOM   2973 C  CA    . GLU A 1 400 ? -79.434 -41.551 -44.549 1.00 206.01 ? 503  GLU A CA    1 
ATOM   2974 C  C     . GLU A 1 400 ? -80.285 -41.041 -43.390 1.00 236.73 ? 503  GLU A C     1 
ATOM   2975 O  O     . GLU A 1 400 ? -79.795 -40.327 -42.514 1.00 220.76 ? 503  GLU A O     1 
ATOM   2976 C  CB    . GLU A 1 400 ? -80.328 -42.165 -45.630 1.00 178.09 ? 503  GLU A CB    1 
ATOM   2977 N  N     . LEU A 1 420 ? -77.941 -22.218 -50.111 1.00 212.75 ? 523  LEU A N     1 
ATOM   2978 C  CA    . LEU A 1 420 ? -76.614 -21.777 -50.523 1.00 220.01 ? 523  LEU A CA    1 
ATOM   2979 C  C     . LEU A 1 420 ? -76.669 -20.335 -51.025 1.00 234.20 ? 523  LEU A C     1 
ATOM   2980 O  O     . LEU A 1 420 ? -75.701 -19.821 -51.587 1.00 232.49 ? 523  LEU A O     1 
ATOM   2981 C  CB    . LEU A 1 420 ? -76.053 -22.707 -51.604 1.00 221.99 ? 523  LEU A CB    1 
ATOM   2982 C  CG    . LEU A 1 420 ? -74.540 -22.692 -51.845 1.00 221.63 ? 523  LEU A CG    1 
ATOM   2983 C  CD1   . LEU A 1 420 ? -73.785 -23.011 -50.564 1.00 222.21 ? 523  LEU A CD1   1 
ATOM   2984 C  CD2   . LEU A 1 420 ? -74.162 -23.665 -52.951 1.00 214.16 ? 523  LEU A CD2   1 
ATOM   2985 N  N     . ARG A 1 421 ? -77.809 -19.684 -50.811 1.00 244.59 ? 524  ARG A N     1 
ATOM   2986 C  CA    . ARG A 1 421 ? -77.978 -18.306 -51.244 1.00 246.75 ? 524  ARG A CA    1 
ATOM   2987 C  C     . ARG A 1 421 ? -77.064 -17.375 -50.450 1.00 231.18 ? 524  ARG A C     1 
ATOM   2988 O  O     . ARG A 1 421 ? -76.600 -17.696 -49.352 1.00 218.05 ? 524  ARG A O     1 
ATOM   2989 C  CB    . ARG A 1 421 ? -79.439 -17.876 -51.102 1.00 228.85 ? 524  ARG A CB    1 
ATOM   2990 C  CG    . ARG A 1 421 ? -80.083 -18.268 -49.784 1.00 212.52 ? 524  ARG A CG    1 
ATOM   2991 C  CD    . ARG A 1 421 ? -81.587 -18.046 -49.825 1.00 211.25 ? 524  ARG A CD    1 
ATOM   2992 N  NE    . ARG A 1 421 ? -82.240 -18.473 -48.593 1.00 218.91 ? 524  ARG A NE    1 
ATOM   2993 C  CZ    . ARG A 1 421 ? -83.552 -18.461 -48.399 1.00 228.58 ? 524  ARG A CZ    1 
ATOM   2994 N  NH1   . ARG A 1 421 ? -84.386 -18.051 -49.341 1.00 220.35 ? 524  ARG A NH1   1 
ATOM   2995 N  NH2   . ARG A 1 421 ? -84.039 -18.873 -47.232 1.00 221.48 ? 524  ARG A NH2   1 
ATOM   2996 N  N     . GLU A 1 422 ? -76.808 -16.199 -51.029 1.00 231.54 ? 525  GLU A N     1 
ATOM   2997 C  CA    . GLU A 1 422 ? -75.829 -15.283 -50.452 1.00 211.48 ? 525  GLU A CA    1 
ATOM   2998 C  C     . GLU A 1 422 ? -76.345 -14.625 -49.178 1.00 215.12 ? 525  GLU A C     1 
ATOM   2999 O  O     . GLU A 1 422 ? -75.547 -14.255 -48.309 1.00 219.37 ? 525  GLU A O     1 
ATOM   3000 C  CB    . GLU A 1 422 ? -75.439 -14.224 -51.485 1.00 208.78 ? 525  GLU A CB    1 
ATOM   3001 C  CG    . GLU A 1 422 ? -74.041 -13.645 -51.306 1.00 209.32 ? 525  GLU A CG    1 
ATOM   3002 C  CD    . GLU A 1 422 ? -73.992 -12.517 -50.294 1.00 217.71 ? 525  GLU A CD    1 
ATOM   3003 O  OE1   . GLU A 1 422 ? -75.059 -11.953 -49.976 1.00 230.85 ? 525  GLU A OE1   1 
ATOM   3004 O  OE2   . GLU A 1 422 ? -72.882 -12.193 -49.820 1.00 206.82 ? 525  GLU A OE2   1 
ATOM   3005 N  N     . ASN A 1 423 ? -77.665 -14.475 -49.041 1.00 224.89 ? 526  ASN A N     1 
ATOM   3006 C  CA    . ASN A 1 423 ? -78.218 -13.826 -47.858 1.00 211.88 ? 526  ASN A CA    1 
ATOM   3007 C  C     . ASN A 1 423 ? -78.063 -14.671 -46.600 1.00 204.89 ? 526  ASN A C     1 
ATOM   3008 O  O     . ASN A 1 423 ? -78.179 -14.135 -45.493 1.00 207.68 ? 526  ASN A O     1 
ATOM   3009 C  CB    . ASN A 1 423 ? -79.694 -13.488 -48.083 1.00 217.37 ? 526  ASN A CB    1 
ATOM   3010 C  CG    . ASN A 1 423 ? -80.507 -14.687 -48.527 1.00 214.79 ? 526  ASN A CG    1 
ATOM   3011 O  OD1   . ASN A 1 423 ? -80.664 -14.935 -49.722 1.00 213.59 ? 526  ASN A OD1   1 
ATOM   3012 N  ND2   . ASN A 1 423 ? -81.031 -15.437 -47.564 1.00 216.75 ? 526  ASN A ND2   1 
ATOM   3013 N  N     . ASP A 1 424 ? -77.807 -15.972 -46.740 1.00 211.34 ? 527  ASP A N     1 
ATOM   3014 C  CA    . ASP A 1 424 ? -77.592 -16.837 -45.587 1.00 214.60 ? 527  ASP A CA    1 
ATOM   3015 C  C     . ASP A 1 424 ? -76.136 -16.859 -45.141 1.00 204.21 ? 527  ASP A C     1 
ATOM   3016 O  O     . ASP A 1 424 ? -75.860 -16.918 -43.938 1.00 189.87 ? 527  ASP A O     1 
ATOM   3017 C  CB    . ASP A 1 424 ? -78.058 -18.262 -45.900 1.00 202.87 ? 527  ASP A CB    1 
ATOM   3018 C  CG    . ASP A 1 424 ? -79.562 -18.415 -45.815 1.00 208.97 ? 527  ASP A CG    1 
ATOM   3019 O  OD1   . ASP A 1 424 ? -80.275 -17.744 -46.589 1.00 234.32 ? 527  ASP A OD1   1 
ATOM   3020 O  OD2   . ASP A 1 424 ? -80.031 -19.210 -44.973 1.00 193.93 ? 527  ASP A OD2   1 
ATOM   3021 N  N     . LYS A 1 425 ? -75.197 -16.808 -46.088 1.00 207.28 ? 528  LYS A N     1 
ATOM   3022 C  CA    . LYS A 1 425 ? -73.782 -16.871 -45.742 1.00 188.56 ? 528  LYS A CA    1 
ATOM   3023 C  C     . LYS A 1 425 ? -73.296 -15.605 -45.047 1.00 184.17 ? 528  LYS A C     1 
ATOM   3024 O  O     . LYS A 1 425 ? -72.319 -15.664 -44.293 1.00 198.36 ? 528  LYS A O     1 
ATOM   3025 C  CB    . LYS A 1 425 ? -72.952 -17.135 -46.999 1.00 194.42 ? 528  LYS A CB    1 
ATOM   3026 C  CG    . LYS A 1 425 ? -73.406 -18.355 -47.782 1.00 213.25 ? 528  LYS A CG    1 
ATOM   3027 C  CD    . LYS A 1 425 ? -73.388 -19.600 -46.911 1.00 205.74 ? 528  LYS A CD    1 
ATOM   3028 C  CE    . LYS A 1 425 ? -74.149 -20.742 -47.562 1.00 203.28 ? 528  LYS A CE    1 
ATOM   3029 N  NZ    . LYS A 1 425 ? -75.604 -20.440 -47.662 1.00 208.44 ? 528  LYS A NZ    1 
ATOM   3030 N  N     . GLU A 1 426 ? -73.953 -14.467 -45.278 1.00 190.46 ? 529  GLU A N     1 
ATOM   3031 C  CA    . GLU A 1 426 ? -73.582 -13.236 -44.591 1.00 191.58 ? 529  GLU A CA    1 
ATOM   3032 C  C     . GLU A 1 426 ? -73.931 -13.261 -43.109 1.00 187.60 ? 529  GLU A C     1 
ATOM   3033 O  O     . GLU A 1 426 ? -73.427 -12.418 -42.360 1.00 188.03 ? 529  GLU A O     1 
ATOM   3034 C  CB    . GLU A 1 426 ? -74.255 -12.034 -45.258 1.00 209.60 ? 529  GLU A CB    1 
ATOM   3035 C  CG    . GLU A 1 426 ? -73.727 -11.715 -46.646 1.00 212.94 ? 529  GLU A CG    1 
ATOM   3036 C  CD    . GLU A 1 426 ? -74.374 -10.484 -47.248 1.00 209.90 ? 529  GLU A CD    1 
ATOM   3037 O  OE1   . GLU A 1 426 ? -75.420 -10.046 -46.727 1.00 210.58 ? 529  GLU A OE1   1 
ATOM   3038 O  OE2   . GLU A 1 426 ? -73.832 -9.954  -48.241 1.00 202.05 ? 529  GLU A OE2   1 
ATOM   3039 N  N     . GLN A 1 427 ? -74.774 -14.198 -42.670 1.00 189.83 ? 530  GLN A N     1 
ATOM   3040 C  CA    . GLN A 1 427 ? -75.118 -14.281 -41.255 1.00 181.32 ? 530  GLN A CA    1 
ATOM   3041 C  C     . GLN A 1 427 ? -74.036 -15.001 -40.459 1.00 175.75 ? 530  GLN A C     1 
ATOM   3042 O  O     . GLN A 1 427 ? -73.768 -14.639 -39.308 1.00 173.94 ? 530  GLN A O     1 
ATOM   3043 C  CB    . GLN A 1 427 ? -76.467 -14.978 -41.081 1.00 179.25 ? 530  GLN A CB    1 
ATOM   3044 C  CG    . GLN A 1 427 ? -76.935 -15.068 -39.636 1.00 183.50 ? 530  GLN A CG    1 
ATOM   3045 C  CD    . GLN A 1 427 ? -77.009 -13.711 -38.965 1.00 204.73 ? 530  GLN A CD    1 
ATOM   3046 O  OE1   . GLN A 1 427 ? -76.273 -13.434 -38.018 1.00 211.27 ? 530  GLN A OE1   1 
ATOM   3047 N  NE2   . GLN A 1 427 ? -77.902 -12.857 -39.452 1.00 196.09 ? 530  GLN A NE2   1 
ATOM   3048 N  N     . LEU A 1 428 ? -73.409 -16.023 -41.050 1.00 184.25 ? 531  LEU A N     1 
ATOM   3049 C  CA    . LEU A 1 428 ? -72.307 -16.700 -40.372 1.00 169.42 ? 531  LEU A CA    1 
ATOM   3050 C  C     . LEU A 1 428 ? -71.142 -15.752 -40.124 1.00 160.69 ? 531  LEU A C     1 
ATOM   3051 O  O     . LEU A 1 428 ? -70.433 -15.889 -39.121 1.00 158.07 ? 531  LEU A O     1 
ATOM   3052 C  CB    . LEU A 1 428 ? -71.839 -17.910 -41.185 1.00 161.16 ? 531  LEU A CB    1 
ATOM   3053 C  CG    . LEU A 1 428 ? -72.787 -19.104 -41.326 1.00 143.81 ? 531  LEU A CG    1 
ATOM   3054 C  CD1   . LEU A 1 428 ? -73.740 -18.919 -42.496 1.00 169.24 ? 531  LEU A CD1   1 
ATOM   3055 C  CD2   . LEU A 1 428 ? -72.001 -20.399 -41.472 1.00 162.26 ? 531  LEU A CD2   1 
ATOM   3056 N  N     . LYS A 1 429 ? -70.928 -14.790 -41.025 1.00 160.61 ? 532  LYS A N     1 
ATOM   3057 C  CA    . LYS A 1 429 ? -69.900 -13.782 -40.800 1.00 166.90 ? 532  LYS A CA    1 
ATOM   3058 C  C     . LYS A 1 429 ? -70.264 -12.866 -39.638 1.00 171.74 ? 532  LYS A C     1 
ATOM   3059 O  O     . LYS A 1 429 ? -69.379 -12.420 -38.899 1.00 178.61 ? 532  LYS A O     1 
ATOM   3060 C  CB    . LYS A 1 429 ? -69.678 -12.968 -42.075 1.00 158.37 ? 532  LYS A CB    1 
ATOM   3061 C  CG    . LYS A 1 429 ? -68.558 -11.943 -41.983 1.00 160.91 ? 532  LYS A CG    1 
ATOM   3062 C  CD    . LYS A 1 429 ? -68.406 -11.179 -43.288 1.00 157.86 ? 532  LYS A CD    1 
ATOM   3063 C  CE    . LYS A 1 429 ? -67.291 -10.149 -43.201 1.00 177.18 ? 532  LYS A CE    1 
ATOM   3064 N  NZ    . LYS A 1 429 ? -67.141 -9.385  -44.470 1.00 162.35 ? 532  LYS A NZ    1 
ATOM   3065 N  N     . ALA A 1 430 ? -71.556 -12.582 -39.456 1.00 157.33 ? 533  ALA A N     1 
ATOM   3066 C  CA    . ALA A 1 430 ? -71.989 -11.748 -38.342 1.00 150.94 ? 533  ALA A CA    1 
ATOM   3067 C  C     . ALA A 1 430 ? -71.922 -12.482 -37.009 1.00 159.98 ? 533  ALA A C     1 
ATOM   3068 O  O     . ALA A 1 430 ? -71.991 -11.837 -35.958 1.00 168.99 ? 533  ALA A O     1 
ATOM   3069 C  CB    . ALA A 1 430 ? -73.411 -11.242 -38.584 1.00 165.40 ? 533  ALA A CB    1 
ATOM   3070 N  N     . ILE A 1 431 ? -71.796 -13.809 -37.029 1.00 161.74 ? 534  ILE A N     1 
ATOM   3071 C  CA    . ILE A 1 431 ? -71.686 -14.566 -35.787 1.00 153.03 ? 534  ILE A CA    1 
ATOM   3072 C  C     . ILE A 1 431 ? -70.239 -14.618 -35.314 1.00 144.73 ? 534  ILE A C     1 
ATOM   3073 O  O     . ILE A 1 431 ? -69.964 -14.544 -34.111 1.00 146.41 ? 534  ILE A O     1 
ATOM   3074 C  CB    . ILE A 1 431 ? -72.276 -15.976 -35.976 1.00 161.73 ? 534  ILE A CB    1 
ATOM   3075 C  CG1   . ILE A 1 431 ? -73.764 -15.887 -36.322 1.00 154.70 ? 534  ILE A CG1   1 
ATOM   3076 C  CG2   . ILE A 1 431 ? -72.069 -16.820 -34.728 1.00 159.44 ? 534  ILE A CG2   1 
ATOM   3077 C  CD1   . ILE A 1 431 ? -74.418 -17.236 -36.544 1.00 150.77 ? 534  ILE A CD1   1 
ATOM   3078 N  N     . SER A 1 432 ? -69.293 -14.738 -36.249 1.00 135.93 ? 535  SER A N     1 
ATOM   3079 C  CA    . SER A 1 432 ? -67.884 -14.794 -35.875 1.00 149.88 ? 535  SER A CA    1 
ATOM   3080 C  C     . SER A 1 432 ? -67.399 -13.470 -35.298 1.00 152.09 ? 535  SER A C     1 
ATOM   3081 O  O     . SER A 1 432 ? -66.464 -13.453 -34.489 1.00 142.27 ? 535  SER A O     1 
ATOM   3082 C  CB    . SER A 1 432 ? -67.036 -15.188 -37.084 1.00 144.32 ? 535  SER A CB    1 
ATOM   3083 O  OG    . SER A 1 432 ? -67.182 -14.248 -38.134 1.00 153.76 ? 535  SER A OG    1 
ATOM   3084 N  N     . THR A 1 433 ? -68.017 -12.356 -35.694 1.00 145.69 ? 536  THR A N     1 
ATOM   3085 C  CA    . THR A 1 433 ? -67.627 -11.048 -35.185 1.00 150.70 ? 536  THR A CA    1 
ATOM   3086 C  C     . THR A 1 433 ? -68.140 -10.779 -33.777 1.00 166.54 ? 536  THR A C     1 
ATOM   3087 O  O     . THR A 1 433 ? -67.777 -9.753  -33.191 1.00 181.94 ? 536  THR A O     1 
ATOM   3088 C  CB    . THR A 1 433 ? -68.122 -9.944  -36.123 1.00 134.73 ? 536  THR A CB    1 
ATOM   3089 O  OG1   . THR A 1 433 ? -69.550 -10.008 -36.229 1.00 145.86 ? 536  THR A OG1   1 
ATOM   3090 C  CG2   . THR A 1 433 ? -67.507 -10.105 -37.505 1.00 157.36 ? 536  THR A CG2   1 
ATOM   3091 N  N     . ARG A 1 434 ? -68.967 -11.661 -33.223 1.00 162.04 ? 537  ARG A N     1 
ATOM   3092 C  CA    . ARG A 1 434 ? -69.472 -11.473 -31.873 1.00 159.91 ? 537  ARG A CA    1 
ATOM   3093 C  C     . ARG A 1 434 ? -68.463 -11.973 -30.846 1.00 151.10 ? 537  ARG A C     1 
ATOM   3094 O  O     . ARG A 1 434 ? -67.668 -12.880 -31.112 1.00 139.91 ? 537  ARG A O     1 
ATOM   3095 C  CB    . ARG A 1 434 ? -70.806 -12.198 -31.685 1.00 154.53 ? 537  ARG A CB    1 
ATOM   3096 C  CG    . ARG A 1 434 ? -71.909 -11.733 -32.623 1.00 148.31 ? 537  ARG A CG    1 
ATOM   3097 C  CD    . ARG A 1 434 ? -73.285 -11.952 -32.010 1.00 165.70 ? 537  ARG A CD    1 
ATOM   3098 N  NE    . ARG A 1 434 ? -73.527 -13.348 -31.667 1.00 173.24 ? 537  ARG A NE    1 
ATOM   3099 C  CZ    . ARG A 1 434 ? -74.218 -14.196 -32.417 1.00 167.58 ? 537  ARG A CZ    1 
ATOM   3100 N  NH1   . ARG A 1 434 ? -74.756 -13.822 -33.566 1.00 151.96 ? 537  ARG A NH1   1 
ATOM   3101 N  NH2   . ARG A 1 434 ? -74.377 -15.449 -32.001 1.00 167.84 ? 537  ARG A NH2   1 
ATOM   3102 N  N     . ASP A 1 435 ? -68.502 -11.366 -29.663 1.00 158.90 ? 538  ASP A N     1 
ATOM   3103 C  CA    . ASP A 1 435 ? -67.601 -11.752 -28.591 1.00 152.03 ? 538  ASP A CA    1 
ATOM   3104 C  C     . ASP A 1 435 ? -67.898 -13.182 -28.137 1.00 145.67 ? 538  ASP A C     1 
ATOM   3105 O  O     . ASP A 1 435 ? -69.021 -13.670 -28.291 1.00 148.41 ? 538  ASP A O     1 
ATOM   3106 C  CB    . ASP A 1 435 ? -67.733 -10.786 -27.416 1.00 147.36 ? 538  ASP A CB    1 
ATOM   3107 C  CG    . ASP A 1 435 ? -69.163 -10.644 -26.934 1.00 159.04 ? 538  ASP A CG    1 
ATOM   3108 O  OD1   . ASP A 1 435 ? -69.647 -11.550 -26.223 1.00 167.31 ? 538  ASP A OD1   1 
ATOM   3109 O  OD2   . ASP A 1 435 ? -69.804 -9.625  -27.267 1.00 165.26 ? 538  ASP A OD2   1 
ATOM   3110 N  N     . PRO A 1 436 ? -66.904 -13.879 -27.577 1.00 148.80 ? 539  PRO A N     1 
ATOM   3111 C  CA    . PRO A 1 436 ? -67.129 -15.273 -27.155 1.00 142.67 ? 539  PRO A CA    1 
ATOM   3112 C  C     . PRO A 1 436 ? -68.147 -15.424 -26.036 1.00 133.90 ? 539  PRO A C     1 
ATOM   3113 O  O     . PRO A 1 436 ? -68.568 -16.555 -25.761 1.00 139.33 ? 539  PRO A O     1 
ATOM   3114 C  CB    . PRO A 1 436 ? -65.736 -15.735 -26.704 1.00 142.15 ? 539  PRO A CB    1 
ATOM   3115 C  CG    . PRO A 1 436 ? -65.006 -14.475 -26.376 1.00 121.18 ? 539  PRO A CG    1 
ATOM   3116 C  CD    . PRO A 1 436 ? -65.511 -13.455 -27.350 1.00 151.06 ? 539  PRO A CD    1 
ATOM   3117 N  N     . LEU A 1 437 ? -68.551 -14.336 -25.384 1.00 131.99 ? 540  LEU A N     1 
ATOM   3118 C  CA    . LEU A 1 437 ? -69.567 -14.386 -24.343 1.00 142.96 ? 540  LEU A CA    1 
ATOM   3119 C  C     . LEU A 1 437 ? -70.959 -14.051 -24.859 1.00 162.93 ? 540  LEU A C     1 
ATOM   3120 O  O     . LEU A 1 437 ? -71.926 -14.147 -24.096 1.00 175.45 ? 540  LEU A O     1 
ATOM   3121 C  CB    . LEU A 1 437 ? -69.201 -13.440 -23.197 1.00 138.29 ? 540  LEU A CB    1 
ATOM   3122 C  CG    . LEU A 1 437 ? -67.924 -13.766 -22.422 1.00 149.97 ? 540  LEU A CG    1 
ATOM   3123 C  CD1   . LEU A 1 437 ? -67.774 -12.827 -21.238 1.00 134.29 ? 540  LEU A CD1   1 
ATOM   3124 C  CD2   . LEU A 1 437 ? -67.923 -15.216 -21.965 1.00 125.27 ? 540  LEU A CD2   1 
ATOM   3125 N  N     . SER A 1 438 ? -71.086 -13.659 -26.125 1.00 158.29 ? 541  SER A N     1 
ATOM   3126 C  CA    . SER A 1 438 ? -72.393 -13.373 -26.701 1.00 161.79 ? 541  SER A CA    1 
ATOM   3127 C  C     . SER A 1 438 ? -73.204 -14.660 -26.788 1.00 173.07 ? 541  SER A C     1 
ATOM   3128 O  O     . SER A 1 438 ? -72.763 -15.640 -27.397 1.00 173.40 ? 541  SER A O     1 
ATOM   3129 C  CB    . SER A 1 438 ? -72.238 -12.738 -28.080 1.00 155.66 ? 541  SER A CB    1 
ATOM   3130 O  OG    . SER A 1 438 ? -73.502 -12.435 -28.643 1.00 154.92 ? 541  SER A OG    1 
ATOM   3131 N  N     . GLU A 1 439 ? -74.384 -14.657 -26.173 1.00 186.29 ? 542  GLU A N     1 
ATOM   3132 C  CA    . GLU A 1 439 ? -75.208 -15.857 -26.109 1.00 187.98 ? 542  GLU A CA    1 
ATOM   3133 C  C     . GLU A 1 439 ? -75.690 -16.241 -27.502 1.00 173.99 ? 542  GLU A C     1 
ATOM   3134 O  O     . GLU A 1 439 ? -76.386 -15.463 -28.165 1.00 180.13 ? 542  GLU A O     1 
ATOM   3135 C  CB    . GLU A 1 439 ? -76.393 -15.632 -25.172 1.00 194.49 ? 542  GLU A CB    1 
ATOM   3136 C  CG    . GLU A 1 439 ? -76.001 -15.274 -23.746 1.00 192.40 ? 542  GLU A CG    1 
ATOM   3137 C  CD    . GLU A 1 439 ? -75.286 -16.405 -23.030 1.00 198.76 ? 542  GLU A CD    1 
ATOM   3138 O  OE1   . GLU A 1 439 ? -75.521 -17.580 -23.383 1.00 209.60 ? 542  GLU A OE1   1 
ATOM   3139 O  OE2   . GLU A 1 439 ? -74.488 -16.118 -22.114 1.00 192.35 ? 542  GLU A OE2   1 
ATOM   3140 N  N     . ILE A 1 440 ? -75.317 -17.436 -27.945 1.00 136.64 ? 543  ILE A N     1 
ATOM   3141 C  CA    . ILE A 1 440 ? -75.762 -17.970 -29.227 1.00 157.40 ? 543  ILE A CA    1 
ATOM   3142 C  C     . ILE A 1 440 ? -77.094 -18.677 -29.010 1.00 179.03 ? 543  ILE A C     1 
ATOM   3143 O  O     . ILE A 1 440 ? -77.167 -19.669 -28.277 1.00 169.69 ? 543  ILE A O     1 
ATOM   3144 C  CB    . ILE A 1 440 ? -74.718 -18.924 -29.826 1.00 142.34 ? 543  ILE A CB    1 
ATOM   3145 C  CG1   . ILE A 1 440 ? -73.423 -18.171 -30.135 1.00 157.98 ? 543  ILE A CG1   1 
ATOM   3146 C  CG2   . ILE A 1 440 ? -75.263 -19.596 -31.076 1.00 140.14 ? 543  ILE A CG2   1 
ATOM   3147 N  N     . THR A 1 441 ? -78.146 -18.166 -29.643 1.00 176.58 ? 544  THR A N     1 
ATOM   3148 C  CA    . THR A 1 441 ? -79.473 -18.735 -29.470 1.00 156.55 ? 544  THR A CA    1 
ATOM   3149 C  C     . THR A 1 441 ? -79.553 -20.124 -30.099 1.00 160.70 ? 544  THR A C     1 
ATOM   3150 O  O     . THR A 1 441 ? -78.701 -20.528 -30.895 1.00 182.71 ? 544  THR A O     1 
ATOM   3151 C  CB    . THR A 1 441 ? -80.537 -17.824 -30.084 1.00 153.92 ? 544  THR A CB    1 
ATOM   3152 O  OG1   . THR A 1 441 ? -80.377 -17.790 -31.507 1.00 146.64 ? 544  THR A OG1   1 
ATOM   3153 C  CG2   . THR A 1 441 ? -80.410 -16.412 -29.532 1.00 187.04 ? 544  THR A CG2   1 
ATOM   3154 N  N     . GLU A 1 442 ? -80.603 -20.860 -29.725 1.00 151.97 ? 545  GLU A N     1 
ATOM   3155 C  CA    . GLU A 1 442 ? -80.781 -22.211 -30.245 1.00 151.34 ? 545  GLU A CA    1 
ATOM   3156 C  C     . GLU A 1 442 ? -81.050 -22.206 -31.744 1.00 166.25 ? 545  GLU A C     1 
ATOM   3157 O  O     . GLU A 1 442 ? -80.663 -23.149 -32.443 1.00 159.53 ? 545  GLU A O     1 
ATOM   3158 C  CB    . GLU A 1 442 ? -81.916 -22.915 -29.502 1.00 175.56 ? 545  GLU A CB    1 
ATOM   3159 C  CG    . GLU A 1 442 ? -81.752 -22.924 -27.990 1.00 184.47 ? 545  GLU A CG    1 
ATOM   3160 C  CD    . GLU A 1 442 ? -80.489 -23.635 -27.542 1.00 179.88 ? 545  GLU A CD    1 
ATOM   3161 O  OE1   . GLU A 1 442 ? -80.078 -24.607 -28.212 1.00 164.38 ? 545  GLU A OE1   1 
ATOM   3162 O  OE2   . GLU A 1 442 ? -79.904 -23.219 -26.521 1.00 179.14 ? 545  GLU A OE2   1 
ATOM   3163 N  N     . GLN A 1 443 ? -81.710 -21.162 -32.253 1.00 179.86 ? 546  GLN A N     1 
ATOM   3164 C  CA    . GLN A 1 443 ? -81.915 -21.053 -33.693 1.00 176.87 ? 546  GLN A CA    1 
ATOM   3165 C  C     . GLN A 1 443 ? -80.593 -20.880 -34.431 1.00 169.65 ? 546  GLN A C     1 
ATOM   3166 O  O     . GLN A 1 443 ? -80.434 -21.395 -35.544 1.00 183.56 ? 546  GLN A O     1 
ATOM   3167 C  CB    . GLN A 1 443 ? -82.857 -19.888 -34.003 1.00 174.05 ? 546  GLN A CB    1 
ATOM   3168 C  CG    . GLN A 1 443 ? -83.228 -19.767 -35.472 1.00 175.40 ? 546  GLN A CG    1 
ATOM   3169 C  CD    . GLN A 1 443 ? -83.988 -20.978 -35.980 1.00 186.95 ? 546  GLN A CD    1 
ATOM   3170 O  OE1   . GLN A 1 443 ? -84.905 -21.470 -35.323 1.00 189.48 ? 546  GLN A OE1   1 
ATOM   3171 N  NE2   . GLN A 1 443 ? -83.606 -21.468 -37.154 1.00 201.26 ? 546  GLN A NE2   1 
ATOM   3172 N  N     . GLU A 1 444 ? -79.637 -20.171 -33.829 1.00 152.79 ? 547  GLU A N     1 
ATOM   3173 C  CA    . GLU A 1 444 ? -78.314 -20.027 -34.420 1.00 145.33 ? 547  GLU A CA    1 
ATOM   3174 C  C     . GLU A 1 444 ? -77.468 -21.283 -34.270 1.00 165.16 ? 547  GLU A C     1 
ATOM   3175 O  O     . GLU A 1 444 ? -76.491 -21.445 -35.009 1.00 169.46 ? 547  GLU A O     1 
ATOM   3176 C  CB    . GLU A 1 444 ? -77.584 -18.837 -33.793 1.00 146.89 ? 547  GLU A CB    1 
ATOM   3177 C  CG    . GLU A 1 444 ? -78.293 -17.505 -33.976 1.00 149.76 ? 547  GLU A CG    1 
ATOM   3178 C  CD    . GLU A 1 444 ? -77.643 -16.384 -33.188 1.00 152.26 ? 547  GLU A CD    1 
ATOM   3179 O  OE1   . GLU A 1 444 ? -76.688 -16.661 -32.433 1.00 150.02 ? 547  GLU A OE1   1 
ATOM   3180 O  OE2   . GLU A 1 444 ? -78.089 -15.225 -33.324 1.00 158.89 ? 547  GLU A OE2   1 
ATOM   3181 N  N     . LYS A 1 445 ? -77.814 -22.167 -33.331 1.00 175.80 ? 548  LYS A N     1 
ATOM   3182 C  CA    . LYS A 1 445 ? -77.080 -23.419 -33.178 1.00 145.94 ? 548  LYS A CA    1 
ATOM   3183 C  C     . LYS A 1 445 ? -77.228 -24.294 -34.416 1.00 157.67 ? 548  LYS A C     1 
ATOM   3184 O  O     . LYS A 1 445 ? -76.233 -24.720 -35.015 1.00 137.37 ? 548  LYS A O     1 
ATOM   3185 C  CB    . LYS A 1 445 ? -77.569 -24.167 -31.937 1.00 150.94 ? 548  LYS A CB    1 
ATOM   3186 C  CG    . LYS A 1 445 ? -77.287 -23.474 -30.616 1.00 144.49 ? 548  LYS A CG    1 
ATOM   3187 C  CD    . LYS A 1 445 ? -75.804 -23.462 -30.297 1.00 134.13 ? 548  LYS A CD    1 
ATOM   3188 C  CE    . LYS A 1 445 ? -75.563 -23.127 -28.834 1.00 150.67 ? 548  LYS A CE    1 
ATOM   3189 N  NZ    . LYS A 1 445 ? -76.216 -21.848 -28.442 1.00 167.48 ? 548  LYS A NZ    1 
ATOM   3190 N  N     . ASP A 1 446 ? -78.471 -24.573 -34.815 1.00 165.68 ? 549  ASP A N     1 
ATOM   3191 C  CA    . ASP A 1 446 ? -78.713 -25.423 -35.974 1.00 163.88 ? 549  ASP A CA    1 
ATOM   3192 C  C     . ASP A 1 446 ? -78.296 -24.759 -37.279 1.00 144.93 ? 549  ASP A C     1 
ATOM   3193 O  O     . ASP A 1 446 ? -78.039 -25.463 -38.261 1.00 141.17 ? 549  ASP A O     1 
ATOM   3194 C  CB    . ASP A 1 446 ? -80.189 -25.816 -36.036 1.00 145.44 ? 549  ASP A CB    1 
ATOM   3195 C  CG    . ASP A 1 446 ? -80.650 -26.540 -34.786 1.00 155.96 ? 549  ASP A CG    1 
ATOM   3196 O  OD1   . ASP A 1 446 ? -79.816 -27.217 -34.148 1.00 159.10 ? 549  ASP A OD1   1 
ATOM   3197 O  OD2   . ASP A 1 446 ? -81.846 -26.431 -34.440 1.00 171.35 ? 549  ASP A OD2   1 
ATOM   3198 N  N     . PHE A 1 447 ? -78.225 -23.426 -37.313 1.00 129.19 ? 550  PHE A N     1 
ATOM   3199 C  CA    . PHE A 1 447 ? -77.776 -22.743 -38.523 1.00 145.72 ? 550  PHE A CA    1 
ATOM   3200 C  C     . PHE A 1 447 ? -76.319 -23.066 -38.826 1.00 165.20 ? 550  PHE A C     1 
ATOM   3201 O  O     . PHE A 1 447 ? -75.959 -23.317 -39.982 1.00 169.30 ? 550  PHE A O     1 
ATOM   3202 C  CB    . PHE A 1 447 ? -77.972 -21.234 -38.377 1.00 153.04 ? 550  PHE A CB    1 
ATOM   3203 C  CG    . PHE A 1 447 ? -77.735 -20.464 -39.646 1.00 145.03 ? 550  PHE A CG    1 
ATOM   3204 C  CD1   . PHE A 1 447 ? -77.951 -21.051 -40.882 1.00 147.74 ? 550  PHE A CD1   1 
ATOM   3205 C  CD2   . PHE A 1 447 ? -77.289 -19.154 -39.602 1.00 146.00 ? 550  PHE A CD2   1 
ATOM   3206 C  CE1   . PHE A 1 447 ? -77.732 -20.345 -42.049 1.00 181.14 ? 550  PHE A CE1   1 
ATOM   3207 C  CE2   . PHE A 1 447 ? -77.068 -18.443 -40.765 1.00 146.62 ? 550  PHE A CE2   1 
ATOM   3208 C  CZ    . PHE A 1 447 ? -77.289 -19.039 -41.990 1.00 181.21 ? 550  PHE A CZ    1 
ATOM   3209 N  N     . LEU A 1 448 ? -75.467 -23.069 -37.798 1.00 167.69 ? 551  LEU A N     1 
ATOM   3210 C  CA    . LEU A 1 448 ? -74.062 -23.397 -38.006 1.00 145.37 ? 551  LEU A CA    1 
ATOM   3211 C  C     . LEU A 1 448 ? -73.861 -24.889 -38.236 1.00 156.29 ? 551  LEU A C     1 
ATOM   3212 O  O     . LEU A 1 448 ? -72.948 -25.284 -38.969 1.00 169.08 ? 551  LEU A O     1 
ATOM   3213 C  CB    . LEU A 1 448 ? -73.232 -22.926 -36.812 1.00 127.23 ? 551  LEU A CB    1 
ATOM   3214 C  CG    . LEU A 1 448 ? -73.260 -21.423 -36.527 1.00 124.20 ? 551  LEU A CG    1 
ATOM   3215 C  CD1   . LEU A 1 448 ? -72.511 -21.106 -35.242 1.00 137.57 ? 551  LEU A CD1   1 
ATOM   3216 C  CD2   . LEU A 1 448 ? -72.677 -20.645 -37.696 1.00 139.60 ? 551  LEU A CD2   1 
ATOM   3217 N  N     . TRP A 1 449 ? -74.700 -25.730 -37.627 1.00 146.33 ? 552  TRP A N     1 
ATOM   3218 C  CA    . TRP A 1 449 ? -74.548 -27.171 -37.796 1.00 129.50 ? 552  TRP A CA    1 
ATOM   3219 C  C     . TRP A 1 449 ? -75.051 -27.634 -39.157 1.00 147.09 ? 552  TRP A C     1 
ATOM   3220 O  O     . TRP A 1 449 ? -74.456 -28.528 -39.768 1.00 140.82 ? 552  TRP A O     1 
ATOM   3221 C  CB    . TRP A 1 449 ? -75.275 -27.916 -36.676 1.00 122.41 ? 552  TRP A CB    1 
ATOM   3222 C  CG    . TRP A 1 449 ? -75.155 -29.403 -36.789 1.00 129.69 ? 552  TRP A CG    1 
ATOM   3223 C  CD1   . TRP A 1 449 ? -76.161 -30.290 -37.042 1.00 171.61 ? 552  TRP A CD1   1 
ATOM   3224 C  CD2   . TRP A 1 449 ? -73.957 -30.179 -36.670 1.00 151.64 ? 552  TRP A CD2   1 
ATOM   3225 N  NE1   . TRP A 1 449 ? -75.664 -31.571 -37.079 1.00 169.93 ? 552  TRP A NE1   1 
ATOM   3226 C  CE2   . TRP A 1 449 ? -74.313 -31.530 -36.854 1.00 152.45 ? 552  TRP A CE2   1 
ATOM   3227 C  CE3   . TRP A 1 449 ? -72.617 -29.863 -36.421 1.00 143.82 ? 552  TRP A CE3   1 
ATOM   3228 C  CZ2   . TRP A 1 449 ? -73.380 -32.563 -36.799 1.00 165.37 ? 552  TRP A CZ2   1 
ATOM   3229 C  CZ3   . TRP A 1 449 ? -71.692 -30.891 -36.366 1.00 130.41 ? 552  TRP A CZ3   1 
ATOM   3230 C  CH2   . TRP A 1 449 ? -72.078 -32.223 -36.554 1.00 163.13 ? 552  TRP A CH2   1 
ATOM   3231 N  N     . SER A 1 450 ? -76.146 -27.047 -39.647 1.00 165.57 ? 553  SER A N     1 
ATOM   3232 C  CA    . SER A 1 450 ? -76.627 -27.384 -40.982 1.00 154.75 ? 553  SER A CA    1 
ATOM   3233 C  C     . SER A 1 450 ? -75.704 -26.858 -42.072 1.00 164.65 ? 553  SER A C     1 
ATOM   3234 O  O     . SER A 1 450 ? -75.743 -27.363 -43.198 1.00 181.07 ? 553  SER A O     1 
ATOM   3235 C  CB    . SER A 1 450 ? -78.042 -26.840 -41.188 1.00 150.72 ? 553  SER A CB    1 
ATOM   3236 O  OG    . SER A 1 450 ? -78.071 -25.430 -41.056 1.00 167.35 ? 553  SER A OG    1 
ATOM   3237 N  N     . HIS A 1 451 ? -74.880 -25.860 -41.762 1.00 151.12 ? 554  HIS A N     1 
ATOM   3238 C  CA    . HIS A 1 451 ? -73.894 -25.314 -42.688 1.00 161.38 ? 554  HIS A CA    1 
ATOM   3239 C  C     . HIS A 1 451 ? -72.475 -25.590 -42.198 1.00 164.28 ? 554  HIS A C     1 
ATOM   3240 O  O     . HIS A 1 451 ? -71.581 -24.750 -42.322 1.00 166.47 ? 554  HIS A O     1 
ATOM   3241 C  CB    . HIS A 1 451 ? -74.109 -23.816 -42.888 1.00 169.63 ? 554  HIS A CB    1 
ATOM   3242 C  CG    . HIS A 1 451 ? -75.420 -23.471 -43.524 1.00 162.97 ? 554  HIS A CG    1 
ATOM   3243 N  ND1   . HIS A 1 451 ? -76.633 -23.762 -42.937 1.00 174.38 ? 554  HIS A ND1   1 
ATOM   3244 C  CD2   . HIS A 1 451 ? -75.707 -22.857 -44.696 1.00 166.11 ? 554  HIS A CD2   1 
ATOM   3245 C  CE1   . HIS A 1 451 ? -77.611 -23.343 -43.720 1.00 174.16 ? 554  HIS A CE1   1 
ATOM   3246 N  NE2   . HIS A 1 451 ? -77.076 -22.790 -44.794 1.00 185.33 ? 554  HIS A NE2   1 
ATOM   3247 N  N     . ARG A 1 452 ? -72.257 -26.779 -41.629 1.00 172.09 ? 555  ARG A N     1 
ATOM   3248 C  CA    . ARG A 1 452 ? -70.947 -27.111 -41.079 1.00 157.35 ? 555  ARG A CA    1 
ATOM   3249 C  C     . ARG A 1 452 ? -69.903 -27.298 -42.173 1.00 175.21 ? 555  ARG A C     1 
ATOM   3250 O  O     . ARG A 1 452 ? -68.725 -26.992 -41.960 1.00 171.33 ? 555  ARG A O     1 
ATOM   3251 C  CB    . ARG A 1 452 ? -71.044 -28.370 -40.215 1.00 147.56 ? 555  ARG A CB    1 
ATOM   3252 C  CG    . ARG A 1 452 ? -71.657 -29.570 -40.923 1.00 152.50 ? 555  ARG A CG    1 
ATOM   3253 C  CD    . ARG A 1 452 ? -71.861 -30.730 -39.962 1.00 158.56 ? 555  ARG A CD    1 
ATOM   3254 N  NE    . ARG A 1 452 ? -72.605 -31.825 -40.572 1.00 149.39 ? 555  ARG A NE    1 
ATOM   3255 C  CZ    . ARG A 1 452 ? -73.927 -31.935 -40.552 1.00 153.00 ? 555  ARG A CZ    1 
ATOM   3256 N  NH1   . ARG A 1 452 ? -74.687 -31.028 -39.961 1.00 155.90 ? 555  ARG A NH1   1 
ATOM   3257 N  NH2   . ARG A 1 452 ? -74.500 -32.982 -41.140 1.00 164.63 ? 555  ARG A NH2   1 
ATOM   3258 N  N     . HIS A 1 453 ? -70.309 -27.794 -43.342 1.00 172.32 ? 556  HIS A N     1 
ATOM   3259 C  CA    . HIS A 1 453 ? -69.377 -27.994 -44.443 1.00 158.96 ? 556  HIS A CA    1 
ATOM   3260 C  C     . HIS A 1 453 ? -69.034 -26.701 -45.171 1.00 163.41 ? 556  HIS A C     1 
ATOM   3261 O  O     . HIS A 1 453 ? -68.143 -26.709 -46.026 1.00 167.18 ? 556  HIS A O     1 
ATOM   3262 C  CB    . HIS A 1 453 ? -69.947 -29.014 -45.433 1.00 155.98 ? 556  HIS A CB    1 
ATOM   3263 C  CG    . HIS A 1 453 ? -70.161 -30.373 -44.841 1.00 175.09 ? 556  HIS A CG    1 
ATOM   3264 N  ND1   . HIS A 1 453 ? -69.743 -30.706 -43.570 1.00 163.35 ? 556  HIS A ND1   1 
ATOM   3265 C  CD2   . HIS A 1 453 ? -70.751 -31.483 -45.345 1.00 195.17 ? 556  HIS A CD2   1 
ATOM   3266 C  CE1   . HIS A 1 453 ? -70.065 -31.962 -43.317 1.00 167.48 ? 556  HIS A CE1   1 
ATOM   3267 N  NE2   . HIS A 1 453 ? -70.678 -32.456 -44.378 1.00 197.18 ? 556  HIS A NE2   1 
ATOM   3268 N  N     . TYR A 1 454 ? -69.716 -25.601 -44.856 1.00 188.03 ? 557  TYR A N     1 
ATOM   3269 C  CA    . TYR A 1 454 ? -69.386 -24.299 -45.419 1.00 196.15 ? 557  TYR A CA    1 
ATOM   3270 C  C     . TYR A 1 454 ? -68.431 -23.500 -44.543 1.00 199.70 ? 557  TYR A C     1 
ATOM   3271 O  O     . TYR A 1 454 ? -67.714 -22.635 -45.059 1.00 196.90 ? 557  TYR A O     1 
ATOM   3272 C  CB    . TYR A 1 454 ? -70.667 -23.486 -45.654 1.00 193.10 ? 557  TYR A CB    1 
ATOM   3273 C  CG    . TYR A 1 454 ? -70.431 -22.005 -45.861 1.00 214.98 ? 557  TYR A CG    1 
ATOM   3274 C  CD1   . TYR A 1 454 ? -70.000 -21.515 -47.087 1.00 228.91 ? 557  TYR A CD1   1 
ATOM   3275 C  CD2   . TYR A 1 454 ? -70.636 -21.098 -44.828 1.00 218.24 ? 557  TYR A CD2   1 
ATOM   3276 C  CE1   . TYR A 1 454 ? -69.779 -20.163 -47.279 1.00 225.37 ? 557  TYR A CE1   1 
ATOM   3277 C  CE2   . TYR A 1 454 ? -70.417 -19.746 -45.010 1.00 224.85 ? 557  TYR A CE2   1 
ATOM   3278 C  CZ    . TYR A 1 454 ? -69.990 -19.284 -46.237 1.00 224.27 ? 557  TYR A CZ    1 
ATOM   3279 O  OH    . TYR A 1 454 ? -69.773 -17.938 -46.423 1.00 234.10 ? 557  TYR A OH    1 
ATOM   3280 N  N     . CYS A 1 455 ? -68.389 -23.784 -43.239 1.00 178.10 ? 558  CYS A N     1 
ATOM   3281 C  CA    . CYS A 1 455 ? -67.589 -22.997 -42.306 1.00 166.51 ? 558  CYS A CA    1 
ATOM   3282 C  C     . CYS A 1 455 ? -66.095 -23.049 -42.600 1.00 165.45 ? 558  CYS A C     1 
ATOM   3283 O  O     . CYS A 1 455 ? -65.338 -22.289 -41.985 1.00 169.43 ? 558  CYS A O     1 
ATOM   3284 C  CB    . CYS A 1 455 ? -67.849 -23.466 -40.873 1.00 165.40 ? 558  CYS A CB    1 
ATOM   3285 S  SG    . CYS A 1 455 ? -69.541 -23.199 -40.297 1.00 167.28 ? 558  CYS A SG    1 
ATOM   3286 N  N     . VAL A 1 456 ? -65.650 -23.916 -43.512 1.00 162.13 ? 559  VAL A N     1 
ATOM   3287 C  CA    . VAL A 1 456 ? -64.243 -23.929 -43.892 1.00 164.05 ? 559  VAL A CA    1 
ATOM   3288 C  C     . VAL A 1 456 ? -63.854 -22.658 -44.637 1.00 164.39 ? 559  VAL A C     1 
ATOM   3289 O  O     . VAL A 1 456 ? -62.667 -22.316 -44.693 1.00 153.24 ? 559  VAL A O     1 
ATOM   3290 C  CB    . VAL A 1 456 ? -63.921 -25.175 -44.738 1.00 171.42 ? 559  VAL A CB    1 
ATOM   3291 C  CG1   . VAL A 1 456 ? -64.135 -26.439 -43.920 1.00 138.32 ? 559  VAL A CG1   1 
ATOM   3292 C  CG2   . VAL A 1 456 ? -64.775 -25.198 -45.997 1.00 176.73 ? 559  VAL A CG2   1 
ATOM   3293 N  N     . THR A 1 457 ? -64.827 -21.947 -45.213 1.00 168.18 ? 560  THR A N     1 
ATOM   3294 C  CA    . THR A 1 457 ? -64.528 -20.678 -45.869 1.00 168.39 ? 560  THR A CA    1 
ATOM   3295 C  C     . THR A 1 457 ? -64.183 -19.602 -44.848 1.00 167.97 ? 560  THR A C     1 
ATOM   3296 O  O     . THR A 1 457 ? -63.276 -18.791 -45.072 1.00 178.55 ? 560  THR A O     1 
ATOM   3297 C  CB    . THR A 1 457 ? -65.714 -20.241 -46.731 1.00 171.72 ? 560  THR A CB    1 
ATOM   3298 O  OG1   . THR A 1 457 ? -66.017 -21.266 -47.685 1.00 171.48 ? 560  THR A OG1   1 
ATOM   3299 C  CG2   . THR A 1 457 ? -65.393 -18.949 -47.470 1.00 180.54 ? 560  THR A CG2   1 
ATOM   3300 N  N     . ILE A 1 458 ? -64.890 -19.580 -43.722 1.00 155.76 ? 561  ILE A N     1 
ATOM   3301 C  CA    . ILE A 1 458 ? -64.616 -18.638 -42.640 1.00 167.91 ? 561  ILE A CA    1 
ATOM   3302 C  C     . ILE A 1 458 ? -64.131 -19.422 -41.426 1.00 154.03 ? 561  ILE A C     1 
ATOM   3303 O  O     . ILE A 1 458 ? -64.934 -19.761 -40.544 1.00 152.98 ? 561  ILE A O     1 
ATOM   3304 C  CB    . ILE A 1 458 ? -65.855 -17.789 -42.313 1.00 151.93 ? 561  ILE A CB    1 
ATOM   3305 C  CG1   . ILE A 1 458 ? -67.130 -18.628 -42.429 1.00 160.22 ? 561  ILE A CG1   1 
ATOM   3306 C  CG2   . ILE A 1 458 ? -65.930 -16.581 -43.235 1.00 177.41 ? 561  ILE A CG2   1 
ATOM   3307 N  N     . PRO A 1 459 ? -62.833 -19.730 -41.332 1.00 147.41 ? 562  PRO A N     1 
ATOM   3308 C  CA    . PRO A 1 459 ? -62.353 -20.575 -40.226 1.00 132.22 ? 562  PRO A CA    1 
ATOM   3309 C  C     . PRO A 1 459 ? -62.402 -19.905 -38.863 1.00 122.97 ? 562  PRO A C     1 
ATOM   3310 O  O     . PRO A 1 459 ? -62.224 -20.597 -37.853 1.00 120.45 ? 562  PRO A O     1 
ATOM   3311 C  CB    . PRO A 1 459 ? -60.909 -20.894 -40.634 1.00 132.42 ? 562  PRO A CB    1 
ATOM   3312 C  CG    . PRO A 1 459 ? -60.505 -19.742 -41.490 1.00 154.81 ? 562  PRO A CG    1 
ATOM   3313 C  CD    . PRO A 1 459 ? -61.744 -19.329 -42.238 1.00 146.31 ? 562  PRO A CD    1 
ATOM   3314 N  N     . GLU A 1 460 ? -62.636 -18.593 -38.795 1.00 130.07 ? 563  GLU A N     1 
ATOM   3315 C  CA    . GLU A 1 460 ? -62.740 -17.922 -37.504 1.00 127.42 ? 563  GLU A CA    1 
ATOM   3316 C  C     . GLU A 1 460 ? -64.037 -18.248 -36.775 1.00 139.69 ? 563  GLU A C     1 
ATOM   3317 O  O     . GLU A 1 460 ? -64.144 -17.955 -35.580 1.00 128.05 ? 563  GLU A O     1 
ATOM   3318 C  CB    . GLU A 1 460 ? -62.611 -16.406 -37.679 1.00 147.41 ? 563  GLU A CB    1 
ATOM   3319 C  CG    . GLU A 1 460 ? -63.649 -15.779 -38.599 1.00 161.71 ? 563  GLU A CG    1 
ATOM   3320 C  CD    . GLU A 1 460 ? -63.258 -15.848 -40.064 1.00 157.43 ? 563  GLU A CD    1 
ATOM   3321 O  OE1   . GLU A 1 460 ? -62.211 -16.452 -40.376 1.00 161.44 ? 563  GLU A OE1   1 
ATOM   3322 O  OE2   . GLU A 1 460 ? -63.998 -15.293 -40.903 1.00 175.64 ? 563  GLU A OE2   1 
ATOM   3323 N  N     . ILE A 1 461 ? -65.019 -18.843 -37.461 1.00 156.76 ? 564  ILE A N     1 
ATOM   3324 C  CA    . ILE A 1 461 ? -66.271 -19.239 -36.818 1.00 132.88 ? 564  ILE A CA    1 
ATOM   3325 C  C     . ILE A 1 461 ? -66.172 -20.602 -36.152 1.00 132.37 ? 564  ILE A C     1 
ATOM   3326 O  O     . ILE A 1 461 ? -67.166 -21.082 -35.590 1.00 131.69 ? 564  ILE A O     1 
ATOM   3327 C  CB    . ILE A 1 461 ? -67.417 -19.214 -37.853 1.00 116.30 ? 564  ILE A CB    1 
ATOM   3328 C  CG1   . ILE A 1 461 ? -68.767 -18.975 -37.170 1.00 131.53 ? 564  ILE A CG1   1 
ATOM   3329 C  CG2   . ILE A 1 461 ? -67.440 -20.501 -38.669 1.00 116.66 ? 564  ILE A CG2   1 
ATOM   3330 N  N     . LEU A 1 462 ? -64.997 -21.234 -36.187 1.00 127.84 ? 565  LEU A N     1 
ATOM   3331 C  CA    . LEU A 1 462 ? -64.831 -22.551 -35.572 1.00 131.33 ? 565  LEU A CA    1 
ATOM   3332 C  C     . LEU A 1 462 ? -65.199 -22.577 -34.093 1.00 127.09 ? 565  LEU A C     1 
ATOM   3333 O  O     . LEU A 1 462 ? -65.896 -23.519 -33.675 1.00 102.31 ? 565  LEU A O     1 
ATOM   3334 C  CB    . LEU A 1 462 ? -63.397 -23.043 -35.797 1.00 112.45 ? 565  LEU A CB    1 
ATOM   3335 C  CG    . LEU A 1 462 ? -63.019 -24.365 -35.126 1.00 129.34 ? 565  LEU A CG    1 
ATOM   3336 C  CD1   . LEU A 1 462 ? -63.891 -25.502 -35.638 1.00 120.74 ? 565  LEU A CD1   1 
ATOM   3337 C  CD2   . LEU A 1 462 ? -61.545 -24.674 -35.340 1.00 118.60 ? 565  LEU A CD2   1 
ATOM   3338 N  N     . PRO A 1 463 ? -64.779 -21.622 -33.251 1.00 127.18 ? 566  PRO A N     1 
ATOM   3339 C  CA    . PRO A 1 463 ? -65.245 -21.650 -31.854 1.00 118.33 ? 566  PRO A CA    1 
ATOM   3340 C  C     . PRO A 1 463 ? -66.751 -21.513 -31.721 1.00 123.85 ? 566  PRO A C     1 
ATOM   3341 O  O     . PRO A 1 463 ? -67.328 -22.028 -30.755 1.00 113.99 ? 566  PRO A O     1 
ATOM   3342 C  CB    . PRO A 1 463 ? -64.505 -20.467 -31.212 1.00 117.54 ? 566  PRO A CB    1 
ATOM   3343 C  CG    . PRO A 1 463 ? -64.121 -19.589 -32.347 1.00 127.10 ? 566  PRO A CG    1 
ATOM   3344 C  CD    . PRO A 1 463 ? -63.821 -20.523 -33.473 1.00 133.31 ? 566  PRO A CD    1 
ATOM   3345 N  N     . LYS A 1 464 ? -67.408 -20.833 -32.664 1.00 139.56 ? 567  LYS A N     1 
ATOM   3346 C  CA    . LYS A 1 464 ? -68.864 -20.764 -32.644 1.00 122.96 ? 567  LYS A CA    1 
ATOM   3347 C  C     . LYS A 1 464 ? -69.491 -22.079 -33.090 1.00 125.86 ? 567  LYS A C     1 
ATOM   3348 O  O     . LYS A 1 464 ? -70.549 -22.466 -32.581 1.00 139.14 ? 567  LYS A O     1 
ATOM   3349 C  CB    . LYS A 1 464 ? -69.351 -19.621 -33.535 1.00 123.40 ? 567  LYS A CB    1 
ATOM   3350 C  CG    . LYS A 1 464 ? -68.715 -18.271 -33.236 1.00 133.81 ? 567  LYS A CG    1 
ATOM   3351 C  CD    . LYS A 1 464 ? -69.120 -17.748 -31.869 1.00 133.74 ? 567  LYS A CD    1 
ATOM   3352 C  CE    . LYS A 1 464 ? -68.531 -16.370 -31.614 1.00 136.81 ? 567  LYS A CE    1 
ATOM   3353 N  NZ    . LYS A 1 464 ? -68.926 -15.830 -30.284 1.00 157.66 ? 567  LYS A NZ    1 
ATOM   3354 N  N     . LEU A 1 465 ? -68.855 -22.777 -34.035 1.00 140.32 ? 568  LEU A N     1 
ATOM   3355 C  CA    . LEU A 1 465 ? -69.399 -24.038 -34.527 1.00 128.38 ? 568  LEU A CA    1 
ATOM   3356 C  C     . LEU A 1 465 ? -69.277 -25.149 -33.493 1.00 120.39 ? 568  LEU A C     1 
ATOM   3357 O  O     . LEU A 1 465 ? -70.146 -26.026 -33.423 1.00 125.94 ? 568  LEU A O     1 
ATOM   3358 C  CB    . LEU A 1 465 ? -68.695 -24.439 -35.824 1.00 126.13 ? 568  LEU A CB    1 
ATOM   3359 C  CG    . LEU A 1 465 ? -69.040 -25.805 -36.420 1.00 121.68 ? 568  LEU A CG    1 
ATOM   3360 C  CD1   . LEU A 1 465 ? -70.518 -25.887 -36.768 1.00 124.11 ? 568  LEU A CD1   1 
ATOM   3361 C  CD2   . LEU A 1 465 ? -68.179 -26.090 -37.642 1.00 138.20 ? 568  LEU A CD2   1 
ATOM   3362 N  N     . LEU A 1 466 ? -68.214 -25.131 -32.684 1.00 119.01 ? 569  LEU A N     1 
ATOM   3363 C  CA    . LEU A 1 466 ? -68.015 -26.191 -31.702 1.00 116.99 ? 569  LEU A CA    1 
ATOM   3364 C  C     . LEU A 1 466 ? -69.072 -26.155 -30.605 1.00 133.59 ? 569  LEU A C     1 
ATOM   3365 O  O     . LEU A 1 466 ? -69.394 -27.198 -30.024 1.00 121.66 ? 569  LEU A O     1 
ATOM   3366 C  CB    . LEU A 1 466 ? -66.612 -26.088 -31.103 1.00 113.89 ? 569  LEU A CB    1 
ATOM   3367 C  CG    . LEU A 1 466 ? -65.472 -26.344 -32.092 1.00 128.12 ? 569  LEU A CG    1 
ATOM   3368 C  CD1   . LEU A 1 466 ? -64.129 -25.988 -31.478 1.00 106.56 ? 569  LEU A CD1   1 
ATOM   3369 C  CD2   . LEU A 1 466 ? -65.485 -27.793 -32.556 1.00 122.52 ? 569  LEU A CD2   1 
ATOM   3370 N  N     . LEU A 1 467 ? -69.621 -24.976 -30.308 1.00 129.05 ? 570  LEU A N     1 
ATOM   3371 C  CA    . LEU A 1 467 ? -70.701 -24.867 -29.335 1.00 117.17 ? 570  LEU A CA    1 
ATOM   3372 C  C     . LEU A 1 467 ? -72.056 -25.264 -29.906 1.00 120.08 ? 570  LEU A C     1 
ATOM   3373 O  O     . LEU A 1 467 ? -73.033 -25.320 -29.152 1.00 119.39 ? 570  LEU A O     1 
ATOM   3374 C  CB    . LEU A 1 467 ? -70.782 -23.440 -28.784 1.00 147.52 ? 570  LEU A CB    1 
ATOM   3375 C  CG    . LEU A 1 467 ? -69.948 -23.109 -27.543 1.00 121.59 ? 570  LEU A CG    1 
ATOM   3376 C  CD1   . LEU A 1 467 ? -68.464 -23.168 -27.847 1.00 95.26  ? 570  LEU A CD1   1 
ATOM   3377 C  CD2   . LEU A 1 467 ? -70.330 -21.744 -26.989 1.00 149.84 ? 570  LEU A CD2   1 
ATOM   3378 N  N     . SER A 1 468 ? -72.139 -25.535 -31.209 1.00 136.74 ? 571  SER A N     1 
ATOM   3379 C  CA    . SER A 1 468 ? -73.384 -25.920 -31.859 1.00 140.34 ? 571  SER A CA    1 
ATOM   3380 C  C     . SER A 1 468 ? -73.459 -27.418 -32.132 1.00 130.18 ? 571  SER A C     1 
ATOM   3381 O  O     . SER A 1 468 ? -74.201 -27.843 -33.023 1.00 146.06 ? 571  SER A O     1 
ATOM   3382 C  CB    . SER A 1 468 ? -73.559 -25.139 -33.162 1.00 137.87 ? 571  SER A CB    1 
ATOM   3383 O  OG    . SER A 1 468 ? -73.489 -23.741 -32.936 1.00 145.07 ? 571  SER A OG    1 
ATOM   3384 N  N     . VAL A 1 469 ? -72.709 -28.224 -31.384 1.00 134.14 ? 572  VAL A N     1 
ATOM   3385 C  CA    . VAL A 1 469 ? -72.628 -29.663 -31.601 1.00 139.54 ? 572  VAL A CA    1 
ATOM   3386 C  C     . VAL A 1 469 ? -73.048 -30.372 -30.322 1.00 136.42 ? 572  VAL A C     1 
ATOM   3387 O  O     . VAL A 1 469 ? -72.516 -30.084 -29.243 1.00 154.40 ? 572  VAL A O     1 
ATOM   3388 C  CB    . VAL A 1 469 ? -71.211 -30.095 -32.019 1.00 136.56 ? 572  VAL A CB    1 
ATOM   3389 C  CG1   . VAL A 1 469 ? -71.167 -31.593 -32.281 1.00 141.32 ? 572  VAL A CG1   1 
ATOM   3390 C  CG2   . VAL A 1 469 ? -70.759 -29.318 -33.241 1.00 149.16 ? 572  VAL A CG2   1 
ATOM   3391 N  N     . LYS A 1 470 ? -73.998 -31.294 -30.444 1.00 132.30 ? 573  LYS A N     1 
ATOM   3392 C  CA    . LYS A 1 470 ? -74.384 -32.152 -29.327 1.00 157.38 ? 573  LYS A CA    1 
ATOM   3393 C  C     . LYS A 1 470 ? -73.298 -33.200 -29.128 1.00 148.51 ? 573  LYS A C     1 
ATOM   3394 O  O     . LYS A 1 470 ? -73.287 -34.236 -29.797 1.00 155.84 ? 573  LYS A O     1 
ATOM   3395 C  CB    . LYS A 1 470 ? -75.738 -32.802 -29.588 1.00 143.31 ? 573  LYS A CB    1 
ATOM   3396 C  CG    . LYS A 1 470 ? -76.929 -31.883 -29.375 1.00 126.17 ? 573  LYS A CG    1 
ATOM   3397 C  CD    . LYS A 1 470 ? -78.236 -32.615 -29.638 1.00 136.41 ? 573  LYS A CD    1 
ATOM   3398 C  CE    . LYS A 1 470 ? -79.434 -31.794 -29.190 1.00 157.56 ? 573  LYS A CE    1 
ATOM   3399 N  NZ    . LYS A 1 470 ? -79.445 -31.586 -27.715 1.00 134.89 ? 573  LYS A NZ    1 
ATOM   3400 N  N     . TRP A 1 471 ? -72.371 -32.931 -28.205 1.00 122.13 ? 574  TRP A N     1 
ATOM   3401 C  CA    . TRP A 1 471 ? -71.285 -33.864 -27.931 1.00 125.88 ? 574  TRP A CA    1 
ATOM   3402 C  C     . TRP A 1 471 ? -71.771 -35.184 -27.348 1.00 155.17 ? 574  TRP A C     1 
ATOM   3403 O  O     . TRP A 1 471 ? -70.988 -36.138 -27.284 1.00 129.26 ? 574  TRP A O     1 
ATOM   3404 C  CB    . TRP A 1 471 ? -70.268 -33.221 -26.987 1.00 146.56 ? 574  TRP A CB    1 
ATOM   3405 C  CG    . TRP A 1 471 ? -69.586 -32.025 -27.576 1.00 143.98 ? 574  TRP A CG    1 
ATOM   3406 C  CD1   . TRP A 1 471 ? -69.938 -30.717 -27.413 1.00 136.21 ? 574  TRP A CD1   1 
ATOM   3407 C  CD2   . TRP A 1 471 ? -68.435 -32.027 -28.431 1.00 141.67 ? 574  TRP A CD2   1 
ATOM   3408 N  NE1   . TRP A 1 471 ? -69.076 -29.904 -28.111 1.00 132.16 ? 574  TRP A NE1   1 
ATOM   3409 C  CE2   . TRP A 1 471 ? -68.145 -30.685 -28.744 1.00 126.70 ? 574  TRP A CE2   1 
ATOM   3410 C  CE3   . TRP A 1 471 ? -67.622 -33.035 -28.960 1.00 121.95 ? 574  TRP A CE3   1 
ATOM   3411 C  CZ2   . TRP A 1 471 ? -67.077 -30.324 -29.562 1.00 124.68 ? 574  TRP A CZ2   1 
ATOM   3412 C  CZ3   . TRP A 1 471 ? -66.563 -32.674 -29.772 1.00 93.65  ? 574  TRP A CZ3   1 
ATOM   3413 C  CH2   . TRP A 1 471 ? -66.299 -31.331 -30.065 1.00 120.26 ? 574  TRP A CH2   1 
ATOM   3414 N  N     . ASN A 1 472 ? -73.031 -35.262 -26.923 1.00 157.23 ? 575  ASN A N     1 
ATOM   3415 C  CA    . ASN A 1 472 ? -73.627 -36.507 -26.458 1.00 145.78 ? 575  ASN A CA    1 
ATOM   3416 C  C     . ASN A 1 472 ? -74.123 -37.385 -27.600 1.00 158.46 ? 575  ASN A C     1 
ATOM   3417 O  O     . ASN A 1 472 ? -74.885 -38.326 -27.354 1.00 175.86 ? 575  ASN A O     1 
ATOM   3418 C  CB    . ASN A 1 472 ? -74.780 -36.208 -25.494 1.00 153.35 ? 575  ASN A CB    1 
ATOM   3419 C  CG    . ASN A 1 472 ? -75.892 -35.406 -26.145 1.00 150.01 ? 575  ASN A CG    1 
ATOM   3420 O  OD1   . ASN A 1 472 ? -76.858 -35.967 -26.661 1.00 156.76 ? 575  ASN A OD1   1 
ATOM   3421 N  ND2   . ASN A 1 472 ? -75.759 -34.085 -26.123 1.00 151.04 ? 575  ASN A ND2   1 
ATOM   3422 N  N     . SER A 1 473 ? -73.715 -37.098 -28.834 1.00 147.89 ? 576  SER A N     1 
ATOM   3423 C  CA    . SER A 1 473 ? -74.118 -37.866 -30.006 1.00 148.96 ? 576  SER A CA    1 
ATOM   3424 C  C     . SER A 1 473 ? -72.876 -38.468 -30.646 1.00 152.96 ? 576  SER A C     1 
ATOM   3425 O  O     . SER A 1 473 ? -71.974 -37.735 -31.065 1.00 158.52 ? 576  SER A O     1 
ATOM   3426 C  CB    . SER A 1 473 ? -74.868 -36.987 -31.009 1.00 167.39 ? 576  SER A CB    1 
ATOM   3427 O  OG    . SER A 1 473 ? -75.198 -37.715 -32.179 1.00 195.95 ? 576  SER A OG    1 
ATOM   3428 N  N     . ARG A 1 474 ? -72.834 -39.801 -30.725 1.00 153.95 ? 577  ARG A N     1 
ATOM   3429 C  CA    . ARG A 1 474 ? -71.704 -40.476 -31.352 1.00 145.79 ? 577  ARG A CA    1 
ATOM   3430 C  C     . ARG A 1 474 ? -71.609 -40.181 -32.843 1.00 151.61 ? 577  ARG A C     1 
ATOM   3431 O  O     . ARG A 1 474 ? -70.556 -40.419 -33.443 1.00 159.23 ? 577  ARG A O     1 
ATOM   3432 C  CB    . ARG A 1 474 ? -71.798 -41.985 -31.122 1.00 142.86 ? 577  ARG A CB    1 
ATOM   3433 C  CG    . ARG A 1 474 ? -73.072 -42.621 -31.657 1.00 183.50 ? 577  ARG A CG    1 
ATOM   3434 C  CD    . ARG A 1 474 ? -73.203 -44.065 -31.195 1.00 180.53 ? 577  ARG A CD    1 
ATOM   3435 N  NE    . ARG A 1 474 ? -72.126 -44.907 -31.700 1.00 177.98 ? 577  ARG A NE    1 
ATOM   3436 C  CZ    . ARG A 1 474 ? -72.233 -45.710 -32.750 1.00 176.46 ? 577  ARG A CZ    1 
ATOM   3437 N  NH1   . ARG A 1 474 ? -73.364 -45.814 -33.429 1.00 170.35 ? 577  ARG A NH1   1 
ATOM   3438 N  NH2   . ARG A 1 474 ? -71.180 -46.430 -33.127 1.00 171.05 ? 577  ARG A NH2   1 
ATOM   3439 N  N     . ASP A 1 475 ? -72.680 -39.672 -33.450 1.00 169.83 ? 578  ASP A N     1 
ATOM   3440 C  CA    . ASP A 1 475 ? -72.666 -39.309 -34.861 1.00 177.65 ? 578  ASP A CA    1 
ATOM   3441 C  C     . ASP A 1 475 ? -72.138 -37.898 -35.087 1.00 174.74 ? 578  ASP A C     1 
ATOM   3442 O  O     . ASP A 1 475 ? -71.383 -37.665 -36.036 1.00 184.33 ? 578  ASP A O     1 
ATOM   3443 C  CB    . ASP A 1 475 ? -74.072 -39.440 -35.452 1.00 193.00 ? 578  ASP A CB    1 
ATOM   3444 C  CG    . ASP A 1 475 ? -74.633 -40.843 -35.319 1.00 198.05 ? 578  ASP A CG    1 
ATOM   3445 O  OD1   . ASP A 1 475 ? -73.927 -41.717 -34.772 1.00 191.87 ? 578  ASP A OD1   1 
ATOM   3446 O  OD2   . ASP A 1 475 ? -75.779 -41.072 -35.760 1.00 199.95 ? 578  ASP A OD2   1 
ATOM   3447 N  N     . GLU A 1 476 ? -72.521 -36.947 -34.230 1.00 159.57 ? 579  GLU A N     1 
ATOM   3448 C  CA    . GLU A 1 476 ? -72.048 -35.577 -34.395 1.00 173.73 ? 579  GLU A CA    1 
ATOM   3449 C  C     . GLU A 1 476 ? -70.599 -35.424 -33.950 1.00 165.35 ? 579  GLU A C     1 
ATOM   3450 O  O     . GLU A 1 476 ? -69.853 -34.633 -34.540 1.00 146.55 ? 579  GLU A O     1 
ATOM   3451 C  CB    . GLU A 1 476 ? -72.945 -34.610 -33.623 1.00 170.66 ? 579  GLU A CB    1 
ATOM   3452 C  CG    . GLU A 1 476 ? -74.392 -34.597 -34.090 1.00 150.20 ? 579  GLU A CG    1 
ATOM   3453 C  CD    . GLU A 1 476 ? -75.195 -33.474 -33.464 1.00 154.86 ? 579  GLU A CD    1 
ATOM   3454 O  OE1   . GLU A 1 476 ? -74.619 -32.704 -32.666 1.00 172.02 ? 579  GLU A OE1   1 
ATOM   3455 O  OE2   . GLU A 1 476 ? -76.400 -33.357 -33.770 1.00 144.20 ? 579  GLU A OE2   1 
ATOM   3456 N  N     . VAL A 1 477 ? -70.182 -36.162 -32.917 1.00 161.41 ? 580  VAL A N     1 
ATOM   3457 C  CA    . VAL A 1 477 ? -68.794 -36.098 -32.479 1.00 139.51 ? 580  VAL A CA    1 
ATOM   3458 C  C     . VAL A 1 477 ? -67.866 -36.759 -33.489 1.00 149.58 ? 580  VAL A C     1 
ATOM   3459 O  O     . VAL A 1 477 ? -66.670 -36.444 -33.529 1.00 159.23 ? 580  VAL A O     1 
ATOM   3460 C  CB    . VAL A 1 477 ? -68.641 -36.733 -31.082 1.00 130.68 ? 580  VAL A CB    1 
ATOM   3461 C  CG1   . VAL A 1 477 ? -68.736 -38.251 -31.162 1.00 148.84 ? 580  VAL A CG1   1 
ATOM   3462 C  CG2   . VAL A 1 477 ? -67.333 -36.302 -30.434 1.00 129.87 ? 580  VAL A CG2   1 
ATOM   3463 N  N     . ALA A 1 478 ? -68.388 -37.662 -34.322 1.00 130.41 ? 581  ALA A N     1 
ATOM   3464 C  CA    . ALA A 1 478 ? -67.567 -38.285 -35.354 1.00 135.64 ? 581  ALA A CA    1 
ATOM   3465 C  C     . ALA A 1 478 ? -67.447 -37.392 -36.582 1.00 143.98 ? 581  ALA A C     1 
ATOM   3466 O  O     . ALA A 1 478 ? -66.391 -37.351 -37.223 1.00 145.15 ? 581  ALA A O     1 
ATOM   3467 C  CB    . ALA A 1 478 ? -68.145 -39.647 -35.736 1.00 137.97 ? 581  ALA A CB    1 
ATOM   3468 N  N     . GLN A 1 479 ? -68.518 -36.672 -36.926 1.00 135.04 ? 582  GLN A N     1 
ATOM   3469 C  CA    . GLN A 1 479 ? -68.457 -35.754 -38.058 1.00 127.37 ? 582  GLN A CA    1 
ATOM   3470 C  C     . GLN A 1 479 ? -67.644 -34.511 -37.730 1.00 148.69 ? 582  GLN A C     1 
ATOM   3471 O  O     . GLN A 1 479 ? -66.982 -33.953 -38.613 1.00 123.67 ? 582  GLN A O     1 
ATOM   3472 C  CB    . GLN A 1 479 ? -69.869 -35.365 -38.497 1.00 136.44 ? 582  GLN A CB    1 
ATOM   3473 C  CG    . GLN A 1 479 ? -70.682 -36.518 -39.059 1.00 173.61 ? 582  GLN A CG    1 
ATOM   3474 C  CD    . GLN A 1 479 ? -70.074 -37.097 -40.321 1.00 189.42 ? 582  GLN A CD    1 
ATOM   3475 O  OE1   . GLN A 1 479 ? -69.493 -36.375 -41.132 1.00 209.25 ? 582  GLN A OE1   1 
ATOM   3476 N  NE2   . GLN A 1 479 ? -70.199 -38.407 -40.491 1.00 170.15 ? 582  GLN A NE2   1 
ATOM   3477 N  N     . MET A 1 480 ? -67.679 -34.061 -36.473 1.00 159.90 ? 583  MET A N     1 
ATOM   3478 C  CA    . MET A 1 480 ? -66.898 -32.891 -36.090 1.00 136.08 ? 583  MET A CA    1 
ATOM   3479 C  C     . MET A 1 480 ? -65.410 -33.209 -36.020 1.00 149.25 ? 583  MET A C     1 
ATOM   3480 O  O     . MET A 1 480 ? -64.578 -32.330 -36.273 1.00 151.08 ? 583  MET A O     1 
ATOM   3481 C  CB    . MET A 1 480 ? -67.401 -32.341 -34.754 1.00 123.24 ? 583  MET A CB    1 
ATOM   3482 C  CG    . MET A 1 480 ? -66.710 -31.065 -34.293 1.00 139.91 ? 583  MET A CG    1 
ATOM   3483 S  SD    . MET A 1 480 ? -66.622 -29.795 -35.573 1.00 146.33 ? 583  MET A SD    1 
ATOM   3484 C  CE    . MET A 1 480 ? -68.356 -29.526 -35.926 1.00 131.18 ? 583  MET A CE    1 
ATOM   3485 N  N     . TYR A 1 481 ? -65.055 -34.455 -35.691 1.00 140.01 ? 584  TYR A N     1 
ATOM   3486 C  CA    . TYR A 1 481 ? -63.646 -34.837 -35.668 1.00 126.82 ? 584  TYR A CA    1 
ATOM   3487 C  C     . TYR A 1 481 ? -63.025 -34.744 -37.056 1.00 140.26 ? 584  TYR A C     1 
ATOM   3488 O  O     . TYR A 1 481 ? -61.877 -34.308 -37.203 1.00 143.78 ? 584  TYR A O     1 
ATOM   3489 C  CB    . TYR A 1 481 ? -63.490 -36.252 -35.109 1.00 123.20 ? 584  TYR A CB    1 
ATOM   3490 C  CG    . TYR A 1 481 ? -63.465 -36.329 -33.598 1.00 128.16 ? 584  TYR A CG    1 
ATOM   3491 C  CD1   . TYR A 1 481 ? -63.523 -35.179 -32.822 1.00 121.66 ? 584  TYR A CD1   1 
ATOM   3492 C  CD2   . TYR A 1 481 ? -63.368 -37.553 -32.949 1.00 119.49 ? 584  TYR A CD2   1 
ATOM   3493 C  CE1   . TYR A 1 481 ? -63.496 -35.248 -31.440 1.00 119.39 ? 584  TYR A CE1   1 
ATOM   3494 C  CE2   . TYR A 1 481 ? -63.339 -37.632 -31.570 1.00 121.58 ? 584  TYR A CE2   1 
ATOM   3495 C  CZ    . TYR A 1 481 ? -63.403 -36.477 -30.821 1.00 131.23 ? 584  TYR A CZ    1 
ATOM   3496 O  OH    . TYR A 1 481 ? -63.374 -36.551 -29.447 1.00 144.64 ? 584  TYR A OH    1 
ATOM   3497 N  N     . CYS A 1 482 ? -63.768 -35.149 -38.090 1.00 137.36 ? 585  CYS A N     1 
ATOM   3498 C  CA    . CYS A 1 482 ? -63.231 -35.101 -39.445 1.00 140.50 ? 585  CYS A CA    1 
ATOM   3499 C  C     . CYS A 1 482 ? -63.099 -33.670 -39.951 1.00 141.54 ? 585  CYS A C     1 
ATOM   3500 O  O     . CYS A 1 482 ? -62.228 -33.386 -40.781 1.00 156.26 ? 585  CYS A O     1 
ATOM   3501 C  CB    . CYS A 1 482 ? -64.110 -35.921 -40.390 1.00 144.20 ? 585  CYS A CB    1 
ATOM   3502 S  SG    . CYS A 1 482 ? -64.119 -37.698 -40.046 1.00 148.22 ? 585  CYS A SG    1 
ATOM   3503 N  N     . LEU A 1 483 ? -63.948 -32.758 -39.470 1.00 131.57 ? 586  LEU A N     1 
ATOM   3504 C  CA    . LEU A 1 483 ? -63.837 -31.363 -39.882 1.00 131.59 ? 586  LEU A CA    1 
ATOM   3505 C  C     . LEU A 1 483 ? -62.630 -30.693 -39.238 1.00 147.47 ? 586  LEU A C     1 
ATOM   3506 O  O     . LEU A 1 483 ? -61.954 -29.875 -39.873 1.00 139.96 ? 586  LEU A O     1 
ATOM   3507 C  CB    . LEU A 1 483 ? -65.120 -30.608 -39.536 1.00 145.28 ? 586  LEU A CB    1 
ATOM   3508 C  CG    . LEU A 1 483 ? -66.393 -31.057 -40.257 1.00 156.91 ? 586  LEU A CG    1 
ATOM   3509 C  CD1   . LEU A 1 483 ? -67.593 -30.257 -39.776 1.00 155.19 ? 586  LEU A CD1   1 
ATOM   3510 C  CD2   . LEU A 1 483 ? -66.229 -30.930 -41.764 1.00 141.54 ? 586  LEU A CD2   1 
ATOM   3511 N  N     . VAL A 1 484 ? -62.345 -31.026 -37.977 1.00 148.00 ? 587  VAL A N     1 
ATOM   3512 C  CA    . VAL A 1 484 ? -61.183 -30.458 -37.302 1.00 116.47 ? 587  VAL A CA    1 
ATOM   3513 C  C     . VAL A 1 484 ? -59.893 -31.038 -37.869 1.00 130.85 ? 587  VAL A C     1 
ATOM   3514 O  O     . VAL A 1 484 ? -58.852 -30.369 -37.878 1.00 162.79 ? 587  VAL A O     1 
ATOM   3515 C  CB    . VAL A 1 484 ? -61.295 -30.686 -35.782 1.00 122.82 ? 587  VAL A CB    1 
ATOM   3516 C  CG1   . VAL A 1 484 ? -60.080 -30.130 -35.056 1.00 132.71 ? 587  VAL A CG1   1 
ATOM   3517 C  CG2   . VAL A 1 484 ? -62.568 -30.051 -35.246 1.00 135.23 ? 587  VAL A CG2   1 
ATOM   3518 N  N     . LYS A 1 485 ? -59.939 -32.278 -38.366 1.00 129.11 ? 588  LYS A N     1 
ATOM   3519 C  CA    . LYS A 1 485 ? -58.741 -32.905 -38.915 1.00 141.65 ? 588  LYS A CA    1 
ATOM   3520 C  C     . LYS A 1 485 ? -58.206 -32.129 -40.114 1.00 126.56 ? 588  LYS A C     1 
ATOM   3521 O  O     . LYS A 1 485 ? -56.989 -32.007 -40.291 1.00 142.88 ? 588  LYS A O     1 
ATOM   3522 C  CB    . LYS A 1 485 ? -59.040 -34.353 -39.303 1.00 115.16 ? 588  LYS A CB    1 
ATOM   3523 C  CG    . LYS A 1 485 ? -57.849 -35.108 -39.870 1.00 129.60 ? 588  LYS A CG    1 
ATOM   3524 C  CD    . LYS A 1 485 ? -58.238 -36.513 -40.304 1.00 137.59 ? 588  LYS A CD    1 
ATOM   3525 C  CE    . LYS A 1 485 ? -59.281 -36.481 -41.409 1.00 137.16 ? 588  LYS A CE    1 
ATOM   3526 N  NZ    . LYS A 1 485 ? -59.662 -37.850 -41.855 1.00 147.19 ? 588  LYS A NZ    1 
ATOM   3527 N  N     . ASP A 1 486 ? -59.098 -31.593 -40.943 1.00 138.85 ? 589  ASP A N     1 
ATOM   3528 C  CA    . ASP A 1 486 ? -58.729 -30.839 -42.135 1.00 152.03 ? 589  ASP A CA    1 
ATOM   3529 C  C     . ASP A 1 486 ? -59.186 -29.389 -42.027 1.00 139.51 ? 589  ASP A C     1 
ATOM   3530 O  O     . ASP A 1 486 ? -59.597 -28.772 -43.012 1.00 140.25 ? 589  ASP A O     1 
ATOM   3531 C  CB    . ASP A 1 486 ? -59.305 -31.491 -43.390 1.00 166.42 ? 589  ASP A CB    1 
ATOM   3532 C  CG    . ASP A 1 486 ? -58.770 -32.893 -43.619 1.00 156.93 ? 589  ASP A CG    1 
ATOM   3533 O  OD1   . ASP A 1 486 ? -57.837 -33.304 -42.898 1.00 171.49 ? 589  ASP A OD1   1 
ATOM   3534 O  OD2   . ASP A 1 486 ? -59.286 -33.586 -44.521 1.00 166.13 ? 589  ASP A OD2   1 
ATOM   3535 N  N     . TRP A 1 487 ? -59.114 -28.824 -40.823 1.00 123.53 ? 590  TRP A N     1 
ATOM   3536 C  CA    . TRP A 1 487 ? -59.574 -27.449 -40.673 1.00 133.89 ? 590  TRP A CA    1 
ATOM   3537 C  C     . TRP A 1 487 ? -58.453 -26.472 -41.024 1.00 140.23 ? 590  TRP A C     1 
ATOM   3538 O  O     . TRP A 1 487 ? -57.287 -26.728 -40.709 1.00 132.01 ? 590  TRP A O     1 
ATOM   3539 C  CB    . TRP A 1 487 ? -60.050 -27.192 -39.246 1.00 137.48 ? 590  TRP A CB    1 
ATOM   3540 C  CG    . TRP A 1 487 ? -60.879 -25.951 -39.099 1.00 132.12 ? 590  TRP A CG    1 
ATOM   3541 C  CD1   . TRP A 1 487 ? -60.442 -24.712 -38.732 1.00 141.44 ? 590  TRP A CD1   1 
ATOM   3542 C  CD2   . TRP A 1 487 ? -62.289 -25.829 -39.320 1.00 122.23 ? 590  TRP A CD2   1 
ATOM   3543 N  NE1   . TRP A 1 487 ? -61.493 -23.826 -38.709 1.00 122.20 ? 590  TRP A NE1   1 
ATOM   3544 C  CE2   . TRP A 1 487 ? -62.638 -24.488 -39.066 1.00 126.12 ? 590  TRP A CE2   1 
ATOM   3545 C  CE3   . TRP A 1 487 ? -63.291 -26.725 -39.706 1.00 122.86 ? 590  TRP A CE3   1 
ATOM   3546 C  CZ2   . TRP A 1 487 ? -63.944 -24.021 -39.187 1.00 134.74 ? 590  TRP A CZ2   1 
ATOM   3547 C  CZ3   . TRP A 1 487 ? -64.587 -26.259 -39.825 1.00 127.60 ? 590  TRP A CZ3   1 
ATOM   3548 C  CH2   . TRP A 1 487 ? -64.902 -24.920 -39.566 1.00 137.99 ? 590  TRP A CH2   1 
ATOM   3549 N  N     . PRO A 1 488 ? -58.782 -25.362 -41.683 1.00 130.09 ? 591  PRO A N     1 
ATOM   3550 C  CA    . PRO A 1 488 ? -57.749 -24.395 -42.039 1.00 131.31 ? 591  PRO A CA    1 
ATOM   3551 C  C     . PRO A 1 488 ? -57.130 -23.789 -40.797 1.00 135.40 ? 591  PRO A C     1 
ATOM   3552 O  O     . PRO A 1 488 ? -57.766 -23.732 -39.727 1.00 146.24 ? 591  PRO A O     1 
ATOM   3553 C  CB    . PRO A 1 488 ? -58.514 -23.345 -42.857 1.00 144.22 ? 591  PRO A CB    1 
ATOM   3554 C  CG    . PRO A 1 488 ? -59.728 -24.055 -43.351 1.00 151.34 ? 591  PRO A CG    1 
ATOM   3555 C  CD    . PRO A 1 488 ? -60.090 -25.016 -42.264 1.00 136.94 ? 591  PRO A CD    1 
ATOM   3556 N  N     . PRO A 1 489 ? -55.887 -23.323 -40.887 1.00 151.66 ? 592  PRO A N     1 
ATOM   3557 C  CA    . PRO A 1 489 ? -55.245 -22.715 -39.718 1.00 151.73 ? 592  PRO A CA    1 
ATOM   3558 C  C     . PRO A 1 489 ? -55.843 -21.355 -39.396 1.00 144.18 ? 592  PRO A C     1 
ATOM   3559 O  O     . PRO A 1 489 ? -56.292 -20.620 -40.278 1.00 153.89 ? 592  PRO A O     1 
ATOM   3560 C  CB    . PRO A 1 489 ? -53.779 -22.592 -40.144 1.00 155.70 ? 592  PRO A CB    1 
ATOM   3561 C  CG    . PRO A 1 489 ? -53.839 -22.483 -41.631 1.00 159.37 ? 592  PRO A CG    1 
ATOM   3562 C  CD    . PRO A 1 489 ? -54.992 -23.351 -42.058 1.00 154.77 ? 592  PRO A CD    1 
ATOM   3563 N  N     . ILE A 1 490 ? -55.843 -21.027 -38.106 1.00 121.62 ? 593  ILE A N     1 
ATOM   3564 C  CA    . ILE A 1 490 ? -56.359 -19.758 -37.616 1.00 97.22  ? 593  ILE A CA    1 
ATOM   3565 C  C     . ILE A 1 490 ? -55.243 -19.033 -36.871 1.00 104.77 ? 593  ILE A C     1 
ATOM   3566 O  O     . ILE A 1 490 ? -54.154 -19.568 -36.659 1.00 109.70 ? 593  ILE A O     1 
ATOM   3567 C  CB    . ILE A 1 490 ? -57.596 -19.936 -36.715 1.00 120.42 ? 593  ILE A CB    1 
ATOM   3568 C  CG1   . ILE A 1 490 ? -57.261 -20.824 -35.515 1.00 146.27 ? 593  ILE A CG1   1 
ATOM   3569 C  CG2   . ILE A 1 490 ? -58.754 -20.520 -37.509 1.00 107.26 ? 593  ILE A CG2   1 
ATOM   3570 C  CD1   . ILE A 1 490 ? -58.430 -21.055 -34.580 1.00 86.31  ? 593  ILE A CD1   1 
ATOM   3571 N  N     . LYS A 1 491 ? -55.532 -17.796 -36.475 1.00 128.89 ? 594  LYS A N     1 
ATOM   3572 C  CA    . LYS A 1 491 ? -54.547 -16.986 -35.780 1.00 120.08 ? 594  LYS A CA    1 
ATOM   3573 C  C     . LYS A 1 491 ? -54.247 -17.573 -34.401 1.00 117.04 ? 594  LYS A C     1 
ATOM   3574 O  O     . LYS A 1 491 ? -55.111 -18.199 -33.781 1.00 124.22 ? 594  LYS A O     1 
ATOM   3575 C  CB    . LYS A 1 491 ? -55.041 -15.549 -35.636 1.00 111.77 ? 594  LYS A CB    1 
ATOM   3576 C  CG    . LYS A 1 491 ? -55.268 -14.837 -36.959 1.00 132.42 ? 594  LYS A CG    1 
ATOM   3577 C  CD    . LYS A 1 491 ? -53.996 -14.803 -37.791 1.00 149.38 ? 594  LYS A CD    1 
ATOM   3578 C  CE    . LYS A 1 491 ? -54.214 -14.073 -39.106 1.00 163.38 ? 594  LYS A CE    1 
ATOM   3579 N  NZ    . LYS A 1 491 ? -55.278 -14.714 -39.929 1.00 140.80 ? 594  LYS A NZ    1 
ATOM   3580 N  N     . PRO A 1 492 ? -53.019 -17.394 -33.904 1.00 115.15 ? 595  PRO A N     1 
ATOM   3581 C  CA    . PRO A 1 492 ? -52.693 -17.925 -32.569 1.00 117.53 ? 595  PRO A CA    1 
ATOM   3582 C  C     . PRO A 1 492 ? -53.538 -17.323 -31.461 1.00 114.62 ? 595  PRO A C     1 
ATOM   3583 O  O     . PRO A 1 492 ? -53.900 -18.028 -30.512 1.00 111.19 ? 595  PRO A O     1 
ATOM   3584 C  CB    . PRO A 1 492 ? -51.207 -17.572 -32.408 1.00 107.26 ? 595  PRO A CB    1 
ATOM   3585 C  CG    . PRO A 1 492 ? -50.701 -17.397 -33.802 1.00 111.31 ? 595  PRO A CG    1 
ATOM   3586 C  CD    . PRO A 1 492 ? -51.843 -16.811 -34.572 1.00 120.92 ? 595  PRO A CD    1 
ATOM   3587 N  N     . GLU A 1 493 ? -53.862 -16.030 -31.554 1.00 135.19 ? 596  GLU A N     1 
ATOM   3588 C  CA    . GLU A 1 493 ? -54.716 -15.410 -30.546 1.00 125.92 ? 596  GLU A CA    1 
ATOM   3589 C  C     . GLU A 1 493 ? -56.127 -15.981 -30.579 1.00 113.64 ? 596  GLU A C     1 
ATOM   3590 O  O     . GLU A 1 493 ? -56.805 -16.016 -29.546 1.00 119.99 ? 596  GLU A O     1 
ATOM   3591 C  CB    . GLU A 1 493 ? -54.753 -13.893 -30.741 1.00 122.66 ? 596  GLU A CB    1 
ATOM   3592 C  CG    . GLU A 1 493 ? -53.464 -13.171 -30.364 1.00 124.23 ? 596  GLU A CG    1 
ATOM   3593 C  CD    . GLU A 1 493 ? -52.373 -13.314 -31.409 1.00 138.94 ? 596  GLU A CD    1 
ATOM   3594 O  OE1   . GLU A 1 493 ? -52.661 -13.827 -32.511 1.00 127.56 ? 596  GLU A OE1   1 
ATOM   3595 O  OE2   . GLU A 1 493 ? -51.225 -12.909 -31.128 1.00 118.97 ? 596  GLU A OE2   1 
ATOM   3596 N  N     . GLN A 1 494 ? -56.585 -16.431 -31.748 1.00 115.45 ? 597  GLN A N     1 
ATOM   3597 C  CA    . GLN A 1 494 ? -57.897 -17.060 -31.844 1.00 130.43 ? 597  GLN A CA    1 
ATOM   3598 C  C     . GLN A 1 494 ? -57.853 -18.527 -31.439 1.00 123.22 ? 597  GLN A C     1 
ATOM   3599 O  O     . GLN A 1 494 ? -58.863 -19.067 -30.974 1.00 117.46 ? 597  GLN A O     1 
ATOM   3600 C  CB    . GLN A 1 494 ? -58.442 -16.922 -33.267 1.00 133.95 ? 597  GLN A CB    1 
ATOM   3601 C  CG    . GLN A 1 494 ? -58.658 -15.484 -33.710 1.00 140.19 ? 597  GLN A CG    1 
ATOM   3602 C  CD    . GLN A 1 494 ? -59.059 -15.377 -35.168 1.00 141.13 ? 597  GLN A CD    1 
ATOM   3603 O  OE1   . GLN A 1 494 ? -58.772 -16.266 -35.969 1.00 131.47 ? 597  GLN A OE1   1 
ATOM   3604 N  NE2   . GLN A 1 494 ? -59.728 -14.285 -35.520 1.00 154.64 ? 597  GLN A NE2   1 
ATOM   3605 N  N     . ALA A 1 495 ? -56.703 -19.183 -31.604 1.00 126.14 ? 598  ALA A N     1 
ATOM   3606 C  CA    . ALA A 1 495 ? -56.578 -20.580 -31.208 1.00 122.32 ? 598  ALA A CA    1 
ATOM   3607 C  C     . ALA A 1 495 ? -56.543 -20.752 -29.696 1.00 128.15 ? 598  ALA A C     1 
ATOM   3608 O  O     . ALA A 1 495 ? -56.888 -21.831 -29.201 1.00 125.94 ? 598  ALA A O     1 
ATOM   3609 C  CB    . ALA A 1 495 ? -55.324 -21.195 -31.832 1.00 122.51 ? 598  ALA A CB    1 
ATOM   3610 N  N     . MET A 1 496 ? -56.136 -19.720 -28.952 1.00 114.38 ? 599  MET A N     1 
ATOM   3611 C  CA    . MET A 1 496 ? -56.128 -19.818 -27.496 1.00 108.47 ? 599  MET A CA    1 
ATOM   3612 C  C     . MET A 1 496 ? -57.537 -19.953 -26.936 1.00 124.26 ? 599  MET A C     1 
ATOM   3613 O  O     . MET A 1 496 ? -57.720 -20.526 -25.856 1.00 111.57 ? 599  MET A O     1 
ATOM   3614 C  CB    . MET A 1 496 ? -55.439 -18.600 -26.884 1.00 105.80 ? 599  MET A CB    1 
ATOM   3615 C  CG    . MET A 1 496 ? -53.991 -18.421 -27.295 1.00 100.14 ? 599  MET A CG    1 
ATOM   3616 S  SD    . MET A 1 496 ? -53.216 -17.054 -26.415 1.00 107.38 ? 599  MET A SD    1 
ATOM   3617 C  CE    . MET A 1 496 ? -54.372 -15.730 -26.760 1.00 123.01 ? 599  MET A CE    1 
ATOM   3618 N  N     . GLU A 1 497 ? -58.539 -19.429 -27.648 1.00 113.22 ? 600  GLU A N     1 
ATOM   3619 C  CA    . GLU A 1 497 ? -59.918 -19.555 -27.191 1.00 106.42 ? 600  GLU A CA    1 
ATOM   3620 C  C     . GLU A 1 497 ? -60.351 -21.013 -27.117 1.00 105.52 ? 600  GLU A C     1 
ATOM   3621 O  O     . GLU A 1 497 ? -61.188 -21.371 -26.281 1.00 117.93 ? 600  GLU A O     1 
ATOM   3622 C  CB    . GLU A 1 497 ? -60.848 -18.767 -28.115 1.00 113.37 ? 600  GLU A CB    1 
ATOM   3623 C  CG    . GLU A 1 497 ? -62.312 -18.795 -27.706 1.00 125.21 ? 600  GLU A CG    1 
ATOM   3624 C  CD    . GLU A 1 497 ? -63.200 -18.029 -28.665 1.00 120.90 ? 600  GLU A CD    1 
ATOM   3625 O  OE1   . GLU A 1 497 ? -62.659 -17.336 -29.552 1.00 138.38 ? 600  GLU A OE1   1 
ATOM   3626 O  OE2   . GLU A 1 497 ? -64.439 -18.121 -28.533 1.00 138.70 ? 600  GLU A OE2   1 
ATOM   3627 N  N     . LEU A 1 498 ? -59.787 -21.868 -27.967 1.00 113.28 ? 601  LEU A N     1 
ATOM   3628 C  CA    . LEU A 1 498 ? -60.108 -23.289 -27.972 1.00 102.18 ? 601  LEU A CA    1 
ATOM   3629 C  C     . LEU A 1 498 ? -59.343 -24.075 -26.913 1.00 106.20 ? 601  LEU A C     1 
ATOM   3630 O  O     . LEU A 1 498 ? -59.397 -25.309 -26.923 1.00 114.46 ? 601  LEU A O     1 
ATOM   3631 C  CB    . LEU A 1 498 ? -59.834 -23.883 -29.355 1.00 104.33 ? 601  LEU A CB    1 
ATOM   3632 C  CG    . LEU A 1 498 ? -60.535 -23.192 -30.526 1.00 102.04 ? 601  LEU A CG    1 
ATOM   3633 C  CD1   . LEU A 1 498 ? -60.233 -23.907 -31.834 1.00 109.05 ? 601  LEU A CD1   1 
ATOM   3634 C  CD2   . LEU A 1 498 ? -62.034 -23.116 -30.282 1.00 113.78 ? 601  LEU A CD2   1 
ATOM   3635 N  N     . LEU A 1 499 ? -58.634 -23.398 -26.008 1.00 102.24 ? 602  LEU A N     1 
ATOM   3636 C  CA    . LEU A 1 499 ? -57.879 -24.063 -24.953 1.00 103.58 ? 602  LEU A CA    1 
ATOM   3637 C  C     . LEU A 1 499 ? -58.386 -23.721 -23.558 1.00 100.73 ? 602  LEU A C     1 
ATOM   3638 O  O     . LEU A 1 499 ? -57.717 -24.052 -22.572 1.00 122.48 ? 602  LEU A O     1 
ATOM   3639 C  CB    . LEU A 1 499 ? -56.389 -23.719 -25.059 1.00 97.40  ? 602  LEU A CB    1 
ATOM   3640 C  CG    . LEU A 1 499 ? -55.606 -24.322 -26.227 1.00 93.84  ? 602  LEU A CG    1 
ATOM   3641 C  CD1   . LEU A 1 499 ? -54.144 -23.911 -26.156 1.00 94.27  ? 602  LEU A CD1   1 
ATOM   3642 C  CD2   . LEU A 1 499 ? -55.737 -25.836 -26.241 1.00 92.17  ? 602  LEU A CD2   1 
ATOM   3643 N  N     . ASP A 1 500 ? -59.539 -23.070 -23.442 1.00 102.76 ? 603  ASP A N     1 
ATOM   3644 C  CA    . ASP A 1 500 ? -60.090 -22.727 -22.139 1.00 114.15 ? 603  ASP A CA    1 
ATOM   3645 C  C     . ASP A 1 500 ? -61.019 -23.854 -21.676 1.00 136.70 ? 603  ASP A C     1 
ATOM   3646 O  O     . ASP A 1 500 ? -60.947 -24.979 -22.177 1.00 117.86 ? 603  ASP A O     1 
ATOM   3647 C  CB    . ASP A 1 500 ? -60.779 -21.358 -22.204 1.00 136.88 ? 603  ASP A CB    1 
ATOM   3648 C  CG    . ASP A 1 500 ? -61.900 -21.306 -23.228 1.00 144.75 ? 603  ASP A CG    1 
ATOM   3649 O  OD1   . ASP A 1 500 ? -62.187 -22.339 -23.867 1.00 138.67 ? 603  ASP A OD1   1 
ATOM   3650 O  OD2   . ASP A 1 500 ? -62.498 -20.221 -23.395 1.00 128.45 ? 603  ASP A OD2   1 
ATOM   3651 N  N     . CYS A 1 501 ? -61.903 -23.565 -20.720 1.00 138.08 ? 604  CYS A N     1 
ATOM   3652 C  CA    . CYS A 1 501 ? -62.772 -24.591 -20.158 1.00 123.47 ? 604  CYS A CA    1 
ATOM   3653 C  C     . CYS A 1 501 ? -63.909 -24.988 -21.091 1.00 134.30 ? 604  CYS A C     1 
ATOM   3654 O  O     . CYS A 1 501 ? -64.494 -26.061 -20.909 1.00 142.69 ? 604  CYS A O     1 
ATOM   3655 C  CB    . CYS A 1 501 ? -63.349 -24.112 -18.823 1.00 127.18 ? 604  CYS A CB    1 
ATOM   3656 S  SG    . CYS A 1 501 ? -64.189 -22.511 -18.903 1.00 150.71 ? 604  CYS A SG    1 
ATOM   3657 N  N     . ASN A 1 502 ? -64.231 -24.159 -22.085 1.00 142.34 ? 605  ASN A N     1 
ATOM   3658 C  CA    . ASN A 1 502 ? -65.365 -24.435 -22.958 1.00 133.68 ? 605  ASN A CA    1 
ATOM   3659 C  C     . ASN A 1 502 ? -65.081 -25.527 -23.981 1.00 131.66 ? 605  ASN A C     1 
ATOM   3660 O  O     . ASN A 1 502 ? -66.028 -26.078 -24.554 1.00 148.39 ? 605  ASN A O     1 
ATOM   3661 C  CB    . ASN A 1 502 ? -65.793 -23.158 -23.685 1.00 141.87 ? 605  ASN A CB    1 
ATOM   3662 C  CG    . ASN A 1 502 ? -66.190 -22.048 -22.731 1.00 146.10 ? 605  ASN A CG    1 
ATOM   3663 O  OD1   . ASN A 1 502 ? -66.716 -22.303 -21.648 1.00 153.18 ? 605  ASN A OD1   1 
ATOM   3664 N  ND2   . ASN A 1 502 ? -65.936 -20.806 -23.129 1.00 145.26 ? 605  ASN A ND2   1 
ATOM   3665 N  N     . TYR A 1 503 ? -63.813 -25.856 -24.224 1.00 110.39 ? 606  TYR A N     1 
ATOM   3666 C  CA    . TYR A 1 503 ? -63.424 -26.817 -25.257 1.00 105.53 ? 606  TYR A CA    1 
ATOM   3667 C  C     . TYR A 1 503 ? -62.514 -27.872 -24.640 1.00 97.89  ? 606  TYR A C     1 
ATOM   3668 O  O     . TYR A 1 503 ? -61.286 -27.819 -24.793 1.00 92.57  ? 606  TYR A O     1 
ATOM   3669 C  CB    . TYR A 1 503 ? -62.738 -26.114 -26.429 1.00 91.46  ? 606  TYR A CB    1 
ATOM   3670 C  CG    . TYR A 1 503 ? -63.513 -24.935 -26.975 1.00 110.38 ? 606  TYR A CG    1 
ATOM   3671 C  CD1   . TYR A 1 503 ? -63.349 -23.664 -26.440 1.00 119.35 ? 606  TYR A CD1   1 
ATOM   3672 C  CD2   . TYR A 1 503 ? -64.408 -25.093 -28.024 1.00 107.96 ? 606  TYR A CD2   1 
ATOM   3673 C  CE1   . TYR A 1 503 ? -64.054 -22.583 -26.932 1.00 109.25 ? 606  TYR A CE1   1 
ATOM   3674 C  CE2   . TYR A 1 503 ? -65.117 -24.016 -28.525 1.00 102.43 ? 606  TYR A CE2   1 
ATOM   3675 C  CZ    . TYR A 1 503 ? -64.936 -22.765 -27.975 1.00 108.57 ? 606  TYR A CZ    1 
ATOM   3676 O  OH    . TYR A 1 503 ? -65.638 -21.689 -28.466 1.00 110.07 ? 606  TYR A OH    1 
ATOM   3677 N  N     . PRO A 1 504 ? -63.084 -28.852 -23.939 1.00 105.25 ? 607  PRO A N     1 
ATOM   3678 C  CA    . PRO A 1 504 ? -62.272 -29.897 -23.302 1.00 99.31  ? 607  PRO A CA    1 
ATOM   3679 C  C     . PRO A 1 504 ? -61.917 -31.073 -24.200 1.00 101.35 ? 607  PRO A C     1 
ATOM   3680 O  O     . PRO A 1 504 ? -61.190 -31.966 -23.749 1.00 124.33 ? 607  PRO A O     1 
ATOM   3681 C  CB    . PRO A 1 504 ? -63.184 -30.355 -22.156 1.00 124.80 ? 607  PRO A CB    1 
ATOM   3682 C  CG    . PRO A 1 504 ? -64.556 -30.208 -22.720 1.00 106.47 ? 607  PRO A CG    1 
ATOM   3683 C  CD    . PRO A 1 504 ? -64.516 -28.992 -23.616 1.00 99.89  ? 607  PRO A CD    1 
ATOM   3684 N  N     . ASP A 1 505 ? -62.399 -31.099 -25.438 1.00 102.61 ? 608  ASP A N     1 
ATOM   3685 C  CA    . ASP A 1 505 ? -62.152 -32.239 -26.307 1.00 103.91 ? 608  ASP A CA    1 
ATOM   3686 C  C     . ASP A 1 505 ? -60.680 -32.283 -26.713 1.00 101.93 ? 608  ASP A C     1 
ATOM   3687 O  O     . ASP A 1 505 ? -60.104 -31.251 -27.069 1.00 112.85 ? 608  ASP A O     1 
ATOM   3688 C  CB    . ASP A 1 505 ? -63.043 -32.163 -27.549 1.00 98.38  ? 608  ASP A CB    1 
ATOM   3689 C  CG    . ASP A 1 505 ? -63.054 -33.457 -28.344 1.00 123.42 ? 608  ASP A CG    1 
ATOM   3690 O  OD1   . ASP A 1 505 ? -62.008 -33.819 -28.921 1.00 130.95 ? 608  ASP A OD1   1 
ATOM   3691 O  OD2   . ASP A 1 505 ? -64.112 -34.120 -28.384 1.00 155.56 ? 608  ASP A OD2   1 
ATOM   3692 N  N     . PRO A 1 506 ? -60.044 -33.457 -26.662 1.00 95.81  ? 609  PRO A N     1 
ATOM   3693 C  CA    . PRO A 1 506 ? -58.623 -33.530 -27.039 1.00 112.85 ? 609  PRO A CA    1 
ATOM   3694 C  C     . PRO A 1 506 ? -58.370 -33.247 -28.509 1.00 111.56 ? 609  PRO A C     1 
ATOM   3695 O  O     . PRO A 1 506 ? -57.326 -32.675 -28.843 1.00 133.67 ? 609  PRO A O     1 
ATOM   3696 C  CB    . PRO A 1 506 ? -58.235 -34.968 -26.664 1.00 99.64  ? 609  PRO A CB    1 
ATOM   3697 C  CG    . PRO A 1 506 ? -59.521 -35.721 -26.682 1.00 98.72  ? 609  PRO A CG    1 
ATOM   3698 C  CD    . PRO A 1 506 ? -60.567 -34.758 -26.209 1.00 100.21 ? 609  PRO A CD    1 
ATOM   3699 N  N     . MET A 1 507 ? -59.288 -33.631 -29.400 1.00 116.39 ? 610  MET A N     1 
ATOM   3700 C  CA    . MET A 1 507 ? -59.108 -33.325 -30.816 1.00 99.05  ? 610  MET A CA    1 
ATOM   3701 C  C     . MET A 1 507 ? -59.228 -31.831 -31.085 1.00 101.35 ? 610  MET A C     1 
ATOM   3702 O  O     . MET A 1 507 ? -58.565 -31.310 -31.988 1.00 120.15 ? 610  MET A O     1 
ATOM   3703 C  CB    . MET A 1 507 ? -60.119 -34.103 -31.658 1.00 105.06 ? 610  MET A CB    1 
ATOM   3704 C  CG    . MET A 1 507 ? -59.919 -35.610 -31.626 1.00 129.48 ? 610  MET A CG    1 
ATOM   3705 S  SD    . MET A 1 507 ? -58.390 -36.126 -32.430 1.00 145.76 ? 610  MET A SD    1 
ATOM   3706 C  CE    . MET A 1 507 ? -58.329 -37.855 -31.964 1.00 158.30 ? 610  MET A CE    1 
ATOM   3707 N  N     . VAL A 1 508 ? -60.062 -31.129 -30.316 1.00 115.42 ? 611  VAL A N     1 
ATOM   3708 C  CA    . VAL A 1 508 ? -60.154 -29.680 -30.455 1.00 113.76 ? 611  VAL A CA    1 
ATOM   3709 C  C     . VAL A 1 508 ? -58.902 -29.012 -29.901 1.00 113.32 ? 611  VAL A C     1 
ATOM   3710 O  O     . VAL A 1 508 ? -58.342 -28.099 -30.520 1.00 120.37 ? 611  VAL A O     1 
ATOM   3711 C  CB    . VAL A 1 508 ? -61.429 -29.159 -29.767 1.00 101.19 ? 611  VAL A CB    1 
ATOM   3712 C  CG1   . VAL A 1 508 ? -61.424 -27.639 -29.716 1.00 100.46 ? 611  VAL A CG1   1 
ATOM   3713 C  CG2   . VAL A 1 508 ? -62.665 -29.668 -30.489 1.00 101.99 ? 611  VAL A CG2   1 
ATOM   3714 N  N     . ARG A 1 509 ? -58.440 -29.459 -28.730 1.00 119.50 ? 612  ARG A N     1 
ATOM   3715 C  CA    . ARG A 1 509 ? -57.247 -28.871 -28.131 1.00 95.92  ? 612  ARG A CA    1 
ATOM   3716 C  C     . ARG A 1 509 ? -55.993 -29.190 -28.933 1.00 104.42 ? 612  ARG A C     1 
ATOM   3717 O  O     . ARG A 1 509 ? -55.074 -28.366 -28.993 1.00 129.28 ? 612  ARG A O     1 
ATOM   3718 C  CB    . ARG A 1 509 ? -57.094 -29.352 -26.690 1.00 106.65 ? 612  ARG A CB    1 
ATOM   3719 C  CG    . ARG A 1 509 ? -58.147 -28.800 -25.752 1.00 94.83  ? 612  ARG A CG    1 
ATOM   3720 C  CD    . ARG A 1 509 ? -57.895 -29.229 -24.321 1.00 95.43  ? 612  ARG A CD    1 
ATOM   3721 N  NE    . ARG A 1 509 ? -58.578 -28.350 -23.382 1.00 100.20 ? 612  ARG A NE    1 
ATOM   3722 C  CZ    . ARG A 1 509 ? -58.048 -27.247 -22.874 1.00 93.83  ? 612  ARG A CZ    1 
ATOM   3723 N  NH1   . ARG A 1 509 ? -56.815 -26.872 -23.172 1.00 93.54  ? 612  ARG A NH1   1 
ATOM   3724 N  NH2   . ARG A 1 509 ? -58.773 -26.500 -22.048 1.00 137.26 ? 612  ARG A NH2   1 
ATOM   3725 N  N     . GLY A 1 510 ? -55.932 -30.373 -29.548 1.00 118.39 ? 613  GLY A N     1 
ATOM   3726 C  CA    . GLY A 1 510 ? -54.796 -30.695 -30.393 1.00 120.57 ? 613  GLY A CA    1 
ATOM   3727 C  C     . GLY A 1 510 ? -54.692 -29.796 -31.608 1.00 113.81 ? 613  GLY A C     1 
ATOM   3728 O  O     . GLY A 1 510 ? -53.592 -29.539 -32.104 1.00 115.64 ? 613  GLY A O     1 
ATOM   3729 N  N     . PHE A 1 511 ? -55.831 -29.305 -32.103 1.00 124.32 ? 614  PHE A N     1 
ATOM   3730 C  CA    . PHE A 1 511 ? -55.810 -28.375 -33.227 1.00 123.24 ? 614  PHE A CA    1 
ATOM   3731 C  C     . PHE A 1 511 ? -55.228 -27.028 -32.818 1.00 108.81 ? 614  PHE A C     1 
ATOM   3732 O  O     . PHE A 1 511 ? -54.456 -26.425 -33.572 1.00 140.87 ? 614  PHE A O     1 
ATOM   3733 C  CB    . PHE A 1 511 ? -57.222 -28.204 -33.789 1.00 106.33 ? 614  PHE A CB    1 
ATOM   3734 C  CG    . PHE A 1 511 ? -57.334 -27.134 -34.840 1.00 90.03  ? 614  PHE A CG    1 
ATOM   3735 C  CD1   . PHE A 1 511 ? -57.017 -27.407 -36.160 1.00 100.85 ? 614  PHE A CD1   1 
ATOM   3736 C  CD2   . PHE A 1 511 ? -57.762 -25.858 -34.509 1.00 86.76  ? 614  PHE A CD2   1 
ATOM   3737 C  CE1   . PHE A 1 511 ? -57.120 -26.426 -37.130 1.00 127.14 ? 614  PHE A CE1   1 
ATOM   3738 C  CE2   . PHE A 1 511 ? -57.865 -24.873 -35.473 1.00 95.73  ? 614  PHE A CE2   1 
ATOM   3739 C  CZ    . PHE A 1 511 ? -57.544 -25.157 -36.785 1.00 109.38 ? 614  PHE A CZ    1 
ATOM   3740 N  N     . ALA A 1 512 ? -55.590 -26.540 -31.630 1.00 95.17  ? 615  ALA A N     1 
ATOM   3741 C  CA    . ALA A 1 512 ? -55.101 -25.240 -31.184 1.00 92.84  ? 615  ALA A CA    1 
ATOM   3742 C  C     . ALA A 1 512 ? -53.598 -25.265 -30.944 1.00 91.10  ? 615  ALA A C     1 
ATOM   3743 O  O     . ALA A 1 512 ? -52.904 -24.279 -31.217 1.00 119.22 ? 615  ALA A O     1 
ATOM   3744 C  CB    . ALA A 1 512 ? -55.842 -24.808 -29.919 1.00 113.85 ? 615  ALA A CB    1 
ATOM   3745 N  N     . VAL A 1 513 ? -53.076 -26.383 -30.434 1.00 98.95  ? 616  VAL A N     1 
ATOM   3746 C  CA    . VAL A 1 513 ? -51.637 -26.494 -30.217 1.00 104.31 ? 616  VAL A CA    1 
ATOM   3747 C  C     . VAL A 1 513 ? -50.894 -26.476 -31.547 1.00 116.64 ? 616  VAL A C     1 
ATOM   3748 O  O     . VAL A 1 513 ? -49.858 -25.815 -31.686 1.00 127.91 ? 616  VAL A O     1 
ATOM   3749 C  CB    . VAL A 1 513 ? -51.316 -27.760 -29.401 1.00 118.09 ? 616  VAL A CB    1 
ATOM   3750 C  CG1   . VAL A 1 513 ? -49.813 -27.920 -29.234 1.00 107.71 ? 616  VAL A CG1   1 
ATOM   3751 C  CG2   . VAL A 1 513 ? -52.002 -27.702 -28.045 1.00 101.71 ? 616  VAL A CG2   1 
ATOM   3752 N  N     . ARG A 1 514 ? -51.416 -27.189 -32.550 1.00 106.45 ? 617  ARG A N     1 
ATOM   3753 C  CA    . ARG A 1 514 ? -50.790 -27.189 -33.868 1.00 101.17 ? 617  ARG A CA    1 
ATOM   3754 C  C     . ARG A 1 514 ? -50.879 -25.830 -34.550 1.00 95.05  ? 617  ARG A C     1 
ATOM   3755 O  O     . ARG A 1 514 ? -50.126 -25.577 -35.497 1.00 114.02 ? 617  ARG A O     1 
ATOM   3756 C  CB    . ARG A 1 514 ? -51.421 -28.263 -34.754 1.00 108.00 ? 617  ARG A CB    1 
ATOM   3757 C  CG    . ARG A 1 514 ? -51.158 -29.685 -34.283 1.00 117.34 ? 617  ARG A CG    1 
ATOM   3758 C  CD    . ARG A 1 514 ? -51.666 -30.708 -35.286 1.00 96.77  ? 617  ARG A CD    1 
ATOM   3759 N  NE    . ARG A 1 514 ? -53.107 -30.614 -35.487 1.00 116.86 ? 617  ARG A NE    1 
ATOM   3760 C  CZ    . ARG A 1 514 ? -54.006 -31.310 -34.804 1.00 143.16 ? 617  ARG A CZ    1 
ATOM   3761 N  NH1   . ARG A 1 514 ? -53.646 -32.163 -33.858 1.00 136.16 ? 617  ARG A NH1   1 
ATOM   3762 N  NH2   . ARG A 1 514 ? -55.297 -31.148 -35.078 1.00 134.18 ? 617  ARG A NH2   1 
ATOM   3763 N  N     . CYS A 1 515 ? -51.779 -24.956 -34.100 1.00 105.07 ? 618  CYS A N     1 
ATOM   3764 C  CA    . CYS A 1 515 ? -51.815 -23.583 -34.585 1.00 114.34 ? 618  CYS A CA    1 
ATOM   3765 C  C     . CYS A 1 515 ? -50.856 -22.671 -33.834 1.00 112.64 ? 618  CYS A C     1 
ATOM   3766 O  O     . CYS A 1 515 ? -50.575 -21.565 -34.309 1.00 113.73 ? 618  CYS A O     1 
ATOM   3767 C  CB    . CYS A 1 515 ? -53.236 -23.018 -34.487 1.00 102.22 ? 618  CYS A CB    1 
ATOM   3768 S  SG    . CYS A 1 515 ? -54.391 -23.702 -35.695 1.00 115.15 ? 618  CYS A SG    1 
ATOM   3769 N  N     . LEU A 1 516 ? -50.354 -23.104 -32.678 1.00 110.36 ? 619  LEU A N     1 
ATOM   3770 C  CA    . LEU A 1 516 ? -49.375 -22.332 -31.923 1.00 118.45 ? 619  LEU A CA    1 
ATOM   3771 C  C     . LEU A 1 516 ? -47.949 -22.653 -32.357 1.00 110.82 ? 619  LEU A C     1 
ATOM   3772 O  O     . LEU A 1 516 ? -47.169 -21.745 -32.656 1.00 132.32 ? 619  LEU A O     1 
ATOM   3773 C  CB    . LEU A 1 516 ? -49.543 -22.588 -30.422 1.00 116.69 ? 619  LEU A CB    1 
ATOM   3774 C  CG    . LEU A 1 516 ? -50.874 -22.168 -29.794 1.00 102.85 ? 619  LEU A CG    1 
ATOM   3775 C  CD1   . LEU A 1 516 ? -50.870 -22.440 -28.298 1.00 102.69 ? 619  LEU A CD1   1 
ATOM   3776 C  CD2   . LEU A 1 516 ? -51.165 -20.702 -30.076 1.00 104.31 ? 619  LEU A CD2   1 
ATOM   3777 N  N     . GLU A 1 517 ? -47.597 -23.938 -32.407 1.00 122.18 ? 620  GLU A N     1 
ATOM   3778 C  CA    . GLU A 1 517 ? -46.255 -24.335 -32.817 1.00 131.49 ? 620  GLU A CA    1 
ATOM   3779 C  C     . GLU A 1 517 ? -45.982 -24.077 -34.293 1.00 135.54 ? 620  GLU A C     1 
ATOM   3780 O  O     . GLU A 1 517 ? -44.864 -24.341 -34.750 1.00 165.31 ? 620  GLU A O     1 
ATOM   3781 C  CB    . GLU A 1 517 ? -46.024 -25.812 -32.491 1.00 142.61 ? 620  GLU A CB    1 
ATOM   3782 C  CG    . GLU A 1 517 ? -47.078 -26.751 -33.051 1.00 125.83 ? 620  GLU A CG    1 
ATOM   3783 C  CD    . GLU A 1 517 ? -46.929 -28.167 -32.528 1.00 130.29 ? 620  GLU A CD    1 
ATOM   3784 O  OE1   . GLU A 1 517 ? -45.929 -28.442 -31.831 1.00 151.71 ? 620  GLU A OE1   1 
ATOM   3785 O  OE2   . GLU A 1 517 ? -47.813 -29.003 -32.809 1.00 135.85 ? 620  GLU A OE2   1 
ATOM   3786 N  N     . LYS A 1 518 ? -46.963 -23.572 -35.044 1.00 113.27 ? 621  LYS A N     1 
ATOM   3787 C  CA    . LYS A 1 518 ? -46.772 -23.218 -36.441 1.00 121.89 ? 621  LYS A CA    1 
ATOM   3788 C  C     . LYS A 1 518 ? -46.971 -21.740 -36.738 1.00 113.79 ? 621  LYS A C     1 
ATOM   3789 O  O     . LYS A 1 518 ? -46.557 -21.288 -37.811 1.00 140.67 ? 621  LYS A O     1 
ATOM   3790 C  CB    . LYS A 1 518 ? -47.724 -24.026 -37.338 1.00 113.25 ? 621  LYS A CB    1 
ATOM   3791 C  CG    . LYS A 1 518 ? -47.434 -25.517 -37.378 1.00 126.70 ? 621  LYS A CG    1 
ATOM   3792 C  CD    . LYS A 1 518 ? -48.443 -26.248 -38.250 1.00 159.01 ? 621  LYS A CD    1 
ATOM   3793 C  CE    . LYS A 1 518 ? -48.463 -25.684 -39.663 1.00 151.66 ? 621  LYS A CE    1 
ATOM   3794 N  NZ    . LYS A 1 518 ? -49.469 -26.370 -40.521 1.00 159.62 ? 621  LYS A NZ    1 
ATOM   3795 N  N     . TYR A 1 519 ? -47.586 -20.977 -35.832 1.00 95.10  ? 622  TYR A N     1 
ATOM   3796 C  CA    . TYR A 1 519 ? -47.862 -19.568 -36.094 1.00 94.18  ? 622  TYR A CA    1 
ATOM   3797 C  C     . TYR A 1 519 ? -47.628 -18.645 -34.908 1.00 97.55  ? 622  TYR A C     1 
ATOM   3798 O  O     . TYR A 1 519 ? -47.662 -17.426 -35.099 1.00 130.90 ? 622  TYR A O     1 
ATOM   3799 C  CB    . TYR A 1 519 ? -49.310 -19.391 -36.578 1.00 98.41  ? 622  TYR A CB    1 
ATOM   3800 C  CG    . TYR A 1 519 ? -49.636 -20.169 -37.833 1.00 112.80 ? 622  TYR A CG    1 
ATOM   3801 C  CD1   . TYR A 1 519 ? -49.402 -19.626 -39.090 1.00 110.22 ? 622  TYR A CD1   1 
ATOM   3802 C  CD2   . TYR A 1 519 ? -50.174 -21.447 -37.761 1.00 118.34 ? 622  TYR A CD2   1 
ATOM   3803 C  CE1   . TYR A 1 519 ? -49.695 -20.335 -40.240 1.00 124.14 ? 622  TYR A CE1   1 
ATOM   3804 C  CE2   . TYR A 1 519 ? -50.470 -22.163 -38.905 1.00 131.79 ? 622  TYR A CE2   1 
ATOM   3805 C  CZ    . TYR A 1 519 ? -50.229 -21.602 -40.142 1.00 123.59 ? 622  TYR A CZ    1 
ATOM   3806 O  OH    . TYR A 1 519 ? -50.523 -22.311 -41.284 1.00 120.16 ? 622  TYR A OH    1 
ATOM   3807 N  N     . LEU A 1 520 ? -47.393 -19.161 -33.704 1.00 96.81  ? 623  LEU A N     1 
ATOM   3808 C  CA    . LEU A 1 520 ? -47.179 -18.324 -32.529 1.00 109.75 ? 623  LEU A CA    1 
ATOM   3809 C  C     . LEU A 1 520 ? -45.690 -18.033 -32.378 1.00 120.03 ? 623  LEU A C     1 
ATOM   3810 O  O     . LEU A 1 520 ? -44.878 -18.960 -32.277 1.00 114.71 ? 623  LEU A O     1 
ATOM   3811 C  CB    . LEU A 1 520 ? -47.725 -19.004 -31.274 1.00 105.45 ? 623  LEU A CB    1 
ATOM   3812 C  CG    . LEU A 1 520 ? -47.573 -18.257 -29.948 1.00 86.85  ? 623  LEU A CG    1 
ATOM   3813 C  CD1   . LEU A 1 520 ? -48.432 -17.004 -29.936 1.00 85.17  ? 623  LEU A CD1   1 
ATOM   3814 C  CD2   . LEU A 1 520 ? -47.926 -19.164 -28.780 1.00 87.36  ? 623  LEU A CD2   1 
ATOM   3815 N  N     . THR A 1 521 ? -45.336 -16.751 -32.361 1.00 122.12 ? 624  THR A N     1 
ATOM   3816 C  CA    . THR A 1 521 ? -43.948 -16.352 -32.198 1.00 126.67 ? 624  THR A CA    1 
ATOM   3817 C  C     . THR A 1 521 ? -43.554 -16.370 -30.724 1.00 124.95 ? 624  THR A C     1 
ATOM   3818 O  O     . THR A 1 521 ? -44.400 -16.364 -29.825 1.00 109.43 ? 624  THR A O     1 
ATOM   3819 C  CB    . THR A 1 521 ? -43.711 -14.958 -32.780 1.00 115.96 ? 624  THR A CB    1 
ATOM   3820 O  OG1   . THR A 1 521 ? -44.506 -13.999 -32.071 1.00 95.91  ? 624  THR A OG1   1 
ATOM   3821 C  CG2   . THR A 1 521 ? -44.081 -14.924 -34.256 1.00 108.21 ? 624  THR A CG2   1 
ATOM   3822 N  N     . ASP A 1 522 ? -42.241 -16.390 -30.483 1.00 129.59 ? 625  ASP A N     1 
ATOM   3823 C  CA    . ASP A 1 522 ? -41.736 -16.384 -29.115 1.00 115.34 ? 625  ASP A CA    1 
ATOM   3824 C  C     . ASP A 1 522 ? -42.012 -15.067 -28.402 1.00 107.64 ? 625  ASP A C     1 
ATOM   3825 O  O     . ASP A 1 522 ? -42.020 -15.036 -27.167 1.00 105.12 ? 625  ASP A O     1 
ATOM   3826 C  CB    . ASP A 1 522 ? -40.236 -16.681 -29.104 1.00 130.60 ? 625  ASP A CB    1 
ATOM   3827 C  CG    . ASP A 1 522 ? -39.920 -18.099 -29.542 1.00 142.76 ? 625  ASP A CG    1 
ATOM   3828 O  OD1   . ASP A 1 522 ? -40.870 -18.860 -29.822 1.00 128.48 ? 625  ASP A OD1   1 
ATOM   3829 O  OD2   . ASP A 1 522 ? -38.724 -18.452 -29.604 1.00 135.47 ? 625  ASP A OD2   1 
ATOM   3830 N  N     . ASP A 1 523 ? -42.234 -13.982 -29.147 1.00 109.21 ? 626  ASP A N     1 
ATOM   3831 C  CA    . ASP A 1 523 ? -42.613 -12.720 -28.519 1.00 110.18 ? 626  ASP A CA    1 
ATOM   3832 C  C     . ASP A 1 523 ? -44.028 -12.795 -27.961 1.00 110.66 ? 626  ASP A C     1 
ATOM   3833 O  O     . ASP A 1 523 ? -44.264 -12.469 -26.792 1.00 106.55 ? 626  ASP A O     1 
ATOM   3834 C  CB    . ASP A 1 523 ? -42.488 -11.574 -29.523 1.00 109.52 ? 626  ASP A CB    1 
ATOM   3835 C  CG    . ASP A 1 523 ? -43.155 -10.300 -29.038 1.00 114.88 ? 626  ASP A CG    1 
ATOM   3836 O  OD1   . ASP A 1 523 ? -42.800 -9.822  -27.941 1.00 137.03 ? 626  ASP A OD1   1 
ATOM   3837 O  OD2   . ASP A 1 523 ? -44.032 -9.775  -29.756 1.00 95.53  ? 626  ASP A OD2   1 
ATOM   3838 N  N     . LYS A 1 524 ? -44.985 -13.226 -28.787 1.00 115.80 ? 627  LYS A N     1 
ATOM   3839 C  CA    . LYS A 1 524 ? -46.359 -13.359 -28.318 1.00 114.35 ? 627  LYS A CA    1 
ATOM   3840 C  C     . LYS A 1 524 ? -46.499 -14.495 -27.312 1.00 115.40 ? 627  LYS A C     1 
ATOM   3841 O  O     . LYS A 1 524 ? -47.381 -14.449 -26.446 1.00 112.19 ? 627  LYS A O     1 
ATOM   3842 C  CB    . LYS A 1 524 ? -47.300 -13.578 -29.503 1.00 105.77 ? 627  LYS A CB    1 
ATOM   3843 C  CG    . LYS A 1 524 ? -47.195 -12.534 -30.613 1.00 105.41 ? 627  LYS A CG    1 
ATOM   3844 C  CD    . LYS A 1 524 ? -48.062 -11.308 -30.343 1.00 105.19 ? 627  LYS A CD    1 
ATOM   3845 C  CE    . LYS A 1 524 ? -47.290 -10.206 -29.632 1.00 108.25 ? 627  LYS A CE    1 
ATOM   3846 N  NZ    . LYS A 1 524 ? -48.124 -8.989  -29.427 1.00 131.18 ? 627  LYS A NZ    1 
ATOM   3847 N  N     . LEU A 1 525 ? -45.645 -15.518 -27.408 1.00 109.28 ? 628  LEU A N     1 
ATOM   3848 C  CA    . LEU A 1 525 ? -45.691 -16.615 -26.447 1.00 111.02 ? 628  LEU A CA    1 
ATOM   3849 C  C     . LEU A 1 525 ? -45.309 -16.136 -25.052 1.00 108.86 ? 628  LEU A C     1 
ATOM   3850 O  O     . LEU A 1 525 ? -46.015 -16.413 -24.075 1.00 115.91 ? 628  LEU A O     1 
ATOM   3851 C  CB    . LEU A 1 525 ? -44.774 -17.752 -26.900 1.00 90.49  ? 628  LEU A CB    1 
ATOM   3852 C  CG    . LEU A 1 525 ? -44.591 -18.902 -25.908 1.00 84.43  ? 628  LEU A CG    1 
ATOM   3853 C  CD1   . LEU A 1 525 ? -45.930 -19.477 -25.486 1.00 106.19 ? 628  LEU A CD1   1 
ATOM   3854 C  CD2   . LEU A 1 525 ? -43.727 -19.982 -26.516 1.00 92.27  ? 628  LEU A CD2   1 
ATOM   3855 N  N     . SER A 1 526 ? -44.191 -15.415 -24.938 1.00 118.06 ? 629  SER A N     1 
ATOM   3856 C  CA    . SER A 1 526 ? -43.837 -14.803 -23.663 1.00 106.82 ? 629  SER A CA    1 
ATOM   3857 C  C     . SER A 1 526 ? -44.855 -13.752 -23.239 1.00 100.45 ? 629  SER A C     1 
ATOM   3858 O  O     . SER A 1 526 ? -44.991 -13.484 -22.041 1.00 107.61 ? 629  SER A O     1 
ATOM   3859 C  CB    . SER A 1 526 ? -42.440 -14.184 -23.745 1.00 103.69 ? 629  SER A CB    1 
ATOM   3860 O  OG    . SER A 1 526 ? -42.003 -13.750 -22.470 1.00 128.51 ? 629  SER A OG    1 
ATOM   3861 N  N     . GLN A 1 527 ? -45.571 -13.157 -24.196 1.00 106.41 ? 630  GLN A N     1 
ATOM   3862 C  CA    . GLN A 1 527 ? -46.635 -12.218 -23.858 1.00 114.59 ? 630  GLN A CA    1 
ATOM   3863 C  C     . GLN A 1 527 ? -47.840 -12.942 -23.268 1.00 118.02 ? 630  GLN A C     1 
ATOM   3864 O  O     . GLN A 1 527 ? -48.410 -12.494 -22.266 1.00 103.24 ? 630  GLN A O     1 
ATOM   3865 C  CB    . GLN A 1 527 ? -47.043 -11.427 -25.102 1.00 117.35 ? 630  GLN A CB    1 
ATOM   3866 C  CG    . GLN A 1 527 ? -48.174 -10.429 -24.881 1.00 112.85 ? 630  GLN A CG    1 
ATOM   3867 C  CD    . GLN A 1 527 ? -47.672 -9.050  -24.505 1.00 124.83 ? 630  GLN A CD    1 
ATOM   3868 O  OE1   . GLN A 1 527 ? -48.176 -8.426  -23.572 1.00 116.79 ? 630  GLN A OE1   1 
ATOM   3869 N  NE2   . GLN A 1 527 ? -46.677 -8.563  -25.238 1.00 132.43 ? 630  GLN A NE2   1 
ATOM   3870 N  N     . TYR A 1 528 ? -48.240 -14.060 -23.874 1.00 109.55 ? 631  TYR A N     1 
ATOM   3871 C  CA    . TYR A 1 528 ? -49.417 -14.812 -23.457 1.00 117.89 ? 631  TYR A CA    1 
ATOM   3872 C  C     . TYR A 1 528 ? -49.067 -16.016 -22.588 1.00 110.10 ? 631  TYR A C     1 
ATOM   3873 O  O     . TYR A 1 528 ? -49.884 -16.933 -22.456 1.00 97.55  ? 631  TYR A O     1 
ATOM   3874 C  CB    . TYR A 1 528 ? -50.211 -15.271 -24.682 1.00 95.90  ? 631  TYR A CB    1 
ATOM   3875 C  CG    . TYR A 1 528 ? -50.572 -14.167 -25.651 1.00 93.50  ? 631  TYR A CG    1 
ATOM   3876 C  CD1   . TYR A 1 528 ? -50.946 -12.908 -25.198 1.00 105.08 ? 631  TYR A CD1   1 
ATOM   3877 C  CD2   . TYR A 1 528 ? -50.535 -14.385 -27.023 1.00 93.00  ? 631  TYR A CD2   1 
ATOM   3878 C  CE1   . TYR A 1 528 ? -51.275 -11.898 -26.086 1.00 105.47 ? 631  TYR A CE1   1 
ATOM   3879 C  CE2   . TYR A 1 528 ? -50.862 -13.383 -27.916 1.00 92.60  ? 631  TYR A CE2   1 
ATOM   3880 C  CZ    . TYR A 1 528 ? -51.231 -12.142 -27.443 1.00 110.83 ? 631  TYR A CZ    1 
ATOM   3881 O  OH    . TYR A 1 528 ? -51.556 -11.143 -28.332 1.00 102.73 ? 631  TYR A OH    1 
ATOM   3882 N  N     . LEU A 1 529 ? -47.873 -16.032 -21.990 1.00 105.05 ? 632  LEU A N     1 
ATOM   3883 C  CA    . LEU A 1 529 ? -47.443 -17.207 -21.237 1.00 96.07  ? 632  LEU A CA    1 
ATOM   3884 C  C     . LEU A 1 529 ? -48.260 -17.400 -19.965 1.00 102.46 ? 632  LEU A C     1 
ATOM   3885 O  O     . LEU A 1 529 ? -48.479 -18.541 -19.541 1.00 110.63 ? 632  LEU A O     1 
ATOM   3886 C  CB    . LEU A 1 529 ? -45.956 -17.102 -20.898 1.00 99.83  ? 632  LEU A CB    1 
ATOM   3887 C  CG    . LEU A 1 529 ? -45.324 -18.332 -20.243 1.00 80.00  ? 632  LEU A CG    1 
ATOM   3888 C  CD1   . LEU A 1 529 ? -45.386 -19.527 -21.182 1.00 104.75 ? 632  LEU A CD1   1 
ATOM   3889 C  CD2   . LEU A 1 529 ? -43.891 -18.048 -19.823 1.00 111.54 ? 632  LEU A CD2   1 
ATOM   3890 N  N     . ILE A 1 530 ? -48.719 -16.310 -19.347 1.00 118.66 ? 633  ILE A N     1 
ATOM   3891 C  CA    . ILE A 1 530 ? -49.471 -16.430 -18.102 1.00 119.29 ? 633  ILE A CA    1 
ATOM   3892 C  C     . ILE A 1 530 ? -50.807 -17.125 -18.344 1.00 121.02 ? 633  ILE A C     1 
ATOM   3893 O  O     . ILE A 1 530 ? -51.239 -17.962 -17.542 1.00 127.76 ? 633  ILE A O     1 
ATOM   3894 C  CB    . ILE A 1 530 ? -49.650 -15.044 -17.451 1.00 119.38 ? 633  ILE A CB    1 
ATOM   3895 C  CG1   . ILE A 1 530 ? -50.631 -15.116 -16.277 1.00 124.35 ? 633  ILE A CG1   1 
ATOM   3896 C  CG2   . ILE A 1 530 ? -50.094 -14.014 -18.480 1.00 128.28 ? 633  ILE A CG2   1 
ATOM   3897 C  CD1   . ILE A 1 530 ? -50.153 -15.977 -15.128 1.00 152.54 ? 633  ILE A CD1   1 
ATOM   3898 N  N     . GLN A 1 531 ? -51.475 -16.809 -19.456 1.00 117.71 ? 634  GLN A N     1 
ATOM   3899 C  CA    . GLN A 1 531 ? -52.739 -17.469 -19.764 1.00 102.22 ? 634  GLN A CA    1 
ATOM   3900 C  C     . GLN A 1 531 ? -52.534 -18.891 -20.271 1.00 101.74 ? 634  GLN A C     1 
ATOM   3901 O  O     . GLN A 1 531 ? -53.398 -19.749 -20.058 1.00 102.98 ? 634  GLN A O     1 
ATOM   3902 C  CB    . GLN A 1 531 ? -53.530 -16.660 -20.793 1.00 112.67 ? 634  GLN A CB    1 
ATOM   3903 C  CG    . GLN A 1 531 ? -54.037 -15.318 -20.288 1.00 107.87 ? 634  GLN A CG    1 
ATOM   3904 C  CD    . GLN A 1 531 ? -53.023 -14.208 -20.464 1.00 96.43  ? 634  GLN A CD    1 
ATOM   3905 O  OE1   . GLN A 1 531 ? -51.990 -14.392 -21.109 1.00 102.97 ? 634  GLN A OE1   1 
ATOM   3906 N  NE2   . GLN A 1 531 ? -53.313 -13.045 -19.893 1.00 115.31 ? 634  GLN A NE2   1 
ATOM   3907 N  N     . LEU A 1 532 ? -51.410 -19.161 -20.940 1.00 116.64 ? 635  LEU A N     1 
ATOM   3908 C  CA    . LEU A 1 532 ? -51.150 -20.513 -21.425 1.00 110.12 ? 635  LEU A CA    1 
ATOM   3909 C  C     . LEU A 1 532 ? -50.771 -21.444 -20.281 1.00 116.00 ? 635  LEU A C     1 
ATOM   3910 O  O     . LEU A 1 532 ? -51.164 -22.616 -20.270 1.00 119.56 ? 635  LEU A O     1 
ATOM   3911 C  CB    . LEU A 1 532 ? -50.055 -20.490 -22.491 1.00 101.32 ? 635  LEU A CB    1 
ATOM   3912 C  CG    . LEU A 1 532 ? -50.534 -20.439 -23.944 1.00 101.59 ? 635  LEU A CG    1 
ATOM   3913 C  CD1   . LEU A 1 532 ? -51.452 -19.252 -24.184 1.00 125.17 ? 635  LEU A CD1   1 
ATOM   3914 C  CD2   . LEU A 1 532 ? -49.351 -20.397 -24.893 1.00 108.56 ? 635  LEU A CD2   1 
ATOM   3915 N  N     . VAL A 1 533 ? -50.001 -20.944 -19.313 1.00 117.03 ? 636  VAL A N     1 
ATOM   3916 C  CA    . VAL A 1 533 ? -49.724 -21.723 -18.112 1.00 113.19 ? 636  VAL A CA    1 
ATOM   3917 C  C     . VAL A 1 533 ? -51.005 -21.953 -17.320 1.00 107.38 ? 636  VAL A C     1 
ATOM   3918 O  O     . VAL A 1 533 ? -51.185 -23.013 -16.706 1.00 104.62 ? 636  VAL A O     1 
ATOM   3919 C  CB    . VAL A 1 533 ? -48.644 -21.015 -17.270 1.00 109.32 ? 636  VAL A CB    1 
ATOM   3920 C  CG1   . VAL A 1 533 ? -48.649 -21.519 -15.837 1.00 90.19  ? 636  VAL A CG1   1 
ATOM   3921 C  CG2   . VAL A 1 533 ? -47.272 -21.211 -17.899 1.00 110.28 ? 636  VAL A CG2   1 
ATOM   3922 N  N     . GLN A 1 534 ? -51.927 -20.989 -17.350 1.00 115.27 ? 637  GLN A N     1 
ATOM   3923 C  CA    . GLN A 1 534 ? -53.133 -21.085 -16.534 1.00 108.57 ? 637  GLN A CA    1 
ATOM   3924 C  C     . GLN A 1 534 ? -54.083 -22.157 -17.058 1.00 113.56 ? 637  GLN A C     1 
ATOM   3925 O  O     . GLN A 1 534 ? -54.755 -22.833 -16.270 1.00 126.78 ? 637  GLN A O     1 
ATOM   3926 C  CB    . GLN A 1 534 ? -53.833 -19.728 -16.480 1.00 112.50 ? 637  GLN A CB    1 
ATOM   3927 C  CG    . GLN A 1 534 ? -54.829 -19.595 -15.346 1.00 129.55 ? 637  GLN A CG    1 
ATOM   3928 C  CD    . GLN A 1 534 ? -54.170 -19.700 -13.987 1.00 126.17 ? 637  GLN A CD    1 
ATOM   3929 O  OE1   . GLN A 1 534 ? -54.714 -20.308 -13.067 1.00 149.27 ? 637  GLN A OE1   1 
ATOM   3930 N  NE2   . GLN A 1 534 ? -52.991 -19.104 -13.852 1.00 121.10 ? 637  GLN A NE2   1 
ATOM   3931 N  N     . VAL A 1 535 ? -54.159 -22.328 -18.383 1.00 116.17 ? 638  VAL A N     1 
ATOM   3932 C  CA    . VAL A 1 535 ? -55.071 -23.317 -18.959 1.00 101.91 ? 638  VAL A CA    1 
ATOM   3933 C  C     . VAL A 1 535 ? -54.522 -24.732 -18.900 1.00 120.53 ? 638  VAL A C     1 
ATOM   3934 O  O     . VAL A 1 535 ? -55.163 -25.654 -19.421 1.00 107.70 ? 638  VAL A O     1 
ATOM   3935 C  CB    . VAL A 1 535 ? -55.427 -22.980 -20.422 1.00 92.70  ? 638  VAL A CB    1 
ATOM   3936 C  CG1   . VAL A 1 535 ? -56.173 -21.658 -20.492 1.00 93.07  ? 638  VAL A CG1   1 
ATOM   3937 C  CG2   . VAL A 1 535 ? -54.178 -22.944 -21.285 1.00 103.47 ? 638  VAL A CG2   1 
ATOM   3938 N  N     . LEU A 1 536 ? -53.353 -24.935 -18.287 1.00 114.48 ? 639  LEU A N     1 
ATOM   3939 C  CA    . LEU A 1 536 ? -52.871 -26.293 -18.055 1.00 112.12 ? 639  LEU A CA    1 
ATOM   3940 C  C     . LEU A 1 536 ? -53.767 -27.039 -17.077 1.00 102.05 ? 639  LEU A C     1 
ATOM   3941 O  O     . LEU A 1 536 ? -53.841 -28.273 -17.123 1.00 116.06 ? 639  LEU A O     1 
ATOM   3942 C  CB    . LEU A 1 536 ? -51.433 -26.263 -17.537 1.00 105.21 ? 639  LEU A CB    1 
ATOM   3943 C  CG    . LEU A 1 536 ? -50.322 -26.584 -18.537 1.00 100.70 ? 639  LEU A CG    1 
ATOM   3944 C  CD1   . LEU A 1 536 ? -50.466 -25.747 -19.791 1.00 134.40 ? 639  LEU A CD1   1 
ATOM   3945 C  CD2   . LEU A 1 536 ? -48.965 -26.357 -17.899 1.00 120.68 ? 639  LEU A CD2   1 
ATOM   3946 N  N     . LYS A 1 537 ? -54.449 -26.312 -16.190 1.00 99.70  ? 640  LYS A N     1 
ATOM   3947 C  CA    . LYS A 1 537 ? -55.352 -26.948 -15.238 1.00 107.81 ? 640  LYS A CA    1 
ATOM   3948 C  C     . LYS A 1 537 ? -56.562 -27.556 -15.934 1.00 115.92 ? 640  LYS A C     1 
ATOM   3949 O  O     . LYS A 1 537 ? -57.129 -28.539 -15.444 1.00 151.41 ? 640  LYS A O     1 
ATOM   3950 C  CB    . LYS A 1 537 ? -55.800 -25.932 -14.188 1.00 100.95 ? 640  LYS A CB    1 
ATOM   3951 C  CG    . LYS A 1 537 ? -54.655 -25.172 -13.542 1.00 110.40 ? 640  LYS A CG    1 
ATOM   3952 C  CD    . LYS A 1 537 ? -55.162 -24.034 -12.672 1.00 128.32 ? 640  LYS A CD    1 
ATOM   3953 C  CE    . LYS A 1 537 ? -54.009 -23.279 -12.032 1.00 144.42 ? 640  LYS A CE    1 
ATOM   3954 N  NZ    . LYS A 1 537 ? -54.482 -22.142 -11.195 1.00 158.62 ? 640  LYS A NZ    1 
ATOM   3955 N  N     . TYR A 1 538 ? -56.970 -26.990 -17.071 1.00 106.35 ? 641  TYR A N     1 
ATOM   3956 C  CA    . TYR A 1 538 ? -58.112 -27.514 -17.808 1.00 117.78 ? 641  TYR A CA    1 
ATOM   3957 C  C     . TYR A 1 538 ? -57.805 -28.823 -18.524 1.00 111.05 ? 641  TYR A C     1 
ATOM   3958 O  O     . TYR A 1 538 ? -58.740 -29.499 -18.966 1.00 131.18 ? 641  TYR A O     1 
ATOM   3959 C  CB    . TYR A 1 538 ? -58.603 -26.474 -18.815 1.00 124.78 ? 641  TYR A CB    1 
ATOM   3960 C  CG    . TYR A 1 538 ? -59.191 -25.234 -18.180 1.00 110.01 ? 641  TYR A CG    1 
ATOM   3961 C  CD1   . TYR A 1 538 ? -59.774 -25.285 -16.921 1.00 115.67 ? 641  TYR A CD1   1 
ATOM   3962 C  CD2   . TYR A 1 538 ? -59.161 -24.013 -18.839 1.00 121.95 ? 641  TYR A CD2   1 
ATOM   3963 C  CE1   . TYR A 1 538 ? -60.313 -24.154 -16.337 1.00 142.05 ? 641  TYR A CE1   1 
ATOM   3964 C  CE2   . TYR A 1 538 ? -59.698 -22.876 -18.264 1.00 137.30 ? 641  TYR A CE2   1 
ATOM   3965 C  CZ    . TYR A 1 538 ? -60.272 -22.953 -17.013 1.00 141.55 ? 641  TYR A CZ    1 
ATOM   3966 O  OH    . TYR A 1 538 ? -60.807 -21.824 -16.436 1.00 160.77 ? 641  TYR A OH    1 
ATOM   3967 N  N     . GLU A 1 539 ? -56.533 -29.192 -18.655 1.00 110.80 ? 642  GLU A N     1 
ATOM   3968 C  CA    . GLU A 1 539 ? -56.187 -30.478 -19.244 1.00 112.38 ? 642  GLU A CA    1 
ATOM   3969 C  C     . GLU A 1 539 ? -56.533 -31.601 -18.275 1.00 124.71 ? 642  GLU A C     1 
ATOM   3970 O  O     . GLU A 1 539 ? -56.116 -31.583 -17.112 1.00 152.43 ? 642  GLU A O     1 
ATOM   3971 C  CB    . GLU A 1 539 ? -54.701 -30.520 -19.600 1.00 111.15 ? 642  GLU A CB    1 
ATOM   3972 C  CG    . GLU A 1 539 ? -54.289 -29.538 -20.688 1.00 122.87 ? 642  GLU A CG    1 
ATOM   3973 C  CD    . GLU A 1 539 ? -54.854 -29.899 -22.051 1.00 130.07 ? 642  GLU A CD    1 
ATOM   3974 O  OE1   . GLU A 1 539 ? -55.178 -31.085 -22.271 1.00 141.10 ? 642  GLU A OE1   1 
ATOM   3975 O  OE2   . GLU A 1 539 ? -54.973 -28.993 -22.903 1.00 108.99 ? 642  GLU A OE2   1 
ATOM   3976 N  N     . GLN A 1 540 ? -57.300 -32.579 -18.754 1.00 121.90 ? 643  GLN A N     1 
ATOM   3977 C  CA    . GLN A 1 540 ? -57.751 -33.674 -17.906 1.00 121.07 ? 643  GLN A CA    1 
ATOM   3978 C  C     . GLN A 1 540 ? -56.670 -34.714 -17.641 1.00 105.04 ? 643  GLN A C     1 
ATOM   3979 O  O     . GLN A 1 540 ? -56.879 -35.596 -16.802 1.00 118.26 ? 643  GLN A O     1 
ATOM   3980 C  CB    . GLN A 1 540 ? -58.974 -34.350 -18.532 1.00 136.16 ? 643  GLN A CB    1 
ATOM   3981 C  CG    . GLN A 1 540 ? -58.800 -34.715 -19.996 1.00 139.12 ? 643  GLN A CG    1 
ATOM   3982 C  CD    . GLN A 1 540 ? -60.024 -35.396 -20.576 1.00 129.24 ? 643  GLN A CD    1 
ATOM   3983 O  OE1   . GLN A 1 540 ? -60.956 -35.744 -19.851 1.00 133.43 ? 643  GLN A OE1   1 
ATOM   3984 N  NE2   . GLN A 1 540 ? -60.028 -35.588 -21.890 1.00 122.65 ? 643  GLN A NE2   1 
ATOM   3985 N  N     . TYR A 1 541 ? -55.529 -34.635 -18.321 1.00 102.35 ? 644  TYR A N     1 
ATOM   3986 C  CA    . TYR A 1 541 ? -54.446 -35.588 -18.134 1.00 122.24 ? 644  TYR A CA    1 
ATOM   3987 C  C     . TYR A 1 541 ? -53.131 -34.843 -17.942 1.00 122.83 ? 644  TYR A C     1 
ATOM   3988 O  O     . TYR A 1 541 ? -53.001 -33.667 -18.289 1.00 135.67 ? 644  TYR A O     1 
ATOM   3989 C  CB    . TYR A 1 541 ? -54.333 -36.555 -19.321 1.00 121.37 ? 644  TYR A CB    1 
ATOM   3990 C  CG    . TYR A 1 541 ? -55.635 -37.233 -19.676 1.00 106.96 ? 644  TYR A CG    1 
ATOM   3991 C  CD1   . TYR A 1 541 ? -56.290 -38.042 -18.759 1.00 113.69 ? 644  TYR A CD1   1 
ATOM   3992 C  CD2   . TYR A 1 541 ? -56.206 -37.071 -20.931 1.00 131.45 ? 644  TYR A CD2   1 
ATOM   3993 C  CE1   . TYR A 1 541 ? -57.481 -38.663 -19.077 1.00 113.36 ? 644  TYR A CE1   1 
ATOM   3994 C  CE2   . TYR A 1 541 ? -57.395 -37.691 -21.261 1.00 127.96 ? 644  TYR A CE2   1 
ATOM   3995 C  CZ    . TYR A 1 541 ? -58.028 -38.486 -20.329 1.00 113.64 ? 644  TYR A CZ    1 
ATOM   3996 O  OH    . TYR A 1 541 ? -59.213 -39.106 -20.651 1.00 129.90 ? 644  TYR A OH    1 
ATOM   3997 N  N     . LEU A 1 542 ? -52.151 -35.551 -17.378 1.00 99.81  ? 645  LEU A N     1 
ATOM   3998 C  CA    . LEU A 1 542 ? -50.832 -34.962 -17.172 1.00 113.00 ? 645  LEU A CA    1 
ATOM   3999 C  C     . LEU A 1 542 ? -50.104 -34.777 -18.498 1.00 110.20 ? 645  LEU A C     1 
ATOM   4000 O  O     . LEU A 1 542 ? -49.758 -33.654 -18.882 1.00 117.06 ? 645  LEU A O     1 
ATOM   4001 C  CB    . LEU A 1 542 ? -50.009 -35.834 -16.222 1.00 106.00 ? 645  LEU A CB    1 
ATOM   4002 C  CG    . LEU A 1 542 ? -50.529 -35.994 -14.792 1.00 102.55 ? 645  LEU A CG    1 
ATOM   4003 C  CD1   . LEU A 1 542 ? -49.629 -36.929 -14.001 1.00 103.64 ? 645  LEU A CD1   1 
ATOM   4004 C  CD2   . LEU A 1 542 ? -50.638 -34.642 -14.104 1.00 88.11  ? 645  LEU A CD2   1 
ATOM   4005 N  N     . ASP A 1 543 ? -49.865 -35.873 -19.213 1.00 109.93 ? 646  ASP A N     1 
ATOM   4006 C  CA    . ASP A 1 543 ? -49.170 -35.821 -20.493 1.00 117.34 ? 646  ASP A CA    1 
ATOM   4007 C  C     . ASP A 1 543 ? -50.167 -35.487 -21.598 1.00 118.05 ? 646  ASP A C     1 
ATOM   4008 O  O     . ASP A 1 543 ? -51.120 -36.238 -21.830 1.00 123.13 ? 646  ASP A O     1 
ATOM   4009 C  CB    . ASP A 1 543 ? -48.475 -37.152 -20.770 1.00 98.81  ? 646  ASP A CB    1 
ATOM   4010 C  CG    . ASP A 1 543 ? -47.549 -37.093 -21.972 1.00 106.04 ? 646  ASP A CG    1 
ATOM   4011 O  OD1   . ASP A 1 543 ? -47.311 -35.983 -22.493 1.00 119.91 ? 646  ASP A OD1   1 
ATOM   4012 O  OD2   . ASP A 1 543 ? -47.059 -38.160 -22.395 1.00 126.09 ? 646  ASP A OD2   1 
ATOM   4013 N  N     . ASN A 1 544 ? -49.949 -34.361 -22.274 1.00 117.79 ? 647  ASN A N     1 
ATOM   4014 C  CA    . ASN A 1 544 ? -50.815 -33.929 -23.361 1.00 96.21  ? 647  ASN A CA    1 
ATOM   4015 C  C     . ASN A 1 544 ? -50.000 -33.081 -24.331 1.00 120.36 ? 647  ASN A C     1 
ATOM   4016 O  O     . ASN A 1 544 ? -48.796 -32.880 -24.152 1.00 135.84 ? 647  ASN A O     1 
ATOM   4017 C  CB    . ASN A 1 544 ? -52.031 -33.165 -22.829 1.00 102.86 ? 647  ASN A CB    1 
ATOM   4018 C  CG    . ASN A 1 544 ? -51.644 -31.997 -21.947 1.00 93.72  ? 647  ASN A CG    1 
ATOM   4019 O  OD1   . ASN A 1 544 ? -51.309 -30.919 -22.436 1.00 101.53 ? 647  ASN A OD1   1 
ATOM   4020 N  ND2   . ASN A 1 544 ? -51.694 -32.204 -20.637 1.00 129.73 ? 647  ASN A ND2   1 
ATOM   4021 N  N     . LEU A 1 545 ? -50.675 -32.576 -25.367 1.00 109.30 ? 648  LEU A N     1 
ATOM   4022 C  CA    . LEU A 1 545 ? -49.984 -31.807 -26.397 1.00 85.11  ? 648  LEU A CA    1 
ATOM   4023 C  C     . LEU A 1 545 ? -49.613 -30.415 -25.902 1.00 105.74 ? 648  LEU A C     1 
ATOM   4024 O  O     . LEU A 1 545 ? -48.545 -29.894 -26.246 1.00 99.24  ? 648  LEU A O     1 
ATOM   4025 C  CB    . LEU A 1 545 ? -50.850 -31.714 -27.654 1.00 88.87  ? 648  LEU A CB    1 
ATOM   4026 C  CG    . LEU A 1 545 ? -50.654 -32.790 -28.727 1.00 84.28  ? 648  LEU A CG    1 
ATOM   4027 C  CD1   . LEU A 1 545 ? -49.225 -32.765 -29.251 1.00 159.14 ? 648  LEU A CD1   1 
ATOM   4028 C  CD2   . LEU A 1 545 ? -51.013 -34.172 -28.204 1.00 124.94 ? 648  LEU A CD2   1 
ATOM   4029 N  N     . LEU A 1 546 ? -50.480 -29.794 -25.099 1.00 97.31  ? 649  LEU A N     1 
ATOM   4030 C  CA    . LEU A 1 546 ? -50.205 -28.442 -24.621 1.00 92.10  ? 649  LEU A CA    1 
ATOM   4031 C  C     . LEU A 1 546 ? -49.007 -28.417 -23.680 1.00 114.40 ? 649  LEU A C     1 
ATOM   4032 O  O     . LEU A 1 546 ? -48.220 -27.463 -23.694 1.00 117.27 ? 649  LEU A O     1 
ATOM   4033 C  CB    . LEU A 1 546 ? -51.444 -27.868 -23.933 1.00 96.58  ? 649  LEU A CB    1 
ATOM   4034 C  CG    . LEU A 1 546 ? -51.318 -26.457 -23.352 1.00 103.51 ? 649  LEU A CG    1 
ATOM   4035 C  CD1   . LEU A 1 546 ? -50.868 -25.471 -24.419 1.00 90.03  ? 649  LEU A CD1   1 
ATOM   4036 C  CD2   . LEU A 1 546 ? -52.634 -26.016 -22.731 1.00 84.86  ? 649  LEU A CD2   1 
ATOM   4037 N  N     . VAL A 1 547 ? -48.849 -29.456 -22.857 1.00 127.26 ? 650  VAL A N     1 
ATOM   4038 C  CA    . VAL A 1 547 ? -47.708 -29.512 -21.950 1.00 104.90 ? 650  VAL A CA    1 
ATOM   4039 C  C     . VAL A 1 547 ? -46.422 -29.778 -22.723 1.00 106.66 ? 650  VAL A C     1 
ATOM   4040 O  O     . VAL A 1 547 ? -45.393 -29.137 -22.479 1.00 104.42 ? 650  VAL A O     1 
ATOM   4041 C  CB    . VAL A 1 547 ? -47.945 -30.571 -20.858 1.00 111.32 ? 650  VAL A CB    1 
ATOM   4042 C  CG1   . VAL A 1 547 ? -46.695 -30.751 -20.010 1.00 105.33 ? 650  VAL A CG1   1 
ATOM   4043 C  CG2   . VAL A 1 547 ? -49.126 -30.173 -19.987 1.00 127.29 ? 650  VAL A CG2   1 
ATOM   4044 N  N     . ARG A 1 548 ? -46.458 -30.721 -23.669 1.00 110.91 ? 651  ARG A N     1 
ATOM   4045 C  CA    . ARG A 1 548 ? -45.274 -31.005 -24.474 1.00 124.46 ? 651  ARG A CA    1 
ATOM   4046 C  C     . ARG A 1 548 ? -44.868 -29.806 -25.320 1.00 123.59 ? 651  ARG A C     1 
ATOM   4047 O  O     . ARG A 1 548 ? -43.686 -29.648 -25.646 1.00 106.67 ? 651  ARG A O     1 
ATOM   4048 C  CB    . ARG A 1 548 ? -45.521 -32.222 -25.367 1.00 99.17  ? 651  ARG A CB    1 
ATOM   4049 C  CG    . ARG A 1 548 ? -45.617 -33.541 -24.619 1.00 98.19  ? 651  ARG A CG    1 
ATOM   4050 C  CD    . ARG A 1 548 ? -45.887 -34.691 -25.577 1.00 125.58 ? 651  ARG A CD    1 
ATOM   4051 N  NE    . ARG A 1 548 ? -45.895 -35.983 -24.902 1.00 113.70 ? 651  ARG A NE    1 
ATOM   4052 C  CZ    . ARG A 1 548 ? -44.867 -36.820 -24.875 1.00 116.89 ? 651  ARG A CZ    1 
ATOM   4053 N  NH1   . ARG A 1 548 ? -43.726 -36.533 -25.479 1.00 121.44 ? 651  ARG A NH1   1 
ATOM   4054 N  NH2   . ARG A 1 548 ? -44.989 -37.977 -24.229 1.00 110.12 ? 651  ARG A NH2   1 
ATOM   4055 N  N     . PHE A 1 549 ? -45.828 -28.953 -25.684 1.00 112.42 ? 652  PHE A N     1 
ATOM   4056 C  CA    . PHE A 1 549 ? -45.509 -27.756 -26.455 1.00 108.88 ? 652  PHE A CA    1 
ATOM   4057 C  C     . PHE A 1 549 ? -44.862 -26.689 -25.580 1.00 109.29 ? 652  PHE A C     1 
ATOM   4058 O  O     . PHE A 1 549 ? -43.806 -26.149 -25.927 1.00 106.18 ? 652  PHE A O     1 
ATOM   4059 C  CB    . PHE A 1 549 ? -46.772 -27.210 -27.123 1.00 102.00 ? 652  PHE A CB    1 
ATOM   4060 C  CG    . PHE A 1 549 ? -46.628 -25.803 -27.628 1.00 110.54 ? 652  PHE A CG    1 
ATOM   4061 C  CD1   . PHE A 1 549 ? -45.919 -25.537 -28.787 1.00 102.23 ? 652  PHE A CD1   1 
ATOM   4062 C  CD2   . PHE A 1 549 ? -47.207 -24.746 -26.944 1.00 120.20 ? 652  PHE A CD2   1 
ATOM   4063 C  CE1   . PHE A 1 549 ? -45.786 -24.243 -29.252 1.00 107.09 ? 652  PHE A CE1   1 
ATOM   4064 C  CE2   . PHE A 1 549 ? -47.078 -23.450 -27.405 1.00 92.42  ? 652  PHE A CE2   1 
ATOM   4065 C  CZ    . PHE A 1 549 ? -46.367 -23.198 -28.560 1.00 101.60 ? 652  PHE A CZ    1 
ATOM   4066 N  N     . LEU A 1 550 ? -45.484 -26.373 -24.442 1.00 103.75 ? 653  LEU A N     1 
ATOM   4067 C  CA    . LEU A 1 550 ? -44.932 -25.360 -23.550 1.00 91.60  ? 653  LEU A CA    1 
ATOM   4068 C  C     . LEU A 1 550 ? -43.648 -25.818 -22.872 1.00 113.06 ? 653  LEU A C     1 
ATOM   4069 O  O     . LEU A 1 550 ? -42.913 -24.979 -22.342 1.00 108.72 ? 653  LEU A O     1 
ATOM   4070 C  CB    . LEU A 1 550 ? -45.964 -24.967 -22.491 1.00 79.95  ? 653  LEU A CB    1 
ATOM   4071 C  CG    . LEU A 1 550 ? -47.195 -24.210 -22.992 1.00 112.31 ? 653  LEU A CG    1 
ATOM   4072 C  CD1   . LEU A 1 550 ? -48.093 -23.819 -21.830 1.00 90.60  ? 653  LEU A CD1   1 
ATOM   4073 C  CD2   . LEU A 1 550 ? -46.780 -22.984 -23.789 1.00 111.46 ? 653  LEU A CD2   1 
ATOM   4074 N  N     . LEU A 1 551 ? -43.362 -27.121 -22.870 1.00 116.15 ? 654  LEU A N     1 
ATOM   4075 C  CA    . LEU A 1 551 ? -42.118 -27.598 -22.277 1.00 107.56 ? 654  LEU A CA    1 
ATOM   4076 C  C     . LEU A 1 551 ? -40.964 -27.510 -23.268 1.00 115.91 ? 654  LEU A C     1 
ATOM   4077 O  O     . LEU A 1 551 ? -39.886 -27.009 -22.932 1.00 114.39 ? 654  LEU A O     1 
ATOM   4078 C  CB    . LEU A 1 551 ? -42.283 -29.034 -21.778 1.00 111.25 ? 654  LEU A CB    1 
ATOM   4079 C  CG    . LEU A 1 551 ? -41.040 -29.634 -21.118 1.00 104.72 ? 654  LEU A CG    1 
ATOM   4080 C  CD1   . LEU A 1 551 ? -40.685 -28.873 -19.849 1.00 101.82 ? 654  LEU A CD1   1 
ATOM   4081 C  CD2   . LEU A 1 551 ? -41.242 -31.110 -20.824 1.00 105.51 ? 654  LEU A CD2   1 
ATOM   4082 N  N     . LYS A 1 552 ? -41.173 -27.995 -24.496 1.00 127.93 ? 655  LYS A N     1 
ATOM   4083 C  CA    . LYS A 1 552 ? -40.114 -27.946 -25.499 1.00 111.89 ? 655  LYS A CA    1 
ATOM   4084 C  C     . LYS A 1 552 ? -39.748 -26.508 -25.844 1.00 115.39 ? 655  LYS A C     1 
ATOM   4085 O  O     . LYS A 1 552 ? -38.574 -26.196 -26.076 1.00 138.63 ? 655  LYS A O     1 
ATOM   4086 C  CB    . LYS A 1 552 ? -40.539 -28.707 -26.754 1.00 109.69 ? 655  LYS A CB    1 
ATOM   4087 C  CG    . LYS A 1 552 ? -39.506 -28.685 -27.872 1.00 104.19 ? 655  LYS A CG    1 
ATOM   4088 C  CD    . LYS A 1 552 ? -39.983 -29.454 -29.093 1.00 153.82 ? 655  LYS A CD    1 
ATOM   4089 C  CE    . LYS A 1 552 ? -40.186 -30.927 -28.777 1.00 154.69 ? 655  LYS A CE    1 
ATOM   4090 N  NZ    . LYS A 1 552 ? -40.619 -31.697 -29.976 1.00 146.97 ? 655  LYS A NZ    1 
ATOM   4091 N  N     . LYS A 1 553 ? -40.738 -25.614 -25.875 1.00 111.57 ? 656  LYS A N     1 
ATOM   4092 C  CA    . LYS A 1 553 ? -40.449 -24.218 -26.178 1.00 125.27 ? 656  LYS A CA    1 
ATOM   4093 C  C     . LYS A 1 553 ? -39.758 -23.523 -25.012 1.00 114.85 ? 656  LYS A C     1 
ATOM   4094 O  O     . LYS A 1 553 ? -38.909 -22.651 -25.227 1.00 129.07 ? 656  LYS A O     1 
ATOM   4095 C  CB    . LYS A 1 553 ? -41.734 -23.483 -26.554 1.00 129.49 ? 656  LYS A CB    1 
ATOM   4096 C  CG    . LYS A 1 553 ? -41.563 -22.486 -27.689 1.00 109.90 ? 656  LYS A CG    1 
ATOM   4097 C  CD    . LYS A 1 553 ? -41.242 -23.186 -28.999 1.00 130.05 ? 656  LYS A CD    1 
ATOM   4098 C  CE    . LYS A 1 553 ? -41.142 -22.191 -30.143 1.00 133.45 ? 656  LYS A CE    1 
ATOM   4099 N  NZ    . LYS A 1 553 ? -40.881 -22.865 -31.445 1.00 176.09 ? 656  LYS A NZ    1 
ATOM   4100 N  N     . ALA A 1 554 ? -40.102 -23.893 -23.775 1.00 127.86 ? 657  ALA A N     1 
ATOM   4101 C  CA    . ALA A 1 554 ? -39.418 -23.331 -22.616 1.00 126.63 ? 657  ALA A CA    1 
ATOM   4102 C  C     . ALA A 1 554 ? -38.024 -23.914 -22.432 1.00 112.23 ? 657  ALA A C     1 
ATOM   4103 O  O     . ALA A 1 554 ? -37.170 -23.264 -21.820 1.00 112.11 ? 657  ALA A O     1 
ATOM   4104 C  CB    . ALA A 1 554 ? -40.244 -23.556 -21.349 1.00 124.49 ? 657  ALA A CB    1 
ATOM   4105 N  N     . LEU A 1 555 ? -37.777 -25.119 -22.940 1.00 114.29 ? 658  LEU A N     1 
ATOM   4106 C  CA    . LEU A 1 555 ? -36.454 -25.724 -22.898 1.00 126.07 ? 658  LEU A CA    1 
ATOM   4107 C  C     . LEU A 1 555 ? -35.583 -25.315 -24.078 1.00 119.34 ? 658  LEU A C     1 
ATOM   4108 O  O     . LEU A 1 555 ? -34.413 -25.704 -24.128 1.00 114.54 ? 658  LEU A O     1 
ATOM   4109 C  CB    . LEU A 1 555 ? -36.568 -27.251 -22.846 1.00 130.79 ? 658  LEU A CB    1 
ATOM   4110 C  CG    . LEU A 1 555 ? -37.103 -27.846 -21.542 1.00 109.66 ? 658  LEU A CG    1 
ATOM   4111 C  CD1   . LEU A 1 555 ? -37.185 -29.362 -21.636 1.00 115.54 ? 658  LEU A CD1   1 
ATOM   4112 C  CD2   . LEU A 1 555 ? -36.236 -27.424 -20.367 1.00 119.56 ? 658  LEU A CD2   1 
ATOM   4113 N  N     . THR A 1 556 ? -36.123 -24.548 -25.026 1.00 124.27 ? 659  THR A N     1 
ATOM   4114 C  CA    . THR A 1 556 ? -35.346 -24.014 -26.135 1.00 130.62 ? 659  THR A CA    1 
ATOM   4115 C  C     . THR A 1 556 ? -35.236 -22.497 -26.113 1.00 110.70 ? 659  THR A C     1 
ATOM   4116 O  O     . THR A 1 556 ? -34.502 -21.934 -26.932 1.00 113.87 ? 659  THR A O     1 
ATOM   4117 C  CB    . THR A 1 556 ? -35.950 -24.457 -27.477 1.00 121.08 ? 659  THR A CB    1 
ATOM   4118 O  OG1   . THR A 1 556 ? -37.348 -24.141 -27.506 1.00 115.95 ? 659  THR A OG1   1 
ATOM   4119 C  CG2   . THR A 1 556 ? -35.766 -25.955 -27.677 1.00 121.28 ? 659  THR A CG2   1 
ATOM   4120 N  N     . ASN A 1 557 ? -35.937 -21.825 -25.200 1.00 91.76  ? 660  ASN A N     1 
ATOM   4121 C  CA    . ASN A 1 557 ? -35.877 -20.370 -25.060 1.00 102.07 ? 660  ASN A CA    1 
ATOM   4122 C  C     . ASN A 1 557 ? -35.872 -20.071 -23.563 1.00 104.97 ? 660  ASN A C     1 
ATOM   4123 O  O     . ASN A 1 557 ? -36.918 -20.136 -22.910 1.00 97.46  ? 660  ASN A O     1 
ATOM   4124 C  CB    . ASN A 1 557 ? -37.048 -19.698 -25.769 1.00 109.88 ? 660  ASN A CB    1 
ATOM   4125 C  CG    . ASN A 1 557 ? -36.937 -18.183 -25.788 1.00 127.57 ? 660  ASN A CG    1 
ATOM   4126 O  OD1   . ASN A 1 557 ? -36.768 -17.545 -24.749 1.00 100.41 ? 660  ASN A OD1   1 
ATOM   4127 N  ND2   . ASN A 1 557 ? -37.033 -17.599 -26.977 1.00 129.11 ? 660  ASN A ND2   1 
ATOM   4128 N  N     . GLN A 1 558 ? -34.693 -19.744 -23.026 1.00 93.43  ? 661  GLN A N     1 
ATOM   4129 C  CA    . GLN A 1 558 ? -34.563 -19.564 -21.584 1.00 109.44 ? 661  GLN A CA    1 
ATOM   4130 C  C     . GLN A 1 558 ? -35.328 -18.342 -21.091 1.00 103.40 ? 661  GLN A C     1 
ATOM   4131 O  O     . GLN A 1 558 ? -35.741 -18.301 -19.927 1.00 122.53 ? 661  GLN A O     1 
ATOM   4132 C  CB    . GLN A 1 558 ? -33.087 -19.465 -21.198 1.00 108.95 ? 661  GLN A CB    1 
ATOM   4133 C  CG    . GLN A 1 558 ? -32.822 -19.561 -19.705 1.00 109.12 ? 661  GLN A CG    1 
ATOM   4134 C  CD    . GLN A 1 558 ? -31.348 -19.709 -19.385 1.00 132.06 ? 661  GLN A CD    1 
ATOM   4135 O  OE1   . GLN A 1 558 ? -30.707 -18.773 -18.909 1.00 156.41 ? 661  GLN A OE1   1 
ATOM   4136 N  NE2   . GLN A 1 558 ? -30.803 -20.892 -19.645 1.00 125.13 ? 661  GLN A NE2   1 
ATOM   4137 N  N     . ARG A 1 559 ? -35.526 -17.340 -21.952 1.00 105.34 ? 662  ARG A N     1 
ATOM   4138 C  CA    . ARG A 1 559 ? -36.368 -16.209 -21.575 1.00 109.63 ? 662  ARG A CA    1 
ATOM   4139 C  C     . ARG A 1 559 ? -37.800 -16.661 -21.323 1.00 118.54 ? 662  ARG A C     1 
ATOM   4140 O  O     . ARG A 1 559 ? -38.475 -16.146 -20.423 1.00 113.99 ? 662  ARG A O     1 
ATOM   4141 C  CB    . ARG A 1 559 ? -36.318 -15.132 -22.660 1.00 119.22 ? 662  ARG A CB    1 
ATOM   4142 C  CG    . ARG A 1 559 ? -37.300 -13.989 -22.465 1.00 117.72 ? 662  ARG A CG    1 
ATOM   4143 C  CD    . ARG A 1 559 ? -37.103 -12.910 -23.518 1.00 112.38 ? 662  ARG A CD    1 
ATOM   4144 N  NE    . ARG A 1 559 ? -36.978 -13.472 -24.858 1.00 135.81 ? 662  ARG A NE    1 
ATOM   4145 C  CZ    . ARG A 1 559 ? -38.002 -13.807 -25.630 1.00 145.54 ? 662  ARG A CZ    1 
ATOM   4146 N  NH1   . ARG A 1 559 ? -39.252 -13.659 -25.224 1.00 132.45 ? 662  ARG A NH1   1 
ATOM   4147 N  NH2   . ARG A 1 559 ? -37.766 -14.305 -26.841 1.00 133.72 ? 662  ARG A NH2   1 
ATOM   4148 N  N     . ILE A 1 560 ? -38.276 -17.632 -22.101 1.00 115.54 ? 663  ILE A N     1 
ATOM   4149 C  CA    . ILE A 1 560 ? -39.598 -18.200 -21.864 1.00 119.77 ? 663  ILE A CA    1 
ATOM   4150 C  C     . ILE A 1 560 ? -39.568 -19.153 -20.676 1.00 126.26 ? 663  ILE A C     1 
ATOM   4151 O  O     . ILE A 1 560 ? -40.506 -19.190 -19.872 1.00 131.93 ? 663  ILE A O     1 
ATOM   4152 C  CB    . ILE A 1 560 ? -40.107 -18.896 -23.140 1.00 105.59 ? 663  ILE A CB    1 
ATOM   4153 C  CG1   . ILE A 1 560 ? -40.164 -17.899 -24.300 1.00 105.48 ? 663  ILE A CG1   1 
ATOM   4154 C  CG2   . ILE A 1 560 ? -41.470 -19.529 -22.901 1.00 97.09  ? 663  ILE A CG2   1 
ATOM   4155 C  CD1   . ILE A 1 560 ? -40.520 -18.526 -25.628 1.00 100.18 ? 663  ILE A CD1   1 
ATOM   4156 N  N     . GLY A 1 561 ? -38.489 -19.927 -20.539 1.00 101.55 ? 664  GLY A N     1 
ATOM   4157 C  CA    . GLY A 1 561 ? -38.411 -20.897 -19.460 1.00 117.25 ? 664  GLY A CA    1 
ATOM   4158 C  C     . GLY A 1 561 ? -38.287 -20.269 -18.087 1.00 103.12 ? 664  GLY A C     1 
ATOM   4159 O  O     . GLY A 1 561 ? -38.669 -20.883 -17.086 1.00 117.92 ? 664  GLY A O     1 
ATOM   4160 N  N     . HIS A 1 562 ? -37.748 -19.050 -18.013 1.00 131.84 ? 665  HIS A N     1 
ATOM   4161 C  CA    . HIS A 1 562 ? -37.627 -18.373 -16.726 1.00 122.28 ? 665  HIS A CA    1 
ATOM   4162 C  C     . HIS A 1 562 ? -38.998 -18.083 -16.130 1.00 111.98 ? 665  HIS A C     1 
ATOM   4163 O  O     . HIS A 1 562 ? -39.292 -18.473 -14.995 1.00 102.58 ? 665  HIS A O     1 
ATOM   4164 C  CB    . HIS A 1 562 ? -36.824 -17.081 -16.885 1.00 110.95 ? 665  HIS A CB    1 
ATOM   4165 C  CG    . HIS A 1 562 ? -36.860 -16.198 -15.677 1.00 114.03 ? 665  HIS A CG    1 
ATOM   4166 N  ND1   . HIS A 1 562 ? -36.284 -16.553 -14.477 1.00 129.87 ? 665  HIS A ND1   1 
ATOM   4167 C  CD2   . HIS A 1 562 ? -37.411 -14.976 -15.482 1.00 125.01 ? 665  HIS A CD2   1 
ATOM   4168 C  CE1   . HIS A 1 562 ? -36.474 -15.587 -13.596 1.00 130.89 ? 665  HIS A CE1   1 
ATOM   4169 N  NE2   . HIS A 1 562 ? -37.155 -14.619 -14.181 1.00 119.30 ? 665  HIS A NE2   1 
ATOM   4170 N  N     . PHE A 1 563 ? -39.856 -17.395 -16.888 1.00 121.77 ? 666  PHE A N     1 
ATOM   4171 C  CA    . PHE A 1 563 ? -41.212 -17.135 -16.423 1.00 111.06 ? 666  PHE A CA    1 
ATOM   4172 C  C     . PHE A 1 563 ? -42.069 -18.392 -16.428 1.00 115.69 ? 666  PHE A C     1 
ATOM   4173 O  O     . PHE A 1 563 ? -43.114 -18.417 -15.769 1.00 108.62 ? 666  PHE A O     1 
ATOM   4174 C  CB    . PHE A 1 563 ? -41.858 -16.047 -17.281 1.00 109.08 ? 666  PHE A CB    1 
ATOM   4175 C  CG    . PHE A 1 563 ? -41.127 -14.737 -17.243 1.00 103.34 ? 666  PHE A CG    1 
ATOM   4176 C  CD1   . PHE A 1 563 ? -41.417 -13.796 -16.269 1.00 119.02 ? 666  PHE A CD1   1 
ATOM   4177 C  CD2   . PHE A 1 563 ? -40.145 -14.448 -18.176 1.00 106.41 ? 666  PHE A CD2   1 
ATOM   4178 C  CE1   . PHE A 1 563 ? -40.744 -12.589 -16.228 1.00 103.35 ? 666  PHE A CE1   1 
ATOM   4179 C  CE2   . PHE A 1 563 ? -39.469 -13.244 -18.140 1.00 114.80 ? 666  PHE A CE2   1 
ATOM   4180 C  CZ    . PHE A 1 563 ? -39.769 -12.313 -17.165 1.00 115.92 ? 666  PHE A CZ    1 
ATOM   4181 N  N     . PHE A 1 564 ? -41.652 -19.431 -17.156 1.00 110.32 ? 667  PHE A N     1 
ATOM   4182 C  CA    . PHE A 1 564 ? -42.359 -20.705 -17.099 1.00 103.76 ? 667  PHE A CA    1 
ATOM   4183 C  C     . PHE A 1 564 ? -42.196 -21.370 -15.739 1.00 100.33 ? 667  PHE A C     1 
ATOM   4184 O  O     . PHE A 1 564 ? -43.079 -22.117 -15.306 1.00 118.71 ? 667  PHE A O     1 
ATOM   4185 C  CB    . PHE A 1 564 ? -41.862 -21.627 -18.213 1.00 115.18 ? 667  PHE A CB    1 
ATOM   4186 C  CG    . PHE A 1 564 ? -42.447 -23.009 -18.166 1.00 105.29 ? 667  PHE A CG    1 
ATOM   4187 C  CD1   . PHE A 1 564 ? -43.776 -23.225 -18.493 1.00 93.80  ? 667  PHE A CD1   1 
ATOM   4188 C  CD2   . PHE A 1 564 ? -41.665 -24.095 -17.809 1.00 128.95 ? 667  PHE A CD2   1 
ATOM   4189 C  CE1   . PHE A 1 564 ? -44.315 -24.497 -18.454 1.00 109.95 ? 667  PHE A CE1   1 
ATOM   4190 C  CE2   . PHE A 1 564 ? -42.198 -25.369 -17.769 1.00 118.80 ? 667  PHE A CE2   1 
ATOM   4191 C  CZ    . PHE A 1 564 ? -43.524 -25.569 -18.092 1.00 111.78 ? 667  PHE A CZ    1 
ATOM   4192 N  N     . PHE A 1 565 ? -41.083 -21.108 -15.053 1.00 118.05 ? 668  PHE A N     1 
ATOM   4193 C  CA    . PHE A 1 565 ? -40.863 -21.686 -13.732 1.00 113.34 ? 668  PHE A CA    1 
ATOM   4194 C  C     . PHE A 1 565 ? -41.595 -20.900 -12.650 1.00 132.87 ? 668  PHE A C     1 
ATOM   4195 O  O     . PHE A 1 565 ? -42.290 -21.485 -11.812 1.00 143.50 ? 668  PHE A O     1 
ATOM   4196 C  CB    . PHE A 1 565 ? -39.364 -21.745 -13.429 1.00 102.98 ? 668  PHE A CB    1 
ATOM   4197 C  CG    . PHE A 1 565 ? -39.046 -22.028 -11.987 1.00 117.17 ? 668  PHE A CG    1 
ATOM   4198 C  CD1   . PHE A 1 565 ? -39.017 -23.328 -11.512 1.00 134.37 ? 668  PHE A CD1   1 
ATOM   4199 C  CD2   . PHE A 1 565 ? -38.767 -20.993 -11.107 1.00 127.35 ? 668  PHE A CD2   1 
ATOM   4200 C  CE1   . PHE A 1 565 ? -38.724 -23.591 -10.188 1.00 129.33 ? 668  PHE A CE1   1 
ATOM   4201 C  CE2   . PHE A 1 565 ? -38.475 -21.250 -9.782  1.00 130.17 ? 668  PHE A CE2   1 
ATOM   4202 C  CZ    . PHE A 1 565 ? -38.453 -22.550 -9.323  1.00 130.39 ? 668  PHE A CZ    1 
ATOM   4203 N  N     . TRP A 1 566 ? -41.445 -19.572 -12.651 1.00 118.68 ? 669  TRP A N     1 
ATOM   4204 C  CA    . TRP A 1 566 ? -42.015 -18.765 -11.577 1.00 128.92 ? 669  TRP A CA    1 
ATOM   4205 C  C     . TRP A 1 566 ? -43.537 -18.741 -11.624 1.00 115.93 ? 669  TRP A C     1 
ATOM   4206 O  O     . TRP A 1 566 ? -44.183 -18.616 -10.577 1.00 115.94 ? 669  TRP A O     1 
ATOM   4207 C  CB    . TRP A 1 566 ? -41.455 -17.345 -11.629 1.00 116.88 ? 669  TRP A CB    1 
ATOM   4208 C  CG    . TRP A 1 566 ? -40.088 -17.231 -11.027 1.00 116.69 ? 669  TRP A CG    1 
ATOM   4209 C  CD1   . TRP A 1 566 ? -38.908 -17.066 -11.692 1.00 115.34 ? 669  TRP A CD1   1 
ATOM   4210 C  CD2   . TRP A 1 566 ? -39.758 -17.290 -9.634  1.00 144.52 ? 669  TRP A CD2   1 
ATOM   4211 N  NE1   . TRP A 1 566 ? -37.865 -17.011 -10.799 1.00 121.73 ? 669  TRP A NE1   1 
ATOM   4212 C  CE2   . TRP A 1 566 ? -38.361 -17.146 -9.529  1.00 147.23 ? 669  TRP A CE2   1 
ATOM   4213 C  CE3   . TRP A 1 566 ? -40.510 -17.448 -8.465  1.00 133.05 ? 669  TRP A CE3   1 
ATOM   4214 C  CZ2   . TRP A 1 566 ? -37.700 -17.155 -8.302  1.00 145.67 ? 669  TRP A CZ2   1 
ATOM   4215 C  CZ3   . TRP A 1 566 ? -39.852 -17.455 -7.249  1.00 129.17 ? 669  TRP A CZ3   1 
ATOM   4216 C  CH2   . TRP A 1 566 ? -38.461 -17.310 -7.176  1.00 148.89 ? 669  TRP A CH2   1 
ATOM   4217 N  N     . HIS A 1 567 ? -44.130 -18.856 -12.813 1.00 111.22 ? 670  HIS A N     1 
ATOM   4218 C  CA    . HIS A 1 567 ? -45.582 -18.958 -12.891 1.00 118.42 ? 670  HIS A CA    1 
ATOM   4219 C  C     . HIS A 1 567 ? -46.087 -20.303 -12.386 1.00 127.55 ? 670  HIS A C     1 
ATOM   4220 O  O     . HIS A 1 567 ? -47.272 -20.421 -12.057 1.00 117.19 ? 670  HIS A O     1 
ATOM   4221 C  CB    . HIS A 1 567 ? -46.058 -18.721 -14.325 1.00 129.05 ? 670  HIS A CB    1 
ATOM   4222 C  CG    . HIS A 1 567 ? -45.997 -17.287 -14.750 1.00 131.04 ? 670  HIS A CG    1 
ATOM   4223 N  ND1   . HIS A 1 567 ? -45.064 -16.815 -15.648 1.00 129.02 ? 670  HIS A ND1   1 
ATOM   4224 C  CD2   . HIS A 1 567 ? -46.750 -16.220 -14.394 1.00 119.11 ? 670  HIS A CD2   1 
ATOM   4225 C  CE1   . HIS A 1 567 ? -45.249 -15.520 -15.831 1.00 136.39 ? 670  HIS A CE1   1 
ATOM   4226 N  NE2   . HIS A 1 567 ? -46.265 -15.134 -15.081 1.00 125.18 ? 670  HIS A NE2   1 
ATOM   4227 N  N     . LEU A 1 568 ? -45.219 -21.312 -12.316 1.00 110.56 ? 671  LEU A N     1 
ATOM   4228 C  CA    . LEU A 1 568 ? -45.593 -22.605 -11.757 1.00 115.93 ? 671  LEU A CA    1 
ATOM   4229 C  C     . LEU A 1 568 ? -45.271 -22.715 -10.274 1.00 130.72 ? 671  LEU A C     1 
ATOM   4230 O  O     . LEU A 1 568 ? -46.017 -23.367 -9.534  1.00 142.35 ? 671  LEU A O     1 
ATOM   4231 C  CB    . LEU A 1 568 ? -44.894 -23.734 -12.520 1.00 114.21 ? 671  LEU A CB    1 
ATOM   4232 C  CG    . LEU A 1 568 ? -45.329 -23.921 -13.976 1.00 125.82 ? 671  LEU A CG    1 
ATOM   4233 C  CD1   . LEU A 1 568 ? -44.633 -25.114 -14.612 1.00 101.45 ? 671  LEU A CD1   1 
ATOM   4234 C  CD2   . LEU A 1 568 ? -46.836 -24.069 -14.067 1.00 111.51 ? 671  LEU A CD2   1 
ATOM   4235 N  N     . LYS A 1 569 ? -44.179 -22.094 -9.820  1.00 116.90 ? 672  LYS A N     1 
ATOM   4236 C  CA    . LYS A 1 569 ? -43.864 -22.117 -8.396  1.00 124.33 ? 672  LYS A CA    1 
ATOM   4237 C  C     . LYS A 1 569 ? -44.813 -21.230 -7.601  1.00 128.16 ? 672  LYS A C     1 
ATOM   4238 O  O     . LYS A 1 569 ? -45.046 -21.482 -6.413  1.00 140.05 ? 672  LYS A O     1 
ATOM   4239 C  CB    . LYS A 1 569 ? -42.415 -21.687 -8.167  1.00 117.72 ? 672  LYS A CB    1 
ATOM   4240 C  CG    . LYS A 1 569 ? -41.939 -21.874 -6.735  1.00 123.13 ? 672  LYS A CG    1 
ATOM   4241 C  CD    . LYS A 1 569 ? -40.534 -21.338 -6.535  1.00 172.06 ? 672  LYS A CD    1 
ATOM   4242 C  CE    . LYS A 1 569 ? -40.085 -21.518 -5.095  1.00 145.20 ? 672  LYS A CE    1 
ATOM   4243 N  NZ    . LYS A 1 569 ? -40.101 -22.950 -4.691  1.00 130.06 ? 672  LYS A NZ    1 
ATOM   4244 N  N     . SER A 1 570 ? -45.373 -20.198 -8.234  1.00 104.86 ? 673  SER A N     1 
ATOM   4245 C  CA    . SER A 1 570 ? -46.330 -19.328 -7.562  1.00 112.20 ? 673  SER A CA    1 
ATOM   4246 C  C     . SER A 1 570 ? -47.661 -20.014 -7.286  1.00 142.89 ? 673  SER A C     1 
ATOM   4247 O  O     . SER A 1 570 ? -48.494 -19.445 -6.573  1.00 157.80 ? 673  SER A O     1 
ATOM   4248 C  CB    . SER A 1 570 ? -46.563 -18.064 -8.393  1.00 120.33 ? 673  SER A CB    1 
ATOM   4249 O  OG    . SER A 1 570 ? -47.043 -18.385 -9.688  1.00 130.54 ? 673  SER A OG    1 
ATOM   4250 N  N     . GLU A 1 571 ? -47.883 -21.209 -7.829  1.00 130.76 ? 674  GLU A N     1 
ATOM   4251 C  CA    . GLU A 1 571 ? -49.104 -21.966 -7.592  1.00 137.02 ? 674  GLU A CA    1 
ATOM   4252 C  C     . GLU A 1 571 ? -48.900 -23.136 -6.639  1.00 147.46 ? 674  GLU A C     1 
ATOM   4253 O  O     . GLU A 1 571 ? -49.836 -23.912 -6.423  1.00 139.55 ? 674  GLU A O     1 
ATOM   4254 C  CB    . GLU A 1 571 ? -49.673 -22.480 -8.920  1.00 122.55 ? 674  GLU A CB    1 
ATOM   4255 C  CG    . GLU A 1 571 ? -50.073 -21.392 -9.907  1.00 119.16 ? 674  GLU A CG    1 
ATOM   4256 C  CD    . GLU A 1 571 ? -51.457 -20.828 -9.638  1.00 134.40 ? 674  GLU A CD    1 
ATOM   4257 O  OE1   . GLU A 1 571 ? -52.021 -21.106 -8.559  1.00 127.04 ? 674  GLU A OE1   1 
ATOM   4258 O  OE2   . GLU A 1 571 ? -51.985 -20.110 -10.514 1.00 120.29 ? 674  GLU A OE2   1 
ATOM   4259 N  N     . MET A 1 572 ? -47.704 -23.281 -6.063  1.00 146.60 ? 675  MET A N     1 
ATOM   4260 C  CA    . MET A 1 572 ? -47.425 -24.419 -5.195  1.00 130.05 ? 675  MET A CA    1 
ATOM   4261 C  C     . MET A 1 572 ? -48.167 -24.342 -3.867  1.00 131.36 ? 675  MET A C     1 
ATOM   4262 O  O     . MET A 1 572 ? -48.325 -25.371 -3.203  1.00 122.86 ? 675  MET A O     1 
ATOM   4263 C  CB    . MET A 1 572 ? -45.921 -24.535 -4.946  1.00 136.36 ? 675  MET A CB    1 
ATOM   4264 C  CG    . MET A 1 572 ? -45.141 -25.024 -6.152  1.00 134.16 ? 675  MET A CG    1 
ATOM   4265 S  SD    . MET A 1 572 ? -45.734 -26.627 -6.729  1.00 134.01 ? 675  MET A SD    1 
ATOM   4266 C  CE    . MET A 1 572 ? -44.691 -26.875 -8.160  1.00 128.51 ? 675  MET A CE    1 
ATOM   4267 N  N     . HIS A 1 573 ? -48.627 -23.156 -3.467  1.00 156.79 ? 676  HIS A N     1 
ATOM   4268 C  CA    . HIS A 1 573 ? -49.388 -23.029 -2.229  1.00 142.02 ? 676  HIS A CA    1 
ATOM   4269 C  C     . HIS A 1 573 ? -50.790 -23.614 -2.336  1.00 140.01 ? 676  HIS A C     1 
ATOM   4270 O  O     . HIS A 1 573 ? -51.509 -23.638 -1.330  1.00 163.15 ? 676  HIS A O     1 
ATOM   4271 C  CB    . HIS A 1 573 ? -49.474 -21.560 -1.814  1.00 161.94 ? 676  HIS A CB    1 
ATOM   4272 C  CG    . HIS A 1 573 ? -50.426 -20.755 -2.642  1.00 154.52 ? 676  HIS A CG    1 
ATOM   4273 N  ND1   . HIS A 1 573 ? -50.152 -20.384 -3.941  1.00 144.48 ? 676  HIS A ND1   1 
ATOM   4274 C  CD2   . HIS A 1 573 ? -51.650 -20.252 -2.356  1.00 155.42 ? 676  HIS A CD2   1 
ATOM   4275 C  CE1   . HIS A 1 573 ? -51.167 -19.687 -4.420  1.00 163.45 ? 676  HIS A CE1   1 
ATOM   4276 N  NE2   . HIS A 1 573 ? -52.088 -19.591 -3.478  1.00 178.48 ? 676  HIS A NE2   1 
ATOM   4277 N  N     . ASN A 1 574 ? -51.193 -24.076 -3.516  1.00 136.48 ? 677  ASN A N     1 
ATOM   4278 C  CA    . ASN A 1 574 ? -52.499 -24.683 -3.737  1.00 139.51 ? 677  ASN A CA    1 
ATOM   4279 C  C     . ASN A 1 574 ? -52.293 -26.127 -4.171  1.00 156.16 ? 677  ASN A C     1 
ATOM   4280 O  O     . ASN A 1 574 ? -51.679 -26.384 -5.212  1.00 153.67 ? 677  ASN A O     1 
ATOM   4281 C  CB    . ASN A 1 574 ? -53.291 -23.903 -4.789  1.00 145.40 ? 677  ASN A CB    1 
ATOM   4282 C  CG    . ASN A 1 574 ? -54.594 -24.579 -5.156  1.00 160.05 ? 677  ASN A CG    1 
ATOM   4283 O  OD1   . ASN A 1 574 ? -54.672 -25.297 -6.152  1.00 172.39 ? 677  ASN A OD1   1 
ATOM   4284 N  ND2   . ASN A 1 574 ? -55.627 -24.353 -4.353  1.00 168.94 ? 677  ASN A ND2   1 
ATOM   4285 N  N     . LYS A 1 575 ? -52.806 -27.066 -3.373  1.00 161.60 ? 678  LYS A N     1 
ATOM   4286 C  CA    . LYS A 1 575 ? -52.568 -28.484 -3.612  1.00 147.51 ? 678  LYS A CA    1 
ATOM   4287 C  C     . LYS A 1 575 ? -53.373 -29.047 -4.777  1.00 146.64 ? 678  LYS A C     1 
ATOM   4288 O  O     . LYS A 1 575 ? -53.089 -30.167 -5.214  1.00 153.83 ? 678  LYS A O     1 
ATOM   4289 C  CB    . LYS A 1 575 ? -52.870 -29.288 -2.346  1.00 139.37 ? 678  LYS A CB    1 
ATOM   4290 C  CG    . LYS A 1 575 ? -51.924 -29.001 -1.191  1.00 139.59 ? 678  LYS A CG    1 
ATOM   4291 C  CD    . LYS A 1 575 ? -52.194 -29.923 -0.014  1.00 167.72 ? 678  LYS A CD    1 
ATOM   4292 C  CE    . LYS A 1 575 ? -51.211 -29.676 1.119   1.00 183.66 ? 678  LYS A CE    1 
ATOM   4293 N  NZ    . LYS A 1 575 ? -51.444 -30.597 2.265   1.00 170.67 ? 678  LYS A NZ    1 
ATOM   4294 N  N     . THR A 1 576 ? -54.360 -28.310 -5.291  1.00 131.14 ? 679  THR A N     1 
ATOM   4295 C  CA    . THR A 1 576 ? -55.139 -28.812 -6.417  1.00 126.56 ? 679  THR A CA    1 
ATOM   4296 C  C     . THR A 1 576 ? -54.346 -28.803 -7.718  1.00 148.78 ? 679  THR A C     1 
ATOM   4297 O  O     . THR A 1 576 ? -54.755 -29.457 -8.683  1.00 138.32 ? 679  THR A O     1 
ATOM   4298 C  CB    . THR A 1 576 ? -56.419 -27.992 -6.591  1.00 121.20 ? 679  THR A CB    1 
ATOM   4299 O  OG1   . THR A 1 576 ? -56.097 -26.712 -7.147  1.00 167.04 ? 679  THR A OG1   1 
ATOM   4300 C  CG2   . THR A 1 576 ? -57.107 -27.792 -5.251  1.00 126.30 ? 679  THR A CG2   1 
ATOM   4301 N  N     . VAL A 1 577 ? -53.228 -28.079 -7.766  1.00 155.90 ? 680  VAL A N     1 
ATOM   4302 C  CA    . VAL A 1 577 ? -52.407 -27.995 -8.969  1.00 138.76 ? 680  VAL A CA    1 
ATOM   4303 C  C     . VAL A 1 577 ? -50.952 -28.265 -8.610  1.00 130.56 ? 680  VAL A C     1 
ATOM   4304 O  O     . VAL A 1 577 ? -50.054 -28.089 -9.441  1.00 123.28 ? 680  VAL A O     1 
ATOM   4305 C  CB    . VAL A 1 577 ? -52.557 -26.624 -9.653  1.00 115.88 ? 680  VAL A CB    1 
ATOM   4306 C  CG1   . VAL A 1 577 ? -53.990 -26.412 -10.114 1.00 143.66 ? 680  VAL A CG1   1 
ATOM   4307 C  CG2   . VAL A 1 577 ? -52.126 -25.511 -8.710  1.00 110.97 ? 680  VAL A CG2   1 
ATOM   4308 N  N     . SER A 1 578 ? -50.710 -28.696 -7.370  1.00 126.91 ? 681  SER A N     1 
ATOM   4309 C  CA    . SER A 1 578 ? -49.339 -28.929 -6.925  1.00 128.10 ? 681  SER A CA    1 
ATOM   4310 C  C     . SER A 1 578 ? -48.741 -30.166 -7.583  1.00 135.64 ? 681  SER A C     1 
ATOM   4311 O  O     . SER A 1 578 ? -47.553 -30.178 -7.927  1.00 137.92 ? 681  SER A O     1 
ATOM   4312 C  CB    . SER A 1 578 ? -49.295 -29.057 -5.403  1.00 135.02 ? 681  SER A CB    1 
ATOM   4313 O  OG    . SER A 1 578 ? -49.618 -27.827 -4.779  1.00 151.16 ? 681  SER A OG    1 
ATOM   4314 N  N     . GLN A 1 579 ? -49.543 -31.218 -7.764  1.00 126.76 ? 682  GLN A N     1 
ATOM   4315 C  CA    . GLN A 1 579 ? -49.017 -32.447 -8.348  1.00 127.02 ? 682  GLN A CA    1 
ATOM   4316 C  C     . GLN A 1 579 ? -48.697 -32.264 -9.827  1.00 125.74 ? 682  GLN A C     1 
ATOM   4317 O  O     . GLN A 1 579 ? -47.672 -32.759 -10.311 1.00 120.42 ? 682  GLN A O     1 
ATOM   4318 C  CB    . GLN A 1 579 ? -50.009 -33.592 -8.149  1.00 142.96 ? 682  GLN A CB    1 
ATOM   4319 C  CG    . GLN A 1 579 ? -49.455 -34.958 -8.524  1.00 153.96 ? 682  GLN A CG    1 
ATOM   4320 C  CD    . GLN A 1 579 ? -50.463 -36.072 -8.322  1.00 167.16 ? 682  GLN A CD    1 
ATOM   4321 O  OE1   . GLN A 1 579 ? -50.094 -37.221 -8.081  1.00 175.57 ? 682  GLN A OE1   1 
ATOM   4322 N  NE2   . GLN A 1 579 ? -51.744 -35.737 -8.424  1.00 164.00 ? 682  GLN A NE2   1 
ATOM   4323 N  N     . ARG A 1 580 ? -49.559 -31.557 -10.560 1.00 118.48 ? 683  ARG A N     1 
ATOM   4324 C  CA    . ARG A 1 580 ? -49.307 -31.327 -11.979 1.00 110.28 ? 683  ARG A CA    1 
ATOM   4325 C  C     . ARG A 1 580 ? -48.107 -30.411 -12.182 1.00 111.96 ? 683  ARG A C     1 
ATOM   4326 O  O     . ARG A 1 580 ? -47.219 -30.705 -12.991 1.00 117.13 ? 683  ARG A O     1 
ATOM   4327 C  CB    . ARG A 1 580 ? -50.550 -30.737 -12.647 1.00 115.98 ? 683  ARG A CB    1 
ATOM   4328 C  CG    . ARG A 1 580 ? -50.298 -30.215 -14.053 1.00 122.39 ? 683  ARG A CG    1 
ATOM   4329 C  CD    . ARG A 1 580 ? -51.525 -29.521 -14.624 1.00 119.36 ? 683  ARG A CD    1 
ATOM   4330 N  NE    . ARG A 1 580 ? -52.610 -30.456 -14.893 1.00 97.88  ? 683  ARG A NE    1 
ATOM   4331 C  CZ    . ARG A 1 580 ? -52.755 -31.124 -16.030 1.00 106.67 ? 683  ARG A CZ    1 
ATOM   4332 N  NH1   . ARG A 1 580 ? -51.895 -30.987 -17.026 1.00 129.40 ? 683  ARG A NH1   1 
ATOM   4333 N  NH2   . ARG A 1 580 ? -53.788 -31.949 -16.170 1.00 105.47 ? 683  ARG A NH2   1 
ATOM   4334 N  N     . PHE A 1 581 ? -48.063 -29.293 -11.454 1.00 115.37 ? 684  PHE A N     1 
ATOM   4335 C  CA    . PHE A 1 581 ? -46.963 -28.349 -11.620 1.00 115.31 ? 684  PHE A CA    1 
ATOM   4336 C  C     . PHE A 1 581 ? -45.673 -28.872 -11.001 1.00 129.45 ? 684  PHE A C     1 
ATOM   4337 O  O     . PHE A 1 581 ? -44.582 -28.531 -11.470 1.00 132.12 ? 684  PHE A O     1 
ATOM   4338 C  CB    . PHE A 1 581 ? -47.333 -26.994 -11.015 1.00 122.50 ? 684  PHE A CB    1 
ATOM   4339 C  CG    . PHE A 1 581 ? -48.416 -26.266 -11.765 1.00 128.28 ? 684  PHE A CG    1 
ATOM   4340 C  CD1   . PHE A 1 581 ? -48.838 -26.707 -13.010 1.00 127.63 ? 684  PHE A CD1   1 
ATOM   4341 C  CD2   . PHE A 1 581 ? -49.005 -25.133 -11.228 1.00 116.82 ? 684  PHE A CD2   1 
ATOM   4342 C  CE1   . PHE A 1 581 ? -49.830 -26.035 -13.699 1.00 124.93 ? 684  PHE A CE1   1 
ATOM   4343 C  CE2   . PHE A 1 581 ? -49.997 -24.457 -11.913 1.00 107.93 ? 684  PHE A CE2   1 
ATOM   4344 C  CZ    . PHE A 1 581 ? -50.410 -24.908 -13.150 1.00 111.83 ? 684  PHE A CZ    1 
ATOM   4345 N  N     . GLY A 1 582 ? -45.774 -29.690 -9.952  1.00 134.22 ? 685  GLY A N     1 
ATOM   4346 C  CA    . GLY A 1 582 ? -44.576 -30.271 -9.366  1.00 101.68 ? 685  GLY A CA    1 
ATOM   4347 C  C     . GLY A 1 582 ? -43.877 -31.225 -10.315 1.00 130.04 ? 685  GLY A C     1 
ATOM   4348 O  O     . GLY A 1 582 ? -42.653 -31.182 -10.470 1.00 127.76 ? 685  GLY A O     1 
ATOM   4349 N  N     . LEU A 1 583 ? -44.648 -32.101 -10.964 1.00 127.47 ? 686  LEU A N     1 
ATOM   4350 C  CA    . LEU A 1 583 ? -44.075 -32.998 -11.961 1.00 136.44 ? 686  LEU A CA    1 
ATOM   4351 C  C     . LEU A 1 583 ? -43.547 -32.232 -13.166 1.00 129.69 ? 686  LEU A C     1 
ATOM   4352 O  O     . LEU A 1 583 ? -42.545 -32.637 -13.766 1.00 112.59 ? 686  LEU A O     1 
ATOM   4353 C  CB    . LEU A 1 583 ? -45.117 -34.024 -12.404 1.00 123.49 ? 686  LEU A CB    1 
ATOM   4354 C  CG    . LEU A 1 583 ? -45.598 -35.019 -11.349 1.00 118.24 ? 686  LEU A CG    1 
ATOM   4355 C  CD1   . LEU A 1 583 ? -46.788 -35.807 -11.868 1.00 113.96 ? 686  LEU A CD1   1 
ATOM   4356 C  CD2   . LEU A 1 583 ? -44.469 -35.950 -10.956 1.00 123.71 ? 686  LEU A CD2   1 
ATOM   4357 N  N     . LEU A 1 584 ? -44.203 -31.130 -13.533 1.00 120.68 ? 687  LEU A N     1 
ATOM   4358 C  CA    . LEU A 1 584 ? -43.752 -30.353 -14.681 1.00 114.86 ? 687  LEU A CA    1 
ATOM   4359 C  C     . LEU A 1 584 ? -42.486 -29.571 -14.355 1.00 120.52 ? 687  LEU A C     1 
ATOM   4360 O  O     . LEU A 1 584 ? -41.581 -29.470 -15.192 1.00 141.28 ? 687  LEU A O     1 
ATOM   4361 C  CB    . LEU A 1 584 ? -44.865 -29.416 -15.146 1.00 107.30 ? 687  LEU A CB    1 
ATOM   4362 C  CG    . LEU A 1 584 ? -44.600 -28.624 -16.426 1.00 109.22 ? 687  LEU A CG    1 
ATOM   4363 C  CD1   . LEU A 1 584 ? -44.120 -29.544 -17.538 1.00 98.71  ? 687  LEU A CD1   1 
ATOM   4364 C  CD2   . LEU A 1 584 ? -45.858 -27.888 -16.847 1.00 93.99  ? 687  LEU A CD2   1 
ATOM   4365 N  N     . LEU A 1 585 ? -42.402 -29.010 -13.146 1.00 117.05 ? 688  LEU A N     1 
ATOM   4366 C  CA    . LEU A 1 585 ? -41.180 -28.321 -12.744 1.00 110.38 ? 688  LEU A CA    1 
ATOM   4367 C  C     . LEU A 1 585 ? -40.021 -29.293 -12.572 1.00 134.43 ? 688  LEU A C     1 
ATOM   4368 O  O     . LEU A 1 585 ? -38.868 -28.930 -12.830 1.00 118.52 ? 688  LEU A O     1 
ATOM   4369 C  CB    . LEU A 1 585 ? -41.412 -27.535 -11.454 1.00 98.56  ? 688  LEU A CB    1 
ATOM   4370 C  CG    . LEU A 1 585 ? -42.173 -26.217 -11.606 1.00 116.00 ? 688  LEU A CG    1 
ATOM   4371 C  CD1   . LEU A 1 585 ? -42.167 -25.436 -10.303 1.00 112.88 ? 688  LEU A CD1   1 
ATOM   4372 C  CD2   . LEU A 1 585 ? -41.574 -25.390 -12.731 1.00 127.38 ? 688  LEU A CD2   1 
ATOM   4373 N  N     . GLU A 1 586 ? -40.303 -30.524 -12.138 1.00 127.53 ? 689  GLU A N     1 
ATOM   4374 C  CA    . GLU A 1 586 ? -39.252 -31.533 -12.049 1.00 108.00 ? 689  GLU A CA    1 
ATOM   4375 C  C     . GLU A 1 586 ? -38.695 -31.866 -13.427 1.00 118.76 ? 689  GLU A C     1 
ATOM   4376 O  O     . GLU A 1 586 ? -37.479 -32.010 -13.596 1.00 132.84 ? 689  GLU A O     1 
ATOM   4377 C  CB    . GLU A 1 586 ? -39.790 -32.792 -11.368 1.00 128.00 ? 689  GLU A CB    1 
ATOM   4378 C  CG    . GLU A 1 586 ? -38.821 -33.964 -11.374 1.00 135.55 ? 689  GLU A CG    1 
ATOM   4379 C  CD    . GLU A 1 586 ? -39.413 -35.214 -10.755 1.00 146.33 ? 689  GLU A CD    1 
ATOM   4380 O  OE1   . GLU A 1 586 ? -40.452 -35.105 -10.070 1.00 131.99 ? 689  GLU A OE1   1 
ATOM   4381 O  OE2   . GLU A 1 586 ? -38.843 -36.307 -10.957 1.00 146.89 ? 689  GLU A OE2   1 
ATOM   4382 N  N     . SER A 1 587 ? -39.572 -31.988 -14.426 1.00 123.09 ? 690  SER A N     1 
ATOM   4383 C  CA    . SER A 1 587 ? -39.111 -32.259 -15.783 1.00 107.62 ? 690  SER A CA    1 
ATOM   4384 C  C     . SER A 1 587 ? -38.348 -31.076 -16.363 1.00 117.56 ? 690  SER A C     1 
ATOM   4385 O  O     . SER A 1 587 ? -37.395 -31.271 -17.126 1.00 128.34 ? 690  SER A O     1 
ATOM   4386 C  CB    . SER A 1 587 ? -40.297 -32.617 -16.678 1.00 112.34 ? 690  SER A CB    1 
ATOM   4387 O  OG    . SER A 1 587 ? -41.279 -31.596 -16.656 1.00 118.02 ? 690  SER A OG    1 
ATOM   4388 N  N     . TYR A 1 588 ? -38.747 -29.851 -16.016 1.00 110.82 ? 691  TYR A N     1 
ATOM   4389 C  CA    . TYR A 1 588 ? -38.039 -28.674 -16.509 1.00 125.79 ? 691  TYR A CA    1 
ATOM   4390 C  C     . TYR A 1 588 ? -36.638 -28.590 -15.916 1.00 137.27 ? 691  TYR A C     1 
ATOM   4391 O  O     . TYR A 1 588 ? -35.651 -28.452 -16.648 1.00 120.31 ? 691  TYR A O     1 
ATOM   4392 C  CB    . TYR A 1 588 ? -38.838 -27.409 -16.191 1.00 121.73 ? 691  TYR A CB    1 
ATOM   4393 C  CG    . TYR A 1 588 ? -38.136 -26.126 -16.580 1.00 111.69 ? 691  TYR A CG    1 
ATOM   4394 C  CD1   . TYR A 1 588 ? -38.158 -25.670 -17.891 1.00 120.35 ? 691  TYR A CD1   1 
ATOM   4395 C  CD2   . TYR A 1 588 ? -37.454 -25.370 -15.635 1.00 107.29 ? 691  TYR A CD2   1 
ATOM   4396 C  CE1   . TYR A 1 588 ? -37.518 -24.499 -18.251 1.00 147.16 ? 691  TYR A CE1   1 
ATOM   4397 C  CE2   . TYR A 1 588 ? -36.811 -24.198 -15.985 1.00 113.46 ? 691  TYR A CE2   1 
ATOM   4398 C  CZ    . TYR A 1 588 ? -36.846 -23.767 -17.295 1.00 146.37 ? 691  TYR A CZ    1 
ATOM   4399 O  OH    . TYR A 1 588 ? -36.207 -22.600 -17.650 1.00 112.54 ? 691  TYR A OH    1 
ATOM   4400 N  N     . CYS A 1 589 ? -36.532 -28.676 -14.587 1.00 132.14 ? 692  CYS A N     1 
ATOM   4401 C  CA    . CYS A 1 589 ? -35.231 -28.597 -13.932 1.00 118.44 ? 692  CYS A CA    1 
ATOM   4402 C  C     . CYS A 1 589 ? -34.317 -29.752 -14.317 1.00 115.68 ? 692  CYS A C     1 
ATOM   4403 O  O     . CYS A 1 589 ? -33.093 -29.617 -14.220 1.00 113.23 ? 692  CYS A O     1 
ATOM   4404 C  CB    . CYS A 1 589 ? -35.410 -28.560 -12.413 1.00 113.12 ? 692  CYS A CB    1 
ATOM   4405 S  SG    . CYS A 1 589 ? -36.396 -27.172 -11.806 1.00 118.33 ? 692  CYS A SG    1 
ATOM   4406 N  N     . ARG A 1 590 ? -34.883 -30.880 -14.752 1.00 113.30 ? 693  ARG A N     1 
ATOM   4407 C  CA    . ARG A 1 590 ? -34.061 -32.013 -15.162 1.00 103.58 ? 693  ARG A CA    1 
ATOM   4408 C  C     . ARG A 1 590 ? -33.255 -31.701 -16.417 1.00 131.98 ? 693  ARG A C     1 
ATOM   4409 O  O     . ARG A 1 590 ? -32.183 -32.282 -16.623 1.00 128.22 ? 693  ARG A O     1 
ATOM   4410 C  CB    . ARG A 1 590 ? -34.943 -33.241 -15.394 1.00 144.22 ? 693  ARG A CB    1 
ATOM   4411 C  CG    . ARG A 1 590 ? -34.179 -34.542 -15.584 1.00 142.95 ? 693  ARG A CG    1 
ATOM   4412 C  CD    . ARG A 1 590 ? -33.656 -35.068 -14.259 1.00 158.34 ? 693  ARG A CD    1 
ATOM   4413 N  NE    . ARG A 1 590 ? -34.742 -35.364 -13.332 1.00 151.91 ? 693  ARG A NE    1 
ATOM   4414 C  CZ    . ARG A 1 590 ? -34.573 -35.828 -12.102 1.00 146.77 ? 693  ARG A CZ    1 
ATOM   4415 N  NH1   . ARG A 1 590 ? -33.367 -36.067 -11.612 1.00 135.21 ? 693  ARG A NH1   1 
ATOM   4416 N  NH2   . ARG A 1 590 ? -35.641 -36.060 -11.343 1.00 145.38 ? 693  ARG A NH2   1 
ATOM   4417 N  N     . ALA A 1 591 ? -33.745 -30.786 -17.262 1.00 131.42 ? 694  ALA A N     1 
ATOM   4418 C  CA    . ALA A 1 591 ? -33.072 -30.504 -18.524 1.00 131.80 ? 694  ALA A CA    1 
ATOM   4419 C  C     . ALA A 1 591 ? -32.973 -29.011 -18.828 1.00 123.43 ? 694  ALA A C     1 
ATOM   4420 O  O     . ALA A 1 591 ? -32.693 -28.643 -19.975 1.00 122.59 ? 694  ALA A O     1 
ATOM   4421 C  CB    . ALA A 1 591 ? -33.783 -31.213 -19.682 1.00 133.25 ? 694  ALA A CB    1 
ATOM   4422 N  N     . CYS A 1 592 ? -33.189 -28.140 -17.840 1.00 138.02 ? 695  CYS A N     1 
ATOM   4423 C  CA    . CYS A 1 592 ? -33.072 -26.707 -18.086 1.00 126.49 ? 695  CYS A CA    1 
ATOM   4424 C  C     . CYS A 1 592 ? -31.626 -26.250 -18.231 1.00 125.74 ? 695  CYS A C     1 
ATOM   4425 O  O     . CYS A 1 592 ? -31.396 -25.090 -18.589 1.00 137.99 ? 695  CYS A O     1 
ATOM   4426 C  CB    . CYS A 1 592 ? -33.752 -25.915 -16.967 1.00 108.73 ? 695  CYS A CB    1 
ATOM   4427 S  SG    . CYS A 1 592 ? -32.966 -26.070 -15.351 1.00 143.14 ? 695  CYS A SG    1 
ATOM   4428 N  N     . GLY A 1 593 ? -30.657 -27.122 -17.962 1.00 131.24 ? 696  GLY A N     1 
ATOM   4429 C  CA    . GLY A 1 593 ? -29.261 -26.789 -18.162 1.00 156.71 ? 696  GLY A CA    1 
ATOM   4430 C  C     . GLY A 1 593 ? -28.615 -26.090 -16.985 1.00 149.20 ? 696  GLY A C     1 
ATOM   4431 O  O     . GLY A 1 593 ? -28.930 -26.381 -15.827 1.00 148.69 ? 696  GLY A O     1 
ATOM   4432 N  N     . MET A 1 594 ? -27.705 -25.157 -17.275 1.00 151.96 ? 697  MET A N     1 
ATOM   4433 C  CA    . MET A 1 594 ? -26.971 -24.469 -16.221 1.00 151.02 ? 697  MET A CA    1 
ATOM   4434 C  C     . MET A 1 594 ? -27.837 -23.473 -15.461 1.00 147.45 ? 697  MET A C     1 
ATOM   4435 O  O     . MET A 1 594 ? -27.473 -23.084 -14.346 1.00 150.76 ? 697  MET A O     1 
ATOM   4436 C  CB    . MET A 1 594 ? -25.759 -23.745 -16.808 1.00 191.40 ? 697  MET A CB    1 
ATOM   4437 C  CG    . MET A 1 594 ? -25.022 -24.526 -17.880 1.00 201.86 ? 697  MET A CG    1 
ATOM   4438 S  SD    . MET A 1 594 ? -26.029 -24.789 -19.353 1.00 227.40 ? 697  MET A SD    1 
ATOM   4439 C  CE    . MET A 1 594 ? -26.459 -23.102 -19.771 1.00 159.33 ? 697  MET A CE    1 
ATOM   4440 N  N     . TYR A 1 595 ? -28.968 -23.054 -16.032 1.00 151.62 ? 698  TYR A N     1 
ATOM   4441 C  CA    . TYR A 1 595 ? -29.806 -22.047 -15.393 1.00 132.43 ? 698  TYR A CA    1 
ATOM   4442 C  C     . TYR A 1 595 ? -30.417 -22.526 -14.082 1.00 130.45 ? 698  TYR A C     1 
ATOM   4443 O  O     . TYR A 1 595 ? -30.900 -21.695 -13.307 1.00 138.34 ? 698  TYR A O     1 
ATOM   4444 C  CB    . TYR A 1 595 ? -30.914 -21.601 -16.351 1.00 124.94 ? 698  TYR A CB    1 
ATOM   4445 C  CG    . TYR A 1 595 ? -31.701 -20.409 -15.854 1.00 143.08 ? 698  TYR A CG    1 
ATOM   4446 C  CD1   . TYR A 1 595 ? -31.129 -19.144 -15.815 1.00 124.35 ? 698  TYR A CD1   1 
ATOM   4447 C  CD2   . TYR A 1 595 ? -33.011 -20.549 -15.418 1.00 138.22 ? 698  TYR A CD2   1 
ATOM   4448 C  CE1   . TYR A 1 595 ? -31.840 -18.052 -15.359 1.00 127.41 ? 698  TYR A CE1   1 
ATOM   4449 C  CE2   . TYR A 1 595 ? -33.732 -19.462 -14.960 1.00 133.88 ? 698  TYR A CE2   1 
ATOM   4450 C  CZ    . TYR A 1 595 ? -33.141 -18.216 -14.933 1.00 131.34 ? 698  TYR A CZ    1 
ATOM   4451 O  OH    . TYR A 1 595 ? -33.855 -17.131 -14.478 1.00 120.30 ? 698  TYR A OH    1 
ATOM   4452 N  N     . LEU A 1 596 ? -30.404 -23.835 -13.814 1.00 119.72 ? 699  LEU A N     1 
ATOM   4453 C  CA    . LEU A 1 596 ? -30.883 -24.329 -12.528 1.00 130.56 ? 699  LEU A CA    1 
ATOM   4454 C  C     . LEU A 1 596 ? -30.082 -23.744 -11.374 1.00 135.75 ? 699  LEU A C     1 
ATOM   4455 O  O     . LEU A 1 596 ? -30.627 -23.528 -10.285 1.00 138.76 ? 699  LEU A O     1 
ATOM   4456 C  CB    . LEU A 1 596 ? -30.822 -25.857 -12.499 1.00 135.06 ? 699  LEU A CB    1 
ATOM   4457 C  CG    . LEU A 1 596 ? -31.351 -26.564 -11.249 1.00 121.52 ? 699  LEU A CG    1 
ATOM   4458 C  CD1   . LEU A 1 596 ? -32.824 -26.253 -11.041 1.00 106.68 ? 699  LEU A CD1   1 
ATOM   4459 C  CD2   . LEU A 1 596 ? -31.126 -28.063 -11.352 1.00 144.76 ? 699  LEU A CD2   1 
ATOM   4460 N  N     . LYS A 1 597 ? -28.792 -23.478 -11.592 1.00 137.23 ? 700  LYS A N     1 
ATOM   4461 C  CA    . LYS A 1 597 ? -27.961 -22.894 -10.545 1.00 138.28 ? 700  LYS A CA    1 
ATOM   4462 C  C     . LYS A 1 597 ? -28.408 -21.475 -10.218 1.00 151.86 ? 700  LYS A C     1 
ATOM   4463 O  O     . LYS A 1 597 ? -28.585 -21.123 -9.045  1.00 151.71 ? 700  LYS A O     1 
ATOM   4464 C  CB    . LYS A 1 597 ? -26.495 -22.915 -10.978 1.00 147.50 ? 700  LYS A CB    1 
ATOM   4465 C  CG    . LYS A 1 597 ? -26.014 -24.280 -11.443 1.00 170.65 ? 700  LYS A CG    1 
ATOM   4466 C  CD    . LYS A 1 597 ? -24.661 -24.189 -12.130 1.00 177.56 ? 700  LYS A CD    1 
ATOM   4467 C  CE    . LYS A 1 597 ? -24.241 -25.538 -12.694 1.00 163.98 ? 700  LYS A CE    1 
ATOM   4468 N  NZ    . LYS A 1 597 ? -22.966 -25.449 -13.457 1.00 182.93 ? 700  LYS A NZ    1 
ATOM   4469 N  N     . HIS A 1 598 ? -28.597 -20.642 -11.245 1.00 149.36 ? 701  HIS A N     1 
ATOM   4470 C  CA    . HIS A 1 598 ? -29.065 -19.280 -11.014 1.00 139.29 ? 701  HIS A CA    1 
ATOM   4471 C  C     . HIS A 1 598 ? -30.505 -19.260 -10.518 1.00 152.39 ? 701  HIS A C     1 
ATOM   4472 O  O     . HIS A 1 598 ? -30.893 -18.347 -9.781  1.00 165.00 ? 701  HIS A O     1 
ATOM   4473 C  CB    . HIS A 1 598 ? -28.943 -18.451 -12.293 1.00 131.74 ? 701  HIS A CB    1 
ATOM   4474 C  CG    . HIS A 1 598 ? -27.632 -18.610 -12.996 1.00 133.84 ? 701  HIS A CG    1 
ATOM   4475 N  ND1   . HIS A 1 598 ? -27.360 -19.669 -13.834 1.00 157.94 ? 701  HIS A ND1   1 
ATOM   4476 C  CD2   . HIS A 1 598 ? -26.517 -17.841 -12.989 1.00 128.14 ? 701  HIS A CD2   1 
ATOM   4477 C  CE1   . HIS A 1 598 ? -26.135 -19.548 -14.312 1.00 138.30 ? 701  HIS A CE1   1 
ATOM   4478 N  NE2   . HIS A 1 598 ? -25.602 -18.446 -13.815 1.00 128.78 ? 701  HIS A NE2   1 
ATOM   4479 N  N     . LEU A 1 599 ? -31.307 -20.252 -10.911 1.00 153.12 ? 702  LEU A N     1 
ATOM   4480 C  CA    . LEU A 1 599 ? -32.711 -20.268 -10.520 1.00 150.35 ? 702  LEU A CA    1 
ATOM   4481 C  C     . LEU A 1 599 ? -32.880 -20.585 -9.040  1.00 134.41 ? 702  LEU A C     1 
ATOM   4482 O  O     . LEU A 1 599 ? -33.829 -20.103 -8.410  1.00 138.31 ? 702  LEU A O     1 
ATOM   4483 C  CB    . LEU A 1 599 ? -33.478 -21.276 -11.377 1.00 143.26 ? 702  LEU A CB    1 
ATOM   4484 C  CG    . LEU A 1 599 ? -35.003 -21.177 -11.378 1.00 127.77 ? 702  LEU A CG    1 
ATOM   4485 C  CD1   . LEU A 1 599 ? -35.447 -19.788 -11.807 1.00 114.88 ? 702  LEU A CD1   1 
ATOM   4486 C  CD2   . LEU A 1 599 ? -35.597 -22.237 -12.291 1.00 116.42 ? 702  LEU A CD2   1 
ATOM   4487 N  N     . ASN A 1 600 ? -31.978 -21.385 -8.469  1.00 146.75 ? 703  ASN A N     1 
ATOM   4488 C  CA    . ASN A 1 600 ? -32.052 -21.680 -7.042  1.00 164.50 ? 703  ASN A CA    1 
ATOM   4489 C  C     . ASN A 1 600 ? -31.580 -20.509 -6.192  1.00 150.50 ? 703  ASN A C     1 
ATOM   4490 O  O     . ASN A 1 600 ? -31.994 -20.384 -5.034  1.00 129.09 ? 703  ASN A O     1 
ATOM   4491 C  CB    . ASN A 1 600 ? -31.233 -22.929 -6.716  1.00 133.59 ? 703  ASN A CB    1 
ATOM   4492 C  CG    . ASN A 1 600 ? -31.845 -24.188 -7.289  1.00 140.44 ? 703  ASN A CG    1 
ATOM   4493 O  OD1   . ASN A 1 600 ? -32.856 -24.681 -6.790  1.00 148.67 ? 703  ASN A OD1   1 
ATOM   4494 N  ND2   . ASN A 1 600 ? -31.232 -24.720 -8.340  1.00 171.26 ? 703  ASN A ND2   1 
ATOM   4495 N  N     . ARG A 1 601 ? -30.717 -19.649 -6.739  1.00 133.31 ? 704  ARG A N     1 
ATOM   4496 C  CA    . ARG A 1 601 ? -30.299 -18.464 -5.999  1.00 144.13 ? 704  ARG A CA    1 
ATOM   4497 C  C     . ARG A 1 601 ? -31.454 -17.486 -5.835  1.00 137.62 ? 704  ARG A C     1 
ATOM   4498 O  O     . ARG A 1 601 ? -31.585 -16.841 -4.788  1.00 133.62 ? 704  ARG A O     1 
ATOM   4499 C  CB    . ARG A 1 601 ? -29.120 -17.789 -6.701  1.00 128.79 ? 704  ARG A CB    1 
ATOM   4500 C  CG    . ARG A 1 601 ? -27.896 -18.674 -6.851  1.00 145.34 ? 704  ARG A CG    1 
ATOM   4501 C  CD    . ARG A 1 601 ? -26.637 -17.838 -6.991  1.00 141.75 ? 704  ARG A CD    1 
ATOM   4502 N  NE    . ARG A 1 601 ? -26.434 -16.982 -5.828  1.00 176.47 ? 704  ARG A NE    1 
ATOM   4503 C  CZ    . ARG A 1 601 ? -25.380 -16.198 -5.646  1.00 178.17 ? 704  ARG A CZ    1 
ATOM   4504 N  NH1   . ARG A 1 601 ? -24.403 -16.137 -6.536  1.00 182.65 ? 704  ARG A NH1   1 
ATOM   4505 N  NH2   . ARG A 1 601 ? -25.304 -15.459 -4.544  1.00 171.87 ? 704  ARG A NH2   1 
ATOM   4506 N  N     . GLN A 1 602 ? -32.305 -17.368 -6.857  1.00 132.84 ? 705  GLN A N     1 
ATOM   4507 C  CA    . GLN A 1 602 ? -33.463 -16.486 -6.760  1.00 125.22 ? 705  GLN A CA    1 
ATOM   4508 C  C     . GLN A 1 602 ? -34.466 -17.005 -5.738  1.00 151.28 ? 705  GLN A C     1 
ATOM   4509 O  O     . GLN A 1 602 ? -35.084 -16.218 -5.012  1.00 138.90 ? 705  GLN A O     1 
ATOM   4510 C  CB    . GLN A 1 602 ? -34.123 -16.340 -8.130  1.00 127.41 ? 705  GLN A CB    1 
ATOM   4511 C  CG    . GLN A 1 602 ? -33.153 -16.027 -9.255  1.00 132.56 ? 705  GLN A CG    1 
ATOM   4512 C  CD    . GLN A 1 602 ? -33.810 -16.088 -10.619 1.00 125.04 ? 705  GLN A CD    1 
ATOM   4513 O  OE1   . GLN A 1 602 ? -35.036 -16.096 -10.730 1.00 122.81 ? 705  GLN A OE1   1 
ATOM   4514 N  NE2   . GLN A 1 602 ? -32.995 -16.138 -11.666 1.00 139.90 ? 705  GLN A NE2   1 
ATOM   4515 N  N     . VAL A 1 603 ? -34.642 -18.326 -5.668  1.00 133.57 ? 706  VAL A N     1 
ATOM   4516 C  CA    . VAL A 1 603 ? -35.577 -18.906 -4.709  1.00 123.39 ? 706  VAL A CA    1 
ATOM   4517 C  C     . VAL A 1 603 ? -35.094 -18.668 -3.284  1.00 145.79 ? 706  VAL A C     1 
ATOM   4518 O  O     . VAL A 1 603 ? -35.869 -18.271 -2.406  1.00 135.43 ? 706  VAL A O     1 
ATOM   4519 C  CB    . VAL A 1 603 ? -35.778 -20.405 -4.995  1.00 144.56 ? 706  VAL A CB    1 
ATOM   4520 C  CG1   . VAL A 1 603 ? -36.660 -21.037 -3.930  1.00 121.94 ? 706  VAL A CG1   1 
ATOM   4521 C  CG2   . VAL A 1 603 ? -36.379 -20.604 -6.378  1.00 140.89 ? 706  VAL A CG2   1 
ATOM   4522 N  N     . GLU A 1 604 ? -33.804 -18.907 -3.033  1.00 147.21 ? 707  GLU A N     1 
ATOM   4523 C  CA    . GLU A 1 604 ? -33.248 -18.636 -1.711  1.00 142.69 ? 707  GLU A CA    1 
ATOM   4524 C  C     . GLU A 1 604 ? -33.275 -17.145 -1.399  1.00 154.63 ? 707  GLU A C     1 
ATOM   4525 O  O     . GLU A 1 604 ? -33.496 -16.749 -0.249  1.00 154.95 ? 707  GLU A O     1 
ATOM   4526 C  CB    . GLU A 1 604 ? -31.823 -19.184 -1.620  1.00 164.50 ? 707  GLU A CB    1 
ATOM   4527 C  CG    . GLU A 1 604 ? -31.103 -18.887 -0.307  1.00 154.88 ? 707  GLU A CG    1 
ATOM   4528 C  CD    . GLU A 1 604 ? -31.715 -19.603 0.886   1.00 179.19 ? 707  GLU A CD    1 
ATOM   4529 O  OE1   . GLU A 1 604 ? -32.802 -19.192 1.345   1.00 186.64 ? 707  GLU A OE1   1 
ATOM   4530 O  OE2   . GLU A 1 604 ? -31.106 -20.583 1.365   1.00 181.15 ? 707  GLU A OE2   1 
ATOM   4531 N  N     . ALA A 1 605 ? -33.058 -16.304 -2.413  1.00 136.57 ? 708  ALA A N     1 
ATOM   4532 C  CA    . ALA A 1 605 ? -33.126 -14.862 -2.205  1.00 111.89 ? 708  ALA A CA    1 
ATOM   4533 C  C     . ALA A 1 605 ? -34.550 -14.413 -1.906  1.00 135.73 ? 708  ALA A C     1 
ATOM   4534 O  O     . ALA A 1 605 ? -34.773 -13.596 -1.005  1.00 118.82 ? 708  ALA A O     1 
ATOM   4535 C  CB    . ALA A 1 605 ? -32.579 -14.129 -3.429  1.00 139.92 ? 708  ALA A CB    1 
ATOM   4536 N  N     . MET A 1 606 ? -35.526 -14.936 -2.651  1.00 146.39 ? 709  MET A N     1 
ATOM   4537 C  CA    . MET A 1 606 ? -36.915 -14.545 -2.433  1.00 155.95 ? 709  MET A CA    1 
ATOM   4538 C  C     . MET A 1 606 ? -37.448 -15.097 -1.117  1.00 147.32 ? 709  MET A C     1 
ATOM   4539 O  O     . MET A 1 606 ? -38.239 -14.435 -0.436  1.00 145.51 ? 709  MET A O     1 
ATOM   4540 C  CB    . MET A 1 606 ? -37.781 -15.009 -3.604  1.00 142.30 ? 709  MET A CB    1 
ATOM   4541 C  CG    . MET A 1 606 ? -37.568 -14.213 -4.880  1.00 135.07 ? 709  MET A CG    1 
ATOM   4542 S  SD    . MET A 1 606 ? -38.079 -12.496 -4.692  1.00 144.88 ? 709  MET A SD    1 
ATOM   4543 C  CE    . MET A 1 606 ? -39.820 -12.717 -4.332  1.00 182.38 ? 709  MET A CE    1 
ATOM   4544 N  N     . GLU A 1 607 ? -37.029 -16.309 -0.743  1.00 172.23 ? 710  GLU A N     1 
ATOM   4545 C  CA    . GLU A 1 607 ? -37.474 -16.879 0.524   1.00 171.55 ? 710  GLU A CA    1 
ATOM   4546 C  C     . GLU A 1 607 ? -36.917 -16.101 1.710   1.00 175.22 ? 710  GLU A C     1 
ATOM   4547 O  O     . GLU A 1 607 ? -37.576 -16.006 2.751   1.00 174.93 ? 710  GLU A O     1 
ATOM   4548 C  CB    . GLU A 1 607 ? -37.072 -18.353 0.607   1.00 172.02 ? 710  GLU A CB    1 
ATOM   4549 C  CG    . GLU A 1 607 ? -38.008 -19.219 1.443   1.00 184.15 ? 710  GLU A CG    1 
ATOM   4550 C  CD    . GLU A 1 607 ? -37.799 -19.050 2.936   1.00 196.68 ? 710  GLU A CD    1 
ATOM   4551 O  OE1   . GLU A 1 607 ? -36.676 -18.691 3.346   1.00 207.77 ? 710  GLU A OE1   1 
ATOM   4552 O  OE2   . GLU A 1 607 ? -38.761 -19.277 3.700   1.00 186.41 ? 710  GLU A OE2   1 
ATOM   4553 N  N     . LYS A 1 608 ? -35.717 -15.534 1.569   1.00 163.72 ? 711  LYS A N     1 
ATOM   4554 C  CA    . LYS A 1 608 ? -35.153 -14.687 2.613   1.00 152.51 ? 711  LYS A CA    1 
ATOM   4555 C  C     . LYS A 1 608 ? -35.880 -13.355 2.747   1.00 163.74 ? 711  LYS A C     1 
ATOM   4556 O  O     . LYS A 1 608 ? -35.646 -12.639 3.726   1.00 181.94 ? 711  LYS A O     1 
ATOM   4557 C  CB    . LYS A 1 608 ? -33.667 -14.442 2.346   1.00 145.20 ? 711  LYS A CB    1 
ATOM   4558 C  CG    . LYS A 1 608 ? -32.770 -15.607 2.727   1.00 141.73 ? 711  LYS A CG    1 
ATOM   4559 C  CD    . LYS A 1 608 ? -32.784 -15.837 4.230   1.00 161.07 ? 711  LYS A CD    1 
ATOM   4560 C  CE    . LYS A 1 608 ? -31.976 -17.066 4.613   1.00 158.36 ? 711  LYS A CE    1 
ATOM   4561 N  NZ    . LYS A 1 608 ? -32.559 -18.311 4.042   1.00 158.02 ? 711  LYS A NZ    1 
ATOM   4562 N  N     . LEU A 1 609 ? -36.743 -13.004 1.793   1.00 152.30 ? 712  LEU A N     1 
ATOM   4563 C  CA    . LEU A 1 609 ? -37.554 -11.799 1.890   1.00 160.70 ? 712  LEU A CA    1 
ATOM   4564 C  C     . LEU A 1 609 ? -38.955 -12.064 2.422   1.00 170.64 ? 712  LEU A C     1 
ATOM   4565 O  O     . LEU A 1 609 ? -39.579 -11.145 2.963   1.00 161.92 ? 712  LEU A O     1 
ATOM   4566 C  CB    . LEU A 1 609 ? -37.663 -11.116 0.520   1.00 160.40 ? 712  LEU A CB    1 
ATOM   4567 C  CG    . LEU A 1 609 ? -36.363 -10.627 -0.121  1.00 153.87 ? 712  LEU A CG    1 
ATOM   4568 C  CD1   . LEU A 1 609 ? -36.635 -10.044 -1.499  1.00 139.27 ? 712  LEU A CD1   1 
ATOM   4569 C  CD2   . LEU A 1 609 ? -35.676 -9.605  0.770   1.00 141.01 ? 712  LEU A CD2   1 
ATOM   4570 N  N     . ILE A 1 610 ? -39.460 -13.292 2.283   1.00 167.57 ? 713  ILE A N     1 
ATOM   4571 C  CA    . ILE A 1 610 ? -40.806 -13.601 2.756   1.00 171.93 ? 713  ILE A CA    1 
ATOM   4572 C  C     . ILE A 1 610 ? -40.827 -13.715 4.275   1.00 187.32 ? 713  ILE A C     1 
ATOM   4573 O  O     . ILE A 1 610 ? -41.758 -13.236 4.934   1.00 188.78 ? 713  ILE A O     1 
ATOM   4574 C  CB    . ILE A 1 610 ? -41.324 -14.886 2.085   1.00 160.86 ? 713  ILE A CB    1 
ATOM   4575 C  CG1   . ILE A 1 610 ? -41.299 -14.745 0.563   1.00 171.34 ? 713  ILE A CG1   1 
ATOM   4576 C  CG2   . ILE A 1 610 ? -42.732 -15.209 2.564   1.00 167.69 ? 713  ILE A CG2   1 
ATOM   4577 C  CD1   . ILE A 1 610 ? -41.730 -15.996 -0.172  1.00 156.48 ? 713  ILE A CD1   1 
ATOM   4578 N  N     . ASN A 1 611 ? -39.805 -14.348 4.857   1.00 208.77 ? 714  ASN A N     1 
ATOM   4579 C  CA    . ASN A 1 611 ? -39.793 -14.547 6.302   1.00 207.94 ? 714  ASN A CA    1 
ATOM   4580 C  C     . ASN A 1 611 ? -39.579 -13.233 7.043   1.00 212.67 ? 714  ASN A C     1 
ATOM   4581 O  O     . ASN A 1 611 ? -40.153 -13.023 8.118   1.00 216.92 ? 714  ASN A O     1 
ATOM   4582 C  CB    . ASN A 1 611 ? -38.719 -15.566 6.687   1.00 219.38 ? 714  ASN A CB    1 
ATOM   4583 C  CG    . ASN A 1 611 ? -37.319 -15.097 6.347   1.00 231.86 ? 714  ASN A CG    1 
ATOM   4584 O  OD1   . ASN A 1 611 ? -37.120 -14.339 5.398   1.00 208.80 ? 714  ASN A OD1   1 
ATOM   4585 N  ND2   . ASN A 1 611 ? -36.339 -15.546 7.122   1.00 228.39 ? 714  ASN A ND2   1 
ATOM   4586 N  N     . LEU A 1 612 ? -38.763 -12.334 6.486   1.00 186.86 ? 715  LEU A N     1 
ATOM   4587 C  CA    . LEU A 1 612 ? -38.532 -11.049 7.140   1.00 183.24 ? 715  LEU A CA    1 
ATOM   4588 C  C     . LEU A 1 612 ? -39.810 -10.225 7.203   1.00 191.96 ? 715  LEU A C     1 
ATOM   4589 O  O     . LEU A 1 612 ? -40.099 -9.590  8.224   1.00 181.68 ? 715  LEU A O     1 
ATOM   4590 C  CB    . LEU A 1 612 ? -37.429 -10.276 6.418   1.00 175.81 ? 715  LEU A CB    1 
ATOM   4591 C  CG    . LEU A 1 612 ? -36.014 -10.844 6.532   1.00 187.78 ? 715  LEU A CG    1 
ATOM   4592 C  CD1   . LEU A 1 612 ? -35.003 -9.861  5.966   1.00 150.36 ? 715  LEU A CD1   1 
ATOM   4593 C  CD2   . LEU A 1 612 ? -35.683 -11.187 7.977   1.00 199.07 ? 715  LEU A CD2   1 
ATOM   4594 N  N     . THR A 1 613 ? -40.592 -10.222 6.120   1.00 197.30 ? 716  THR A N     1 
ATOM   4595 C  CA    . THR A 1 613 ? -41.874 -9.527  6.143   1.00 182.85 ? 716  THR A CA    1 
ATOM   4596 C  C     . THR A 1 613 ? -42.856 -10.198 7.094   1.00 183.51 ? 716  THR A C     1 
ATOM   4597 O  O     . THR A 1 613 ? -43.733 -9.528  7.651   1.00 178.99 ? 716  THR A O     1 
ATOM   4598 C  CB    . THR A 1 613 ? -42.464 -9.454  4.735   1.00 166.85 ? 716  THR A CB    1 
ATOM   4599 O  OG1   . THR A 1 613 ? -42.553 -10.773 4.182   1.00 175.89 ? 716  THR A OG1   1 
ATOM   4600 C  CG2   . THR A 1 613 ? -41.595 -8.590  3.838   1.00 157.58 ? 716  THR A CG2   1 
ATOM   4601 N  N     . ASP A 1 614 ? -42.728 -11.512 7.293   1.00 185.75 ? 717  ASP A N     1 
ATOM   4602 C  CA    . ASP A 1 614 ? -43.575 -12.194 8.267   1.00 186.96 ? 717  ASP A CA    1 
ATOM   4603 C  C     . ASP A 1 614 ? -43.170 -11.837 9.691   1.00 189.68 ? 717  ASP A C     1 
ATOM   4604 O  O     . ASP A 1 614 ? -44.028 -11.710 10.573  1.00 202.14 ? 717  ASP A O     1 
ATOM   4605 C  CB    . ASP A 1 614 ? -43.513 -13.707 8.052   1.00 190.21 ? 717  ASP A CB    1 
ATOM   4606 C  CG    . ASP A 1 614 ? -44.163 -14.138 6.751   1.00 182.08 ? 717  ASP A CG    1 
ATOM   4607 O  OD1   . ASP A 1 614 ? -45.130 -13.475 6.319   1.00 192.07 ? 717  ASP A OD1   1 
ATOM   4608 O  OD2   . ASP A 1 614 ? -43.710 -15.141 6.161   1.00 181.63 ? 717  ASP A OD2   1 
ATOM   4609 N  N     . ILE A 1 615 ? -41.868 -11.671 9.937   1.00 178.94 ? 718  ILE A N     1 
ATOM   4610 C  CA    . ILE A 1 615 ? -41.415 -11.253 11.260  1.00 181.84 ? 718  ILE A CA    1 
ATOM   4611 C  C     . ILE A 1 615 ? -41.759 -9.789  11.503  1.00 189.71 ? 718  ILE A C     1 
ATOM   4612 O  O     . ILE A 1 615 ? -41.956 -9.371  12.651  1.00 205.99 ? 718  ILE A O     1 
ATOM   4613 C  CB    . ILE A 1 615 ? -39.906 -11.523 11.417  1.00 174.71 ? 718  ILE A CB    1 
ATOM   4614 C  CG1   . ILE A 1 615 ? -39.604 -13.007 11.208  1.00 197.42 ? 718  ILE A CG1   1 
ATOM   4615 C  CG2   . ILE A 1 615 ? -39.416 -11.095 12.792  1.00 187.56 ? 718  ILE A CG2   1 
ATOM   4616 C  CD1   . ILE A 1 615 ? -40.307 -13.919 12.191  1.00 176.75 ? 718  ILE A CD1   1 
ATOM   4617 N  N     . LEU A 1 616 ? -41.854 -8.988  10.440  1.00 188.54 ? 719  LEU A N     1 
ATOM   4618 C  CA    . LEU A 1 616 ? -42.219 -7.584  10.578  1.00 173.52 ? 719  LEU A CA    1 
ATOM   4619 C  C     . LEU A 1 616 ? -43.722 -7.364  10.686  1.00 184.23 ? 719  LEU A C     1 
ATOM   4620 O  O     . LEU A 1 616 ? -44.141 -6.268  11.076  1.00 183.87 ? 719  LEU A O     1 
ATOM   4621 C  CB    . LEU A 1 616 ? -41.671 -6.776  9.398   1.00 167.89 ? 719  LEU A CB    1 
ATOM   4622 C  CG    . LEU A 1 616 ? -40.154 -6.582  9.344   1.00 166.27 ? 719  LEU A CG    1 
ATOM   4623 C  CD1   . LEU A 1 616 ? -39.763 -5.763  8.124   1.00 148.26 ? 719  LEU A CD1   1 
ATOM   4624 C  CD2   . LEU A 1 616 ? -39.651 -5.926  10.621  1.00 155.84 ? 719  LEU A CD2   1 
ATOM   4625 N  N     . LYS A 1 617 ? -44.539 -8.363  10.353  1.00 202.99 ? 720  LYS A N     1 
ATOM   4626 C  CA    . LYS A 1 617 ? -45.990 -8.243  10.430  1.00 204.00 ? 720  LYS A CA    1 
ATOM   4627 C  C     . LYS A 1 617 ? -46.569 -9.040  11.592  1.00 217.28 ? 720  LYS A C     1 
ATOM   4628 O  O     . LYS A 1 617 ? -47.278 -8.480  12.433  1.00 216.58 ? 720  LYS A O     1 
ATOM   4629 C  CB    . LYS A 1 617 ? -46.630 -8.683  9.106   1.00 198.90 ? 720  LYS A CB    1 
ATOM   4630 C  CG    . LYS A 1 617 ? -46.398 -7.716  7.954   1.00 208.29 ? 720  LYS A CG    1 
ATOM   4631 C  CD    . LYS A 1 617 ? -47.109 -8.156  6.678   1.00 200.32 ? 720  LYS A CD    1 
ATOM   4632 C  CE    . LYS A 1 617 ? -48.598 -7.822  6.699   1.00 204.05 ? 720  LYS A CE    1 
ATOM   4633 N  NZ    . LYS A 1 617 ? -49.404 -8.751  7.542   1.00 204.64 ? 720  LYS A NZ    1 
ATOM   4634 N  N     . GLN A 1 618 ? -46.289 -10.344 11.660  1.00 230.41 ? 721  GLN A N     1 
ATOM   4635 C  CA    . GLN A 1 618 ? -46.805 -11.149 12.763  1.00 228.56 ? 721  GLN A CA    1 
ATOM   4636 C  C     . GLN A 1 618 ? -46.140 -10.770 14.081  1.00 226.27 ? 721  GLN A C     1 
ATOM   4637 O  O     . GLN A 1 618 ? -46.811 -10.668 15.115  1.00 229.80 ? 721  GLN A O     1 
ATOM   4638 C  CB    . GLN A 1 618 ? -46.608 -12.636 12.467  1.00 216.72 ? 721  GLN A CB    1 
ATOM   4639 C  CG    . GLN A 1 618 ? -47.361 -13.128 11.241  1.00 216.62 ? 721  GLN A CG    1 
ATOM   4640 C  CD    . GLN A 1 618 ? -47.226 -14.624 11.035  1.00 235.29 ? 721  GLN A CD    1 
ATOM   4641 O  OE1   . GLN A 1 618 ? -46.567 -15.313 11.813  1.00 241.09 ? 721  GLN A OE1   1 
ATOM   4642 N  NE2   . GLN A 1 618 ? -47.854 -15.134 9.982   1.00 231.02 ? 721  GLN A NE2   1 
ATOM   4643 N  N     . GLU A 1 619 ? -44.829 -10.560 14.065  1.00 225.08 ? 722  GLU A N     1 
ATOM   4644 C  CA    . GLU A 1 619 ? -44.089 -10.114 15.234  1.00 222.23 ? 722  GLU A CA    1 
ATOM   4645 C  C     . GLU A 1 619 ? -43.787 -8.624  15.127  1.00 227.91 ? 722  GLU A C     1 
ATOM   4646 O  O     . GLU A 1 619 ? -43.875 -8.025  14.052  1.00 230.62 ? 722  GLU A O     1 
ATOM   4647 C  CB    . GLU A 1 619 ? -42.787 -10.905 15.390  1.00 223.76 ? 722  GLU A CB    1 
ATOM   4648 C  CG    . GLU A 1 619 ? -42.972 -12.413 15.432  1.00 225.18 ? 722  GLU A CG    1 
ATOM   4649 C  CD    . GLU A 1 619 ? -41.656 -13.157 15.553  1.00 221.19 ? 722  GLU A CD    1 
ATOM   4650 O  OE1   . GLU A 1 619 ? -40.621 -12.503 15.798  1.00 222.05 ? 722  GLU A OE1   1 
ATOM   4651 O  OE2   . GLU A 1 619 ? -41.656 -14.397 15.400  1.00 211.47 ? 722  GLU A OE2   1 
ATOM   4652 N  N     . LYS A 1 620 ? -43.433 -8.033  16.266  1.00 234.65 ? 723  LYS A N     1 
ATOM   4653 C  CA    . LYS A 1 620 ? -43.051 -6.616  16.361  1.00 245.04 ? 723  LYS A CA    1 
ATOM   4654 C  C     . LYS A 1 620 ? -44.205 -5.786  15.801  1.00 242.04 ? 723  LYS A C     1 
ATOM   4655 O  O     . LYS A 1 620 ? -45.349 -5.968  16.248  1.00 247.56 ? 723  LYS A O     1 
ATOM   4656 C  CB    . LYS A 1 620 ? -41.701 -6.418  15.681  1.00 231.99 ? 723  LYS A CB    1 
ATOM   4657 C  CG    . LYS A 1 620 ? -40.605 -7.330  16.208  1.00 237.28 ? 723  LYS A CG    1 
ATOM   4658 C  CD    . LYS A 1 620 ? -39.303 -7.124  15.453  1.00 217.63 ? 723  LYS A CD    1 
ATOM   4659 C  CE    . LYS A 1 620 ? -38.222 -8.066  15.957  1.00 226.43 ? 723  LYS A CE    1 
ATOM   4660 N  NZ    . LYS A 1 620 ? -38.600 -9.495  15.774  1.00 221.92 ? 723  LYS A NZ    1 
ATOM   4661 N  N     . LYS A 1 621 ? -43.963 -4.878  14.855  1.00 241.93 ? 724  LYS A N     1 
ATOM   4662 C  CA    . LYS A 1 621 ? -44.976 -4.052  14.201  1.00 244.17 ? 724  LYS A CA    1 
ATOM   4663 C  C     . LYS A 1 621 ? -45.738 -3.160  15.176  1.00 243.13 ? 724  LYS A C     1 
ATOM   4664 O  O     . LYS A 1 621 ? -46.705 -2.499  14.779  1.00 259.69 ? 724  LYS A O     1 
ATOM   4665 C  CB    . LYS A 1 621 ? -45.963 -4.911  13.395  1.00 242.58 ? 724  LYS A CB    1 
ATOM   4666 C  CG    . LYS A 1 621 ? -46.580 -4.205  12.195  1.00 244.21 ? 724  LYS A CG    1 
ATOM   4667 C  CD    . LYS A 1 621 ? -47.592 -5.093  11.491  1.00 242.41 ? 724  LYS A CD    1 
ATOM   4668 C  CE    . LYS A 1 621 ? -48.724 -5.488  12.425  1.00 239.27 ? 724  LYS A CE    1 
ATOM   4669 N  NZ    . LYS A 1 621 ? -49.714 -6.374  11.754  1.00 219.41 ? 724  LYS A NZ    1 
ATOM   4670 N  N     . ASP A 1 622 ? -45.327 -3.114  16.444  1.00 227.31 ? 725  ASP A N     1 
ATOM   4671 C  CA    . ASP A 1 622 ? -46.016 -2.270  17.414  1.00 224.55 ? 725  ASP A CA    1 
ATOM   4672 C  C     . ASP A 1 622 ? -45.697 -0.799  17.178  1.00 222.18 ? 725  ASP A C     1 
ATOM   4673 O  O     . ASP A 1 622 ? -46.603 0.037   17.087  1.00 215.77 ? 725  ASP A O     1 
ATOM   4674 C  CB    . ASP A 1 622 ? -45.634 -2.689  18.834  1.00 235.77 ? 725  ASP A CB    1 
ATOM   4675 C  CG    . ASP A 1 622 ? -46.521 -2.056  19.889  1.00 235.44 ? 725  ASP A CG    1 
ATOM   4676 O  OD1   . ASP A 1 622 ? -47.527 -1.414  19.519  1.00 247.23 ? 725  ASP A OD1   1 
ATOM   4677 O  OD2   . ASP A 1 622 ? -46.212 -2.201  21.091  1.00 231.38 ? 725  ASP A OD2   1 
ATOM   4678 N  N     . GLU A 1 623 ? -44.415 -0.467  17.073  1.00 229.86 ? 726  GLU A N     1 
ATOM   4679 C  CA    . GLU A 1 623 ? -43.965 0.892   16.820  1.00 231.32 ? 726  GLU A CA    1 
ATOM   4680 C  C     . GLU A 1 623 ? -43.336 0.971   15.435  1.00 233.94 ? 726  GLU A C     1 
ATOM   4681 O  O     . GLU A 1 623 ? -42.704 0.020   14.968  1.00 245.36 ? 726  GLU A O     1 
ATOM   4682 C  CB    . GLU A 1 623 ? -42.964 1.343   17.889  1.00 219.15 ? 726  GLU A CB    1 
ATOM   4683 C  CG    . GLU A 1 623 ? -42.757 2.844   17.967  1.00 231.90 ? 726  GLU A CG    1 
ATOM   4684 C  CD    . GLU A 1 623 ? -41.419 3.278   17.406  1.00 248.36 ? 726  GLU A CD    1 
ATOM   4685 O  OE1   . GLU A 1 623 ? -40.910 2.601   16.488  1.00 231.39 ? 726  GLU A OE1   1 
ATOM   4686 O  OE2   . GLU A 1 623 ? -40.874 4.291   17.891  1.00 257.04 ? 726  GLU A OE2   1 
ATOM   4687 N  N     . THR A 1 624 ? -43.522 2.112   14.775  1.00 229.93 ? 727  THR A N     1 
ATOM   4688 C  CA    . THR A 1 624 ? -43.090 2.303   13.393  1.00 249.29 ? 727  THR A CA    1 
ATOM   4689 C  C     . THR A 1 624 ? -42.212 3.543   13.267  1.00 247.61 ? 727  THR A C     1 
ATOM   4690 O  O     . THR A 1 624 ? -42.419 4.400   12.406  1.00 245.03 ? 727  THR A O     1 
ATOM   4691 C  CB    . THR A 1 624 ? -44.290 2.401   12.453  1.00 253.42 ? 727  THR A CB    1 
ATOM   4692 O  OG1   . THR A 1 624 ? -45.124 3.495   12.852  1.00 265.71 ? 727  THR A OG1   1 
ATOM   4693 C  CG2   . THR A 1 624 ? -45.101 1.112   12.487  1.00 225.48 ? 727  THR A CG2   1 
ATOM   4694 N  N     . GLN A 1 625 ? -41.206 3.648   14.133  1.00 241.85 ? 728  GLN A N     1 
ATOM   4695 C  CA    . GLN A 1 625 ? -40.229 4.726   14.034  1.00 246.88 ? 728  GLN A CA    1 
ATOM   4696 C  C     . GLN A 1 625 ? -38.820 4.160   14.148  1.00 246.40 ? 728  GLN A C     1 
ATOM   4697 O  O     . GLN A 1 625 ? -38.047 4.206   13.185  1.00 238.82 ? 728  GLN A O     1 
ATOM   4698 C  CB    . GLN A 1 625 ? -40.483 5.788   15.107  1.00 246.67 ? 728  GLN A CB    1 
ATOM   4699 C  CG    . GLN A 1 625 ? -39.506 6.954   15.078  1.00 252.94 ? 728  GLN A CG    1 
ATOM   4700 C  CD    . GLN A 1 625 ? -38.386 6.804   16.088  1.00 241.83 ? 728  GLN A CD    1 
ATOM   4701 O  OE1   . GLN A 1 625 ? -38.569 6.209   17.149  1.00 226.30 ? 728  GLN A OE1   1 
ATOM   4702 N  NE2   . GLN A 1 625 ? -37.216 7.344   15.761  1.00 241.15 ? 728  GLN A NE2   1 
ATOM   4703 N  N     . LYS A 1 626 ? -38.476 3.625   15.319  1.00 245.28 ? 729  LYS A N     1 
ATOM   4704 C  CA    . LYS A 1 626 ? -37.213 2.917   15.485  1.00 240.89 ? 729  LYS A CA    1 
ATOM   4705 C  C     . LYS A 1 626 ? -37.357 1.424   15.220  1.00 228.04 ? 729  LYS A C     1 
ATOM   4706 O  O     . LYS A 1 626 ? -36.466 0.816   14.618  1.00 226.53 ? 729  LYS A O     1 
ATOM   4707 C  CB    . LYS A 1 626 ? -36.653 3.142   16.893  1.00 225.75 ? 729  LYS A CB    1 
ATOM   4708 C  CG    . LYS A 1 626 ? -35.909 4.456   17.066  1.00 218.15 ? 729  LYS A CG    1 
ATOM   4709 C  CD    . LYS A 1 626 ? -35.322 4.577   18.464  1.00 216.07 ? 729  LYS A CD    1 
ATOM   4710 C  CE    . LYS A 1 626 ? -34.554 5.879   18.629  1.00 234.96 ? 729  LYS A CE    1 
ATOM   4711 N  NZ    . LYS A 1 626 ? -33.962 6.008   19.989  1.00 228.15 ? 729  LYS A NZ    1 
ATOM   4712 N  N     . VAL A 1 627 ? -38.469 0.824   15.653  1.00 217.31 ? 730  VAL A N     1 
ATOM   4713 C  CA    . VAL A 1 627 ? -38.680 -0.606  15.444  1.00 224.08 ? 730  VAL A CA    1 
ATOM   4714 C  C     . VAL A 1 627 ? -38.792 -0.925  13.959  1.00 225.72 ? 730  VAL A C     1 
ATOM   4715 O  O     . VAL A 1 627 ? -38.352 -1.991  13.510  1.00 216.47 ? 730  VAL A O     1 
ATOM   4716 C  CB    . VAL A 1 627 ? -39.923 -1.079  16.223  1.00 229.51 ? 730  VAL A CB    1 
ATOM   4717 C  CG1   . VAL A 1 627 ? -40.090 -2.587  16.106  1.00 216.26 ? 730  VAL A CG1   1 
ATOM   4718 C  CG2   . VAL A 1 627 ? -39.825 -0.659  17.682  1.00 191.98 ? 730  VAL A CG2   1 
ATOM   4719 N  N     . GLN A 1 628 ? -39.371 -0.014  13.173  1.00 227.72 ? 731  GLN A N     1 
ATOM   4720 C  CA    . GLN A 1 628 ? -39.434 -0.218  11.731  1.00 239.19 ? 731  GLN A CA    1 
ATOM   4721 C  C     . GLN A 1 628 ? -38.060 -0.148  11.080  1.00 228.70 ? 731  GLN A C     1 
ATOM   4722 O  O     . GLN A 1 628 ? -37.892 -0.642  9.960   1.00 242.33 ? 731  GLN A O     1 
ATOM   4723 C  CB    . GLN A 1 628 ? -40.358 0.816   11.083  1.00 241.79 ? 731  GLN A CB    1 
ATOM   4724 C  CG    . GLN A 1 628 ? -39.792 2.228   11.069  1.00 229.56 ? 731  GLN A CG    1 
ATOM   4725 C  CD    . GLN A 1 628 ? -40.525 3.141   10.104  1.00 227.88 ? 731  GLN A CD    1 
ATOM   4726 O  OE1   . GLN A 1 628 ? -41.412 2.705   9.371   1.00 226.55 ? 731  GLN A OE1   1 
ATOM   4727 N  NE2   . GLN A 1 628 ? -40.153 4.416   10.098  1.00 230.21 ? 731  GLN A NE2   1 
ATOM   4728 N  N     . MET A 1 629 ? -37.078 0.454   11.753  1.00 219.73 ? 732  MET A N     1 
ATOM   4729 C  CA    . MET A 1 629 ? -35.733 0.592   11.212  1.00 221.13 ? 732  MET A CA    1 
ATOM   4730 C  C     . MET A 1 629 ? -34.677 -0.043  12.109  1.00 231.79 ? 732  MET A C     1 
ATOM   4731 O  O     . MET A 1 629 ? -33.480 0.159   11.878  1.00 241.37 ? 732  MET A O     1 
ATOM   4732 C  CB    . MET A 1 629 ? -35.406 2.070   10.977  1.00 232.15 ? 732  MET A CB    1 
ATOM   4733 C  CG    . MET A 1 629 ? -34.527 2.329   9.763   1.00 231.65 ? 732  MET A CG    1 
ATOM   4734 S  SD    . MET A 1 629 ? -35.280 1.753   8.229   1.00 239.53 ? 732  MET A SD    1 
ATOM   4735 C  CE    . MET A 1 629 ? -36.819 2.670   8.238   1.00 226.02 ? 732  MET A CE    1 
ATOM   4736 N  N     . LYS A 1 630 ? -35.085 -0.797  13.130  1.00 231.44 ? 733  LYS A N     1 
ATOM   4737 C  CA    . LYS A 1 630 ? -34.133 -1.534  13.971  1.00 233.84 ? 733  LYS A CA    1 
ATOM   4738 C  C     . LYS A 1 630 ? -33.932 -2.937  13.406  1.00 232.98 ? 733  LYS A C     1 
ATOM   4739 O  O     . LYS A 1 630 ? -32.874 -3.248  12.850  1.00 236.00 ? 733  LYS A O     1 
ATOM   4740 C  CB    . LYS A 1 630 ? -34.619 -1.584  15.421  1.00 235.30 ? 733  LYS A CB    1 
ATOM   4741 C  CG    . LYS A 1 630 ? -33.746 -2.429  16.336  1.00 235.24 ? 733  LYS A CG    1 
ATOM   4742 C  CD    . LYS A 1 630 ? -34.373 -2.590  17.712  1.00 245.10 ? 733  LYS A CD    1 
ATOM   4743 C  CE    . LYS A 1 630 ? -33.541 -3.510  18.592  1.00 241.39 ? 733  LYS A CE    1 
ATOM   4744 N  NZ    . LYS A 1 630 ? -34.163 -3.715  19.929  1.00 229.23 ? 733  LYS A NZ    1 
ATOM   4745 N  N     . PHE A 1 631 ? -34.951 -3.790  13.538  1.00 220.25 ? 734  PHE A N     1 
ATOM   4746 C  CA    . PHE A 1 631 ? -34.864 -5.150  13.022  1.00 208.52 ? 734  PHE A CA    1 
ATOM   4747 C  C     . PHE A 1 631 ? -34.695 -5.181  11.510  1.00 208.68 ? 734  PHE A C     1 
ATOM   4748 O  O     . PHE A 1 631 ? -34.173 -6.166  10.976  1.00 222.54 ? 734  PHE A O     1 
ATOM   4749 C  CB    . PHE A 1 631 ? -36.109 -5.940  13.431  1.00 206.68 ? 734  PHE A CB    1 
ATOM   4750 C  CG    . PHE A 1 631 ? -36.056 -7.396  13.062  1.00 213.98 ? 734  PHE A CG    1 
ATOM   4751 C  CD1   . PHE A 1 631 ? -35.376 -8.301  13.859  1.00 217.20 ? 734  PHE A CD1   1 
ATOM   4752 C  CD2   . PHE A 1 631 ? -36.695 -7.860  11.924  1.00 216.78 ? 734  PHE A CD2   1 
ATOM   4753 C  CE1   . PHE A 1 631 ? -35.328 -9.642  13.525  1.00 223.12 ? 734  PHE A CE1   1 
ATOM   4754 C  CE2   . PHE A 1 631 ? -36.649 -9.199  11.583  1.00 224.10 ? 734  PHE A CE2   1 
ATOM   4755 C  CZ    . PHE A 1 631 ? -35.966 -10.091 12.386  1.00 229.04 ? 734  PHE A CZ    1 
ATOM   4756 N  N     . LEU A 1 632 ? -35.115 -4.127  10.809  1.00 195.06 ? 735  LEU A N     1 
ATOM   4757 C  CA    . LEU A 1 632 ? -34.971 -4.100  9.357   1.00 190.02 ? 735  LEU A CA    1 
ATOM   4758 C  C     . LEU A 1 632 ? -33.508 -3.964  8.953   1.00 200.74 ? 735  LEU A C     1 
ATOM   4759 O  O     . LEU A 1 632 ? -33.012 -4.726  8.115   1.00 208.15 ? 735  LEU A O     1 
ATOM   4760 C  CB    . LEU A 1 632 ? -35.805 -2.962  8.768   1.00 191.12 ? 735  LEU A CB    1 
ATOM   4761 C  CG    . LEU A 1 632 ? -35.765 -2.814  7.246   1.00 196.65 ? 735  LEU A CG    1 
ATOM   4762 C  CD1   . LEU A 1 632 ? -37.172 -2.742  6.680   1.00 160.65 ? 735  LEU A CD1   1 
ATOM   4763 C  CD2   . LEU A 1 632 ? -34.966 -1.584  6.846   1.00 212.00 ? 735  LEU A CD2   1 
ATOM   4764 N  N     . VAL A 1 633 ? -32.797 -2.999  9.540   1.00 193.19 ? 736  VAL A N     1 
ATOM   4765 C  CA    . VAL A 1 633 ? -31.397 -2.799  9.181   1.00 198.61 ? 736  VAL A CA    1 
ATOM   4766 C  C     . VAL A 1 633 ? -30.484 -3.839  9.816   1.00 192.13 ? 736  VAL A C     1 
ATOM   4767 O  O     . VAL A 1 633 ? -29.364 -4.042  9.333   1.00 197.72 ? 736  VAL A O     1 
ATOM   4768 C  CB    . VAL A 1 633 ? -30.922 -1.387  9.563   1.00 203.96 ? 736  VAL A CB    1 
ATOM   4769 C  CG1   . VAL A 1 633 ? -31.886 -0.337  9.029   1.00 201.37 ? 736  VAL A CG1   1 
ATOM   4770 C  CG2   . VAL A 1 633 ? -30.756 -1.263  11.072  1.00 196.58 ? 736  VAL A CG2   1 
ATOM   4771 N  N     . GLU A 1 634 ? -30.928 -4.506  10.885  1.00 196.08 ? 737  GLU A N     1 
ATOM   4772 C  CA    . GLU A 1 634 ? -30.092 -5.524  11.513  1.00 197.10 ? 737  GLU A CA    1 
ATOM   4773 C  C     . GLU A 1 634 ? -30.051 -6.803  10.688  1.00 207.97 ? 737  GLU A C     1 
ATOM   4774 O  O     . GLU A 1 634 ? -29.033 -7.505  10.687  1.00 217.61 ? 737  GLU A O     1 
ATOM   4775 C  CB    . GLU A 1 634 ? -30.590 -5.823  12.927  1.00 204.70 ? 737  GLU A CB    1 
ATOM   4776 C  CG    . GLU A 1 634 ? -30.299 -4.723  13.935  1.00 218.73 ? 737  GLU A CG    1 
ATOM   4777 C  CD    . GLU A 1 634 ? -30.858 -5.031  15.311  1.00 234.80 ? 737  GLU A CD    1 
ATOM   4778 O  OE1   . GLU A 1 634 ? -31.436 -6.125  15.488  1.00 235.13 ? 737  GLU A OE1   1 
ATOM   4779 O  OE2   . GLU A 1 634 ? -30.720 -4.181  16.216  1.00 231.97 ? 737  GLU A OE2   1 
ATOM   4780 N  N     . GLN A 1 635 ? -31.139 -7.125  9.987   1.00 209.94 ? 738  GLN A N     1 
ATOM   4781 C  CA    . GLN A 1 635 ? -31.153 -8.323  9.155   1.00 202.57 ? 738  GLN A CA    1 
ATOM   4782 C  C     . GLN A 1 635 ? -30.445 -8.088  7.827   1.00 199.48 ? 738  GLN A C     1 
ATOM   4783 O  O     . GLN A 1 635 ? -29.753 -8.980  7.324   1.00 205.03 ? 738  GLN A O     1 
ATOM   4784 C  CB    . GLN A 1 635 ? -32.591 -8.784  8.921   1.00 205.33 ? 738  GLN A CB    1 
ATOM   4785 C  CG    . GLN A 1 635 ? -33.335 -9.150  10.193  1.00 211.23 ? 738  GLN A CG    1 
ATOM   4786 C  CD    . GLN A 1 635 ? -32.667 -10.275 10.958  1.00 229.87 ? 738  GLN A CD    1 
ATOM   4787 O  OE1   . GLN A 1 635 ? -32.527 -10.213 12.179  1.00 231.41 ? 738  GLN A OE1   1 
ATOM   4788 N  NE2   . GLN A 1 635 ? -32.254 -11.315 10.242  1.00 236.91 ? 738  GLN A NE2   1 
ATOM   4789 N  N     . MET A 1 636 ? -30.602 -6.896  7.247   1.00 182.16 ? 739  MET A N     1 
ATOM   4790 C  CA    . MET A 1 636 ? -29.935 -6.590  5.987   1.00 177.77 ? 739  MET A CA    1 
ATOM   4791 C  C     . MET A 1 636 ? -28.424 -6.500  6.141   1.00 192.09 ? 739  MET A C     1 
ATOM   4792 O  O     . MET A 1 636 ? -27.701 -6.704  5.160   1.00 177.61 ? 739  MET A O     1 
ATOM   4793 C  CB    . MET A 1 636 ? -30.479 -5.286  5.403   1.00 190.05 ? 739  MET A CB    1 
ATOM   4794 C  CG    . MET A 1 636 ? -31.971 -5.305  5.116   1.00 162.00 ? 739  MET A CG    1 
ATOM   4795 S  SD    . MET A 1 636 ? -32.520 -3.821  4.253   1.00 209.11 ? 739  MET A SD    1 
ATOM   4796 C  CE    . MET A 1 636 ? -31.791 -2.546  5.279   1.00 201.67 ? 739  MET A CE    1 
ATOM   4797 N  N     . ARG A 1 637 ? -27.932 -6.197  7.341   1.00 193.48 ? 740  ARG A N     1 
ATOM   4798 C  CA    . ARG A 1 637 ? -26.501 -6.174  7.612   1.00 201.28 ? 740  ARG A CA    1 
ATOM   4799 C  C     . ARG A 1 637 ? -25.987 -7.503  8.148   1.00 210.65 ? 740  ARG A C     1 
ATOM   4800 O  O     . ARG A 1 637 ? -24.776 -7.647  8.348   1.00 207.44 ? 740  ARG A O     1 
ATOM   4801 C  CB    . ARG A 1 637 ? -26.166 -5.057  8.606   1.00 192.19 ? 740  ARG A CB    1 
ATOM   4802 C  CG    . ARG A 1 637 ? -26.571 -5.358  10.039  1.00 196.02 ? 740  ARG A CG    1 
ATOM   4803 C  CD    . ARG A 1 637 ? -26.345 -4.157  10.940  1.00 195.68 ? 740  ARG A CD    1 
ATOM   4804 N  NE    . ARG A 1 637 ? -26.737 -4.427  12.318  1.00 204.62 ? 740  ARG A NE    1 
ATOM   4805 C  CZ    . ARG A 1 637 ? -26.704 -3.532  13.295  1.00 207.46 ? 740  ARG A CZ    1 
ATOM   4806 N  NH1   . ARG A 1 637 ? -26.308 -2.288  13.080  1.00 183.57 ? 740  ARG A NH1   1 
ATOM   4807 N  NH2   . ARG A 1 637 ? -27.080 -3.893  14.519  1.00 215.47 ? 740  ARG A NH2   1 
ATOM   4808 N  N     . ARG A 1 638 ? -26.871 -8.466  8.387   1.00 216.60 ? 741  ARG A N     1 
ATOM   4809 C  CA    . ARG A 1 638 ? -26.443 -9.772  8.862   1.00 193.28 ? 741  ARG A CA    1 
ATOM   4810 C  C     . ARG A 1 638 ? -25.669 -10.498 7.764   1.00 192.78 ? 741  ARG A C     1 
ATOM   4811 O  O     . ARG A 1 638 ? -26.084 -10.486 6.600   1.00 190.42 ? 741  ARG A O     1 
ATOM   4812 C  CB    . ARG A 1 638 ? -27.651 -10.599 9.302   1.00 184.31 ? 741  ARG A CB    1 
ATOM   4813 C  CG    . ARG A 1 638 ? -27.333 -12.034 9.685   1.00 193.64 ? 741  ARG A CG    1 
ATOM   4814 C  CD    . ARG A 1 638 ? -28.465 -12.663 10.484  1.00 207.10 ? 741  ARG A CD    1 
ATOM   4815 N  NE    . ARG A 1 638 ? -28.346 -12.392 11.912  1.00 219.32 ? 741  ARG A NE    1 
ATOM   4816 C  CZ    . ARG A 1 638 ? -28.919 -11.371 12.536  1.00 234.24 ? 741  ARG A CZ    1 
ATOM   4817 N  NH1   . ARG A 1 638 ? -29.668 -10.495 11.886  1.00 223.82 ? 741  ARG A NH1   1 
ATOM   4818 N  NH2   . ARG A 1 638 ? -28.737 -11.227 13.846  1.00 230.92 ? 741  ARG A NH2   1 
ATOM   4819 N  N     . PRO A 1 639 ? -24.536 -11.126 8.098   1.00 178.58 ? 742  PRO A N     1 
ATOM   4820 C  CA    . PRO A 1 639 ? -23.707 -11.745 7.048   1.00 187.37 ? 742  PRO A CA    1 
ATOM   4821 C  C     . PRO A 1 639 ? -24.427 -12.811 6.240   1.00 202.71 ? 742  PRO A C     1 
ATOM   4822 O  O     . PRO A 1 639 ? -24.302 -12.831 5.009   1.00 202.15 ? 742  PRO A O     1 
ATOM   4823 C  CB    . PRO A 1 639 ? -22.530 -12.332 7.841   1.00 184.43 ? 742  PRO A CB    1 
ATOM   4824 C  CG    . PRO A 1 639 ? -22.462 -11.504 9.080   1.00 186.89 ? 742  PRO A CG    1 
ATOM   4825 C  CD    . PRO A 1 639 ? -23.884 -11.170 9.418   1.00 183.69 ? 742  PRO A CD    1 
ATOM   4826 N  N     . ASP A 1 640 ? -25.182 -13.700 6.892   1.00 193.90 ? 743  ASP A N     1 
ATOM   4827 C  CA    . ASP A 1 640 ? -25.845 -14.777 6.164   1.00 196.29 ? 743  ASP A CA    1 
ATOM   4828 C  C     . ASP A 1 640 ? -26.974 -14.274 5.273   1.00 200.36 ? 743  ASP A C     1 
ATOM   4829 O  O     . ASP A 1 640 ? -27.378 -14.986 4.348   1.00 196.83 ? 743  ASP A O     1 
ATOM   4830 C  CB    . ASP A 1 640 ? -26.377 -15.829 7.141   1.00 201.21 ? 743  ASP A CB    1 
ATOM   4831 C  CG    . ASP A 1 640 ? -27.249 -15.233 8.228   1.00 209.68 ? 743  ASP A CG    1 
ATOM   4832 O  OD1   . ASP A 1 640 ? -28.369 -14.776 7.916   1.00 205.86 ? 743  ASP A OD1   1 
ATOM   4833 O  OD2   . ASP A 1 640 ? -26.814 -15.228 9.399   1.00 207.53 ? 743  ASP A OD2   1 
ATOM   4834 N  N     . PHE A 1 641 ? -27.491 -13.071 5.525   1.00 202.96 ? 744  PHE A N     1 
ATOM   4835 C  CA    . PHE A 1 641 ? -28.541 -12.512 4.683   1.00 171.47 ? 744  PHE A CA    1 
ATOM   4836 C  C     . PHE A 1 641 ? -27.993 -11.645 3.558   1.00 176.90 ? 744  PHE A C     1 
ATOM   4837 O  O     . PHE A 1 641 ? -28.650 -11.507 2.520   1.00 172.27 ? 744  PHE A O     1 
ATOM   4838 C  CB    . PHE A 1 641 ? -29.522 -11.694 5.529   1.00 164.05 ? 744  PHE A CB    1 
ATOM   4839 C  CG    . PHE A 1 641 ? -30.637 -11.074 4.734   1.00 159.40 ? 744  PHE A CG    1 
ATOM   4840 C  CD1   . PHE A 1 641 ? -31.723 -11.833 4.331   1.00 159.18 ? 744  PHE A CD1   1 
ATOM   4841 C  CD2   . PHE A 1 641 ? -30.599 -9.732  4.390   1.00 189.78 ? 744  PHE A CD2   1 
ATOM   4842 C  CE1   . PHE A 1 641 ? -32.748 -11.265 3.598   1.00 168.61 ? 744  PHE A CE1   1 
ATOM   4843 C  CE2   . PHE A 1 641 ? -31.622 -9.160  3.658   1.00 173.51 ? 744  PHE A CE2   1 
ATOM   4844 C  CZ    . PHE A 1 641 ? -32.698 -9.928  3.263   1.00 154.06 ? 744  PHE A CZ    1 
ATOM   4845 N  N     . MET A 1 642 ? -26.807 -11.058 3.738   1.00 189.58 ? 745  MET A N     1 
ATOM   4846 C  CA    . MET A 1 642 ? -26.227 -10.228 2.687   1.00 166.36 ? 745  MET A CA    1 
ATOM   4847 C  C     . MET A 1 642 ? -25.939 -11.050 1.437   1.00 158.28 ? 745  MET A C     1 
ATOM   4848 O  O     . MET A 1 642 ? -26.403 -10.715 0.341   1.00 172.11 ? 745  MET A O     1 
ATOM   4849 C  CB    . MET A 1 642 ? -24.953 -9.548  3.190   1.00 183.10 ? 745  MET A CB    1 
ATOM   4850 C  CG    . MET A 1 642 ? -25.194 -8.456  4.219   1.00 193.82 ? 745  MET A CG    1 
ATOM   4851 S  SD    . MET A 1 642 ? -23.721 -7.471  4.555   1.00 257.50 ? 745  MET A SD    1 
ATOM   4852 C  CE    . MET A 1 642 ? -22.594 -8.728  5.152   1.00 206.66 ? 745  MET A CE    1 
ATOM   4853 N  N     . ASP A 1 643 ? -25.184 -12.142 1.585   1.00 184.89 ? 746  ASP A N     1 
ATOM   4854 C  CA    . ASP A 1 643 ? -24.836 -12.974 0.438   1.00 181.27 ? 746  ASP A CA    1 
ATOM   4855 C  C     . ASP A 1 643 ? -26.057 -13.606 -0.218  1.00 175.73 ? 746  ASP A C     1 
ATOM   4856 O  O     . ASP A 1 643 ? -25.974 -14.025 -1.377  1.00 171.65 ? 746  ASP A O     1 
ATOM   4857 C  CB    . ASP A 1 643 ? -23.846 -14.063 0.858   1.00 200.80 ? 746  ASP A CB    1 
ATOM   4858 C  CG    . ASP A 1 643 ? -24.304 -14.829 2.084   1.00 199.88 ? 746  ASP A CG    1 
ATOM   4859 O  OD1   . ASP A 1 643 ? -25.372 -15.475 2.026   1.00 202.84 ? 746  ASP A OD1   1 
ATOM   4860 O  OD2   . ASP A 1 643 ? -23.590 -14.789 3.107   1.00 208.59 ? 746  ASP A OD2   1 
ATOM   4861 N  N     . ALA A 1 644 ? -27.185 -13.689 0.493   1.00 171.97 ? 747  ALA A N     1 
ATOM   4862 C  CA    . ALA A 1 644 ? -28.407 -14.199 -0.114  1.00 168.22 ? 747  ALA A CA    1 
ATOM   4863 C  C     . ALA A 1 644 ? -28.960 -13.256 -1.175  1.00 120.34 ? 747  ALA A C     1 
ATOM   4864 O  O     . ALA A 1 644 ? -29.675 -13.707 -2.075  1.00 145.50 ? 747  ALA A O     1 
ATOM   4865 C  CB    . ALA A 1 644 ? -29.466 -14.451 0.963   1.00 170.31 ? 747  ALA A CB    1 
ATOM   4866 N  N     . LEU A 1 645 ? -28.646 -11.963 -1.090  1.00 139.62 ? 748  LEU A N     1 
ATOM   4867 C  CA    . LEU A 1 645 ? -29.104 -10.995 -2.079  1.00 156.17 ? 748  LEU A CA    1 
ATOM   4868 C  C     . LEU A 1 645 ? -27.926 -10.373 -2.819  1.00 147.42 ? 748  LEU A C     1 
ATOM   4869 O  O     . LEU A 1 645 ? -27.845 -9.147  -2.948  1.00 141.76 ? 748  LEU A O     1 
ATOM   4870 C  CB    . LEU A 1 645 ? -29.942 -9.899  -1.415  1.00 161.31 ? 748  LEU A CB    1 
ATOM   4871 C  CG    . LEU A 1 645 ? -31.193 -10.326 -0.645  1.00 141.57 ? 748  LEU A CG    1 
ATOM   4872 C  CD1   . LEU A 1 645 ? -31.891 -9.112  -0.057  1.00 186.12 ? 748  LEU A CD1   1 
ATOM   4873 C  CD2   . LEU A 1 645 ? -32.139 -11.097 -1.544  1.00 171.80 ? 748  LEU A CD2   1 
ATOM   4874 N  N     . GLN A 1 646 ? -27.011 -11.207 -3.312  1.00 159.98 ? 749  GLN A N     1 
ATOM   4875 C  CA    . GLN A 1 646 ? -25.822 -10.731 -4.011  1.00 158.16 ? 749  GLN A CA    1 
ATOM   4876 C  C     . GLN A 1 646 ? -25.589 -11.592 -5.242  1.00 170.89 ? 749  GLN A C     1 
ATOM   4877 O  O     . GLN A 1 646 ? -25.472 -12.816 -5.132  1.00 187.12 ? 749  GLN A O     1 
ATOM   4878 C  CB    . GLN A 1 646 ? -24.589 -10.764 -3.100  1.00 171.58 ? 749  GLN A CB    1 
ATOM   4879 C  CG    . GLN A 1 646 ? -24.603 -9.735  -1.983  1.00 191.00 ? 749  GLN A CG    1 
ATOM   4880 C  CD    . GLN A 1 646 ? -24.517 -8.313  -2.494  1.00 186.06 ? 749  GLN A CD    1 
ATOM   4881 O  OE1   . GLN A 1 646 ? -23.882 -8.046  -3.514  1.00 185.37 ? 749  GLN A OE1   1 
ATOM   4882 N  NE2   . GLN A 1 646 ? -25.159 -7.390  -1.788  1.00 180.76 ? 749  GLN A NE2   1 
ATOM   4883 N  N     . GLY A 1 647 ? -25.519 -10.950 -6.406  1.00 154.79 ? 750  GLY A N     1 
ATOM   4884 C  CA    . GLY A 1 647 ? -25.154 -11.626 -7.636  1.00 163.25 ? 750  GLY A CA    1 
ATOM   4885 C  C     . GLY A 1 647 ? -26.124 -12.696 -8.094  1.00 161.61 ? 750  GLY A C     1 
ATOM   4886 O  O     . GLY A 1 647 ? -25.730 -13.847 -8.303  1.00 160.45 ? 750  GLY A O     1 
ATOM   4887 N  N     . PHE A 1 648 ? -27.393 -12.332 -8.258  1.00 158.05 ? 751  PHE A N     1 
ATOM   4888 C  CA    . PHE A 1 648 ? -28.392 -13.245 -8.791  1.00 150.89 ? 751  PHE A CA    1 
ATOM   4889 C  C     . PHE A 1 648 ? -29.295 -12.485 -9.750  1.00 152.41 ? 751  PHE A C     1 
ATOM   4890 O  O     . PHE A 1 648 ? -29.547 -11.290 -9.576  1.00 143.57 ? 751  PHE A O     1 
ATOM   4891 C  CB    . PHE A 1 648 ? -29.222 -13.905 -7.677  1.00 142.17 ? 751  PHE A CB    1 
ATOM   4892 C  CG    . PHE A 1 648 ? -30.162 -12.965 -6.975  1.00 123.04 ? 751  PHE A CG    1 
ATOM   4893 C  CD1   . PHE A 1 648 ? -29.702 -12.112 -5.986  1.00 133.36 ? 751  PHE A CD1   1 
ATOM   4894 C  CD2   . PHE A 1 648 ? -31.510 -12.949 -7.292  1.00 130.52 ? 751  PHE A CD2   1 
ATOM   4895 C  CE1   . PHE A 1 648 ? -30.566 -11.252 -5.336  1.00 142.06 ? 751  PHE A CE1   1 
ATOM   4896 C  CE2   . PHE A 1 648 ? -32.380 -12.091 -6.646  1.00 123.06 ? 751  PHE A CE2   1 
ATOM   4897 C  CZ    . PHE A 1 648 ? -31.907 -11.242 -5.666  1.00 132.54 ? 751  PHE A CZ    1 
ATOM   4898 N  N     . LEU A 1 649 ? -29.775 -13.192 -10.770 1.00 144.24 ? 752  LEU A N     1 
ATOM   4899 C  CA    . LEU A 1 649 ? -30.611 -12.569 -11.786 1.00 125.10 ? 752  LEU A CA    1 
ATOM   4900 C  C     . LEU A 1 649 ? -31.946 -12.137 -11.191 1.00 114.36 ? 752  LEU A C     1 
ATOM   4901 O  O     . LEU A 1 649 ? -32.500 -12.804 -10.313 1.00 115.94 ? 752  LEU A O     1 
ATOM   4902 C  CB    . LEU A 1 649 ? -30.837 -13.533 -12.949 1.00 140.10 ? 752  LEU A CB    1 
ATOM   4903 C  CG    . LEU A 1 649 ? -29.572 -14.104 -13.595 1.00 125.69 ? 752  LEU A CG    1 
ATOM   4904 C  CD1   . LEU A 1 649 ? -29.922 -14.999 -14.773 1.00 143.74 ? 752  LEU A CD1   1 
ATOM   4905 C  CD2   . LEU A 1 649 ? -28.633 -12.986 -14.025 1.00 128.27 ? 752  LEU A CD2   1 
ATOM   4906 N  N     . SER A 1 650 ? -32.457 -11.012 -11.674 1.00 134.32 ? 753  SER A N     1 
ATOM   4907 C  CA    . SER A 1 650 ? -33.703 -10.471 -11.146 1.00 141.07 ? 753  SER A CA    1 
ATOM   4908 C  C     . SER A 1 650 ? -34.873 -11.367 -11.536 1.00 132.91 ? 753  SER A C     1 
ATOM   4909 O  O     . SER A 1 650 ? -34.996 -11.742 -12.708 1.00 129.17 ? 753  SER A O     1 
ATOM   4910 C  CB    . SER A 1 650 ? -33.931 -9.054  -11.666 1.00 139.70 ? 753  SER A CB    1 
ATOM   4911 O  OG    . SER A 1 650 ? -35.170 -8.536  -11.213 1.00 128.32 ? 753  SER A OG    1 
ATOM   4912 N  N     . PRO A 1 651 ? -35.741 -11.740 -10.593 1.00 130.38 ? 754  PRO A N     1 
ATOM   4913 C  CA    . PRO A 1 651 ? -36.933 -12.516 -10.970 1.00 126.23 ? 754  PRO A CA    1 
ATOM   4914 C  C     . PRO A 1 651 ? -37.885 -11.749 -11.870 1.00 136.30 ? 754  PRO A C     1 
ATOM   4915 O  O     . PRO A 1 651 ? -38.622 -12.368 -12.648 1.00 136.86 ? 754  PRO A O     1 
ATOM   4916 C  CB    . PRO A 1 651 ? -37.576 -12.850 -9.615  1.00 117.41 ? 754  PRO A CB    1 
ATOM   4917 C  CG    . PRO A 1 651 ? -36.466 -12.713 -8.617  1.00 130.63 ? 754  PRO A CG    1 
ATOM   4918 C  CD    . PRO A 1 651 ? -35.607 -11.602 -9.134  1.00 127.00 ? 754  PRO A CD    1 
ATOM   4919 N  N     . LEU A 1 652 ? -37.893 -10.416 -11.787 1.00 130.44 ? 755  LEU A N     1 
ATOM   4920 C  CA    . LEU A 1 652 ? -38.747 -9.624  -12.667 1.00 112.99 ? 755  LEU A CA    1 
ATOM   4921 C  C     . LEU A 1 652 ? -38.203 -9.579  -14.088 1.00 119.61 ? 755  LEU A C     1 
ATOM   4922 O  O     . LEU A 1 652 ? -38.974 -9.415  -15.041 1.00 135.29 ? 755  LEU A O     1 
ATOM   4923 C  CB    . LEU A 1 652 ? -38.899 -8.206  -12.118 1.00 114.32 ? 755  LEU A CB    1 
ATOM   4924 C  CG    . LEU A 1 652 ? -39.742 -8.045  -10.854 1.00 129.90 ? 755  LEU A CG    1 
ATOM   4925 C  CD1   . LEU A 1 652 ? -39.676 -6.614  -10.344 1.00 135.74 ? 755  LEU A CD1   1 
ATOM   4926 C  CD2   . LEU A 1 652 ? -41.180 -8.449  -11.126 1.00 128.78 ? 755  LEU A CD2   1 
ATOM   4927 N  N     . ASN A 1 653 ? -36.890 -9.714  -14.251 1.00 115.60 ? 756  ASN A N     1 
ATOM   4928 C  CA    . ASN A 1 653 ? -36.264 -9.698  -15.566 1.00 105.83 ? 756  ASN A CA    1 
ATOM   4929 C  C     . ASN A 1 653 ? -34.933 -10.436 -15.493 1.00 125.83 ? 756  ASN A C     1 
ATOM   4930 O  O     . ASN A 1 653 ? -34.012 -9.989  -14.797 1.00 117.00 ? 756  ASN A O     1 
ATOM   4931 C  CB    . ASN A 1 653 ? -36.066 -8.260  -16.051 1.00 117.83 ? 756  ASN A CB    1 
ATOM   4932 C  CG    . ASN A 1 653 ? -35.820 -8.175  -17.546 1.00 141.66 ? 756  ASN A CG    1 
ATOM   4933 O  OD1   . ASN A 1 653 ? -35.254 -9.087  -18.149 1.00 126.47 ? 756  ASN A OD1   1 
ATOM   4934 N  ND2   . ASN A 1 653 ? -36.249 -7.073  -18.152 1.00 119.61 ? 756  ASN A ND2   1 
ATOM   4935 N  N     . PRO A 1 654 ? -34.791 -11.567 -16.191 1.00 134.02 ? 757  PRO A N     1 
ATOM   4936 C  CA    . PRO A 1 654 ? -33.547 -12.345 -16.081 1.00 112.97 ? 757  PRO A CA    1 
ATOM   4937 C  C     . PRO A 1 654 ? -32.329 -11.637 -16.649 1.00 129.12 ? 757  PRO A C     1 
ATOM   4938 O  O     . PRO A 1 654 ? -31.202 -12.030 -16.324 1.00 119.21 ? 757  PRO A O     1 
ATOM   4939 C  CB    . PRO A 1 654 ? -33.863 -13.626 -16.864 1.00 111.46 ? 757  PRO A CB    1 
ATOM   4940 C  CG    . PRO A 1 654 ? -34.925 -13.218 -17.831 1.00 136.60 ? 757  PRO A CG    1 
ATOM   4941 C  CD    . PRO A 1 654 ? -35.754 -12.187 -17.117 1.00 149.85 ? 757  PRO A CD    1 
ATOM   4942 N  N     . ALA A 1 655 ? -32.514 -10.614 -17.484 1.00 135.85 ? 758  ALA A N     1 
ATOM   4943 C  CA    . ALA A 1 655 ? -31.389 -9.869  -18.033 1.00 112.29 ? 758  ALA A CA    1 
ATOM   4944 C  C     . ALA A 1 655 ? -30.837 -8.829  -17.067 1.00 126.00 ? 758  ALA A C     1 
ATOM   4945 O  O     . ALA A 1 655 ? -29.766 -8.271  -17.331 1.00 133.72 ? 758  ALA A O     1 
ATOM   4946 C  CB    . ALA A 1 655 ? -31.796 -9.188  -19.342 1.00 115.38 ? 758  ALA A CB    1 
ATOM   4947 N  N     . HIS A 1 656 ? -31.532 -8.557  -15.966 1.00 128.03 ? 759  HIS A N     1 
ATOM   4948 C  CA    . HIS A 1 656 ? -31.079 -7.606  -14.960 1.00 123.27 ? 759  HIS A CA    1 
ATOM   4949 C  C     . HIS A 1 656 ? -30.375 -8.351  -13.834 1.00 138.29 ? 759  HIS A C     1 
ATOM   4950 O  O     . HIS A 1 656 ? -30.937 -9.287  -13.256 1.00 140.93 ? 759  HIS A O     1 
ATOM   4951 C  CB    . HIS A 1 656 ? -32.251 -6.797  -14.403 1.00 128.76 ? 759  HIS A CB    1 
ATOM   4952 C  CG    . HIS A 1 656 ? -32.882 -5.879  -15.402 1.00 117.16 ? 759  HIS A CG    1 
ATOM   4953 N  ND1   . HIS A 1 656 ? -34.011 -5.139  -15.123 1.00 116.22 ? 759  HIS A ND1   1 
ATOM   4954 C  CD2   . HIS A 1 656 ? -32.540 -5.577  -16.677 1.00 112.95 ? 759  HIS A CD2   1 
ATOM   4955 C  CE1   . HIS A 1 656 ? -34.339 -4.423  -16.184 1.00 154.68 ? 759  HIS A CE1   1 
ATOM   4956 N  NE2   . HIS A 1 656 ? -33.462 -4.671  -17.140 1.00 136.62 ? 759  HIS A NE2   1 
ATOM   4957 N  N     . GLN A 1 657 ? -29.151 -7.933  -13.526 1.00 149.05 ? 760  GLN A N     1 
ATOM   4958 C  CA    . GLN A 1 657 ? -28.360 -8.535  -12.460 1.00 140.61 ? 760  GLN A CA    1 
ATOM   4959 C  C     . GLN A 1 657 ? -28.483 -7.680  -11.205 1.00 126.54 ? 760  GLN A C     1 
ATOM   4960 O  O     . GLN A 1 657 ? -28.139 -6.494  -11.221 1.00 134.42 ? 760  GLN A O     1 
ATOM   4961 C  CB    . GLN A 1 657 ? -26.895 -8.672  -12.874 1.00 136.39 ? 760  GLN A CB    1 
ATOM   4962 C  CG    . GLN A 1 657 ? -26.670 -9.574  -14.076 1.00 163.85 ? 760  GLN A CG    1 
ATOM   4963 C  CD    . GLN A 1 657 ? -25.199 -9.811  -14.358 1.00 164.24 ? 760  GLN A CD    1 
ATOM   4964 O  OE1   . GLN A 1 657 ? -24.334 -9.407  -13.581 1.00 171.68 ? 760  GLN A OE1   1 
ATOM   4965 N  NE2   . GLN A 1 657 ? -24.908 -10.472 -15.473 1.00 153.99 ? 760  GLN A NE2   1 
ATOM   4966 N  N     . LEU A 1 658 ? -28.977 -8.283  -10.126 1.00 122.10 ? 761  LEU A N     1 
ATOM   4967 C  CA    . LEU A 1 658 ? -29.086 -7.609  -8.834  1.00 138.36 ? 761  LEU A CA    1 
ATOM   4968 C  C     . LEU A 1 658 ? -27.789 -7.849  -8.073  1.00 146.91 ? 761  LEU A C     1 
ATOM   4969 O  O     . LEU A 1 658 ? -27.582 -8.919  -7.494  1.00 173.29 ? 761  LEU A O     1 
ATOM   4970 C  CB    . LEU A 1 658 ? -30.300 -8.114  -8.061  1.00 132.39 ? 761  LEU A CB    1 
ATOM   4971 C  CG    . LEU A 1 658 ? -31.582 -7.282  -8.158  1.00 133.24 ? 761  LEU A CG    1 
ATOM   4972 C  CD1   . LEU A 1 658 ? -31.896 -6.910  -9.597  1.00 135.60 ? 761  LEU A CD1   1 
ATOM   4973 C  CD2   . LEU A 1 658 ? -32.748 -8.031  -7.532  1.00 123.19 ? 761  LEU A CD2   1 
ATOM   4974 N  N     . GLY A 1 659 ? -26.909 -6.851  -8.075  1.00 132.10 ? 762  GLY A N     1 
ATOM   4975 C  CA    . GLY A 1 659 ? -25.599 -6.997  -7.474  1.00 146.30 ? 762  GLY A CA    1 
ATOM   4976 C  C     . GLY A 1 659 ? -25.519 -6.536  -6.033  1.00 175.67 ? 762  GLY A C     1 
ATOM   4977 O  O     . GLY A 1 659 ? -26.166 -7.109  -5.152  1.00 172.04 ? 762  GLY A O     1 
ATOM   4978 N  N     . ASN A 1 660 ? -24.723 -5.499  -5.785  1.00 180.72 ? 763  ASN A N     1 
ATOM   4979 C  CA    . ASN A 1 660 ? -24.501 -5.032  -4.424  1.00 165.80 ? 763  ASN A CA    1 
ATOM   4980 C  C     . ASN A 1 660 ? -25.723 -4.293  -3.894  1.00 158.49 ? 763  ASN A C     1 
ATOM   4981 O  O     . ASN A 1 660 ? -26.397 -3.563  -4.626  1.00 160.92 ? 763  ASN A O     1 
ATOM   4982 C  CB    . ASN A 1 660 ? -23.274 -4.124  -4.369  1.00 192.89 ? 763  ASN A CB    1 
ATOM   4983 C  CG    . ASN A 1 660 ? -21.994 -4.852  -4.727  1.00 193.39 ? 763  ASN A CG    1 
ATOM   4984 O  OD1   . ASN A 1 660 ? -21.853 -6.048  -4.468  1.00 174.52 ? 763  ASN A OD1   1 
ATOM   4985 N  ND2   . ASN A 1 660 ? -21.051 -4.134  -5.326  1.00 207.24 ? 763  ASN A ND2   1 
ATOM   4986 N  N     . LEU A 1 661 ? -26.005 -4.490  -2.610  1.00 155.57 ? 764  LEU A N     1 
ATOM   4987 C  CA    . LEU A 1 661 ? -27.101 -3.797  -1.955  1.00 147.25 ? 764  LEU A CA    1 
ATOM   4988 C  C     . LEU A 1 661 ? -26.682 -2.390  -1.548  1.00 187.56 ? 764  LEU A C     1 
ATOM   4989 O  O     . LEU A 1 661 ? -25.509 -2.120  -1.276  1.00 209.06 ? 764  LEU A O     1 
ATOM   4990 C  CB    . LEU A 1 661 ? -27.568 -4.571  -0.721  1.00 162.12 ? 764  LEU A CB    1 
ATOM   4991 C  CG    . LEU A 1 661 ? -28.524 -5.743  -0.939  1.00 150.91 ? 764  LEU A CG    1 
ATOM   4992 C  CD1   . LEU A 1 661 ? -28.644 -6.571  0.329   1.00 141.34 ? 764  LEU A CD1   1 
ATOM   4993 C  CD2   . LEU A 1 661 ? -29.887 -5.231  -1.369  1.00 151.32 ? 764  LEU A CD2   1 
ATOM   4994 N  N     . ARG A 1 662 ? -27.661 -1.491  -1.508  1.00 183.93 ? 765  ARG A N     1 
ATOM   4995 C  CA    . ARG A 1 662 ? -27.473 -0.119  -1.043  1.00 189.61 ? 765  ARG A CA    1 
ATOM   4996 C  C     . ARG A 1 662 ? -28.467 0.103   0.092   1.00 179.50 ? 765  ARG A C     1 
ATOM   4997 O  O     . ARG A 1 662 ? -29.593 0.556   -0.129  1.00 178.55 ? 765  ARG A O     1 
ATOM   4998 C  CB    . ARG A 1 662 ? -27.660 0.884   -2.179  1.00 178.21 ? 765  ARG A CB    1 
ATOM   4999 C  CG    . ARG A 1 662 ? -26.594 0.784   -3.260  1.00 193.02 ? 765  ARG A CG    1 
ATOM   5000 C  CD    . ARG A 1 662 ? -25.202 0.947   -2.666  1.00 215.83 ? 765  ARG A CD    1 
ATOM   5001 N  NE    . ARG A 1 662 ? -24.151 0.718   -3.649  1.00 202.65 ? 765  ARG A NE    1 
ATOM   5002 C  CZ    . ARG A 1 662 ? -22.852 0.788   -3.388  1.00 219.16 ? 765  ARG A CZ    1 
ATOM   5003 N  NH1   . ARG A 1 662 ? -22.405 1.086   -2.179  1.00 226.46 ? 765  ARG A NH1   1 
ATOM   5004 N  NH2   . ARG A 1 662 ? -21.980 0.553   -4.365  1.00 207.89 ? 765  ARG A NH2   1 
ATOM   5005 N  N     . LEU A 1 663 ? -28.040 -0.223  1.314   1.00 164.39 ? 766  LEU A N     1 
ATOM   5006 C  CA    . LEU A 1 663 ? -28.919 -0.172  2.476   1.00 153.01 ? 766  LEU A CA    1 
ATOM   5007 C  C     . LEU A 1 663 ? -29.315 1.246   2.866   1.00 188.17 ? 766  LEU A C     1 
ATOM   5008 O  O     . LEU A 1 663 ? -30.243 1.409   3.665   1.00 195.07 ? 766  LEU A O     1 
ATOM   5009 C  CB    . LEU A 1 663 ? -28.251 -0.864  3.665   1.00 151.13 ? 766  LEU A CB    1 
ATOM   5010 C  CG    . LEU A 1 663 ? -27.747 -2.288  3.422   1.00 155.61 ? 766  LEU A CG    1 
ATOM   5011 C  CD1   . LEU A 1 663 ? -27.166 -2.879  4.698   1.00 176.63 ? 766  LEU A CD1   1 
ATOM   5012 C  CD2   . LEU A 1 663 ? -28.860 -3.169  2.877   1.00 159.38 ? 766  LEU A CD2   1 
ATOM   5013 N  N     . GLU A 1 664 ? -28.641 2.268   2.331   1.00 202.64 ? 767  GLU A N     1 
ATOM   5014 C  CA    . GLU A 1 664 ? -28.994 3.640   2.680   1.00 194.01 ? 767  GLU A CA    1 
ATOM   5015 C  C     . GLU A 1 664 ? -30.347 4.039   2.103   1.00 195.03 ? 767  GLU A C     1 
ATOM   5016 O  O     . GLU A 1 664 ? -31.024 4.908   2.664   1.00 200.20 ? 767  GLU A O     1 
ATOM   5017 C  CB    . GLU A 1 664 ? -27.904 4.606   2.212   1.00 183.67 ? 767  GLU A CB    1 
ATOM   5018 C  CG    . GLU A 1 664 ? -27.431 4.398   0.780   1.00 181.10 ? 767  GLU A CG    1 
ATOM   5019 C  CD    . GLU A 1 664 ? -26.301 3.390   0.673   1.00 180.93 ? 767  GLU A CD    1 
ATOM   5020 O  OE1   . GLU A 1 664 ? -25.983 2.737   1.689   1.00 186.79 ? 767  GLU A OE1   1 
ATOM   5021 O  OE2   . GLU A 1 664 ? -25.728 3.254   -0.428  1.00 197.76 ? 767  GLU A OE2   1 
ATOM   5022 N  N     . GLU A 1 665 ? -30.760 3.421   0.995   1.00 204.41 ? 768  GLU A N     1 
ATOM   5023 C  CA    . GLU A 1 665 ? -32.076 3.676   0.425   1.00 198.20 ? 768  GLU A CA    1 
ATOM   5024 C  C     . GLU A 1 665 ? -33.096 2.594   0.755   1.00 186.78 ? 768  GLU A C     1 
ATOM   5025 O  O     . GLU A 1 665 ? -34.299 2.840   0.615   1.00 176.30 ? 768  GLU A O     1 
ATOM   5026 C  CB    . GLU A 1 665 ? -31.985 3.824   -1.100  1.00 189.46 ? 768  GLU A CB    1 
ATOM   5027 C  CG    . GLU A 1 665 ? -31.256 5.072   -1.571  1.00 188.40 ? 768  GLU A CG    1 
ATOM   5028 C  CD    . GLU A 1 665 ? -29.767 4.850   -1.737  1.00 193.27 ? 768  GLU A CD    1 
ATOM   5029 O  OE1   . GLU A 1 665 ? -29.338 3.678   -1.742  1.00 198.56 ? 768  GLU A OE1   1 
ATOM   5030 O  OE2   . GLU A 1 665 ? -29.026 5.848   -1.863  1.00 191.01 ? 768  GLU A OE2   1 
ATOM   5031 N  N     . CYS A 1 666 ? -32.651 1.415   1.184   1.00 184.98 ? 769  CYS A N     1 
ATOM   5032 C  CA    . CYS A 1 666 ? -33.577 0.347   1.538   1.00 188.24 ? 769  CYS A CA    1 
ATOM   5033 C  C     . CYS A 1 666 ? -34.365 0.727   2.785   1.00 190.53 ? 769  CYS A C     1 
ATOM   5034 O  O     . CYS A 1 666 ? -33.786 1.074   3.819   1.00 197.36 ? 769  CYS A O     1 
ATOM   5035 C  CB    . CYS A 1 666 ? -32.821 -0.961  1.763   1.00 183.64 ? 769  CYS A CB    1 
ATOM   5036 S  SG    . CYS A 1 666 ? -31.995 -1.610  0.292   1.00 160.28 ? 769  CYS A SG    1 
ATOM   5037 N  N     . ARG A 1 667 ? -35.690 0.658   2.686   1.00 164.16 ? 770  ARG A N     1 
ATOM   5038 C  CA    . ARG A 1 667 ? -36.568 1.066   3.772   1.00 170.52 ? 770  ARG A CA    1 
ATOM   5039 C  C     . ARG A 1 667 ? -37.849 0.246   3.701   1.00 159.59 ? 770  ARG A C     1 
ATOM   5040 O  O     . ARG A 1 667 ? -38.037 -0.576  2.800   1.00 143.20 ? 770  ARG A O     1 
ATOM   5041 C  CB    . ARG A 1 667 ? -36.871 2.565   3.697   1.00 175.43 ? 770  ARG A CB    1 
ATOM   5042 C  CG    . ARG A 1 667 ? -37.689 2.949   2.475   1.00 161.34 ? 770  ARG A CG    1 
ATOM   5043 C  CD    . ARG A 1 667 ? -37.867 4.451   2.360   1.00 172.22 ? 770  ARG A CD    1 
ATOM   5044 N  NE    . ARG A 1 667 ? -38.679 4.804   1.202   1.00 163.97 ? 770  ARG A NE    1 
ATOM   5045 C  CZ    . ARG A 1 667 ? -38.210 4.924   -0.033  1.00 167.43 ? 770  ARG A CZ    1 
ATOM   5046 N  NH1   . ARG A 1 667 ? -36.932 4.726   -0.309  1.00 182.86 ? 770  ARG A NH1   1 
ATOM   5047 N  NH2   . ARG A 1 667 ? -39.046 5.250   -1.015  1.00 144.76 ? 770  ARG A NH2   1 
ATOM   5048 N  N     . ILE A 1 668 ? -38.738 0.483   4.662   1.00 179.21 ? 771  ILE A N     1 
ATOM   5049 C  CA    . ILE A 1 668 ? -40.046 -0.157  4.714   1.00 162.93 ? 771  ILE A CA    1 
ATOM   5050 C  C     . ILE A 1 668 ? -41.105 0.914   4.487   1.00 163.82 ? 771  ILE A C     1 
ATOM   5051 O  O     . ILE A 1 668 ? -41.058 1.986   5.103   1.00 177.94 ? 771  ILE A O     1 
ATOM   5052 C  CB    . ILE A 1 668 ? -40.263 -0.893  6.049   1.00 164.23 ? 771  ILE A CB    1 
ATOM   5053 C  CG1   . ILE A 1 668 ? -41.694 -1.424  6.150   1.00 161.98 ? 771  ILE A CG1   1 
ATOM   5054 C  CG2   . ILE A 1 668 ? -39.919 0.006   7.232   1.00 209.42 ? 771  ILE A CG2   1 
ATOM   5055 C  CD1   . ILE A 1 668 ? -41.926 -2.302  7.359   1.00 177.46 ? 771  ILE A CD1   1 
ATOM   5056 N  N     . MET A 1 669 ? -42.046 0.630   3.592   1.00 164.45 ? 772  MET A N     1 
ATOM   5057 C  CA    . MET A 1 669 ? -43.065 1.602   3.235   1.00 151.67 ? 772  MET A CA    1 
ATOM   5058 C  C     . MET A 1 669 ? -44.119 1.719   4.332   1.00 168.62 ? 772  MET A C     1 
ATOM   5059 O  O     . MET A 1 669 ? -44.266 0.846   5.192   1.00 179.11 ? 772  MET A O     1 
ATOM   5060 C  CB    . MET A 1 669 ? -43.734 1.221   1.915   1.00 157.40 ? 772  MET A CB    1 
ATOM   5061 C  CG    . MET A 1 669 ? -42.845 1.386   0.698   1.00 159.39 ? 772  MET A CG    1 
ATOM   5062 S  SD    . MET A 1 669 ? -43.695 0.938   -0.826  1.00 169.56 ? 772  MET A SD    1 
ATOM   5063 C  CE    . MET A 1 669 ? -42.571 1.615   -2.042  1.00 158.45 ? 772  MET A CE    1 
ATOM   5064 N  N     . SER A 1 670 ? -44.860 2.827   4.289   1.00 170.41 ? 773  SER A N     1 
ATOM   5065 C  CA    . SER A 1 670 ? -45.971 3.076   5.198   1.00 197.36 ? 773  SER A CA    1 
ATOM   5066 C  C     . SER A 1 670 ? -47.322 2.834   4.532   1.00 195.49 ? 773  SER A C     1 
ATOM   5067 O  O     . SER A 1 670 ? -48.325 3.444   4.918   1.00 183.79 ? 773  SER A O     1 
ATOM   5068 C  CB    . SER A 1 670 ? -45.895 4.499   5.751   1.00 174.28 ? 773  SER A CB    1 
ATOM   5069 O  OG    . SER A 1 670 ? -45.911 5.455   4.705   1.00 164.57 ? 773  SER A OG    1 
ATOM   5070 N  N     . SER A 1 671 ? -47.364 1.955   3.535   1.00 195.06 ? 774  SER A N     1 
ATOM   5071 C  CA    . SER A 1 671 ? -48.590 1.650   2.814   1.00 199.85 ? 774  SER A CA    1 
ATOM   5072 C  C     . SER A 1 671 ? -49.257 0.430   3.451   1.00 206.88 ? 774  SER A C     1 
ATOM   5073 O  O     . SER A 1 671 ? -48.994 0.096   4.610   1.00 213.02 ? 774  SER A O     1 
ATOM   5074 C  CB    . SER A 1 671 ? -48.280 1.445   1.327   1.00 199.94 ? 774  SER A CB    1 
ATOM   5075 O  OG    . SER A 1 671 ? -47.643 2.583   0.775   1.00 207.31 ? 774  SER A OG    1 
ATOM   5076 N  N     . ALA A 1 672 ? -50.126 -0.249  2.706   1.00 200.48 ? 775  ALA A N     1 
ATOM   5077 C  CA    . ALA A 1 672 ? -50.788 -1.437  3.224   1.00 198.17 ? 775  ALA A CA    1 
ATOM   5078 C  C     . ALA A 1 672 ? -49.805 -2.598  3.313   1.00 196.57 ? 775  ALA A C     1 
ATOM   5079 O  O     . ALA A 1 672 ? -48.984 -2.807  2.415   1.00 196.79 ? 775  ALA A O     1 
ATOM   5080 C  CB    . ALA A 1 672 ? -51.972 -1.817  2.336   1.00 190.62 ? 775  ALA A CB    1 
ATOM   5081 N  N     . LYS A 1 673 ? -49.880 -3.339  4.422   1.00 206.94 ? 776  LYS A N     1 
ATOM   5082 C  CA    . LYS A 1 673 ? -49.031 -4.499  4.684   1.00 212.43 ? 776  LYS A CA    1 
ATOM   5083 C  C     . LYS A 1 673 ? -47.555 -4.124  4.782   1.00 198.69 ? 776  LYS A C     1 
ATOM   5084 O  O     . LYS A 1 673 ? -46.702 -4.999  4.960   1.00 216.39 ? 776  LYS A O     1 
ATOM   5085 C  CB    . LYS A 1 673 ? -49.234 -5.572  3.609   1.00 190.58 ? 776  LYS A CB    1 
ATOM   5086 N  N     . ARG A 1 674 ? -47.249 -2.827  4.674   1.00 164.43 ? 777  ARG A N     1 
ATOM   5087 C  CA    . ARG A 1 674 ? -45.903 -2.280  4.799   1.00 159.69 ? 777  ARG A CA    1 
ATOM   5088 C  C     . ARG A 1 674 ? -44.929 -2.981  3.857   1.00 163.04 ? 777  ARG A C     1 
ATOM   5089 O  O     . ARG A 1 674 ? -44.133 -3.819  4.299   1.00 168.85 ? 777  ARG A O     1 
ATOM   5090 C  CB    . ARG A 1 674 ? -45.422 -2.391  6.247   1.00 185.87 ? 777  ARG A CB    1 
ATOM   5091 C  CG    . ARG A 1 674 ? -46.401 -1.817  7.259   1.00 185.70 ? 777  ARG A CG    1 
ATOM   5092 C  CD    . ARG A 1 674 ? -45.879 -1.938  8.680   1.00 181.82 ? 777  ARG A CD    1 
ATOM   5093 N  NE    . ARG A 1 674 ? -44.642 -1.191  8.872   1.00 197.72 ? 777  ARG A NE    1 
ATOM   5094 C  CZ    . ARG A 1 674 ? -44.583 0.111   9.115   1.00 204.73 ? 777  ARG A CZ    1 
ATOM   5095 N  NH1   . ARG A 1 674 ? -45.678 0.850   9.192   1.00 202.57 ? 777  ARG A NH1   1 
ATOM   5096 N  NH2   . ARG A 1 674 ? -43.396 0.687   9.282   1.00 212.97 ? 777  ARG A NH2   1 
ATOM   5097 N  N     . PRO A 1 675 ? -44.960 -2.671  2.562   1.00 160.75 ? 778  PRO A N     1 
ATOM   5098 C  CA    . PRO A 1 675 ? -44.027 -3.306  1.625   1.00 143.96 ? 778  PRO A CA    1 
ATOM   5099 C  C     . PRO A 1 675 ? -42.596 -2.857  1.881   1.00 142.01 ? 778  PRO A C     1 
ATOM   5100 O  O     . PRO A 1 675 ? -42.327 -1.899  2.608   1.00 172.74 ? 778  PRO A O     1 
ATOM   5101 C  CB    . PRO A 1 675 ? -44.520 -2.840  0.250   1.00 135.20 ? 778  PRO A CB    1 
ATOM   5102 C  CG    . PRO A 1 675 ? -45.916 -2.335  0.481   1.00 151.98 ? 778  PRO A CG    1 
ATOM   5103 C  CD    . PRO A 1 675 ? -45.915 -1.788  1.873   1.00 167.86 ? 778  PRO A CD    1 
ATOM   5104 N  N     . LEU A 1 676 ? -41.664 -3.575  1.260   1.00 122.24 ? 779  LEU A N     1 
ATOM   5105 C  CA    . LEU A 1 676 ? -40.239 -3.305  1.396   1.00 137.04 ? 779  LEU A CA    1 
ATOM   5106 C  C     . LEU A 1 676 ? -39.721 -2.676  0.110   1.00 152.72 ? 779  LEU A C     1 
ATOM   5107 O  O     . LEU A 1 676 ? -39.751 -3.310  -0.951  1.00 156.32 ? 779  LEU A O     1 
ATOM   5108 C  CB    . LEU A 1 676 ? -39.463 -4.583  1.715   1.00 122.40 ? 779  LEU A CB    1 
ATOM   5109 C  CG    . LEU A 1 676 ? -39.735 -5.232  3.072   1.00 127.94 ? 779  LEU A CG    1 
ATOM   5110 C  CD1   . LEU A 1 676 ? -38.757 -6.369  3.318   1.00 159.87 ? 779  LEU A CD1   1 
ATOM   5111 C  CD2   . LEU A 1 676 ? -39.656 -4.200  4.186   1.00 145.39 ? 779  LEU A CD2   1 
ATOM   5112 N  N     . TRP A 1 677 ? -39.250 -1.436  0.208   1.00 149.65 ? 780  TRP A N     1 
ATOM   5113 C  CA    . TRP A 1 677 ? -38.610 -0.752  -0.911  1.00 154.56 ? 780  TRP A CA    1 
ATOM   5114 C  C     . TRP A 1 677 ? -37.133 -1.130  -0.906  1.00 157.88 ? 780  TRP A C     1 
ATOM   5115 O  O     . TRP A 1 677 ? -36.397 -0.778  0.022   1.00 159.04 ? 780  TRP A O     1 
ATOM   5116 C  CB    . TRP A 1 677 ? -38.799 0.758   -0.801  1.00 161.13 ? 780  TRP A CB    1 
ATOM   5117 C  CG    . TRP A 1 677 ? -38.451 1.510   -2.051  1.00 157.98 ? 780  TRP A CG    1 
ATOM   5118 C  CD1   . TRP A 1 677 ? -39.314 1.931   -3.021  1.00 165.11 ? 780  TRP A CD1   1 
ATOM   5119 C  CD2   . TRP A 1 677 ? -37.146 1.934   -2.466  1.00 166.70 ? 780  TRP A CD2   1 
ATOM   5120 N  NE1   . TRP A 1 677 ? -38.629 2.589   -4.013  1.00 149.81 ? 780  TRP A NE1   1 
ATOM   5121 C  CE2   . TRP A 1 677 ? -37.296 2.604   -3.696  1.00 158.15 ? 780  TRP A CE2   1 
ATOM   5122 C  CE3   . TRP A 1 677 ? -35.867 1.811   -1.917  1.00 186.61 ? 780  TRP A CE3   1 
ATOM   5123 C  CZ2   . TRP A 1 677 ? -36.216 3.150   -4.384  1.00 159.03 ? 780  TRP A CZ2   1 
ATOM   5124 C  CZ3   . TRP A 1 677 ? -34.796 2.352   -2.603  1.00 196.09 ? 780  TRP A CZ3   1 
ATOM   5125 C  CH2   . TRP A 1 677 ? -34.977 3.013   -3.824  1.00 179.37 ? 780  TRP A CH2   1 
ATOM   5126 N  N     . LEU A 1 678 ? -36.701 -1.850  -1.935  1.00 154.96 ? 781  LEU A N     1 
ATOM   5127 C  CA    . LEU A 1 678 ? -35.349 -2.381  -2.009  1.00 136.91 ? 781  LEU A CA    1 
ATOM   5128 C  C     . LEU A 1 678 ? -34.562 -1.687  -3.113  1.00 130.47 ? 781  LEU A C     1 
ATOM   5129 O  O     . LEU A 1 678 ? -35.127 -1.068  -4.018  1.00 143.95 ? 781  LEU A O     1 
ATOM   5130 C  CB    . LEU A 1 678 ? -35.376 -3.895  -2.245  1.00 151.02 ? 781  LEU A CB    1 
ATOM   5131 C  CG    . LEU A 1 678 ? -36.257 -4.685  -1.273  1.00 163.03 ? 781  LEU A CG    1 
ATOM   5132 C  CD1   . LEU A 1 678 ? -36.261 -6.167  -1.616  1.00 165.29 ? 781  LEU A CD1   1 
ATOM   5133 C  CD2   . LEU A 1 678 ? -35.807 -4.465  0.164   1.00 124.07 ? 781  LEU A CD2   1 
ATOM   5134 N  N     . ASN A 1 679 ? -33.238 -1.799  -3.025  1.00 144.46 ? 782  ASN A N     1 
ATOM   5135 C  CA    . ASN A 1 679 ? -32.340 -1.134  -3.958  1.00 143.68 ? 782  ASN A CA    1 
ATOM   5136 C  C     . ASN A 1 679 ? -31.122 -2.016  -4.187  1.00 132.13 ? 782  ASN A C     1 
ATOM   5137 O  O     . ASN A 1 679 ? -30.600 -2.620  -3.247  1.00 146.35 ? 782  ASN A O     1 
ATOM   5138 C  CB    . ASN A 1 679 ? -31.915 0.243   -3.428  1.00 152.00 ? 782  ASN A CB    1 
ATOM   5139 C  CG    . ASN A 1 679 ? -31.270 1.113   -4.494  1.00 154.95 ? 782  ASN A CG    1 
ATOM   5140 O  OD1   . ASN A 1 679 ? -30.502 0.635   -5.327  1.00 165.25 ? 782  ASN A OD1   1 
ATOM   5141 N  ND2   . ASN A 1 679 ? -31.584 2.403   -4.469  1.00 166.44 ? 782  ASN A ND2   1 
ATOM   5142 N  N     . TRP A 1 680 ? -30.674 -2.081  -5.440  1.00 140.46 ? 783  TRP A N     1 
ATOM   5143 C  CA    . TRP A 1 680 ? -29.513 -2.875  -5.818  1.00 151.07 ? 783  TRP A CA    1 
ATOM   5144 C  C     . TRP A 1 680 ? -28.626 -2.055  -6.745  1.00 154.98 ? 783  TRP A C     1 
ATOM   5145 O  O     . TRP A 1 680 ? -28.935 -0.911  -7.091  1.00 167.89 ? 783  TRP A O     1 
ATOM   5146 C  CB    . TRP A 1 680 ? -29.926 -4.188  -6.494  1.00 147.55 ? 783  TRP A CB    1 
ATOM   5147 C  CG    . TRP A 1 680 ? -30.200 -5.306  -5.541  1.00 149.46 ? 783  TRP A CG    1 
ATOM   5148 C  CD1   . TRP A 1 680 ? -29.283 -6.140  -4.972  1.00 152.70 ? 783  TRP A CD1   1 
ATOM   5149 C  CD2   . TRP A 1 680 ? -31.480 -5.723  -5.053  1.00 153.38 ? 783  TRP A CD2   1 
ATOM   5150 N  NE1   . TRP A 1 680 ? -29.911 -7.048  -4.156  1.00 141.14 ? 783  TRP A NE1   1 
ATOM   5151 C  CE2   . TRP A 1 680 ? -31.261 -6.814  -4.188  1.00 146.63 ? 783  TRP A CE2   1 
ATOM   5152 C  CE3   . TRP A 1 680 ? -32.789 -5.279  -5.261  1.00 154.62 ? 783  TRP A CE3   1 
ATOM   5153 C  CZ2   . TRP A 1 680 ? -32.301 -7.466  -3.532  1.00 154.40 ? 783  TRP A CZ2   1 
ATOM   5154 C  CZ3   . TRP A 1 680 ? -33.820 -5.929  -4.611  1.00 158.74 ? 783  TRP A CZ3   1 
ATOM   5155 C  CH2   . TRP A 1 680 ? -33.570 -7.010  -3.756  1.00 157.64 ? 783  TRP A CH2   1 
ATOM   5156 N  N     . GLU A 1 681 ? -27.512 -2.655  -7.149  1.00 157.15 ? 784  GLU A N     1 
ATOM   5157 C  CA    . GLU A 1 681 ? -26.592 -2.067  -8.108  1.00 162.26 ? 784  GLU A CA    1 
ATOM   5158 C  C     . GLU A 1 681 ? -26.592 -2.883  -9.394  1.00 156.51 ? 784  GLU A C     1 
ATOM   5159 O  O     . GLU A 1 681 ? -27.036 -4.034  -9.427  1.00 157.86 ? 784  GLU A O     1 
ATOM   5160 C  CB    . GLU A 1 681 ? -25.170 -1.993  -7.538  1.00 178.75 ? 784  GLU A CB    1 
ATOM   5161 C  CG    . GLU A 1 681 ? -25.011 -1.077  -6.332  1.00 183.16 ? 784  GLU A CG    1 
ATOM   5162 C  CD    . GLU A 1 681 ? -24.896 0.390   -6.711  1.00 212.42 ? 784  GLU A CD    1 
ATOM   5163 O  OE1   . GLU A 1 681 ? -25.768 0.895   -7.450  1.00 209.78 ? 784  GLU A OE1   1 
ATOM   5164 O  OE2   . GLU A 1 681 ? -23.925 1.040   -6.271  1.00 224.00 ? 784  GLU A OE2   1 
ATOM   5165 N  N     . ASN A 1 682 ? -26.086 -2.266  -10.462 1.00 157.73 ? 785  ASN A N     1 
ATOM   5166 C  CA    . ASN A 1 682 ? -25.943 -2.944  -11.741 1.00 146.08 ? 785  ASN A CA    1 
ATOM   5167 C  C     . ASN A 1 682 ? -24.480 -3.321  -11.928 1.00 149.31 ? 785  ASN A C     1 
ATOM   5168 O  O     . ASN A 1 682 ? -23.670 -2.466  -12.318 1.00 162.10 ? 785  ASN A O     1 
ATOM   5169 C  CB    . ASN A 1 682 ? -26.423 -2.050  -12.887 1.00 154.54 ? 785  ASN A CB    1 
ATOM   5170 C  CG    . ASN A 1 682 ? -26.371 -2.747  -14.233 1.00 152.45 ? 785  ASN A CG    1 
ATOM   5171 O  OD1   . ASN A 1 682 ? -26.336 -3.975  -14.310 1.00 154.53 ? 785  ASN A OD1   1 
ATOM   5172 N  ND2   . ASN A 1 682 ? -26.367 -1.963  -15.306 1.00 164.37 ? 785  ASN A ND2   1 
ATOM   5173 N  N     . PRO A 1 683 ? -24.086 -4.572  -11.668 1.00 127.70 ? 786  PRO A N     1 
ATOM   5174 C  CA    . PRO A 1 683 ? -22.669 -4.946  -11.787 1.00 130.42 ? 786  PRO A CA    1 
ATOM   5175 C  C     . PRO A 1 683 ? -22.142 -4.949  -13.213 1.00 146.69 ? 786  PRO A C     1 
ATOM   5176 O  O     . PRO A 1 683 ? -20.977 -5.309  -13.418 1.00 151.15 ? 786  PRO A O     1 
ATOM   5177 C  CB    . PRO A 1 683 ? -22.632 -6.358  -11.184 1.00 134.27 ? 786  PRO A CB    1 
ATOM   5178 C  CG    . PRO A 1 683 ? -24.009 -6.884  -11.385 1.00 128.59 ? 786  PRO A CG    1 
ATOM   5179 C  CD    . PRO A 1 683 ? -24.925 -5.703  -11.235 1.00 140.96 ? 786  PRO A CD    1 
ATOM   5180 N  N     . ASP A 1 684 ? -22.953 -4.573  -14.199 1.00 136.01 ? 787  ASP A N     1 
ATOM   5181 C  CA    . ASP A 1 684 ? -22.464 -4.466  -15.565 1.00 144.12 ? 787  ASP A CA    1 
ATOM   5182 C  C     . ASP A 1 684 ? -21.413 -3.367  -15.656 1.00 152.32 ? 787  ASP A C     1 
ATOM   5183 O  O     . ASP A 1 684 ? -21.540 -2.310  -15.031 1.00 144.28 ? 787  ASP A O     1 
ATOM   5184 C  CB    . ASP A 1 684 ? -23.625 -4.177  -16.521 1.00 138.90 ? 787  ASP A CB    1 
ATOM   5185 C  CG    . ASP A 1 684 ? -23.271 -4.437  -17.977 1.00 144.86 ? 787  ASP A CG    1 
ATOM   5186 O  OD1   . ASP A 1 684 ? -22.124 -4.156  -18.385 1.00 163.12 ? 787  ASP A OD1   1 
ATOM   5187 O  OD2   . ASP A 1 684 ? -24.148 -4.927  -18.720 1.00 144.46 ? 787  ASP A OD2   1 
ATOM   5188 N  N     . ILE A 1 685 ? -20.362 -3.627  -16.437 1.00 147.35 ? 788  ILE A N     1 
ATOM   5189 C  CA    . ILE A 1 685 ? -19.307 -2.638  -16.617 1.00 162.33 ? 788  ILE A CA    1 
ATOM   5190 C  C     . ILE A 1 685 ? -19.816 -1.394  -17.331 1.00 162.80 ? 788  ILE A C     1 
ATOM   5191 O  O     . ILE A 1 685 ? -19.209 -0.323  -17.211 1.00 181.28 ? 788  ILE A O     1 
ATOM   5192 C  CB    . ILE A 1 685 ? -18.120 -3.260  -17.375 1.00 176.17 ? 788  ILE A CB    1 
ATOM   5193 C  CG1   . ILE A 1 685 ? -18.614 -3.989  -18.627 1.00 152.54 ? 788  ILE A CG1   1 
ATOM   5194 C  CG2   . ILE A 1 685 ? -17.346 -4.205  -16.469 1.00 157.52 ? 788  ILE A CG2   1 
ATOM   5195 C  CD1   . ILE A 1 685 ? -17.523 -4.708  -19.386 1.00 153.93 ? 788  ILE A CD1   1 
ATOM   5196 N  N     . MET A 1 686 ? -20.920 -1.505  -18.071 1.00 130.05 ? 789  MET A N     1 
ATOM   5197 C  CA    . MET A 1 686 ? -21.543 -0.372  -18.744 1.00 120.81 ? 789  MET A CA    1 
ATOM   5198 C  C     . MET A 1 686 ? -22.766 0.141   -17.990 1.00 141.98 ? 789  MET A C     1 
ATOM   5199 O  O     . MET A 1 686 ? -23.734 0.595   -18.611 1.00 154.23 ? 789  MET A O     1 
ATOM   5200 C  CB    . MET A 1 686 ? -21.924 -0.752  -20.175 1.00 158.85 ? 789  MET A CB    1 
ATOM   5201 C  CG    . MET A 1 686 ? -20.803 -1.404  -20.964 1.00 133.37 ? 789  MET A CG    1 
ATOM   5202 S  SD    . MET A 1 686 ? -19.410 -0.299  -21.255 1.00 141.56 ? 789  MET A SD    1 
ATOM   5203 C  CE    . MET A 1 686 ? -20.154 0.904   -22.353 1.00 126.97 ? 789  MET A CE    1 
ATOM   5204 N  N     . SER A 1 687 ? -22.740 0.075   -16.657 1.00 133.63 ? 790  SER A N     1 
ATOM   5205 C  CA    . SER A 1 687 ? -23.886 0.496   -15.858 1.00 139.72 ? 790  SER A CA    1 
ATOM   5206 C  C     . SER A 1 687 ? -24.140 1.995   -15.939 1.00 168.66 ? 790  SER A C     1 
ATOM   5207 O  O     . SER A 1 687 ? -25.234 2.443   -15.583 1.00 168.62 ? 790  SER A O     1 
ATOM   5208 C  CB    . SER A 1 687 ? -23.686 0.086   -14.399 1.00 141.79 ? 790  SER A CB    1 
ATOM   5209 O  OG    . SER A 1 687 ? -24.719 0.603   -13.578 1.00 159.08 ? 790  SER A OG    1 
ATOM   5210 N  N     . GLU A 1 688 ? -23.159 2.777   -16.397 1.00 167.52 ? 791  GLU A N     1 
ATOM   5211 C  CA    . GLU A 1 688 ? -23.337 4.223   -16.464 1.00 150.00 ? 791  GLU A CA    1 
ATOM   5212 C  C     . GLU A 1 688 ? -24.335 4.622   -17.545 1.00 158.09 ? 791  GLU A C     1 
ATOM   5213 O  O     . GLU A 1 688 ? -24.977 5.673   -17.436 1.00 145.37 ? 791  GLU A O     1 
ATOM   5214 C  CB    . GLU A 1 688 ? -21.991 4.904   -16.708 1.00 154.20 ? 791  GLU A CB    1 
ATOM   5215 C  CG    . GLU A 1 688 ? -20.876 4.428   -15.788 1.00 176.01 ? 791  GLU A CG    1 
ATOM   5216 C  CD    . GLU A 1 688 ? -21.127 4.771   -14.332 1.00 191.99 ? 791  GLU A CD    1 
ATOM   5217 O  OE1   . GLU A 1 688 ? -21.825 5.771   -14.063 1.00 208.22 ? 791  GLU A OE1   1 
ATOM   5218 O  OE2   . GLU A 1 688 ? -20.626 4.037   -13.454 1.00 173.50 ? 791  GLU A OE2   1 
ATOM   5219 N  N     . LEU A 1 689 ? -24.482 3.802   -18.585 1.00 150.97 ? 792  LEU A N     1 
ATOM   5220 C  CA    . LEU A 1 689 ? -25.377 4.125   -19.689 1.00 139.13 ? 792  LEU A CA    1 
ATOM   5221 C  C     . LEU A 1 689 ? -26.816 3.704   -19.427 1.00 147.00 ? 792  LEU A C     1 
ATOM   5222 O  O     . LEU A 1 689 ? -27.743 4.353   -19.926 1.00 158.23 ? 792  LEU A O     1 
ATOM   5223 C  CB    . LEU A 1 689 ? -24.873 3.472   -20.979 1.00 141.43 ? 792  LEU A CB    1 
ATOM   5224 C  CG    . LEU A 1 689 ? -23.431 3.817   -21.357 1.00 134.00 ? 792  LEU A CG    1 
ATOM   5225 C  CD1   . LEU A 1 689 ? -23.043 3.168   -22.675 1.00 130.39 ? 792  LEU A CD1   1 
ATOM   5226 C  CD2   . LEU A 1 689 ? -23.237 5.325   -21.421 1.00 148.50 ? 792  LEU A CD2   1 
ATOM   5227 N  N     . LEU A 1 690 ? -27.025 2.638   -18.663 1.00 144.09 ? 793  LEU A N     1 
ATOM   5228 C  CA    . LEU A 1 690 ? -28.354 2.192   -18.286 1.00 136.11 ? 793  LEU A CA    1 
ATOM   5229 C  C     . LEU A 1 690 ? -28.635 2.625   -16.846 1.00 160.99 ? 793  LEU A C     1 
ATOM   5230 O  O     . LEU A 1 690 ? -27.904 3.431   -16.263 1.00 196.65 ? 793  LEU A O     1 
ATOM   5231 C  CB    . LEU A 1 690 ? -28.467 0.676   -18.472 1.00 151.41 ? 793  LEU A CB    1 
ATOM   5232 C  CG    . LEU A 1 690 ? -29.861 0.087   -18.711 1.00 150.58 ? 793  LEU A CG    1 
ATOM   5233 C  CD1   . LEU A 1 690 ? -30.413 0.523   -20.060 1.00 116.17 ? 793  LEU A CD1   1 
ATOM   5234 C  CD2   . LEU A 1 690 ? -29.828 -1.426  -18.601 1.00 121.07 ? 793  LEU A CD2   1 
ATOM   5235 N  N     . PHE A 1 691 ? -29.706 2.093   -16.263 1.00 150.88 ? 794  PHE A N     1 
ATOM   5236 C  CA    . PHE A 1 691 ? -30.032 2.399   -14.879 1.00 152.82 ? 794  PHE A CA    1 
ATOM   5237 C  C     . PHE A 1 691 ? -28.982 1.815   -13.939 1.00 156.12 ? 794  PHE A C     1 
ATOM   5238 O  O     . PHE A 1 691 ? -28.319 0.822   -14.250 1.00 148.91 ? 794  PHE A O     1 
ATOM   5239 C  CB    . PHE A 1 691 ? -31.415 1.857   -14.521 1.00 165.37 ? 794  PHE A CB    1 
ATOM   5240 C  CG    . PHE A 1 691 ? -32.534 2.473   -15.313 1.00 193.36 ? 794  PHE A CG    1 
ATOM   5241 C  CD1   . PHE A 1 691 ? -33.151 3.635   -14.878 1.00 183.74 ? 794  PHE A CD1   1 
ATOM   5242 C  CD2   . PHE A 1 691 ? -32.971 1.889   -16.491 1.00 202.10 ? 794  PHE A CD2   1 
ATOM   5243 C  CE1   . PHE A 1 691 ? -34.182 4.204   -15.604 1.00 166.85 ? 794  PHE A CE1   1 
ATOM   5244 C  CE2   . PHE A 1 691 ? -34.001 2.453   -17.221 1.00 175.99 ? 794  PHE A CE2   1 
ATOM   5245 C  CZ    . PHE A 1 691 ? -34.607 3.612   -16.776 1.00 159.27 ? 794  PHE A CZ    1 
ATOM   5246 N  N     . GLN A 1 692 ? -28.833 2.450   -12.776 1.00 165.94 ? 795  GLN A N     1 
ATOM   5247 C  CA    . GLN A 1 692 ? -27.876 2.014   -11.771 1.00 158.39 ? 795  GLN A CA    1 
ATOM   5248 C  C     . GLN A 1 692 ? -28.511 1.539   -10.475 1.00 155.42 ? 795  GLN A C     1 
ATOM   5249 O  O     . GLN A 1 692 ? -27.852 0.816   -9.719  1.00 165.37 ? 795  GLN A O     1 
ATOM   5250 C  CB    . GLN A 1 692 ? -26.887 3.144   -11.443 1.00 154.44 ? 795  GLN A CB    1 
ATOM   5251 C  CG    . GLN A 1 692 ? -25.994 3.544   -12.603 1.00 165.28 ? 795  GLN A CG    1 
ATOM   5252 C  CD    . GLN A 1 692 ? -25.080 4.704   -12.261 1.00 181.72 ? 795  GLN A CD    1 
ATOM   5253 O  OE1   . GLN A 1 692 ? -25.335 5.453   -11.318 1.00 177.40 ? 795  GLN A OE1   1 
ATOM   5254 N  NE2   . GLN A 1 692 ? -24.006 4.856   -13.026 1.00 174.28 ? 795  GLN A NE2   1 
ATOM   5255 N  N     . ASN A 1 693 ? -29.754 1.918   -10.193 1.00 174.15 ? 796  ASN A N     1 
ATOM   5256 C  CA    . ASN A 1 693 ? -30.445 1.535   -8.965  1.00 184.96 ? 796  ASN A CA    1 
ATOM   5257 C  C     . ASN A 1 693 ? -31.628 0.646   -9.336  1.00 173.47 ? 796  ASN A C     1 
ATOM   5258 O  O     . ASN A 1 693 ? -32.690 1.141   -9.724  1.00 166.79 ? 796  ASN A O     1 
ATOM   5259 C  CB    . ASN A 1 693 ? -30.899 2.769   -8.188  1.00 185.17 ? 796  ASN A CB    1 
ATOM   5260 C  CG    . ASN A 1 693 ? -29.737 3.579   -7.645  1.00 180.59 ? 796  ASN A CG    1 
ATOM   5261 O  OD1   . ASN A 1 693 ? -28.590 3.393   -8.053  1.00 173.12 ? 796  ASN A OD1   1 
ATOM   5262 N  ND2   . ASN A 1 693 ? -30.029 4.485   -6.720  1.00 175.60 ? 796  ASN A ND2   1 
ATOM   5263 N  N     . ASN A 1 694 ? -31.439 -0.666  -9.220  1.00 148.25 ? 797  ASN A N     1 
ATOM   5264 C  CA    . ASN A 1 694 ? -32.521 -1.625  -9.435  1.00 138.00 ? 797  ASN A CA    1 
ATOM   5265 C  C     . ASN A 1 694 ? -33.424 -1.600  -8.210  1.00 134.74 ? 797  ASN A C     1 
ATOM   5266 O  O     . ASN A 1 694 ? -33.078 -2.133  -7.154  1.00 166.66 ? 797  ASN A O     1 
ATOM   5267 C  CB    . ASN A 1 694 ? -31.967 -3.021  -9.694  1.00 157.10 ? 797  ASN A CB    1 
ATOM   5268 C  CG    . ASN A 1 694 ? -31.856 -3.338  -11.172 1.00 127.90 ? 797  ASN A CG    1 
ATOM   5269 O  OD1   . ASN A 1 694 ? -32.690 -2.915  -11.972 1.00 114.14 ? 797  ASN A OD1   1 
ATOM   5270 N  ND2   . ASN A 1 694 ? -30.823 -4.086  -11.542 1.00 143.95 ? 797  ASN A ND2   1 
ATOM   5271 N  N     . GLU A 1 695 ? -34.588 -0.975  -8.351  1.00 130.74 ? 798  GLU A N     1 
ATOM   5272 C  CA    . GLU A 1 695 ? -35.523 -0.779  -7.253  1.00 137.58 ? 798  GLU A CA    1 
ATOM   5273 C  C     . GLU A 1 695 ? -36.719 -1.703  -7.437  1.00 143.11 ? 798  GLU A C     1 
ATOM   5274 O  O     . GLU A 1 695 ? -37.351 -1.701  -8.498  1.00 151.10 ? 798  GLU A O     1 
ATOM   5275 C  CB    . GLU A 1 695 ? -35.973 0.682   -7.188  1.00 158.15 ? 798  GLU A CB    1 
ATOM   5276 C  CG    . GLU A 1 695 ? -34.821 1.674   -7.270  1.00 163.03 ? 798  GLU A CG    1 
ATOM   5277 C  CD    . GLU A 1 695 ? -35.283 3.092   -7.538  1.00 175.47 ? 798  GLU A CD    1 
ATOM   5278 O  OE1   . GLU A 1 695 ? -36.509 3.318   -7.610  1.00 183.15 ? 798  GLU A OE1   1 
ATOM   5279 O  OE2   . GLU A 1 695 ? -34.419 3.983   -7.676  1.00 185.66 ? 798  GLU A OE2   1 
ATOM   5280 N  N     . ILE A 1 696 ? -37.018 -2.495  -6.409  1.00 141.87 ? 799  ILE A N     1 
ATOM   5281 C  CA    . ILE A 1 696 ? -38.096 -3.477  -6.450  1.00 138.21 ? 799  ILE A CA    1 
ATOM   5282 C  C     . ILE A 1 696 ? -38.904 -3.365  -5.165  1.00 140.97 ? 799  ILE A C     1 
ATOM   5283 O  O     . ILE A 1 696 ? -38.332 -3.292  -4.072  1.00 153.88 ? 799  ILE A O     1 
ATOM   5284 C  CB    . ILE A 1 696 ? -37.562 -4.914  -6.626  1.00 115.32 ? 799  ILE A CB    1 
ATOM   5285 C  CG1   . ILE A 1 696 ? -36.797 -5.062  -7.944  1.00 139.28 ? 799  ILE A CG1   1 
ATOM   5286 C  CG2   . ILE A 1 696 ? -38.700 -5.917  -6.570  1.00 117.95 ? 799  ILE A CG2   1 
ATOM   5287 C  CD1   . ILE A 1 696 ? -35.298 -4.877  -7.814  1.00 137.83 ? 799  ILE A CD1   1 
ATOM   5288 N  N     . ILE A 1 697 ? -40.228 -3.352  -5.297  1.00 140.97 ? 800  ILE A N     1 
ATOM   5289 C  CA    . ILE A 1 697 ? -41.130 -3.341  -4.151  1.00 149.88 ? 800  ILE A CA    1 
ATOM   5290 C  C     . ILE A 1 697 ? -41.540 -4.774  -3.840  1.00 151.61 ? 800  ILE A C     1 
ATOM   5291 O  O     . ILE A 1 697 ? -41.951 -5.521  -4.736  1.00 139.14 ? 800  ILE A O     1 
ATOM   5292 C  CB    . ILE A 1 697 ? -42.363 -2.465  -4.428  1.00 150.88 ? 800  ILE A CB    1 
ATOM   5293 C  CG1   . ILE A 1 697 ? -41.948 -1.013  -4.665  1.00 140.50 ? 800  ILE A CG1   1 
ATOM   5294 C  CG2   . ILE A 1 697 ? -43.353 -2.551  -3.276  1.00 138.11 ? 800  ILE A CG2   1 
ATOM   5295 C  CD1   . ILE A 1 697 ? -43.070 -0.138  -5.182  1.00 145.58 ? 800  ILE A CD1   1 
ATOM   5296 N  N     . PHE A 1 698 ? -41.429 -5.160  -2.572  1.00 152.32 ? 801  PHE A N     1 
ATOM   5297 C  CA    . PHE A 1 698 ? -41.794 -6.499  -2.113  1.00 120.86 ? 801  PHE A CA    1 
ATOM   5298 C  C     . PHE A 1 698 ? -43.098 -6.384  -1.326  1.00 136.34 ? 801  PHE A C     1 
ATOM   5299 O  O     . PHE A 1 698 ? -43.095 -6.125  -0.122  1.00 163.55 ? 801  PHE A O     1 
ATOM   5300 C  CB    . PHE A 1 698 ? -40.678 -7.115  -1.272  1.00 113.84 ? 801  PHE A CB    1 
ATOM   5301 C  CG    . PHE A 1 698 ? -40.915 -8.553  -0.910  1.00 128.86 ? 801  PHE A CG    1 
ATOM   5302 C  CD1   . PHE A 1 698 ? -40.496 -9.570  -1.751  1.00 122.74 ? 801  PHE A CD1   1 
ATOM   5303 C  CD2   . PHE A 1 698 ? -41.557 -8.889  0.271   1.00 137.02 ? 801  PHE A CD2   1 
ATOM   5304 C  CE1   . PHE A 1 698 ? -40.713 -10.894 -1.422  1.00 123.20 ? 801  PHE A CE1   1 
ATOM   5305 C  CE2   . PHE A 1 698 ? -41.778 -10.212 0.605   1.00 134.37 ? 801  PHE A CE2   1 
ATOM   5306 C  CZ    . PHE A 1 698 ? -41.355 -11.215 -0.243  1.00 119.66 ? 801  PHE A CZ    1 
ATOM   5307 N  N     . LYS A 1 699 ? -44.216 -6.578  -2.021  1.00 140.46 ? 802  LYS A N     1 
ATOM   5308 C  CA    . LYS A 1 699 ? -45.540 -6.528  -1.409  1.00 140.11 ? 802  LYS A CA    1 
ATOM   5309 C  C     . LYS A 1 699 ? -45.855 -7.900  -0.823  1.00 126.98 ? 802  LYS A C     1 
ATOM   5310 O  O     . LYS A 1 699 ? -46.010 -8.877  -1.562  1.00 137.00 ? 802  LYS A O     1 
ATOM   5311 C  CB    . LYS A 1 699 ? -46.589 -6.111  -2.436  1.00 147.04 ? 802  LYS A CB    1 
ATOM   5312 C  CG    . LYS A 1 699 ? -47.364 -4.856  -2.077  1.00 136.61 ? 802  LYS A CG    1 
ATOM   5313 C  CD    . LYS A 1 699 ? -48.258 -5.083  -0.872  1.00 163.33 ? 802  LYS A CD    1 
ATOM   5314 C  CE    . LYS A 1 699 ? -49.143 -3.876  -0.613  1.00 183.88 ? 802  LYS A CE    1 
ATOM   5315 N  NZ    . LYS A 1 699 ? -50.044 -4.092  0.552   1.00 191.96 ? 802  LYS A NZ    1 
ATOM   5316 N  N     . ASN A 1 700 ? -45.953 -7.973  0.504   1.00 134.43 ? 803  ASN A N     1 
ATOM   5317 C  CA    . ASN A 1 700 ? -46.165 -9.244  1.192   1.00 125.79 ? 803  ASN A CA    1 
ATOM   5318 C  C     . ASN A 1 700 ? -47.648 -9.581  1.326   1.00 148.76 ? 803  ASN A C     1 
ATOM   5319 O  O     . ASN A 1 700 ? -48.118 -10.578 0.770   1.00 132.04 ? 803  ASN A O     1 
ATOM   5320 C  CB    . ASN A 1 700 ? -45.496 -9.209  2.571   1.00 144.21 ? 803  ASN A CB    1 
ATOM   5321 C  CG    . ASN A 1 700 ? -45.729 -10.480 3.369   1.00 163.63 ? 803  ASN A CG    1 
ATOM   5322 O  OD1   . ASN A 1 700 ? -45.956 -11.550 2.806   1.00 155.30 ? 803  ASN A OD1   1 
ATOM   5323 N  ND2   . ASN A 1 700 ? -45.677 -10.365 4.690   1.00 180.65 ? 803  ASN A ND2   1 
ATOM   5324 N  N     . GLY A 1 701 ? -48.393 -8.759  2.062   1.00 172.50 ? 804  GLY A N     1 
ATOM   5325 C  CA    . GLY A 1 701 ? -49.779 -9.053  2.370   1.00 155.27 ? 804  GLY A CA    1 
ATOM   5326 C  C     . GLY A 1 701 ? -50.718 -9.067  1.180   1.00 159.97 ? 804  GLY A C     1 
ATOM   5327 O  O     . GLY A 1 701 ? -51.392 -10.070 0.929   1.00 133.12 ? 804  GLY A O     1 
ATOM   5328 N  N     . ASP A 1 702 ? -50.774 -7.960  0.444   1.00 180.87 ? 805  ASP A N     1 
ATOM   5329 C  CA    . ASP A 1 702 ? -51.722 -7.837  -0.655  1.00 174.07 ? 805  ASP A CA    1 
ATOM   5330 C  C     . ASP A 1 702 ? -51.357 -8.771  -1.802  1.00 170.37 ? 805  ASP A C     1 
ATOM   5331 O  O     . ASP A 1 702 ? -50.180 -8.960  -2.124  1.00 170.23 ? 805  ASP A O     1 
ATOM   5332 C  CB    . ASP A 1 702 ? -51.772 -6.392  -1.150  1.00 185.15 ? 805  ASP A CB    1 
ATOM   5333 C  CG    . ASP A 1 702 ? -52.671 -6.219  -2.358  1.00 206.65 ? 805  ASP A CG    1 
ATOM   5334 O  OD1   . ASP A 1 702 ? -53.893 -6.443  -2.229  1.00 217.26 ? 805  ASP A OD1   1 
ATOM   5335 O  OD2   . ASP A 1 702 ? -52.156 -5.857  -3.437  1.00 204.46 ? 805  ASP A OD2   1 
ATOM   5336 N  N     . ASP A 1 703 ? -52.380 -9.357  -2.419  1.00 147.11 ? 806  ASP A N     1 
ATOM   5337 C  CA    . ASP A 1 703 ? -52.169 -10.231 -3.564  1.00 149.82 ? 806  ASP A CA    1 
ATOM   5338 C  C     . ASP A 1 703 ? -51.768 -9.415  -4.787  1.00 163.20 ? 806  ASP A C     1 
ATOM   5339 O  O     . ASP A 1 703 ? -52.356 -8.369  -5.077  1.00 155.79 ? 806  ASP A O     1 
ATOM   5340 C  CB    . ASP A 1 703 ? -53.438 -11.032 -3.858  1.00 141.81 ? 806  ASP A CB    1 
ATOM   5341 C  CG    . ASP A 1 703 ? -53.249 -12.042 -4.974  1.00 152.00 ? 806  ASP A CG    1 
ATOM   5342 O  OD1   . ASP A 1 703 ? -52.087 -12.345 -5.319  1.00 157.86 ? 806  ASP A OD1   1 
ATOM   5343 O  OD2   . ASP A 1 703 ? -54.266 -12.532 -5.510  1.00 137.52 ? 806  ASP A OD2   1 
ATOM   5344 N  N     . LEU A 1 704 ? -50.758 -9.901  -5.510  1.00 161.14 ? 807  LEU A N     1 
ATOM   5345 C  CA    . LEU A 1 704 ? -50.246 -9.227  -6.696  1.00 153.29 ? 807  LEU A CA    1 
ATOM   5346 C  C     . LEU A 1 704 ? -50.582 -9.984  -7.978  1.00 139.42 ? 807  LEU A C     1 
ATOM   5347 O  O     . LEU A 1 704 ? -49.845 -9.904  -8.964  1.00 143.28 ? 807  LEU A O     1 
ATOM   5348 C  CB    . LEU A 1 704 ? -48.738 -9.013  -6.585  1.00 143.09 ? 807  LEU A CB    1 
ATOM   5349 C  CG    . LEU A 1 704 ? -48.257 -8.104  -5.453  1.00 157.80 ? 807  LEU A CG    1 
ATOM   5350 C  CD1   . LEU A 1 704 ? -46.792 -7.751  -5.647  1.00 152.00 ? 807  LEU A CD1   1 
ATOM   5351 C  CD2   . LEU A 1 704 ? -49.109 -6.846  -5.361  1.00 143.83 ? 807  LEU A CD2   1 
ATOM   5352 N  N     . ARG A 1 705 ? -51.688 -10.726 -7.979  1.00 139.82 ? 808  ARG A N     1 
ATOM   5353 C  CA    . ARG A 1 705 ? -52.157 -11.381 -9.193  1.00 134.59 ? 808  ARG A CA    1 
ATOM   5354 C  C     . ARG A 1 705 ? -53.082 -10.493 -10.008 1.00 137.15 ? 808  ARG A C     1 
ATOM   5355 O  O     . ARG A 1 705 ? -53.146 -10.636 -11.235 1.00 123.29 ? 808  ARG A O     1 
ATOM   5356 C  CB    . ARG A 1 705 ? -52.872 -12.689 -8.847  1.00 149.73 ? 808  ARG A CB    1 
ATOM   5357 C  CG    . ARG A 1 705 ? -51.946 -13.767 -8.320  1.00 136.49 ? 808  ARG A CG    1 
ATOM   5358 C  CD    . ARG A 1 705 ? -52.720 -14.967 -7.807  1.00 139.24 ? 808  ARG A CD    1 
ATOM   5359 N  NE    . ARG A 1 705 ? -51.822 -16.004 -7.315  1.00 171.01 ? 808  ARG A NE    1 
ATOM   5360 C  CZ    . ARG A 1 705 ? -51.262 -15.999 -6.114  1.00 176.87 ? 808  ARG A CZ    1 
ATOM   5361 N  NH1   . ARG A 1 705 ? -51.492 -15.026 -5.247  1.00 184.70 ? 808  ARG A NH1   1 
ATOM   5362 N  NH2   . ARG A 1 705 ? -50.446 -16.992 -5.774  1.00 160.44 ? 808  ARG A NH2   1 
ATOM   5363 N  N     . GLN A 1 706 ? -53.801 -9.579  -9.352  1.00 157.10 ? 809  GLN A N     1 
ATOM   5364 C  CA    . GLN A 1 706 ? -54.636 -8.631  -10.078 1.00 136.16 ? 809  GLN A CA    1 
ATOM   5365 C  C     . GLN A 1 706 ? -53.793 -7.639  -10.867 1.00 126.22 ? 809  GLN A C     1 
ATOM   5366 O  O     . GLN A 1 706 ? -54.227 -7.156  -11.919 1.00 130.52 ? 809  GLN A O     1 
ATOM   5367 C  CB    . GLN A 1 706 ? -55.557 -7.888  -9.109  1.00 151.76 ? 809  GLN A CB    1 
ATOM   5368 C  CG    . GLN A 1 706 ? -56.519 -8.778  -8.329  1.00 160.62 ? 809  GLN A CG    1 
ATOM   5369 C  CD    . GLN A 1 706 ? -55.868 -9.455  -7.136  1.00 166.93 ? 809  GLN A CD    1 
ATOM   5370 O  OE1   . GLN A 1 706 ? -54.675 -9.284  -6.885  1.00 169.33 ? 809  GLN A OE1   1 
ATOM   5371 N  NE2   . GLN A 1 706 ? -56.652 -10.227 -6.394  1.00 158.73 ? 809  GLN A NE2   1 
ATOM   5372 N  N     . ASP A 1 707 ? -52.589 -7.330  -10.381 1.00 126.80 ? 810  ASP A N     1 
ATOM   5373 C  CA    . ASP A 1 707 ? -51.732 -6.378  -11.079 1.00 134.06 ? 810  ASP A CA    1 
ATOM   5374 C  C     . ASP A 1 707 ? -51.169 -6.975  -12.363 1.00 127.85 ? 810  ASP A C     1 
ATOM   5375 O  O     . ASP A 1 707 ? -51.104 -6.292  -13.391 1.00 126.94 ? 810  ASP A O     1 
ATOM   5376 C  CB    . ASP A 1 707 ? -50.601 -5.919  -10.159 1.00 145.00 ? 810  ASP A CB    1 
ATOM   5377 C  CG    . ASP A 1 707 ? -51.102 -5.116  -8.975  1.00 157.24 ? 810  ASP A CG    1 
ATOM   5378 O  OD1   . ASP A 1 707 ? -52.041 -4.313  -9.154  1.00 142.13 ? 810  ASP A OD1   1 
ATOM   5379 O  OD2   . ASP A 1 707 ? -50.558 -5.288  -7.864  1.00 175.54 ? 810  ASP A OD2   1 
ATOM   5380 N  N     . MET A 1 708 ? -50.761 -8.247  -12.325 1.00 123.73 ? 811  MET A N     1 
ATOM   5381 C  CA    . MET A 1 708 ? -50.148 -8.864  -13.499 1.00 122.82 ? 811  MET A CA    1 
ATOM   5382 C  C     . MET A 1 708 ? -51.091 -8.851  -14.694 1.00 101.15 ? 811  MET A C     1 
ATOM   5383 O  O     . MET A 1 708 ? -50.677 -8.541  -15.817 1.00 111.05 ? 811  MET A O     1 
ATOM   5384 C  CB    . MET A 1 708 ? -49.717 -10.295 -13.184 1.00 116.41 ? 811  MET A CB    1 
ATOM   5385 C  CG    . MET A 1 708 ? -48.552 -10.407 -12.221 1.00 98.60  ? 811  MET A CG    1 
ATOM   5386 S  SD    . MET A 1 708 ? -47.874 -12.076 -12.207 1.00 118.15 ? 811  MET A SD    1 
ATOM   5387 C  CE    . MET A 1 708 ? -49.352 -13.038 -11.897 1.00 150.07 ? 811  MET A CE    1 
ATOM   5388 N  N     . LEU A 1 709 ? -52.364 -9.187  -14.474 1.00 112.67 ? 812  LEU A N     1 
ATOM   5389 C  CA    . LEU A 1 709 ? -53.317 -9.208  -15.579 1.00 111.14 ? 812  LEU A CA    1 
ATOM   5390 C  C     . LEU A 1 709 ? -53.577 -7.803  -16.110 1.00 130.00 ? 812  LEU A C     1 
ATOM   5391 O  O     . LEU A 1 709 ? -53.741 -7.612  -17.321 1.00 127.31 ? 812  LEU A O     1 
ATOM   5392 C  CB    . LEU A 1 709 ? -54.621 -9.867  -15.136 1.00 89.33  ? 812  LEU A CB    1 
ATOM   5393 C  CG    . LEU A 1 709 ? -55.635 -10.132 -16.250 1.00 105.78 ? 812  LEU A CG    1 
ATOM   5394 C  CD1   . LEU A 1 709 ? -55.045 -11.067 -17.294 1.00 104.76 ? 812  LEU A CD1   1 
ATOM   5395 C  CD2   . LEU A 1 709 ? -56.920 -10.701 -15.680 1.00 109.86 ? 812  LEU A CD2   1 
ATOM   5396 N  N     . THR A 1 710 ? -53.614 -6.807  -15.222 1.00 113.17 ? 813  THR A N     1 
ATOM   5397 C  CA    . THR A 1 710 ? -53.818 -5.434  -15.670 1.00 99.25  ? 813  THR A CA    1 
ATOM   5398 C  C     . THR A 1 710 ? -52.566 -4.881  -16.340 1.00 131.22 ? 813  THR A C     1 
ATOM   5399 O  O     . THR A 1 710 ? -52.650 -4.248  -17.398 1.00 130.82 ? 813  THR A O     1 
ATOM   5400 C  CB    . THR A 1 710 ? -54.231 -4.550  -14.493 1.00 121.73 ? 813  THR A CB    1 
ATOM   5401 O  OG1   . THR A 1 710 ? -55.388 -5.107  -13.859 1.00 116.56 ? 813  THR A OG1   1 
ATOM   5402 C  CG2   . THR A 1 710 ? -54.555 -3.143  -14.974 1.00 113.35 ? 813  THR A CG2   1 
ATOM   5403 N  N     . LEU A 1 711 ? -51.394 -5.114  -15.742 1.00 123.60 ? 814  LEU A N     1 
ATOM   5404 C  CA    . LEU A 1 711 ? -50.147 -4.656  -16.343 1.00 108.09 ? 814  LEU A CA    1 
ATOM   5405 C  C     . LEU A 1 711 ? -49.849 -5.350  -17.667 1.00 112.71 ? 814  LEU A C     1 
ATOM   5406 O  O     . LEU A 1 711 ? -49.062 -4.827  -18.462 1.00 119.97 ? 814  LEU A O     1 
ATOM   5407 C  CB    . LEU A 1 711 ? -48.980 -4.866  -15.374 1.00 125.06 ? 814  LEU A CB    1 
ATOM   5408 C  CG    . LEU A 1 711 ? -48.627 -3.730  -14.405 1.00 119.22 ? 814  LEU A CG    1 
ATOM   5409 C  CD1   . LEU A 1 711 ? -48.282 -2.463  -15.168 1.00 136.42 ? 814  LEU A CD1   1 
ATOM   5410 C  CD2   . LEU A 1 711 ? -49.740 -3.459  -13.405 1.00 133.81 ? 814  LEU A CD2   1 
ATOM   5411 N  N     . GLN A 1 712 ? -50.457 -6.511  -17.922 1.00 108.18 ? 815  GLN A N     1 
ATOM   5412 C  CA    . GLN A 1 712 ? -50.241 -7.196  -19.191 1.00 124.42 ? 815  GLN A CA    1 
ATOM   5413 C  C     . GLN A 1 712 ? -51.180 -6.676  -20.272 1.00 122.76 ? 815  GLN A C     1 
ATOM   5414 O  O     . GLN A 1 712 ? -50.762 -6.478  -21.418 1.00 136.92 ? 815  GLN A O     1 
ATOM   5415 C  CB    . GLN A 1 712 ? -50.420 -8.704  -19.019 1.00 131.17 ? 815  GLN A CB    1 
ATOM   5416 C  CG    . GLN A 1 712 ? -50.132 -9.504  -20.278 1.00 136.23 ? 815  GLN A CG    1 
ATOM   5417 C  CD    . GLN A 1 712 ? -50.865 -10.830 -20.309 1.00 113.71 ? 815  GLN A CD    1 
ATOM   5418 O  OE1   . GLN A 1 712 ? -51.914 -10.988 -19.683 1.00 99.39  ? 815  GLN A OE1   1 
ATOM   5419 N  NE2   . GLN A 1 712 ? -50.318 -11.792 -21.043 1.00 103.61 ? 815  GLN A NE2   1 
ATOM   5420 N  N     . ILE A 1 713 ? -52.452 -6.459  -19.926 1.00 124.45 ? 816  ILE A N     1 
ATOM   5421 C  CA    . ILE A 1 713 ? -53.413 -5.944  -20.897 1.00 120.00 ? 816  ILE A CA    1 
ATOM   5422 C  C     . ILE A 1 713 ? -53.021 -4.539  -21.339 1.00 115.47 ? 816  ILE A C     1 
ATOM   5423 O  O     . ILE A 1 713 ? -53.187 -4.170  -22.509 1.00 111.38 ? 816  ILE A O     1 
ATOM   5424 C  CB    . ILE A 1 713 ? -54.838 -5.992  -20.310 1.00 121.32 ? 816  ILE A CB    1 
ATOM   5425 C  CG1   . ILE A 1 713 ? -55.557 -7.276  -20.740 1.00 129.94 ? 816  ILE A CG1   1 
ATOM   5426 C  CG2   . ILE A 1 713 ? -55.648 -4.769  -20.717 1.00 119.83 ? 816  ILE A CG2   1 
ATOM   5427 C  CD1   . ILE A 1 713 ? -54.921 -8.552  -20.229 1.00 136.96 ? 816  ILE A CD1   1 
ATOM   5428 N  N     . ILE A 1 714 ? -52.478 -3.741  -20.416 1.00 117.26 ? 817  ILE A N     1 
ATOM   5429 C  CA    . ILE A 1 714 ? -52.000 -2.406  -20.768 1.00 114.86 ? 817  ILE A CA    1 
ATOM   5430 C  C     . ILE A 1 714 ? -50.913 -2.492  -21.832 1.00 117.24 ? 817  ILE A C     1 
ATOM   5431 O  O     . ILE A 1 714 ? -50.876 -1.686  -22.771 1.00 123.30 ? 817  ILE A O     1 
ATOM   5432 C  CB    . ILE A 1 714 ? -51.510 -1.668  -19.507 1.00 131.23 ? 817  ILE A CB    1 
ATOM   5433 C  CG1   . ILE A 1 714 ? -52.698 -1.263  -18.631 1.00 101.93 ? 817  ILE A CG1   1 
ATOM   5434 C  CG2   . ILE A 1 714 ? -50.677 -0.451  -19.878 1.00 129.65 ? 817  ILE A CG2   1 
ATOM   5435 C  CD1   . ILE A 1 714 ? -52.302 -0.539  -17.364 1.00 107.38 ? 817  ILE A CD1   1 
ATOM   5436 N  N     . ARG A 1 715 ? -50.017 -3.475  -21.712 1.00 105.99 ? 818  ARG A N     1 
ATOM   5437 C  CA    . ARG A 1 715 ? -49.009 -3.680  -22.747 1.00 112.71 ? 818  ARG A CA    1 
ATOM   5438 C  C     . ARG A 1 715 ? -49.647 -4.136  -24.053 1.00 110.36 ? 818  ARG A C     1 
ATOM   5439 O  O     . ARG A 1 715 ? -49.242 -3.696  -25.136 1.00 140.82 ? 818  ARG A O     1 
ATOM   5440 C  CB    . ARG A 1 715 ? -47.964 -4.691  -22.274 1.00 105.12 ? 818  ARG A CB    1 
ATOM   5441 C  CG    . ARG A 1 715 ? -47.034 -5.174  -23.377 1.00 128.21 ? 818  ARG A CG    1 
ATOM   5442 C  CD    . ARG A 1 715 ? -45.837 -5.926  -22.821 1.00 110.77 ? 818  ARG A CD    1 
ATOM   5443 N  NE    . ARG A 1 715 ? -44.963 -5.054  -22.045 1.00 107.37 ? 818  ARG A NE    1 
ATOM   5444 C  CZ    . ARG A 1 715 ? -43.755 -5.394  -21.617 1.00 142.78 ? 818  ARG A CZ    1 
ATOM   5445 N  NH1   . ARG A 1 715 ? -43.238 -6.583  -21.878 1.00 136.34 ? 818  ARG A NH1   1 
ATOM   5446 N  NH2   . ARG A 1 715 ? -43.046 -4.516  -20.912 1.00 138.90 ? 818  ARG A NH2   1 
ATOM   5447 N  N     . ILE A 1 716 ? -50.650 -5.012  -23.973 1.00 113.60 ? 819  ILE A N     1 
ATOM   5448 C  CA    . ILE A 1 716 ? -51.334 -5.466  -25.179 1.00 116.09 ? 819  ILE A CA    1 
ATOM   5449 C  C     . ILE A 1 716 ? -52.154 -4.335  -25.785 1.00 100.02 ? 819  ILE A C     1 
ATOM   5450 O  O     . ILE A 1 716 ? -52.208 -4.178  -27.011 1.00 98.36  ? 819  ILE A O     1 
ATOM   5451 C  CB    . ILE A 1 716 ? -52.199 -6.701  -24.867 1.00 102.79 ? 819  ILE A CB    1 
ATOM   5452 C  CG1   . ILE A 1 716 ? -51.325 -7.826  -24.311 1.00 118.61 ? 819  ILE A CG1   1 
ATOM   5453 C  CG2   . ILE A 1 716 ? -52.935 -7.170  -26.112 1.00 91.44  ? 819  ILE A CG2   1 
ATOM   5454 C  CD1   . ILE A 1 716 ? -52.086 -9.082  -23.973 1.00 93.15  ? 819  ILE A CD1   1 
ATOM   5455 N  N     . MET A 1 717 ? -52.800 -3.525  -24.941 1.00 107.37 ? 820  MET A N     1 
ATOM   5456 C  CA    . MET A 1 717 ? -53.524 -2.362  -25.445 1.00 108.08 ? 820  MET A CA    1 
ATOM   5457 C  C     . MET A 1 717 ? -52.584 -1.360  -26.102 1.00 112.73 ? 820  MET A C     1 
ATOM   5458 O  O     . MET A 1 717 ? -52.963 -0.700  -27.076 1.00 122.66 ? 820  MET A O     1 
ATOM   5459 C  CB    . MET A 1 717 ? -54.303 -1.686  -24.315 1.00 104.12 ? 820  MET A CB    1 
ATOM   5460 C  CG    . MET A 1 717 ? -55.560 -2.424  -23.888 1.00 116.72 ? 820  MET A CG    1 
ATOM   5461 S  SD    . MET A 1 717 ? -56.529 -1.503  -22.677 1.00 114.47 ? 820  MET A SD    1 
ATOM   5462 C  CE    . MET A 1 717 ? -57.990 -2.532  -22.558 1.00 107.18 ? 820  MET A CE    1 
ATOM   5463 N  N     . GLU A 1 718 ? -51.359 -1.231  -25.586 1.00 110.96 ? 821  GLU A N     1 
ATOM   5464 C  CA    . GLU A 1 718 ? -50.406 -0.301  -26.181 1.00 112.71 ? 821  GLU A CA    1 
ATOM   5465 C  C     . GLU A 1 718 ? -49.909 -0.808  -27.530 1.00 117.80 ? 821  GLU A C     1 
ATOM   5466 O  O     . GLU A 1 718 ? -49.722 -0.020  -28.464 1.00 109.45 ? 821  GLU A O     1 
ATOM   5467 C  CB    . GLU A 1 718 ? -49.235 -0.065  -25.227 1.00 112.77 ? 821  GLU A CB    1 
ATOM   5468 C  CG    . GLU A 1 718 ? -48.303 1.059   -25.653 1.00 111.42 ? 821  GLU A CG    1 
ATOM   5469 C  CD    . GLU A 1 718 ? -47.156 1.267   -24.683 1.00 123.50 ? 821  GLU A CD    1 
ATOM   5470 O  OE1   . GLU A 1 718 ? -46.929 0.384   -23.829 1.00 138.80 ? 821  GLU A OE1   1 
ATOM   5471 O  OE2   . GLU A 1 718 ? -46.483 2.315   -24.774 1.00 116.58 ? 821  GLU A OE2   1 
ATOM   5472 N  N     . ASN A 1 719 ? -49.695 -2.121  -27.653 1.00 112.98 ? 822  ASN A N     1 
ATOM   5473 C  CA    . ASN A 1 719 ? -49.245 -2.678  -28.925 1.00 113.68 ? 822  ASN A CA    1 
ATOM   5474 C  C     . ASN A 1 719 ? -50.316 -2.544  -30.000 1.00 123.85 ? 822  ASN A C     1 
ATOM   5475 O  O     . ASN A 1 719 ? -50.000 -2.322  -31.174 1.00 110.71 ? 822  ASN A O     1 
ATOM   5476 C  CB    . ASN A 1 719 ? -48.842 -4.142  -28.748 1.00 115.20 ? 822  ASN A CB    1 
ATOM   5477 C  CG    . ASN A 1 719 ? -47.556 -4.302  -27.962 1.00 138.41 ? 822  ASN A CG    1 
ATOM   5478 O  OD1   . ASN A 1 719 ? -46.696 -3.422  -27.972 1.00 112.34 ? 822  ASN A OD1   1 
ATOM   5479 N  ND2   . ASN A 1 719 ? -47.417 -5.432  -27.278 1.00 166.91 ? 822  ASN A ND2   1 
ATOM   5480 N  N     . ILE A 1 720 ? -51.588 -2.679  -29.620 1.00 110.54 ? 823  ILE A N     1 
ATOM   5481 C  CA    . ILE A 1 720 ? -52.670 -2.503  -30.584 1.00 119.78 ? 823  ILE A CA    1 
ATOM   5482 C  C     . ILE A 1 720 ? -52.735 -1.053  -31.049 1.00 111.81 ? 823  ILE A C     1 
ATOM   5483 O  O     . ILE A 1 720 ? -53.016 -0.773  -32.221 1.00 115.95 ? 823  ILE A O     1 
ATOM   5484 C  CB    . ILE A 1 720 ? -54.006 -2.970  -29.976 1.00 117.49 ? 823  ILE A CB    1 
ATOM   5485 C  CG1   . ILE A 1 720 ? -53.964 -4.473  -29.694 1.00 98.01  ? 823  ILE A CG1   1 
ATOM   5486 C  CG2   . ILE A 1 720 ? -55.170 -2.638  -30.899 1.00 124.75 ? 823  ILE A CG2   1 
ATOM   5487 C  CD1   . ILE A 1 720 ? -55.253 -5.024  -29.129 1.00 106.87 ? 823  ILE A CD1   1 
ATOM   5488 N  N     . TRP A 1 721 ? -52.458 -0.110  -30.146 1.00 110.25 ? 824  TRP A N     1 
ATOM   5489 C  CA    . TRP A 1 721 ? -52.505 1.301   -30.513 1.00 125.28 ? 824  TRP A CA    1 
ATOM   5490 C  C     . TRP A 1 721 ? -51.295 1.700   -31.350 1.00 115.32 ? 824  TRP A C     1 
ATOM   5491 O  O     . TRP A 1 721 ? -51.430 2.444   -32.328 1.00 120.84 ? 824  TRP A O     1 
ATOM   5492 C  CB    . TRP A 1 721 ? -52.600 2.164   -29.255 1.00 122.12 ? 824  TRP A CB    1 
ATOM   5493 C  CG    . TRP A 1 721 ? -53.900 2.016   -28.529 1.00 105.69 ? 824  TRP A CG    1 
ATOM   5494 C  CD1   . TRP A 1 721 ? -55.083 1.572   -29.046 1.00 122.61 ? 824  TRP A CD1   1 
ATOM   5495 C  CD2   . TRP A 1 721 ? -54.149 2.305   -27.148 1.00 105.23 ? 824  TRP A CD2   1 
ATOM   5496 N  NE1   . TRP A 1 721 ? -56.055 1.572   -28.073 1.00 118.99 ? 824  TRP A NE1   1 
ATOM   5497 C  CE2   . TRP A 1 721 ? -55.506 2.016   -26.899 1.00 123.90 ? 824  TRP A CE2   1 
ATOM   5498 C  CE3   . TRP A 1 721 ? -53.357 2.780   -26.099 1.00 106.42 ? 824  TRP A CE3   1 
ATOM   5499 C  CZ2   . TRP A 1 721 ? -56.088 2.188   -25.644 1.00 111.66 ? 824  TRP A CZ2   1 
ATOM   5500 C  CZ3   . TRP A 1 721 ? -53.937 2.950   -24.853 1.00 122.26 ? 824  TRP A CZ3   1 
ATOM   5501 C  CH2   . TRP A 1 721 ? -55.289 2.655   -24.637 1.00 105.26 ? 824  TRP A CH2   1 
ATOM   5502 N  N     . GLN A 1 722 ? -50.104 1.220   -30.980 1.00 104.93 ? 825  GLN A N     1 
ATOM   5503 C  CA    . GLN A 1 722 ? -48.904 1.566   -31.736 1.00 97.01  ? 825  GLN A CA    1 
ATOM   5504 C  C     . GLN A 1 722 ? -48.937 0.985   -33.144 1.00 114.26 ? 825  GLN A C     1 
ATOM   5505 O  O     . GLN A 1 722 ? -48.338 1.557   -34.062 1.00 129.42 ? 825  GLN A O     1 
ATOM   5506 C  CB    . GLN A 1 722 ? -47.655 1.086   -30.995 1.00 87.41  ? 825  GLN A CB    1 
ATOM   5507 C  CG    . GLN A 1 722 ? -47.401 1.785   -29.667 1.00 105.99 ? 825  GLN A CG    1 
ATOM   5508 C  CD    . GLN A 1 722 ? -46.966 3.230   -29.830 1.00 111.71 ? 825  GLN A CD    1 
ATOM   5509 O  OE1   . GLN A 1 722 ? -46.566 3.654   -30.915 1.00 128.90 ? 825  GLN A OE1   1 
ATOM   5510 N  NE2   . GLN A 1 722 ? -47.042 3.994   -28.747 1.00 116.33 ? 825  GLN A NE2   1 
ATOM   5511 N  N     . ASN A 1 723 ? -49.623 -0.139  -33.337 1.00 110.35 ? 826  ASN A N     1 
ATOM   5512 C  CA    . ASN A 1 723 ? -49.732 -0.748  -34.656 1.00 102.27 ? 826  ASN A CA    1 
ATOM   5513 C  C     . ASN A 1 723 ? -50.830 -0.124  -35.508 1.00 127.49 ? 826  ASN A C     1 
ATOM   5514 O  O     . ASN A 1 723 ? -50.976 -0.506  -36.674 1.00 145.96 ? 826  ASN A O     1 
ATOM   5515 C  CB    . ASN A 1 723 ? -49.972 -2.255  -34.522 1.00 104.01 ? 826  ASN A CB    1 
ATOM   5516 C  CG    . ASN A 1 723 ? -48.793 -2.980  -33.899 1.00 135.22 ? 826  ASN A CG    1 
ATOM   5517 O  OD1   . ASN A 1 723 ? -47.641 -2.582  -34.074 1.00 112.43 ? 826  ASN A OD1   1 
ATOM   5518 N  ND2   . ASN A 1 723 ? -49.077 -4.049  -33.164 1.00 152.73 ? 826  ASN A ND2   1 
ATOM   5519 N  N     . GLN A 1 724 ? -51.598 0.819   -34.963 1.00 124.62 ? 827  GLN A N     1 
ATOM   5520 C  CA    . GLN A 1 724 ? -52.632 1.514   -35.717 1.00 123.10 ? 827  GLN A CA    1 
ATOM   5521 C  C     . GLN A 1 724 ? -52.371 3.007   -35.859 1.00 136.49 ? 827  GLN A C     1 
ATOM   5522 O  O     . GLN A 1 724 ? -53.158 3.696   -36.519 1.00 160.24 ? 827  GLN A O     1 
ATOM   5523 C  CB    . GLN A 1 724 ? -54.007 1.301   -35.068 1.00 127.74 ? 827  GLN A CB    1 
ATOM   5524 C  CG    . GLN A 1 724 ? -54.542 -0.117  -35.183 1.00 150.21 ? 827  GLN A CG    1 
ATOM   5525 C  CD    . GLN A 1 724 ? -55.979 -0.234  -34.713 1.00 164.44 ? 827  GLN A CD    1 
ATOM   5526 O  OE1   . GLN A 1 724 ? -56.596 0.754   -34.314 1.00 153.48 ? 827  GLN A OE1   1 
ATOM   5527 N  NE2   . GLN A 1 724 ? -56.520 -1.446  -34.760 1.00 163.09 ? 827  GLN A NE2   1 
ATOM   5528 N  N     . GLY A 1 725 ? -51.301 3.527   -35.263 1.00 109.88 ? 828  GLY A N     1 
ATOM   5529 C  CA    . GLY A 1 725 ? -50.959 4.932   -35.361 1.00 99.33  ? 828  GLY A CA    1 
ATOM   5530 C  C     . GLY A 1 725 ? -51.168 5.726   -34.091 1.00 125.96 ? 828  GLY A C     1 
ATOM   5531 O  O     . GLY A 1 725 ? -50.694 6.867   -34.012 1.00 159.40 ? 828  GLY A O     1 
ATOM   5532 N  N     . LEU A 1 726 ? -51.860 5.171   -33.098 1.00 126.38 ? 829  LEU A N     1 
ATOM   5533 C  CA    . LEU A 1 726 ? -52.094 5.865   -31.833 1.00 128.51 ? 829  LEU A CA    1 
ATOM   5534 C  C     . LEU A 1 726 ? -50.829 5.770   -30.989 1.00 122.64 ? 829  LEU A C     1 
ATOM   5535 O  O     . LEU A 1 726 ? -50.523 4.719   -30.421 1.00 136.13 ? 829  LEU A O     1 
ATOM   5536 C  CB    . LEU A 1 726 ? -53.293 5.271   -31.101 1.00 107.44 ? 829  LEU A CB    1 
ATOM   5537 C  CG    . LEU A 1 726 ? -54.700 5.616   -31.603 1.00 126.94 ? 829  LEU A CG    1 
ATOM   5538 C  CD1   . LEU A 1 726 ? -54.841 7.116   -31.832 1.00 121.95 ? 829  LEU A CD1   1 
ATOM   5539 C  CD2   . LEU A 1 726 ? -55.068 4.834   -32.859 1.00 138.15 ? 829  LEU A CD2   1 
ATOM   5540 N  N     . ASP A 1 727 ? -50.089 6.873   -30.902 1.00 107.49 ? 830  ASP A N     1 
ATOM   5541 C  CA    . ASP A 1 727 ? -48.853 6.919   -30.119 1.00 109.41 ? 830  ASP A CA    1 
ATOM   5542 C  C     . ASP A 1 727 ? -49.154 7.312   -28.671 1.00 113.03 ? 830  ASP A C     1 
ATOM   5543 O  O     . ASP A 1 727 ? -48.687 8.324   -28.151 1.00 125.71 ? 830  ASP A O     1 
ATOM   5544 C  CB    . ASP A 1 727 ? -47.856 7.876   -30.763 1.00 123.24 ? 830  ASP A CB    1 
ATOM   5545 C  CG    . ASP A 1 727 ? -46.478 7.799   -30.129 1.00 117.88 ? 830  ASP A CG    1 
ATOM   5546 O  OD1   . ASP A 1 727 ? -46.227 6.850   -29.355 1.00 110.02 ? 830  ASP A OD1   1 
ATOM   5547 O  OD2   . ASP A 1 727 ? -45.647 8.690   -30.401 1.00 138.67 ? 830  ASP A OD2   1 
ATOM   5548 N  N     . LEU A 1 728 ? -49.961 6.477   -28.021 1.00 124.22 ? 831  LEU A N     1 
ATOM   5549 C  CA    . LEU A 1 728 ? -50.321 6.671   -26.618 1.00 121.89 ? 831  LEU A CA    1 
ATOM   5550 C  C     . LEU A 1 728 ? -49.345 5.864   -25.772 1.00 114.41 ? 831  LEU A C     1 
ATOM   5551 O  O     . LEU A 1 728 ? -49.483 4.646   -25.635 1.00 119.44 ? 831  LEU A O     1 
ATOM   5552 C  CB    . LEU A 1 728 ? -51.765 6.252   -26.368 1.00 104.63 ? 831  LEU A CB    1 
ATOM   5553 C  CG    . LEU A 1 728 ? -52.818 6.883   -27.281 1.00 98.16  ? 831  LEU A CG    1 
ATOM   5554 C  CD1   . LEU A 1 728 ? -54.217 6.451   -26.870 1.00 118.19 ? 831  LEU A CD1   1 
ATOM   5555 C  CD2   . LEU A 1 728 ? -52.699 8.399   -27.279 1.00 129.22 ? 831  LEU A CD2   1 
ATOM   5556 N  N     . ARG A 1 729 ? -48.351 6.543   -25.204 1.00 110.44 ? 832  ARG A N     1 
ATOM   5557 C  CA    . ARG A 1 729 ? -47.296 5.865   -24.458 1.00 104.89 ? 832  ARG A CA    1 
ATOM   5558 C  C     . ARG A 1 729 ? -47.845 5.357   -23.131 1.00 119.63 ? 832  ARG A C     1 
ATOM   5559 O  O     . ARG A 1 729 ? -48.073 6.138   -22.201 1.00 110.00 ? 832  ARG A O     1 
ATOM   5560 C  CB    . ARG A 1 729 ? -46.114 6.803   -24.232 1.00 113.16 ? 832  ARG A CB    1 
ATOM   5561 C  CG    . ARG A 1 729 ? -44.963 6.156   -23.475 1.00 106.45 ? 832  ARG A CG    1 
ATOM   5562 C  CD    . ARG A 1 729 ? -43.841 7.143   -23.196 1.00 113.63 ? 832  ARG A CD    1 
ATOM   5563 N  NE    . ARG A 1 729 ? -43.230 7.644   -24.421 1.00 133.13 ? 832  ARG A NE    1 
ATOM   5564 C  CZ    . ARG A 1 729 ? -42.178 8.451   -24.456 1.00 134.53 ? 832  ARG A CZ    1 
ATOM   5565 N  NH1   . ARG A 1 729 ? -41.588 8.866   -23.346 1.00 140.89 ? 832  ARG A NH1   1 
ATOM   5566 N  NH2   . ARG A 1 729 ? -41.705 8.851   -25.633 1.00 125.28 ? 832  ARG A NH2   1 
ATOM   5567 N  N     . MET A 1 730 ? -48.061 4.050   -23.043 1.00 129.24 ? 833  MET A N     1 
ATOM   5568 C  CA    . MET A 1 730 ? -48.416 3.408   -21.789 1.00 107.62 ? 833  MET A CA    1 
ATOM   5569 C  C     . MET A 1 730 ? -47.152 2.931   -21.086 1.00 122.37 ? 833  MET A C     1 
ATOM   5570 O  O     . MET A 1 730 ? -46.133 2.652   -21.723 1.00 116.16 ? 833  MET A O     1 
ATOM   5571 C  CB    . MET A 1 730 ? -49.359 2.228   -22.030 1.00 106.22 ? 833  MET A CB    1 
ATOM   5572 C  CG    . MET A 1 730 ? -50.561 2.557   -22.900 1.00 118.14 ? 833  MET A CG    1 
ATOM   5573 S  SD    . MET A 1 730 ? -51.706 3.714   -22.126 1.00 120.94 ? 833  MET A SD    1 
ATOM   5574 C  CE    . MET A 1 730 ? -52.345 2.715   -20.784 1.00 125.47 ? 833  MET A CE    1 
ATOM   5575 N  N     . LEU A 1 731 ? -47.222 2.847   -19.757 1.00 123.82 ? 834  LEU A N     1 
ATOM   5576 C  CA    . LEU A 1 731 ? -46.100 2.399   -18.933 1.00 114.73 ? 834  LEU A CA    1 
ATOM   5577 C  C     . LEU A 1 731 ? -46.498 1.114   -18.221 1.00 123.43 ? 834  LEU A C     1 
ATOM   5578 O  O     . LEU A 1 731 ? -46.968 1.147   -17.072 1.00 128.76 ? 834  LEU A O     1 
ATOM   5579 C  CB    . LEU A 1 731 ? -45.679 3.476   -17.935 1.00 125.35 ? 834  LEU A CB    1 
ATOM   5580 C  CG    . LEU A 1 731 ? -44.424 3.160   -17.118 1.00 121.18 ? 834  LEU A CG    1 
ATOM   5581 C  CD1   . LEU A 1 731 ? -43.272 2.778   -18.034 1.00 128.49 ? 834  LEU A CD1   1 
ATOM   5582 C  CD2   . LEU A 1 731 ? -44.041 4.340   -16.240 1.00 136.44 ? 834  LEU A CD2   1 
ATOM   5583 N  N     . PRO A 1 732 ? -46.334 -0.042  -18.864 1.00 123.79 ? 835  PRO A N     1 
ATOM   5584 C  CA    . PRO A 1 732 ? -46.625 -1.308  -18.185 1.00 109.03 ? 835  PRO A CA    1 
ATOM   5585 C  C     . PRO A 1 732 ? -45.411 -1.840  -17.440 1.00 98.24  ? 835  PRO A C     1 
ATOM   5586 O  O     . PRO A 1 732 ? -44.645 -2.646  -17.978 1.00 106.81 ? 835  PRO A O     1 
ATOM   5587 C  CB    . PRO A 1 732 ? -47.039 -2.234  -19.337 1.00 107.80 ? 835  PRO A CB    1 
ATOM   5588 C  CG    . PRO A 1 732 ? -46.439 -1.610  -20.592 1.00 115.91 ? 835  PRO A CG    1 
ATOM   5589 C  CD    . PRO A 1 732 ? -45.861 -0.259  -20.240 1.00 136.86 ? 835  PRO A CD    1 
ATOM   5590 N  N     . TYR A 1 733 ? -45.228 -1.388  -16.202 1.00 111.25 ? 836  TYR A N     1 
ATOM   5591 C  CA    . TYR A 1 733 ? -44.080 -1.798  -15.411 1.00 122.61 ? 836  TYR A CA    1 
ATOM   5592 C  C     . TYR A 1 733 ? -44.166 -3.281  -15.059 1.00 128.98 ? 836  TYR A C     1 
ATOM   5593 O  O     . TYR A 1 733 ? -45.233 -3.900  -15.100 1.00 146.57 ? 836  TYR A O     1 
ATOM   5594 C  CB    . TYR A 1 733 ? -43.973 -0.954  -14.139 1.00 120.57 ? 836  TYR A CB    1 
ATOM   5595 C  CG    . TYR A 1 733 ? -45.250 -0.874  -13.331 1.00 119.04 ? 836  TYR A CG    1 
ATOM   5596 C  CD1   . TYR A 1 733 ? -46.182 0.129   -13.568 1.00 129.59 ? 836  TYR A CD1   1 
ATOM   5597 C  CD2   . TYR A 1 733 ? -45.519 -1.793  -12.326 1.00 126.00 ? 836  TYR A CD2   1 
ATOM   5598 C  CE1   . TYR A 1 733 ? -47.349 0.209   -12.833 1.00 128.24 ? 836  TYR A CE1   1 
ATOM   5599 C  CE2   . TYR A 1 733 ? -46.684 -1.721  -11.585 1.00 132.75 ? 836  TYR A CE2   1 
ATOM   5600 C  CZ    . TYR A 1 733 ? -47.594 -0.718  -11.842 1.00 126.57 ? 836  TYR A CZ    1 
ATOM   5601 O  OH    . TYR A 1 733 ? -48.755 -0.640  -11.108 1.00 141.76 ? 836  TYR A OH    1 
ATOM   5602 N  N     . GLY A 1 734 ? -43.015 -3.849  -14.710 1.00 131.55 ? 837  GLY A N     1 
ATOM   5603 C  CA    . GLY A 1 734 ? -42.955 -5.267  -14.419 1.00 140.85 ? 837  GLY A CA    1 
ATOM   5604 C  C     . GLY A 1 734 ? -43.637 -5.618  -13.110 1.00 123.48 ? 837  GLY A C     1 
ATOM   5605 O  O     . GLY A 1 734 ? -43.615 -4.859  -12.140 1.00 120.64 ? 837  GLY A O     1 
ATOM   5606 N  N     . CYS A 1 735 ? -44.254 -6.797  -13.091 1.00 133.36 ? 838  CYS A N     1 
ATOM   5607 C  CA    . CYS A 1 735 ? -44.927 -7.298  -11.900 1.00 143.08 ? 838  CYS A CA    1 
ATOM   5608 C  C     . CYS A 1 735 ? -45.002 -8.814  -11.993 1.00 136.79 ? 838  CYS A C     1 
ATOM   5609 O  O     . CYS A 1 735 ? -45.418 -9.350  -13.024 1.00 142.22 ? 838  CYS A O     1 
ATOM   5610 C  CB    . CYS A 1 735 ? -46.329 -6.695  -11.758 1.00 140.16 ? 838  CYS A CB    1 
ATOM   5611 S  SG    . CYS A 1 735 ? -47.200 -7.175  -10.248 1.00 123.60 ? 838  CYS A SG    1 
ATOM   5612 N  N     . LEU A 1 736 ? -44.599 -9.496  -10.923 1.00 124.77 ? 839  LEU A N     1 
ATOM   5613 C  CA    . LEU A 1 736 ? -44.563 -10.954 -10.897 1.00 126.41 ? 839  LEU A CA    1 
ATOM   5614 C  C     . LEU A 1 736 ? -45.048 -11.433 -9.538  1.00 117.90 ? 839  LEU A C     1 
ATOM   5615 O  O     . LEU A 1 736 ? -44.453 -11.093 -8.511  1.00 133.20 ? 839  LEU A O     1 
ATOM   5616 C  CB    . LEU A 1 736 ? -43.150 -11.475 -11.177 1.00 114.63 ? 839  LEU A CB    1 
ATOM   5617 C  CG    . LEU A 1 736 ? -42.988 -12.980 -11.390 1.00 131.55 ? 839  LEU A CG    1 
ATOM   5618 C  CD1   . LEU A 1 736 ? -43.621 -13.406 -12.706 1.00 135.26 ? 839  LEU A CD1   1 
ATOM   5619 C  CD2   . LEU A 1 736 ? -41.520 -13.372 -11.343 1.00 121.61 ? 839  LEU A CD2   1 
ATOM   5620 N  N     . SER A 1 737 ? -46.122 -12.218 -9.533  1.00 129.62 ? 840  SER A N     1 
ATOM   5621 C  CA    . SER A 1 737 ? -46.649 -12.774 -8.295  1.00 143.46 ? 840  SER A CA    1 
ATOM   5622 C  C     . SER A 1 737 ? -45.863 -14.017 -7.902  1.00 131.41 ? 840  SER A C     1 
ATOM   5623 O  O     . SER A 1 737 ? -45.555 -14.867 -8.742  1.00 114.68 ? 840  SER A O     1 
ATOM   5624 C  CB    . SER A 1 737 ? -48.131 -13.114 -8.448  1.00 130.68 ? 840  SER A CB    1 
ATOM   5625 O  OG    . SER A 1 737 ? -48.668 -13.614 -7.235  1.00 130.94 ? 840  SER A OG    1 
ATOM   5626 N  N     . ILE A 1 738 ? -45.539 -14.118 -6.615  1.00 138.60 ? 841  ILE A N     1 
ATOM   5627 C  CA    . ILE A 1 738 ? -44.724 -15.204 -6.083  1.00 149.83 ? 841  ILE A CA    1 
ATOM   5628 C  C     . ILE A 1 738 ? -45.508 -15.907 -4.984  1.00 141.77 ? 841  ILE A C     1 
ATOM   5629 O  O     . ILE A 1 738 ? -46.061 -15.251 -4.094  1.00 161.50 ? 841  ILE A O     1 
ATOM   5630 C  CB    . ILE A 1 738 ? -43.377 -14.689 -5.542  1.00 141.81 ? 841  ILE A CB    1 
ATOM   5631 C  CG1   . ILE A 1 738 ? -42.680 -13.808 -6.579  1.00 140.69 ? 841  ILE A CG1   1 
ATOM   5632 C  CG2   . ILE A 1 738 ? -42.482 -15.853 -5.144  1.00 163.14 ? 841  ILE A CG2   1 
ATOM   5633 C  CD1   . ILE A 1 738 ? -42.377 -14.516 -7.879  1.00 147.35 ? 841  ILE A CD1   1 
ATOM   5634 N  N     . GLY A 1 739 ? -45.560 -17.234 -5.055  1.00 105.40 ? 842  GLY A N     1 
ATOM   5635 C  CA    . GLY A 1 739 ? -46.126 -18.016 -3.966  1.00 171.46 ? 842  GLY A CA    1 
ATOM   5636 C  C     . GLY A 1 739 ? -47.563 -17.640 -3.658  1.00 173.87 ? 842  GLY A C     1 
ATOM   5637 O  O     . GLY A 1 739 ? -48.404 -17.506 -4.553  1.00 169.20 ? 842  GLY A O     1 
ATOM   5638 N  N     . ASP A 1 740 ? -47.848 -17.458 -2.369  1.00 160.44 ? 843  ASP A N     1 
ATOM   5639 C  CA    . ASP A 1 740 ? -49.200 -17.171 -1.906  1.00 158.11 ? 843  ASP A CA    1 
ATOM   5640 C  C     . ASP A 1 740 ? -49.614 -15.751 -2.273  1.00 157.29 ? 843  ASP A C     1 
ATOM   5641 O  O     . ASP A 1 740 ? -50.443 -15.552 -3.167  1.00 163.10 ? 843  ASP A O     1 
ATOM   5642 C  CB    . ASP A 1 740 ? -49.297 -17.383 -0.392  1.00 168.34 ? 843  ASP A CB    1 
ATOM   5643 C  CG    . ASP A 1 740 ? -50.730 -17.554 0.088   1.00 173.05 ? 843  ASP A CG    1 
ATOM   5644 O  OD1   . ASP A 1 740 ? -51.636 -16.898 -0.467  1.00 175.63 ? 843  ASP A OD1   1 
ATOM   5645 O  OD2   . ASP A 1 740 ? -50.949 -18.349 1.026   1.00 169.90 ? 843  ASP A OD2   1 
ATOM   5646 N  N     . CYS A 1 741 ? -49.048 -14.758 -1.588  1.00 154.90 ? 844  CYS A N     1 
ATOM   5647 C  CA    . CYS A 1 741 ? -49.431 -13.372 -1.804  1.00 150.58 ? 844  CYS A CA    1 
ATOM   5648 C  C     . CYS A 1 741 ? -48.251 -12.425 -1.968  1.00 151.37 ? 844  CYS A C     1 
ATOM   5649 O  O     . CYS A 1 741 ? -48.470 -11.243 -2.253  1.00 157.07 ? 844  CYS A O     1 
ATOM   5650 C  CB    . CYS A 1 741 ? -50.320 -12.879 -0.651  1.00 152.92 ? 844  CYS A CB    1 
ATOM   5651 S  SG    . CYS A 1 741 ? -49.703 -13.292 0.998   1.00 211.69 ? 844  CYS A SG    1 
ATOM   5652 N  N     . VAL A 1 742 ? -47.016 -12.898 -1.805  1.00 135.64 ? 845  VAL A N     1 
ATOM   5653 C  CA    . VAL A 1 742 ? -45.851 -12.041 -1.992  1.00 167.69 ? 845  VAL A CA    1 
ATOM   5654 C  C     . VAL A 1 742 ? -45.633 -11.824 -3.483  1.00 137.98 ? 845  VAL A C     1 
ATOM   5655 O  O     . VAL A 1 742 ? -46.221 -12.521 -4.317  1.00 127.74 ? 845  VAL A O     1 
ATOM   5656 C  CB    . VAL A 1 742 ? -44.594 -12.633 -1.324  1.00 167.86 ? 845  VAL A CB    1 
ATOM   5657 C  CG1   . VAL A 1 742 ? -44.852 -12.901 0.149   1.00 155.56 ? 845  VAL A CG1   1 
ATOM   5658 C  CG2   . VAL A 1 742 ? -44.153 -13.900 -2.032  1.00 125.54 ? 845  VAL A CG2   1 
ATOM   5659 N  N     . GLY A 1 743 ? -44.800 -10.852 -3.828  1.00 137.82 ? 846  GLY A N     1 
ATOM   5660 C  CA    . GLY A 1 743 ? -44.538 -10.561 -5.225  1.00 124.04 ? 846  GLY A CA    1 
ATOM   5661 C  C     . GLY A 1 743 ? -43.631 -9.358  -5.345  1.00 108.65 ? 846  GLY A C     1 
ATOM   5662 O  O     . GLY A 1 743 ? -43.418 -8.609  -4.386  1.00 140.74 ? 846  GLY A O     1 
ATOM   5663 N  N     . LEU A 1 744 ? -43.101 -9.181  -6.551  1.00 110.85 ? 847  LEU A N     1 
ATOM   5664 C  CA    . LEU A 1 744 ? -42.167 -8.109  -6.851  1.00 138.51 ? 847  LEU A CA    1 
ATOM   5665 C  C     . LEU A 1 744 ? -42.815 -7.085  -7.774  1.00 130.06 ? 847  LEU A C     1 
ATOM   5666 O  O     . LEU A 1 744 ? -43.649 -7.423  -8.619  1.00 121.30 ? 847  LEU A O     1 
ATOM   5667 C  CB    . LEU A 1 744 ? -40.893 -8.660  -7.495  1.00 121.03 ? 847  LEU A CB    1 
ATOM   5668 C  CG    . LEU A 1 744 ? -40.135 -9.722  -6.698  1.00 122.41 ? 847  LEU A CG    1 
ATOM   5669 C  CD1   . LEU A 1 744 ? -38.894 -10.169 -7.453  1.00 105.41 ? 847  LEU A CD1   1 
ATOM   5670 C  CD2   . LEU A 1 744 ? -39.772 -9.200  -5.317  1.00 116.41 ? 847  LEU A CD2   1 
ATOM   5671 N  N     . ILE A 1 745 ? -42.422 -5.825  -7.602  1.00 138.65 ? 848  ILE A N     1 
ATOM   5672 C  CA    . ILE A 1 745 ? -42.954 -4.712  -8.380  1.00 133.55 ? 848  ILE A CA    1 
ATOM   5673 C  C     . ILE A 1 745 ? -41.780 -3.895  -8.902  1.00 126.65 ? 848  ILE A C     1 
ATOM   5674 O  O     . ILE A 1 745 ? -40.967 -3.398  -8.113  1.00 131.65 ? 848  ILE A O     1 
ATOM   5675 C  CB    . ILE A 1 745 ? -43.900 -3.827  -7.551  1.00 113.64 ? 848  ILE A CB    1 
ATOM   5676 C  CG1   . ILE A 1 745 ? -45.113 -4.632  -7.081  1.00 120.76 ? 848  ILE A CG1   1 
ATOM   5677 C  CG2   . ILE A 1 745 ? -44.338 -2.613  -8.358  1.00 131.61 ? 848  ILE A CG2   1 
ATOM   5678 C  CD1   . ILE A 1 745 ? -46.049 -3.856  -6.182  1.00 118.45 ? 848  ILE A CD1   1 
ATOM   5679 N  N     . GLU A 1 746 ? -41.692 -3.757  -10.223 1.00 133.61 ? 849  GLU A N     1 
ATOM   5680 C  CA    . GLU A 1 746 ? -40.637 -2.951  -10.823 1.00 143.44 ? 849  GLU A CA    1 
ATOM   5681 C  C     . GLU A 1 746 ? -40.909 -1.473  -10.571 1.00 136.92 ? 849  GLU A C     1 
ATOM   5682 O  O     . GLU A 1 746 ? -42.029 -0.995  -10.771 1.00 138.18 ? 849  GLU A O     1 
ATOM   5683 C  CB    . GLU A 1 746 ? -40.544 -3.235  -12.323 1.00 137.50 ? 849  GLU A CB    1 
ATOM   5684 C  CG    . GLU A 1 746 ? -39.337 -2.614  -13.016 1.00 143.26 ? 849  GLU A CG    1 
ATOM   5685 C  CD    . GLU A 1 746 ? -39.599 -1.205  -13.512 1.00 169.82 ? 849  GLU A CD    1 
ATOM   5686 O  OE1   . GLU A 1 746 ? -40.780 -0.805  -13.574 1.00 179.26 ? 849  GLU A OE1   1 
ATOM   5687 O  OE2   . GLU A 1 746 ? -38.624 -0.497  -13.841 1.00 184.39 ? 849  GLU A OE2   1 
ATOM   5688 N  N     . VAL A 1 747 ? -39.883 -0.750  -10.130 1.00 139.59 ? 850  VAL A N     1 
ATOM   5689 C  CA    . VAL A 1 747 ? -39.997 0.662   -9.781  1.00 128.43 ? 850  VAL A CA    1 
ATOM   5690 C  C     . VAL A 1 747 ? -39.353 1.490   -10.882 1.00 138.49 ? 850  VAL A C     1 
ATOM   5691 O  O     . VAL A 1 747 ? -38.246 1.178   -11.338 1.00 136.89 ? 850  VAL A O     1 
ATOM   5692 C  CB    . VAL A 1 747 ? -39.347 0.962   -8.419  1.00 123.64 ? 850  VAL A CB    1 
ATOM   5693 C  CG1   . VAL A 1 747 ? -39.608 2.403   -8.011  1.00 127.78 ? 850  VAL A CG1   1 
ATOM   5694 C  CG2   . VAL A 1 747 ? -39.867 0.005   -7.365  1.00 150.45 ? 850  VAL A CG2   1 
ATOM   5695 N  N     . VAL A 1 748 ? -40.046 2.544   -11.307 1.00 135.66 ? 851  VAL A N     1 
ATOM   5696 C  CA    . VAL A 1 748 ? -39.547 3.469   -12.317 1.00 136.42 ? 851  VAL A CA    1 
ATOM   5697 C  C     . VAL A 1 748 ? -38.918 4.663   -11.611 1.00 138.13 ? 851  VAL A C     1 
ATOM   5698 O  O     . VAL A 1 748 ? -39.520 5.247   -10.701 1.00 131.36 ? 851  VAL A O     1 
ATOM   5699 C  CB    . VAL A 1 748 ? -40.670 3.910   -13.273 1.00 140.98 ? 851  VAL A CB    1 
ATOM   5700 C  CG1   . VAL A 1 748 ? -41.922 4.295   -12.495 1.00 123.93 ? 851  VAL A CG1   1 
ATOM   5701 C  CG2   . VAL A 1 748 ? -40.205 5.062   -14.153 1.00 165.94 ? 851  VAL A CG2   1 
ATOM   5702 N  N     . ARG A 1 749 ? -37.702 5.016   -12.018 1.00 146.75 ? 852  ARG A N     1 
ATOM   5703 C  CA    . ARG A 1 749 ? -36.988 6.122   -11.400 1.00 160.53 ? 852  ARG A CA    1 
ATOM   5704 C  C     . ARG A 1 749 ? -37.631 7.455   -11.783 1.00 167.60 ? 852  ARG A C     1 
ATOM   5705 O  O     . ARG A 1 749 ? -38.375 7.556   -12.764 1.00 161.89 ? 852  ARG A O     1 
ATOM   5706 C  CB    . ARG A 1 749 ? -35.513 6.093   -11.811 1.00 167.75 ? 852  ARG A CB    1 
ATOM   5707 C  CG    . ARG A 1 749 ? -34.594 6.980   -10.979 1.00 198.25 ? 852  ARG A CG    1 
ATOM   5708 C  CD    . ARG A 1 749 ? -34.756 6.706   -9.492  1.00 190.38 ? 852  ARG A CD    1 
ATOM   5709 N  NE    . ARG A 1 749 ? -33.938 7.599   -8.680  1.00 198.45 ? 852  ARG A NE    1 
ATOM   5710 C  CZ    . ARG A 1 749 ? -34.330 8.792   -8.253  1.00 217.08 ? 852  ARG A CZ    1 
ATOM   5711 N  NH1   . ARG A 1 749 ? -35.528 9.272   -8.544  1.00 216.50 ? 852  ARG A NH1   1 
ATOM   5712 N  NH2   . ARG A 1 749 ? -33.498 9.523   -7.516  1.00 213.45 ? 852  ARG A NH2   1 
ATOM   5713 N  N     . ASN A 1 750 ? -37.324 8.481   -10.989 1.00 158.71 ? 853  ASN A N     1 
ATOM   5714 C  CA    . ASN A 1 750 ? -37.836 9.847   -11.141 1.00 165.29 ? 853  ASN A CA    1 
ATOM   5715 C  C     . ASN A 1 750 ? -39.323 9.856   -11.497 1.00 158.06 ? 853  ASN A C     1 
ATOM   5716 O  O     . ASN A 1 750 ? -39.750 10.364  -12.534 1.00 145.89 ? 853  ASN A O     1 
ATOM   5717 C  CB    . ASN A 1 750 ? -37.012 10.649  -12.155 1.00 162.61 ? 853  ASN A CB    1 
ATOM   5718 C  CG    . ASN A 1 750 ? -36.800 9.916   -13.466 1.00 168.47 ? 853  ASN A CG    1 
ATOM   5719 O  OD1   . ASN A 1 750 ? -37.646 9.955   -14.359 1.00 186.16 ? 853  ASN A OD1   1 
ATOM   5720 N  ND2   . ASN A 1 750 ? -35.660 9.245   -13.588 1.00 168.39 ? 853  ASN A ND2   1 
ATOM   5721 N  N     . SER A 1 751 ? -40.114 9.278   -10.596 1.00 159.71 ? 854  SER A N     1 
ATOM   5722 C  CA    . SER A 1 751 ? -41.563 9.250   -10.716 1.00 158.75 ? 854  SER A CA    1 
ATOM   5723 C  C     . SER A 1 751 ? -42.179 9.707   -9.403  1.00 141.15 ? 854  SER A C     1 
ATOM   5724 O  O     . SER A 1 751 ? -41.751 9.282   -8.326  1.00 135.21 ? 854  SER A O     1 
ATOM   5725 C  CB    . SER A 1 751 ? -42.070 7.848   -11.078 1.00 153.71 ? 854  SER A CB    1 
ATOM   5726 O  OG    . SER A 1 751 ? -41.717 6.905   -10.081 1.00 153.48 ? 854  SER A OG    1 
ATOM   5727 N  N     . HIS A 1 752 ? -43.182 10.576  -9.499  1.00 131.23 ? 855  HIS A N     1 
ATOM   5728 C  CA    . HIS A 1 752 ? -43.844 11.139  -8.331  1.00 150.45 ? 855  HIS A CA    1 
ATOM   5729 C  C     . HIS A 1 752 ? -45.351 11.076  -8.525  1.00 149.02 ? 855  HIS A C     1 
ATOM   5730 O  O     . HIS A 1 752 ? -45.848 11.244  -9.643  1.00 159.98 ? 855  HIS A O     1 
ATOM   5731 C  CB    . HIS A 1 752 ? -43.406 12.590  -8.092  1.00 151.12 ? 855  HIS A CB    1 
ATOM   5732 C  CG    . HIS A 1 752 ? -41.971 12.851  -8.429  1.00 142.74 ? 855  HIS A CG    1 
ATOM   5733 N  ND1   . HIS A 1 752 ? -40.926 12.327  -7.699  1.00 153.72 ? 855  HIS A ND1   1 
ATOM   5734 C  CD2   . HIS A 1 752 ? -41.407 13.579  -9.422  1.00 143.42 ? 855  HIS A CD2   1 
ATOM   5735 C  CE1   . HIS A 1 752 ? -39.781 12.721  -8.226  1.00 139.05 ? 855  HIS A CE1   1 
ATOM   5736 N  NE2   . HIS A 1 752 ? -40.045 13.483  -9.273  1.00 134.08 ? 855  HIS A NE2   1 
ATOM   5737 N  N     . THR A 1 753 ? -46.074 10.834  -7.436  1.00 133.28 ? 856  THR A N     1 
ATOM   5738 C  CA    . THR A 1 753 ? -47.524 10.777  -7.502  1.00 134.79 ? 856  THR A CA    1 
ATOM   5739 C  C     . THR A 1 753 ? -48.107 12.186  -7.598  1.00 161.80 ? 856  THR A C     1 
ATOM   5740 O  O     . THR A 1 753 ? -47.397 13.192  -7.509  1.00 181.83 ? 856  THR A O     1 
ATOM   5741 C  CB    . THR A 1 753 ? -48.095 10.052  -6.283  1.00 163.52 ? 856  THR A CB    1 
ATOM   5742 O  OG1   . THR A 1 753 ? -48.255 10.981  -5.204  1.00 178.67 ? 856  THR A OG1   1 
ATOM   5743 C  CG2   . THR A 1 753 ? -47.162 8.935   -5.842  1.00 152.80 ? 856  THR A CG2   1 
ATOM   5744 N  N     . ILE A 1 754 ? -49.427 12.250  -7.785  1.00 167.04 ? 857  ILE A N     1 
ATOM   5745 C  CA    . ILE A 1 754 ? -50.100 13.543  -7.854  1.00 177.34 ? 857  ILE A CA    1 
ATOM   5746 C  C     . ILE A 1 754 ? -50.058 14.237  -6.498  1.00 181.00 ? 857  ILE A C     1 
ATOM   5747 O  O     . ILE A 1 754 ? -49.881 15.459  -6.414  1.00 192.53 ? 857  ILE A O     1 
ATOM   5748 C  CB    . ILE A 1 754 ? -51.542 13.371  -8.364  1.00 162.60 ? 857  ILE A CB    1 
ATOM   5749 C  CG1   . ILE A 1 754 ? -51.545 12.677  -9.727  1.00 152.16 ? 857  ILE A CG1   1 
ATOM   5750 C  CG2   . ILE A 1 754 ? -52.245 14.717  -8.452  1.00 157.87 ? 857  ILE A CG2   1 
ATOM   5751 C  CD1   . ILE A 1 754 ? -50.768 13.420  -10.791 1.00 145.92 ? 857  ILE A CD1   1 
ATOM   5752 N  N     . MET A 1 755 ? -50.213 13.471  -5.414  1.00 169.77 ? 858  MET A N     1 
ATOM   5753 C  CA    . MET A 1 755 ? -50.091 14.040  -4.078  1.00 178.54 ? 858  MET A CA    1 
ATOM   5754 C  C     . MET A 1 755 ? -48.658 14.446  -3.757  1.00 187.87 ? 858  MET A C     1 
ATOM   5755 O  O     . MET A 1 755 ? -48.451 15.338  -2.927  1.00 185.77 ? 858  MET A O     1 
ATOM   5756 C  CB    . MET A 1 755 ? -50.604 13.042  -3.034  1.00 188.31 ? 858  MET A CB    1 
ATOM   5757 C  CG    . MET A 1 755 ? -50.686 13.600  -1.620  1.00 189.29 ? 858  MET A CG    1 
ATOM   5758 S  SD    . MET A 1 755 ? -51.322 12.412  -0.424  1.00 212.88 ? 858  MET A SD    1 
ATOM   5759 C  CE    . MET A 1 755 ? -52.981 12.160  -1.048  1.00 205.61 ? 858  MET A CE    1 
ATOM   5760 N  N     . GLN A 1 756 ? -47.667 13.822  -4.400  1.00 199.68 ? 859  GLN A N     1 
ATOM   5761 C  CA    . GLN A 1 756 ? -46.273 14.182  -4.166  1.00 198.51 ? 859  GLN A CA    1 
ATOM   5762 C  C     . GLN A 1 756 ? -45.917 15.545  -4.745  1.00 182.30 ? 859  GLN A C     1 
ATOM   5763 O  O     . GLN A 1 756 ? -44.878 16.105  -4.378  1.00 198.86 ? 859  GLN A O     1 
ATOM   5764 C  CB    . GLN A 1 756 ? -45.345 13.118  -4.757  1.00 194.90 ? 859  GLN A CB    1 
ATOM   5765 C  CG    . GLN A 1 756 ? -45.407 11.762  -4.068  1.00 178.13 ? 859  GLN A CG    1 
ATOM   5766 C  CD    . GLN A 1 756 ? -44.669 11.739  -2.745  1.00 198.15 ? 859  GLN A CD    1 
ATOM   5767 O  OE1   . GLN A 1 756 ? -44.017 12.712  -2.366  1.00 230.31 ? 859  GLN A OE1   1 
ATOM   5768 N  NE2   . GLN A 1 756 ? -44.765 10.621  -2.034  1.00 191.57 ? 859  GLN A NE2   1 
ATOM   5769 N  N     . ILE A 1 757 ? -46.743 16.088  -5.634  1.00 179.00 ? 860  ILE A N     1 
ATOM   5770 C  CA    . ILE A 1 757 ? -46.491 17.373  -6.276  1.00 197.44 ? 860  ILE A CA    1 
ATOM   5771 C  C     . ILE A 1 757 ? -47.462 18.386  -5.685  1.00 186.87 ? 860  ILE A C     1 
ATOM   5772 O  O     . ILE A 1 757 ? -48.655 18.382  -6.013  1.00 170.50 ? 860  ILE A O     1 
ATOM   5773 C  CB    . ILE A 1 757 ? -46.636 17.288  -7.801  1.00 191.68 ? 860  ILE A CB    1 
ATOM   5774 C  CG1   . ILE A 1 757 ? -45.677 16.240  -8.370  1.00 190.28 ? 860  ILE A CG1   1 
ATOM   5775 C  CG2   . ILE A 1 757 ? -46.385 18.648  -8.435  1.00 165.08 ? 860  ILE A CG2   1 
ATOM   5776 C  CD1   . ILE A 1 757 ? -44.220 16.527  -8.081  1.00 201.82 ? 860  ILE A CD1   1 
ATOM   5777 N  N     . GLN A 1 758 ? -46.953 19.257  -4.817  1.00 181.28 ? 861  GLN A N     1 
ATOM   5778 C  CA    . GLN A 1 758 ? -47.764 20.277  -4.166  1.00 187.13 ? 861  GLN A CA    1 
ATOM   5779 C  C     . GLN A 1 758 ? -46.834 21.288  -3.512  1.00 186.51 ? 861  GLN A C     1 
ATOM   5780 O  O     . GLN A 1 758 ? -45.668 20.994  -3.232  1.00 168.13 ? 861  GLN A O     1 
ATOM   5781 C  CB    . GLN A 1 758 ? -48.715 19.670  -3.126  1.00 160.57 ? 861  GLN A CB    1 
ATOM   5782 C  CG    . GLN A 1 758 ? -48.076 19.401  -1.768  1.00 160.49 ? 861  GLN A CG    1 
ATOM   5783 C  CD    . GLN A 1 758 ? -46.858 18.502  -1.855  1.00 170.98 ? 861  GLN A CD    1 
ATOM   5784 O  OE1   . GLN A 1 758 ? -46.831 17.546  -2.627  1.00 191.65 ? 861  GLN A OE1   1 
ATOM   5785 N  NE2   . GLN A 1 758 ? -45.834 18.816  -1.070  1.00 179.16 ? 861  GLN A NE2   1 
ATOM   5786 N  N     . CYS A 1 759 ? -47.367 22.482  -3.270  1.00 171.59 ? 862  CYS A N     1 
ATOM   5787 C  CA    . CYS A 1 759 ? -46.617 23.538  -2.597  1.00 173.76 ? 862  CYS A CA    1 
ATOM   5788 C  C     . CYS A 1 759 ? -47.533 24.374  -1.709  1.00 187.36 ? 862  CYS A C     1 
ATOM   5789 O  O     . CYS A 1 759 ? -48.564 24.874  -2.161  1.00 198.17 ? 862  CYS A O     1 
ATOM   5790 C  CB    . CYS A 1 759 ? -45.910 24.436  -3.615  1.00 182.90 ? 862  CYS A CB    1 
ATOM   5791 S  SG    . CYS A 1 759 ? -44.509 23.664  -4.460  1.00 199.62 ? 862  CYS A SG    1 
ATOM   5792 N  N     . PHE A 1 769 ? -50.587 25.533  1.276   1.00 209.06 ? 872  PHE A N     1 
ATOM   5793 C  CA    . PHE A 1 769 ? -51.940 25.135  0.905   1.00 220.55 ? 872  PHE A CA    1 
ATOM   5794 C  C     . PHE A 1 769 ? -51.934 24.293  -0.367  1.00 239.63 ? 872  PHE A C     1 
ATOM   5795 O  O     . PHE A 1 769 ? -50.889 23.801  -0.792  1.00 224.51 ? 872  PHE A O     1 
ATOM   5796 C  CB    . PHE A 1 769 ? -52.830 26.365  0.719   1.00 205.66 ? 872  PHE A CB    1 
ATOM   5797 N  N     . ASN A 1 770 ? -53.108 24.133  -0.970  1.00 265.18 ? 873  ASN A N     1 
ATOM   5798 C  CA    . ASN A 1 770 ? -53.271 23.357  -2.191  1.00 245.53 ? 873  ASN A CA    1 
ATOM   5799 C  C     . ASN A 1 770 ? -53.522 24.290  -3.368  1.00 235.04 ? 873  ASN A C     1 
ATOM   5800 O  O     . ASN A 1 770 ? -54.223 25.298  -3.237  1.00 251.33 ? 873  ASN A O     1 
ATOM   5801 C  CB    . ASN A 1 770 ? -54.425 22.359  -2.058  1.00 244.44 ? 873  ASN A CB    1 
ATOM   5802 C  CG    . ASN A 1 770 ? -55.740 23.030  -1.711  1.00 265.31 ? 873  ASN A CG    1 
ATOM   5803 O  OD1   . ASN A 1 770 ? -56.500 23.426  -2.595  1.00 280.64 ? 873  ASN A OD1   1 
ATOM   5804 N  ND2   . ASN A 1 770 ? -56.015 23.161  -0.419  1.00 246.17 ? 873  ASN A ND2   1 
ATOM   5805 N  N     . SER A 1 771 ? -52.945 23.948  -4.516  1.00 196.57 ? 874  SER A N     1 
ATOM   5806 C  CA    . SER A 1 771 ? -53.090 24.748  -5.725  1.00 178.99 ? 874  SER A CA    1 
ATOM   5807 C  C     . SER A 1 771 ? -52.829 23.850  -6.928  1.00 185.52 ? 874  SER A C     1 
ATOM   5808 O  O     . SER A 1 771 ? -52.478 22.675  -6.788  1.00 180.12 ? 874  SER A O     1 
ATOM   5809 C  CB    . SER A 1 771 ? -52.148 25.955  -5.708  1.00 159.91 ? 874  SER A CB    1 
ATOM   5810 O  OG    . SER A 1 771 ? -52.264 26.710  -6.901  1.00 180.90 ? 874  SER A OG    1 
ATOM   5811 N  N     . HIS A 1 772 ? -53.003 24.417  -8.120  1.00 200.21 ? 875  HIS A N     1 
ATOM   5812 C  CA    . HIS A 1 772 ? -52.770 23.690  -9.368  1.00 182.15 ? 875  HIS A CA    1 
ATOM   5813 C  C     . HIS A 1 772 ? -51.306 23.817  -9.793  1.00 187.71 ? 875  HIS A C     1 
ATOM   5814 O  O     . HIS A 1 772 ? -50.969 24.358  -10.846 1.00 182.37 ? 875  HIS A O     1 
ATOM   5815 C  CB    . HIS A 1 772 ? -53.712 24.193  -10.456 1.00 186.81 ? 875  HIS A CB    1 
ATOM   5816 C  CG    . HIS A 1 772 ? -55.160 23.944  -10.166 1.00 195.75 ? 875  HIS A CG    1 
ATOM   5817 N  ND1   . HIS A 1 772 ? -56.174 24.467  -10.939 1.00 210.92 ? 875  HIS A ND1   1 
ATOM   5818 C  CD2   . HIS A 1 772 ? -55.763 23.227  -9.189  1.00 188.70 ? 875  HIS A CD2   1 
ATOM   5819 C  CE1   . HIS A 1 772 ? -57.340 24.083  -10.450 1.00 189.98 ? 875  HIS A CE1   1 
ATOM   5820 N  NE2   . HIS A 1 772 ? -57.118 23.330  -9.388  1.00 182.09 ? 875  HIS A NE2   1 
ATOM   5821 N  N     . THR A 1 773 ? -50.428 23.297  -8.937  1.00 178.74 ? 876  THR A N     1 
ATOM   5822 C  CA    . THR A 1 773 ? -48.993 23.339  -9.185  1.00 182.60 ? 876  THR A CA    1 
ATOM   5823 C  C     . THR A 1 773 ? -48.512 22.211  -10.088 1.00 184.89 ? 876  THR A C     1 
ATOM   5824 O  O     . THR A 1 773 ? -47.302 22.098  -10.316 1.00 197.31 ? 876  THR A O     1 
ATOM   5825 C  CB    . THR A 1 773 ? -48.226 23.294  -7.860  1.00 176.53 ? 876  THR A CB    1 
ATOM   5826 O  OG1   . THR A 1 773 ? -48.513 22.066  -7.181  1.00 169.96 ? 876  THR A OG1   1 
ATOM   5827 C  CG2   . THR A 1 773 ? -48.626 24.464  -6.973  1.00 179.19 ? 876  THR A CG2   1 
ATOM   5828 N  N     . LEU A 1 774 ? -49.419 21.376  -10.602 1.00 176.28 ? 877  LEU A N     1 
ATOM   5829 C  CA    . LEU A 1 774 ? -49.011 20.310  -11.511 1.00 164.29 ? 877  LEU A CA    1 
ATOM   5830 C  C     . LEU A 1 774 ? -48.470 20.878  -12.817 1.00 167.25 ? 877  LEU A C     1 
ATOM   5831 O  O     . LEU A 1 774 ? -47.503 20.349  -13.378 1.00 159.67 ? 877  LEU A O     1 
ATOM   5832 C  CB    . LEU A 1 774 ? -50.186 19.369  -11.779 1.00 144.55 ? 877  LEU A CB    1 
ATOM   5833 C  CG    . LEU A 1 774 ? -49.939 18.240  -12.782 1.00 148.70 ? 877  LEU A CG    1 
ATOM   5834 C  CD1   . LEU A 1 774 ? -48.790 17.353  -12.325 1.00 119.01 ? 877  LEU A CD1   1 
ATOM   5835 C  CD2   . LEU A 1 774 ? -51.203 17.421  -12.993 1.00 139.62 ? 877  LEU A CD2   1 
ATOM   5836 N  N     . HIS A 1 775 ? -49.079 21.956  -13.315 1.00 171.97 ? 878  HIS A N     1 
ATOM   5837 C  CA    . HIS A 1 775 ? -48.583 22.583  -14.535 1.00 144.68 ? 878  HIS A CA    1 
ATOM   5838 C  C     . HIS A 1 775 ? -47.245 23.273  -14.304 1.00 152.49 ? 878  HIS A C     1 
ATOM   5839 O  O     . HIS A 1 775 ? -46.414 23.332  -15.217 1.00 156.58 ? 878  HIS A O     1 
ATOM   5840 C  CB    . HIS A 1 775 ? -49.612 23.580  -15.067 1.00 140.80 ? 878  HIS A CB    1 
ATOM   5841 C  CG    . HIS A 1 775 ? -49.337 24.048  -16.462 1.00 136.78 ? 878  HIS A CG    1 
ATOM   5842 N  ND1   . HIS A 1 775 ? -49.947 25.155  -17.009 1.00 167.35 ? 878  HIS A ND1   1 
ATOM   5843 C  CD2   . HIS A 1 775 ? -48.521 23.554  -17.423 1.00 160.21 ? 878  HIS A CD2   1 
ATOM   5844 C  CE1   . HIS A 1 775 ? -49.516 25.326  -18.246 1.00 174.63 ? 878  HIS A CE1   1 
ATOM   5845 N  NE2   . HIS A 1 775 ? -48.650 24.368  -18.522 1.00 155.99 ? 878  HIS A NE2   1 
ATOM   5846 N  N     . GLN A 1 776 ? -47.017 23.794  -13.096 1.00 180.81 ? 879  GLN A N     1 
ATOM   5847 C  CA    . GLN A 1 776 ? -45.742 24.436  -12.799 1.00 194.80 ? 879  GLN A CA    1 
ATOM   5848 C  C     . GLN A 1 776 ? -44.617 23.417  -12.667 1.00 188.39 ? 879  GLN A C     1 
ATOM   5849 O  O     . GLN A 1 776 ? -43.473 23.709  -13.035 1.00 185.62 ? 879  GLN A O     1 
ATOM   5850 C  CB    . GLN A 1 776 ? -45.860 25.272  -11.523 1.00 190.14 ? 879  GLN A CB    1 
ATOM   5851 C  CG    . GLN A 1 776 ? -44.582 25.997  -11.125 1.00 194.55 ? 879  GLN A CG    1 
ATOM   5852 C  CD    . GLN A 1 776 ? -44.123 26.998  -12.170 1.00 179.39 ? 879  GLN A CD    1 
ATOM   5853 O  OE1   . GLN A 1 776 ? -44.931 27.552  -12.915 1.00 173.05 ? 879  GLN A OE1   1 
ATOM   5854 N  NE2   . GLN A 1 776 ? -42.817 27.232  -12.230 1.00 178.62 ? 879  GLN A NE2   1 
ATOM   5855 N  N     . TRP A 1 777 ? -44.919 22.222  -12.153 1.00 171.93 ? 880  TRP A N     1 
ATOM   5856 C  CA    . TRP A 1 777 ? -43.893 21.192  -12.026 1.00 173.55 ? 880  TRP A CA    1 
ATOM   5857 C  C     . TRP A 1 777 ? -43.392 20.739  -13.391 1.00 165.61 ? 880  TRP A C     1 
ATOM   5858 O  O     . TRP A 1 777 ? -42.193 20.490  -13.567 1.00 173.19 ? 880  TRP A O     1 
ATOM   5859 C  CB    . TRP A 1 777 ? -44.433 20.006  -11.226 1.00 168.32 ? 880  TRP A CB    1 
ATOM   5860 C  CG    . TRP A 1 777 ? -43.603 18.762  -11.350 1.00 164.84 ? 880  TRP A CG    1 
ATOM   5861 C  CD1   . TRP A 1 777 ? -44.007 17.554  -11.841 1.00 158.86 ? 880  TRP A CD1   1 
ATOM   5862 C  CD2   . TRP A 1 777 ? -42.224 18.606  -10.989 1.00 164.92 ? 880  TRP A CD2   1 
ATOM   5863 N  NE1   . TRP A 1 777 ? -42.969 16.655  -11.802 1.00 159.86 ? 880  TRP A NE1   1 
ATOM   5864 C  CE2   . TRP A 1 777 ? -41.863 17.276  -11.284 1.00 178.66 ? 880  TRP A CE2   1 
ATOM   5865 C  CE3   . TRP A 1 777 ? -41.261 19.461  -10.443 1.00 171.18 ? 880  TRP A CE3   1 
ATOM   5866 C  CZ2   . TRP A 1 777 ? -40.582 16.781  -11.052 1.00 182.58 ? 880  TRP A CZ2   1 
ATOM   5867 C  CZ3   . TRP A 1 777 ? -39.989 18.967  -10.214 1.00 190.09 ? 880  TRP A CZ3   1 
ATOM   5868 C  CH2   . TRP A 1 777 ? -39.661 17.640  -10.518 1.00 182.62 ? 880  TRP A CH2   1 
ATOM   5869 N  N     . LEU A 1 778 ? -44.291 20.626  -14.371 1.00 151.11 ? 881  LEU A N     1 
ATOM   5870 C  CA    . LEU A 1 778 ? -43.860 20.281  -15.721 1.00 152.60 ? 881  LEU A CA    1 
ATOM   5871 C  C     . LEU A 1 778 ? -43.191 21.463  -16.410 1.00 156.02 ? 881  LEU A C     1 
ATOM   5872 O  O     . LEU A 1 778 ? -42.349 21.268  -17.294 1.00 180.59 ? 881  LEU A O     1 
ATOM   5873 C  CB    . LEU A 1 778 ? -45.047 19.779  -16.542 1.00 137.31 ? 881  LEU A CB    1 
ATOM   5874 C  CG    . LEU A 1 778 ? -45.724 18.513  -16.012 1.00 144.23 ? 881  LEU A CG    1 
ATOM   5875 C  CD1   . LEU A 1 778 ? -46.811 18.042  -16.963 1.00 142.61 ? 881  LEU A CD1   1 
ATOM   5876 C  CD2   . LEU A 1 778 ? -44.703 17.411  -15.774 1.00 136.52 ? 881  LEU A CD2   1 
ATOM   5877 N  N     . LYS A 1 779 ? -43.548 22.690  -16.023 1.00 155.28 ? 882  LYS A N     1 
ATOM   5878 C  CA    . LYS A 1 779 ? -42.854 23.861  -16.550 1.00 155.75 ? 882  LYS A CA    1 
ATOM   5879 C  C     . LYS A 1 779 ? -41.454 23.981  -15.964 1.00 171.49 ? 882  LYS A C     1 
ATOM   5880 O  O     . LYS A 1 779 ? -40.507 24.349  -16.670 1.00 187.15 ? 882  LYS A O     1 
ATOM   5881 C  CB    . LYS A 1 779 ? -43.656 25.130  -16.260 1.00 175.17 ? 882  LYS A CB    1 
ATOM   5882 C  CG    . LYS A 1 779 ? -44.823 25.379  -17.198 1.00 172.19 ? 882  LYS A CG    1 
ATOM   5883 C  CD    . LYS A 1 779 ? -45.463 26.731  -16.916 1.00 154.57 ? 882  LYS A CD    1 
ATOM   5884 C  CE    . LYS A 1 779 ? -46.534 27.067  -17.940 1.00 148.30 ? 882  LYS A CE    1 
ATOM   5885 N  NZ    . LYS A 1 779 ? -47.159 28.392  -17.676 1.00 152.74 ? 882  LYS A NZ    1 
ATOM   5886 N  N     . ASP A 1 780 ? -41.303 23.673  -14.674 1.00 185.47 ? 883  ASP A N     1 
ATOM   5887 C  CA    . ASP A 1 780 ? -40.019 23.868  -14.009 1.00 205.85 ? 883  ASP A CA    1 
ATOM   5888 C  C     . ASP A 1 780 ? -38.990 22.835  -14.449 1.00 199.90 ? 883  ASP A C     1 
ATOM   5889 O  O     . ASP A 1 780 ? -37.796 23.147  -14.525 1.00 216.33 ? 883  ASP A O     1 
ATOM   5890 C  CB    . ASP A 1 780 ? -40.208 23.821  -12.492 1.00 213.14 ? 883  ASP A CB    1 
ATOM   5891 C  CG    . ASP A 1 780 ? -39.173 24.643  -11.747 1.00 230.54 ? 883  ASP A CG    1 
ATOM   5892 O  OD1   . ASP A 1 780 ? -38.042 24.789  -12.255 1.00 239.60 ? 883  ASP A OD1   1 
ATOM   5893 O  OD2   . ASP A 1 780 ? -39.494 25.147  -10.650 1.00 224.79 ? 883  ASP A OD2   1 
ATOM   5894 N  N     . LYS A 1 781 ? -39.424 21.611  -14.748 1.00 174.00 ? 884  LYS A N     1 
ATOM   5895 C  CA    . LYS A 1 781 ? -38.497 20.550  -15.116 1.00 171.81 ? 884  LYS A CA    1 
ATOM   5896 C  C     . LYS A 1 781 ? -38.226 20.482  -16.613 1.00 170.29 ? 884  LYS A C     1 
ATOM   5897 O  O     . LYS A 1 781 ? -37.169 19.983  -17.014 1.00 165.44 ? 884  LYS A O     1 
ATOM   5898 C  CB    . LYS A 1 781 ? -39.027 19.195  -14.633 1.00 175.04 ? 884  LYS A CB    1 
ATOM   5899 C  CG    . LYS A 1 781 ? -37.969 18.106  -14.569 1.00 178.65 ? 884  LYS A CG    1 
ATOM   5900 C  CD    . LYS A 1 781 ? -36.816 18.518  -13.667 1.00 176.31 ? 884  LYS A CD    1 
ATOM   5901 C  CE    . LYS A 1 781 ? -35.705 17.479  -13.671 1.00 150.67 ? 884  LYS A CE    1 
ATOM   5902 N  NZ    . LYS A 1 781 ? -36.165 16.168  -13.139 1.00 183.02 ? 884  LYS A NZ    1 
ATOM   5903 N  N     . ASN A 1 782 ? -39.144 20.971  -17.443 1.00 185.26 ? 885  ASN A N     1 
ATOM   5904 C  CA    . ASN A 1 782 ? -38.991 20.963  -18.897 1.00 176.82 ? 885  ASN A CA    1 
ATOM   5905 C  C     . ASN A 1 782 ? -39.100 22.403  -19.391 1.00 166.87 ? 885  ASN A C     1 
ATOM   5906 O  O     . ASN A 1 782 ? -40.196 22.895  -19.669 1.00 159.81 ? 885  ASN A O     1 
ATOM   5907 C  CB    . ASN A 1 782 ? -40.036 20.060  -19.554 1.00 177.09 ? 885  ASN A CB    1 
ATOM   5908 C  CG    . ASN A 1 782 ? -39.926 18.617  -19.103 1.00 170.29 ? 885  ASN A CG    1 
ATOM   5909 O  OD1   . ASN A 1 782 ? -40.849 18.073  -18.497 1.00 164.60 ? 885  ASN A OD1   1 
ATOM   5910 N  ND2   . ASN A 1 782 ? -38.793 17.989  -19.397 1.00 164.54 ? 885  ASN A ND2   1 
ATOM   5911 N  N     . LYS A 1 783 ? -37.959 23.075  -19.501 1.00 187.18 ? 886  LYS A N     1 
ATOM   5912 C  CA    . LYS A 1 783 ? -37.899 24.452  -19.967 1.00 187.54 ? 886  LYS A CA    1 
ATOM   5913 C  C     . LYS A 1 783 ? -37.508 24.505  -21.441 1.00 180.89 ? 886  LYS A C     1 
ATOM   5914 O  O     . LYS A 1 783 ? -37.036 23.526  -22.026 1.00 177.98 ? 886  LYS A O     1 
ATOM   5915 C  CB    . LYS A 1 783 ? -36.910 25.263  -19.124 1.00 182.48 ? 886  LYS A CB    1 
ATOM   5916 C  CG    . LYS A 1 783 ? -37.295 25.388  -17.660 1.00 193.22 ? 886  LYS A CG    1 
ATOM   5917 C  CD    . LYS A 1 783 ? -36.320 26.282  -16.912 1.00 209.92 ? 886  LYS A CD    1 
ATOM   5918 C  CE    . LYS A 1 783 ? -36.722 26.443  -15.456 1.00 203.61 ? 886  LYS A CE    1 
ATOM   5919 N  NZ    . LYS A 1 783 ? -35.796 27.349  -14.722 1.00 218.56 ? 886  LYS A NZ    1 
ATOM   5920 N  N     . GLY A 1 784 ? -37.708 25.677  -22.041 1.00 168.70 ? 887  GLY A N     1 
ATOM   5921 C  CA    . GLY A 1 784 ? -37.412 25.874  -23.445 1.00 163.45 ? 887  GLY A CA    1 
ATOM   5922 C  C     . GLY A 1 784 ? -38.398 25.184  -24.364 1.00 162.98 ? 887  GLY A C     1 
ATOM   5923 O  O     . GLY A 1 784 ? -39.604 25.174  -24.099 1.00 140.61 ? 887  GLY A O     1 
ATOM   5924 N  N     . GLU A 1 785 ? -37.894 24.591  -25.447 1.00 167.02 ? 888  GLU A N     1 
ATOM   5925 C  CA    . GLU A 1 785 ? -38.750 23.876  -26.384 1.00 166.68 ? 888  GLU A CA    1 
ATOM   5926 C  C     . GLU A 1 785 ? -39.188 22.512  -25.867 1.00 187.76 ? 888  GLU A C     1 
ATOM   5927 O  O     . GLU A 1 785 ? -39.999 21.852  -26.525 1.00 184.27 ? 888  GLU A O     1 
ATOM   5928 C  CB    . GLU A 1 785 ? -38.037 23.706  -27.731 1.00 161.91 ? 888  GLU A CB    1 
ATOM   5929 C  CG    . GLU A 1 785 ? -37.785 25.005  -28.489 1.00 181.44 ? 888  GLU A CG    1 
ATOM   5930 C  CD    . GLU A 1 785 ? -36.589 25.777  -27.960 1.00 185.85 ? 888  GLU A CD    1 
ATOM   5931 O  OE1   . GLU A 1 785 ? -35.851 25.230  -27.113 1.00 177.46 ? 888  GLU A OE1   1 
ATOM   5932 O  OE2   . GLU A 1 785 ? -36.386 26.931  -28.393 1.00 182.71 ? 888  GLU A OE2   1 
ATOM   5933 N  N     . ILE A 1 786 ? -38.677 22.076  -24.713 1.00 196.11 ? 889  ILE A N     1 
ATOM   5934 C  CA    . ILE A 1 786 ? -39.069 20.786  -24.158 1.00 170.28 ? 889  ILE A CA    1 
ATOM   5935 C  C     . ILE A 1 786 ? -40.447 20.839  -23.509 1.00 167.30 ? 889  ILE A C     1 
ATOM   5936 O  O     . ILE A 1 786 ? -41.096 19.795  -23.366 1.00 177.67 ? 889  ILE A O     1 
ATOM   5937 C  CB    . ILE A 1 786 ? -38.017 20.302  -23.145 1.00 184.13 ? 889  ILE A CB    1 
ATOM   5938 C  CG1   . ILE A 1 786 ? -36.608 20.576  -23.674 1.00 188.28 ? 889  ILE A CG1   1 
ATOM   5939 C  CG2   . ILE A 1 786 ? -38.180 18.816  -22.863 1.00 197.22 ? 889  ILE A CG2   1 
ATOM   5940 C  CD1   . ILE A 1 786 ? -35.507 20.137  -22.733 1.00 196.77 ? 889  ILE A CD1   1 
ATOM   5941 N  N     . TYR A 1 787 ? -40.914 22.028  -23.119 1.00 175.26 ? 890  TYR A N     1 
ATOM   5942 C  CA    . TYR A 1 787 ? -42.234 22.145  -22.507 1.00 160.58 ? 890  TYR A CA    1 
ATOM   5943 C  C     . TYR A 1 787 ? -43.331 21.688  -23.461 1.00 153.80 ? 890  TYR A C     1 
ATOM   5944 O  O     . TYR A 1 787 ? -44.275 21.005  -23.050 1.00 148.79 ? 890  TYR A O     1 
ATOM   5945 C  CB    . TYR A 1 787 ? -42.480 23.587  -22.060 1.00 167.16 ? 890  TYR A CB    1 
ATOM   5946 C  CG    . TYR A 1 787 ? -43.928 23.898  -21.744 1.00 160.37 ? 890  TYR A CG    1 
ATOM   5947 C  CD1   . TYR A 1 787 ? -44.475 23.576  -20.509 1.00 160.31 ? 890  TYR A CD1   1 
ATOM   5948 C  CD2   . TYR A 1 787 ? -44.746 24.522  -22.680 1.00 162.05 ? 890  TYR A CD2   1 
ATOM   5949 C  CE1   . TYR A 1 787 ? -45.797 23.861  -20.217 1.00 141.78 ? 890  TYR A CE1   1 
ATOM   5950 C  CE2   . TYR A 1 787 ? -46.068 24.808  -22.397 1.00 147.73 ? 890  TYR A CE2   1 
ATOM   5951 C  CZ    . TYR A 1 787 ? -46.588 24.476  -21.165 1.00 156.27 ? 890  TYR A CZ    1 
ATOM   5952 O  OH    . TYR A 1 787 ? -47.904 24.762  -20.879 1.00 152.43 ? 890  TYR A OH    1 
ATOM   5953 N  N     . ASP A 1 788 ? -43.224 22.058  -24.739 1.00 179.02 ? 891  ASP A N     1 
ATOM   5954 C  CA    . ASP A 1 788 ? -44.253 21.687  -25.704 1.00 179.47 ? 891  ASP A CA    1 
ATOM   5955 C  C     . ASP A 1 788 ? -44.311 20.179  -25.912 1.00 177.73 ? 891  ASP A C     1 
ATOM   5956 O  O     . ASP A 1 788 ? -45.368 19.643  -26.263 1.00 167.23 ? 891  ASP A O     1 
ATOM   5957 C  CB    . ASP A 1 788 ? -44.007 22.402  -27.032 1.00 189.35 ? 891  ASP A CB    1 
ATOM   5958 C  CG    . ASP A 1 788 ? -45.254 22.486  -27.892 1.00 224.05 ? 891  ASP A CG    1 
ATOM   5959 O  OD1   . ASP A 1 788 ? -46.330 22.052  -27.431 1.00 232.87 ? 891  ASP A OD1   1 
ATOM   5960 O  OD2   . ASP A 1 788 ? -45.157 22.991  -29.030 1.00 234.27 ? 891  ASP A OD2   1 
ATOM   5961 N  N     . ALA A 1 789 ? -43.195 19.481  -25.696 1.00 180.35 ? 892  ALA A N     1 
ATOM   5962 C  CA    . ALA A 1 789 ? -43.186 18.031  -25.844 1.00 156.54 ? 892  ALA A CA    1 
ATOM   5963 C  C     . ALA A 1 789 ? -43.633 17.323  -24.572 1.00 150.40 ? 892  ALA A C     1 
ATOM   5964 O  O     . ALA A 1 789 ? -44.238 16.248  -24.647 1.00 159.57 ? 892  ALA A O     1 
ATOM   5965 C  CB    . ALA A 1 789 ? -41.791 17.551  -26.249 1.00 163.39 ? 892  ALA A CB    1 
ATOM   5966 N  N     . ALA A 1 790 ? -43.348 17.903  -23.403 1.00 146.78 ? 893  ALA A N     1 
ATOM   5967 C  CA    . ALA A 1 790 ? -43.760 17.279  -22.150 1.00 141.06 ? 893  ALA A CA    1 
ATOM   5968 C  C     . ALA A 1 790 ? -45.270 17.353  -21.965 1.00 113.85 ? 893  ALA A C     1 
ATOM   5969 O  O     . ALA A 1 790 ? -45.880 16.429  -21.415 1.00 141.84 ? 893  ALA A O     1 
ATOM   5970 C  CB    . ALA A 1 790 ? -43.039 17.938  -20.974 1.00 147.24 ? 893  ALA A CB    1 
ATOM   5971 N  N     . ILE A 1 791 ? -45.891 18.445  -22.417 1.00 149.78 ? 894  ILE A N     1 
ATOM   5972 C  CA    . ILE A 1 791 ? -47.344 18.558  -22.336 1.00 160.94 ? 894  ILE A CA    1 
ATOM   5973 C  C     . ILE A 1 791 ? -48.007 17.543  -23.258 1.00 149.24 ? 894  ILE A C     1 
ATOM   5974 O  O     . ILE A 1 791 ? -49.045 16.960  -22.919 1.00 130.15 ? 894  ILE A O     1 
ATOM   5975 C  CB    . ILE A 1 791 ? -47.786 19.997  -22.659 1.00 130.74 ? 894  ILE A CB    1 
ATOM   5976 C  CG1   . ILE A 1 791 ? -47.166 20.979  -21.665 1.00 132.46 ? 894  ILE A CG1   1 
ATOM   5977 C  CG2   . ILE A 1 791 ? -49.302 20.112  -22.643 1.00 118.85 ? 894  ILE A CG2   1 
ATOM   5978 C  CD1   . ILE A 1 791 ? -47.508 20.685  -20.222 1.00 139.70 ? 894  ILE A CD1   1 
ATOM   5979 N  N     . ASP A 1 792 ? -47.420 17.312  -24.435 1.00 154.24 ? 895  ASP A N     1 
ATOM   5980 C  CA    . ASP A 1 792 ? -47.957 16.305  -25.343 1.00 145.54 ? 895  ASP A CA    1 
ATOM   5981 C  C     . ASP A 1 792 ? -47.862 14.912  -24.735 1.00 152.97 ? 895  ASP A C     1 
ATOM   5982 O  O     . ASP A 1 792 ? -48.795 14.110  -24.853 1.00 155.20 ? 895  ASP A O     1 
ATOM   5983 C  CB    . ASP A 1 792 ? -47.223 16.360  -26.682 1.00 158.15 ? 895  ASP A CB    1 
ATOM   5984 C  CG    . ASP A 1 792 ? -47.684 15.284  -27.643 1.00 157.35 ? 895  ASP A CG    1 
ATOM   5985 O  OD1   . ASP A 1 792 ? -48.853 15.335  -28.080 1.00 140.37 ? 895  ASP A OD1   1 
ATOM   5986 O  OD2   . ASP A 1 792 ? -46.876 14.386  -27.963 1.00 168.08 ? 895  ASP A OD2   1 
ATOM   5987 N  N     . LEU A 1 793 ? -46.740 14.607  -24.077 1.00 158.76 ? 896  LEU A N     1 
ATOM   5988 C  CA    . LEU A 1 793 ? -46.605 13.317  -23.409 1.00 151.92 ? 896  LEU A CA    1 
ATOM   5989 C  C     . LEU A 1 793 ? -47.612 13.170  -22.276 1.00 122.84 ? 896  LEU A C     1 
ATOM   5990 O  O     . LEU A 1 793 ? -48.057 12.055  -21.981 1.00 133.08 ? 896  LEU A O     1 
ATOM   5991 C  CB    . LEU A 1 793 ? -45.179 13.148  -22.882 1.00 121.79 ? 896  LEU A CB    1 
ATOM   5992 C  CG    . LEU A 1 793 ? -44.822 11.790  -22.276 1.00 100.91 ? 896  LEU A CG    1 
ATOM   5993 C  CD1   . LEU A 1 793 ? -44.943 10.691  -23.320 1.00 89.88  ? 896  LEU A CD1   1 
ATOM   5994 C  CD2   . LEU A 1 793 ? -43.424 11.820  -21.682 1.00 129.15 ? 896  LEU A CD2   1 
ATOM   5995 N  N     . PHE A 1 794 ? -47.987 14.280  -21.636 1.00 126.01 ? 897  PHE A N     1 
ATOM   5996 C  CA    . PHE A 1 794 ? -48.976 14.221  -20.567 1.00 126.71 ? 897  PHE A CA    1 
ATOM   5997 C  C     . PHE A 1 794 ? -50.374 13.954  -21.107 1.00 127.09 ? 897  PHE A C     1 
ATOM   5998 O  O     . PHE A 1 794 ? -51.203 13.366  -20.406 1.00 132.01 ? 897  PHE A O     1 
ATOM   5999 C  CB    . PHE A 1 794 ? -48.955 15.522  -19.762 1.00 144.80 ? 897  PHE A CB    1 
ATOM   6000 C  CG    . PHE A 1 794 ? -49.904 15.533  -18.595 1.00 153.20 ? 897  PHE A CG    1 
ATOM   6001 C  CD1   . PHE A 1 794 ? -49.519 15.019  -17.368 1.00 142.78 ? 897  PHE A CD1   1 
ATOM   6002 C  CD2   . PHE A 1 794 ? -51.178 16.065  -18.723 1.00 158.55 ? 897  PHE A CD2   1 
ATOM   6003 C  CE1   . PHE A 1 794 ? -50.388 15.030  -16.292 1.00 154.53 ? 897  PHE A CE1   1 
ATOM   6004 C  CE2   . PHE A 1 794 ? -52.051 16.079  -17.651 1.00 159.08 ? 897  PHE A CE2   1 
ATOM   6005 C  CZ    . PHE A 1 794 ? -51.655 15.561  -16.434 1.00 168.29 ? 897  PHE A CZ    1 
ATOM   6006 N  N     . THR A 1 795 ? -50.654 14.372  -22.341 1.00 135.92 ? 898  THR A N     1 
ATOM   6007 C  CA    . THR A 1 795 ? -51.981 14.203  -22.920 1.00 146.76 ? 898  THR A CA    1 
ATOM   6008 C  C     . THR A 1 795 ? -52.159 12.845  -23.589 1.00 138.85 ? 898  THR A C     1 
ATOM   6009 O  O     . THR A 1 795 ? -53.236 12.246  -23.490 1.00 142.47 ? 898  THR A O     1 
ATOM   6010 C  CB    . THR A 1 795 ? -52.263 15.317  -23.933 1.00 132.65 ? 898  THR A CB    1 
ATOM   6011 O  OG1   . THR A 1 795 ? -51.243 15.319  -24.940 1.00 164.06 ? 898  THR A OG1   1 
ATOM   6012 C  CG2   . THR A 1 795 ? -52.289 16.671  -23.242 1.00 131.05 ? 898  THR A CG2   1 
ATOM   6013 N  N     . ARG A 1 796 ? -51.126 12.346  -24.272 1.00 140.37 ? 899  ARG A N     1 
ATOM   6014 C  CA    . ARG A 1 796 ? -51.246 11.056  -24.943 1.00 139.09 ? 899  ARG A CA    1 
ATOM   6015 C  C     . ARG A 1 796 ? -51.282 9.912   -23.938 1.00 136.82 ? 899  ARG A C     1 
ATOM   6016 O  O     . ARG A 1 796 ? -52.018 8.936   -24.125 1.00 121.87 ? 899  ARG A O     1 
ATOM   6017 C  CB    . ARG A 1 796 ? -50.097 10.870  -25.934 1.00 140.07 ? 899  ARG A CB    1 
ATOM   6018 C  CG    . ARG A 1 796 ? -49.948 12.013  -26.926 1.00 135.38 ? 899  ARG A CG    1 
ATOM   6019 C  CD    . ARG A 1 796 ? -48.850 11.738  -27.940 1.00 139.58 ? 899  ARG A CD    1 
ATOM   6020 N  NE    . ARG A 1 796 ? -49.314 10.891  -29.032 1.00 151.87 ? 899  ARG A NE    1 
ATOM   6021 C  CZ    . ARG A 1 796 ? -49.803 11.348  -30.177 1.00 141.91 ? 899  ARG A CZ    1 
ATOM   6022 N  NH1   . ARG A 1 796 ? -49.903 12.646  -30.416 1.00 125.55 ? 899  ARG A NH1   1 
ATOM   6023 N  NH2   . ARG A 1 796 ? -50.200 10.483  -31.105 1.00 151.55 ? 899  ARG A NH2   1 
ATOM   6024 N  N     . SER A 1 797 ? -50.496 10.013  -22.862 1.00 131.09 ? 900  SER A N     1 
ATOM   6025 C  CA    . SER A 1 797 ? -50.525 8.980   -21.834 1.00 117.31 ? 900  SER A CA    1 
ATOM   6026 C  C     . SER A 1 797 ? -51.784 9.072   -20.982 1.00 123.29 ? 900  SER A C     1 
ATOM   6027 O  O     . SER A 1 797 ? -52.251 8.055   -20.458 1.00 143.76 ? 900  SER A O     1 
ATOM   6028 C  CB    . SER A 1 797 ? -49.279 9.076   -20.954 1.00 124.12 ? 900  SER A CB    1 
ATOM   6029 O  OG    . SER A 1 797 ? -49.217 10.325  -20.289 1.00 126.91 ? 900  SER A OG    1 
ATOM   6030 N  N     . CYS A 1 798 ? -52.346 10.275  -20.830 1.00 123.63 ? 901  CYS A N     1 
ATOM   6031 C  CA    . CYS A 1 798 ? -53.582 10.417  -20.068 1.00 119.45 ? 901  CYS A CA    1 
ATOM   6032 C  C     . CYS A 1 798 ? -54.766 9.832   -20.825 1.00 124.08 ? 901  CYS A C     1 
ATOM   6033 O  O     . CYS A 1 798 ? -55.610 9.149   -20.235 1.00 127.31 ? 901  CYS A O     1 
ATOM   6034 C  CB    . CYS A 1 798 ? -53.832 11.888  -19.737 1.00 118.87 ? 901  CYS A CB    1 
ATOM   6035 S  SG    . CYS A 1 798 ? -55.288 12.193  -18.710 1.00 186.49 ? 901  CYS A SG    1 
ATOM   6036 N  N     . ALA A 1 799 ? -54.845 10.090  -22.134 1.00 155.69 ? 902  ALA A N     1 
ATOM   6037 C  CA    . ALA A 1 799 ? -55.925 9.523   -22.934 1.00 160.58 ? 902  ALA A CA    1 
ATOM   6038 C  C     . ALA A 1 799 ? -55.857 8.002   -22.966 1.00 157.32 ? 902  ALA A C     1 
ATOM   6039 O  O     . ALA A 1 799 ? -56.896 7.336   -23.031 1.00 153.62 ? 902  ALA A O     1 
ATOM   6040 C  CB    . ALA A 1 799 ? -55.880 10.087  -24.355 1.00 152.23 ? 902  ALA A CB    1 
ATOM   6041 N  N     . GLY A 1 800 ? -54.650 7.437   -22.916 1.00 136.34 ? 903  GLY A N     1 
ATOM   6042 C  CA    . GLY A 1 800 ? -54.527 5.989   -22.885 1.00 133.41 ? 903  GLY A CA    1 
ATOM   6043 C  C     . GLY A 1 800 ? -54.912 5.406   -21.538 1.00 141.89 ? 903  GLY A C     1 
ATOM   6044 O  O     . GLY A 1 800 ? -55.669 4.434   -21.463 1.00 143.20 ? 903  GLY A O     1 
ATOM   6045 N  N     . TYR A 1 801 ? -54.401 5.995   -20.455 1.00 137.65 ? 904  TYR A N     1 
ATOM   6046 C  CA    . TYR A 1 801 ? -54.711 5.507   -19.117 1.00 130.57 ? 904  TYR A CA    1 
ATOM   6047 C  C     . TYR A 1 801 ? -56.116 5.874   -18.659 1.00 137.58 ? 904  TYR A C     1 
ATOM   6048 O  O     . TYR A 1 801 ? -56.550 5.390   -17.609 1.00 149.93 ? 904  TYR A O     1 
ATOM   6049 C  CB    . TYR A 1 801 ? -53.684 6.034   -18.112 1.00 114.77 ? 904  TYR A CB    1 
ATOM   6050 C  CG    . TYR A 1 801 ? -52.471 5.143   -17.965 1.00 118.50 ? 904  TYR A CG    1 
ATOM   6051 C  CD1   . TYR A 1 801 ? -52.496 4.042   -17.120 1.00 123.10 ? 904  TYR A CD1   1 
ATOM   6052 C  CD2   . TYR A 1 801 ? -51.304 5.401   -18.671 1.00 122.65 ? 904  TYR A CD2   1 
ATOM   6053 C  CE1   . TYR A 1 801 ? -51.394 3.221   -16.981 1.00 123.41 ? 904  TYR A CE1   1 
ATOM   6054 C  CE2   . TYR A 1 801 ? -50.195 4.584   -18.540 1.00 137.22 ? 904  TYR A CE2   1 
ATOM   6055 C  CZ    . TYR A 1 801 ? -50.247 3.496   -17.693 1.00 132.30 ? 904  TYR A CZ    1 
ATOM   6056 O  OH    . TYR A 1 801 ? -49.148 2.679   -17.554 1.00 148.68 ? 904  TYR A OH    1 
ATOM   6057 N  N     . CYS A 1 802 ? -56.832 6.712   -19.407 1.00 128.32 ? 905  CYS A N     1 
ATOM   6058 C  CA    . CYS A 1 802 ? -58.226 6.998   -19.092 1.00 138.95 ? 905  CYS A CA    1 
ATOM   6059 C  C     . CYS A 1 802 ? -59.179 6.101   -19.870 1.00 139.47 ? 905  CYS A C     1 
ATOM   6060 O  O     . CYS A 1 802 ? -60.166 5.611   -19.310 1.00 126.41 ? 905  CYS A O     1 
ATOM   6061 C  CB    . CYS A 1 802 ? -58.546 8.468   -19.376 1.00 136.52 ? 905  CYS A CB    1 
ATOM   6062 S  SG    . CYS A 1 802 ? -60.276 8.923   -19.112 1.00 188.41 ? 905  CYS A SG    1 
ATOM   6063 N  N     . VAL A 1 803 ? -58.897 5.871   -21.154 1.00 144.83 ? 906  VAL A N     1 
ATOM   6064 C  CA    . VAL A 1 803 ? -59.761 5.020   -21.965 1.00 137.10 ? 906  VAL A CA    1 
ATOM   6065 C  C     . VAL A 1 803 ? -59.563 3.543   -21.651 1.00 126.79 ? 906  VAL A C     1 
ATOM   6066 O  O     . VAL A 1 803 ? -60.419 2.723   -22.005 1.00 122.36 ? 906  VAL A O     1 
ATOM   6067 C  CB    . VAL A 1 803 ? -59.526 5.287   -23.462 1.00 123.13 ? 906  VAL A CB    1 
ATOM   6068 C  CG1   . VAL A 1 803 ? -58.290 4.548   -23.954 1.00 136.33 ? 906  VAL A CG1   1 
ATOM   6069 C  CG2   . VAL A 1 803 ? -60.753 4.906   -24.274 1.00 130.00 ? 906  VAL A CG2   1 
ATOM   6070 N  N     . ALA A 1 804 ? -58.465 3.178   -20.989 1.00 133.79 ? 907  ALA A N     1 
ATOM   6071 C  CA    . ALA A 1 804 ? -58.218 1.786   -20.633 1.00 116.63 ? 907  ALA A CA    1 
ATOM   6072 C  C     . ALA A 1 804 ? -58.850 1.411   -19.299 1.00 124.75 ? 907  ALA A C     1 
ATOM   6073 O  O     . ALA A 1 804 ? -59.430 0.327   -19.174 1.00 124.48 ? 907  ALA A O     1 
ATOM   6074 C  CB    . ALA A 1 804 ? -56.713 1.509   -20.590 1.00 109.92 ? 907  ALA A CB    1 
ATOM   6075 N  N     . THR A 1 805 ? -58.748 2.289   -18.298 1.00 137.76 ? 908  THR A N     1 
ATOM   6076 C  CA    . THR A 1 805 ? -59.360 2.005   -17.004 1.00 114.75 ? 908  THR A CA    1 
ATOM   6077 C  C     . THR A 1 805 ? -60.881 1.998   -17.091 1.00 130.91 ? 908  THR A C     1 
ATOM   6078 O  O     . THR A 1 805 ? -61.542 1.322   -16.295 1.00 136.56 ? 908  THR A O     1 
ATOM   6079 C  CB    . THR A 1 805 ? -58.895 3.024   -15.964 1.00 113.34 ? 908  THR A CB    1 
ATOM   6080 O  OG1   . THR A 1 805 ? -59.180 4.349   -16.428 1.00 128.28 ? 908  THR A OG1   1 
ATOM   6081 C  CG2   . THR A 1 805 ? -57.400 2.885   -15.716 1.00 103.91 ? 908  THR A CG2   1 
ATOM   6082 N  N     . PHE A 1 806 ? -61.452 2.741   -18.043 1.00 137.66 ? 909  PHE A N     1 
ATOM   6083 C  CA    . PHE A 1 806 ? -62.898 2.702   -18.232 1.00 123.79 ? 909  PHE A CA    1 
ATOM   6084 C  C     . PHE A 1 806 ? -63.348 1.365   -18.807 1.00 139.32 ? 909  PHE A C     1 
ATOM   6085 O  O     . PHE A 1 806 ? -64.445 0.892   -18.488 1.00 154.99 ? 909  PHE A O     1 
ATOM   6086 C  CB    . PHE A 1 806 ? -63.342 3.851   -19.138 1.00 119.04 ? 909  PHE A CB    1 
ATOM   6087 C  CG    . PHE A 1 806 ? -64.832 3.967   -19.281 1.00 137.76 ? 909  PHE A CG    1 
ATOM   6088 C  CD1   . PHE A 1 806 ? -65.581 4.640   -18.330 1.00 167.62 ? 909  PHE A CD1   1 
ATOM   6089 C  CD2   . PHE A 1 806 ? -65.485 3.405   -20.366 1.00 147.62 ? 909  PHE A CD2   1 
ATOM   6090 C  CE1   . PHE A 1 806 ? -66.952 4.749   -18.457 1.00 179.22 ? 909  PHE A CE1   1 
ATOM   6091 C  CE2   . PHE A 1 806 ? -66.856 3.510   -20.498 1.00 149.44 ? 909  PHE A CE2   1 
ATOM   6092 C  CZ    . PHE A 1 806 ? -67.590 4.182   -19.543 1.00 174.54 ? 909  PHE A CZ    1 
ATOM   6093 N  N     . ILE A 1 807 ? -62.520 0.744   -19.649 1.00 138.93 ? 910  ILE A N     1 
ATOM   6094 C  CA    . ILE A 1 807 ? -62.844 -0.578  -20.172 1.00 134.29 ? 910  ILE A CA    1 
ATOM   6095 C  C     . ILE A 1 807 ? -62.612 -1.646  -19.110 1.00 135.57 ? 910  ILE A C     1 
ATOM   6096 O  O     . ILE A 1 807 ? -63.367 -2.620  -19.015 1.00 138.74 ? 910  ILE A O     1 
ATOM   6097 C  CB    . ILE A 1 807 ? -62.030 -0.856  -21.449 1.00 116.01 ? 910  ILE A CB    1 
ATOM   6098 C  CG1   . ILE A 1 807 ? -62.311 0.218   -22.502 1.00 113.71 ? 910  ILE A CG1   1 
ATOM   6099 C  CG2   . ILE A 1 807 ? -62.354 -2.234  -22.006 1.00 100.42 ? 910  ILE A CG2   1 
ATOM   6100 C  CD1   . ILE A 1 807 ? -61.427 0.118   -23.727 1.00 112.41 ? 910  ILE A CD1   1 
ATOM   6101 N  N     . LEU A 1 808 ? -61.574 -1.480  -18.290 1.00 114.28 ? 911  LEU A N     1 
ATOM   6102 C  CA    . LEU A 1 808 ? -61.301 -2.443  -17.229 1.00 128.61 ? 911  LEU A CA    1 
ATOM   6103 C  C     . LEU A 1 808 ? -62.253 -2.259  -16.053 1.00 129.87 ? 911  LEU A C     1 
ATOM   6104 O  O     . LEU A 1 808 ? -62.805 -3.233  -15.532 1.00 132.94 ? 911  LEU A O     1 
ATOM   6105 C  CB    . LEU A 1 808 ? -59.848 -2.321  -16.766 1.00 139.68 ? 911  LEU A CB    1 
ATOM   6106 C  CG    . LEU A 1 808 ? -58.823 -3.238  -17.439 1.00 126.87 ? 911  LEU A CG    1 
ATOM   6107 C  CD1   . LEU A 1 808 ? -59.166 -4.696  -17.174 1.00 159.74 ? 911  LEU A CD1   1 
ATOM   6108 C  CD2   . LEU A 1 808 ? -58.734 -2.970  -18.933 1.00 98.28  ? 911  LEU A CD2   1 
ATOM   6109 N  N     . GLY A 1 809 ? -62.461 -1.017  -15.625 1.00 138.51 ? 912  GLY A N     1 
ATOM   6110 C  CA    . GLY A 1 809 ? -63.305 -0.756  -14.477 1.00 134.91 ? 912  GLY A CA    1 
ATOM   6111 C  C     . GLY A 1 809 ? -62.540 -0.841  -13.174 1.00 143.79 ? 912  GLY A C     1 
ATOM   6112 O  O     . GLY A 1 809 ? -63.024 -1.417  -12.195 1.00 176.54 ? 912  GLY A O     1 
ATOM   6113 N  N     . ILE A 1 810 ? -61.332 -0.271  -13.157 1.00 148.84 ? 913  ILE A N     1 
ATOM   6114 C  CA    . ILE A 1 810 ? -60.519 -0.274  -11.947 1.00 163.11 ? 913  ILE A CA    1 
ATOM   6115 C  C     . ILE A 1 810 ? -61.201 0.556   -10.862 1.00 167.83 ? 913  ILE A C     1 
ATOM   6116 O  O     . ILE A 1 810 ? -62.101 1.363   -11.122 1.00 180.04 ? 913  ILE A O     1 
ATOM   6117 C  CB    . ILE A 1 810 ? -59.105 0.250   -12.250 1.00 146.52 ? 913  ILE A CB    1 
ATOM   6118 C  CG1   . ILE A 1 810 ? -58.658 -0.206  -13.640 1.00 124.92 ? 913  ILE A CG1   1 
ATOM   6119 C  CG2   . ILE A 1 810 ? -58.105 -0.242  -11.213 1.00 171.34 ? 913  ILE A CG2   1 
ATOM   6120 N  N     . GLY A 1 811 ? -60.769 0.342   -9.623  1.00 169.61 ? 914  GLY A N     1 
ATOM   6121 C  CA    . GLY A 1 811 ? -61.313 1.080   -8.500  1.00 185.84 ? 914  GLY A CA    1 
ATOM   6122 C  C     . GLY A 1 811 ? -61.085 2.575   -8.628  1.00 180.76 ? 914  GLY A C     1 
ATOM   6123 O  O     . GLY A 1 811 ? -60.361 3.067   -9.494  1.00 174.38 ? 914  GLY A O     1 
ATOM   6124 N  N     . ASP A 1 812 ? -61.734 3.313   -7.727  1.00 200.59 ? 915  ASP A N     1 
ATOM   6125 C  CA    . ASP A 1 812 ? -61.671 4.770   -7.733  1.00 207.72 ? 915  ASP A CA    1 
ATOM   6126 C  C     . ASP A 1 812 ? -60.236 5.260   -7.587  1.00 204.37 ? 915  ASP A C     1 
ATOM   6127 O  O     . ASP A 1 812 ? -59.622 5.105   -6.527  1.00 213.15 ? 915  ASP A O     1 
ATOM   6128 C  CB    . ASP A 1 812 ? -62.549 5.345   -6.619  1.00 229.20 ? 915  ASP A CB    1 
ATOM   6129 C  CG    . ASP A 1 812 ? -64.004 4.937   -6.755  1.00 231.77 ? 915  ASP A CG    1 
ATOM   6130 O  OD1   . ASP A 1 812 ? -64.453 4.702   -7.897  1.00 230.60 ? 915  ASP A OD1   1 
ATOM   6131 O  OD2   . ASP A 1 812 ? -64.700 4.851   -5.721  1.00 228.24 ? 915  ASP A OD2   1 
ATOM   6132 N  N     . ARG A 1 813 ? -59.696 5.849   -8.652  1.00 190.75 ? 916  ARG A N     1 
ATOM   6133 C  CA    . ARG A 1 813 ? -58.321 6.326   -8.650  1.00 178.08 ? 916  ARG A CA    1 
ATOM   6134 C  C     . ARG A 1 813 ? -58.241 7.698   -7.993  1.00 183.76 ? 916  ARG A C     1 
ATOM   6135 O  O     . ARG A 1 813 ? -58.961 8.624   -8.379  1.00 188.40 ? 916  ARG A O     1 
ATOM   6136 C  CB    . ARG A 1 813 ? -57.784 6.400   -10.080 1.00 174.11 ? 916  ARG A CB    1 
ATOM   6137 C  CG    . ARG A 1 813 ? -58.050 5.164   -10.926 1.00 168.21 ? 916  ARG A CG    1 
ATOM   6138 C  CD    . ARG A 1 813 ? -56.827 4.266   -11.010 1.00 169.23 ? 916  ARG A CD    1 
ATOM   6139 N  NE    . ARG A 1 813 ? -56.612 3.499   -9.790  1.00 163.96 ? 916  ARG A NE    1 
ATOM   6140 C  CZ    . ARG A 1 813 ? -55.560 2.722   -9.573  1.00 170.01 ? 916  ARG A CZ    1 
ATOM   6141 N  NH1   . ARG A 1 813 ? -54.591 2.605   -10.466 1.00 172.19 ? 916  ARG A NH1   1 
ATOM   6142 N  NH2   . ARG A 1 813 ? -55.475 2.048   -8.429  1.00 195.70 ? 916  ARG A NH2   1 
ATOM   6143 N  N     . HIS A 1 814 ? -57.365 7.829   -7.001  1.00 186.82 ? 917  HIS A N     1 
ATOM   6144 C  CA    . HIS A 1 814 ? -57.119 9.096   -6.334  1.00 184.90 ? 917  HIS A CA    1 
ATOM   6145 C  C     . HIS A 1 814 ? -55.731 9.615   -6.708  1.00 172.74 ? 917  HIS A C     1 
ATOM   6146 O  O     . HIS A 1 814 ? -55.089 9.123   -7.644  1.00 171.84 ? 917  HIS A O     1 
ATOM   6147 C  CB    . HIS A 1 814 ? -57.293 8.944   -4.820  1.00 181.62 ? 917  HIS A CB    1 
ATOM   6148 C  CG    . HIS A 1 814 ? -56.951 7.582   -4.301  1.00 178.39 ? 917  HIS A CG    1 
ATOM   6149 N  ND1   . HIS A 1 814 ? -55.653 7.148   -4.140  1.00 177.62 ? 917  HIS A ND1   1 
ATOM   6150 C  CD2   . HIS A 1 814 ? -57.742 6.559   -3.898  1.00 194.07 ? 917  HIS A CD2   1 
ATOM   6151 C  CE1   . HIS A 1 814 ? -55.659 5.915   -3.662  1.00 194.36 ? 917  HIS A CE1   1 
ATOM   6152 N  NE2   . HIS A 1 814 ? -56.914 5.534   -3.509  1.00 194.81 ? 917  HIS A NE2   1 
ATOM   6153 N  N     . ASN A 1 815 ? -55.265 10.626  -5.969  1.00 180.05 ? 918  ASN A N     1 
ATOM   6154 C  CA    . ASN A 1 815 ? -53.995 11.265  -6.295  1.00 169.79 ? 918  ASN A CA    1 
ATOM   6155 C  C     . ASN A 1 815 ? -52.796 10.362  -6.034  1.00 175.25 ? 918  ASN A C     1 
ATOM   6156 O  O     . ASN A 1 815 ? -51.738 10.574  -6.635  1.00 174.25 ? 918  ASN A O     1 
ATOM   6157 C  CB    . ASN A 1 815 ? -53.846 12.570  -5.511  1.00 173.56 ? 918  ASN A CB    1 
ATOM   6158 C  CG    . ASN A 1 815 ? -54.864 13.615  -5.922  1.00 189.41 ? 918  ASN A CG    1 
ATOM   6159 O  OD1   . ASN A 1 815 ? -55.943 13.286  -6.416  1.00 182.90 ? 918  ASN A OD1   1 
ATOM   6160 N  ND2   . ASN A 1 815 ? -54.523 14.883  -5.726  1.00 212.91 ? 918  ASN A ND2   1 
ATOM   6161 N  N     . SER A 1 816 ? -52.931 9.369   -5.157  1.00 180.40 ? 919  SER A N     1 
ATOM   6162 C  CA    . SER A 1 816 ? -51.848 8.427   -4.907  1.00 175.09 ? 919  SER A CA    1 
ATOM   6163 C  C     . SER A 1 816 ? -51.872 7.231   -5.850  1.00 168.96 ? 919  SER A C     1 
ATOM   6164 O  O     . SER A 1 816 ? -50.885 6.489   -5.908  1.00 153.67 ? 919  SER A O     1 
ATOM   6165 C  CB    . SER A 1 816 ? -51.891 7.941   -3.454  1.00 184.41 ? 919  SER A CB    1 
ATOM   6166 O  OG    . SER A 1 816 ? -53.162 7.413   -3.127  1.00 194.62 ? 919  SER A OG    1 
ATOM   6167 N  N     . ASN A 1 817 ? -52.967 7.024   -6.585  1.00 163.13 ? 920  ASN A N     1 
ATOM   6168 C  CA    . ASN A 1 817 ? -53.004 5.985   -7.607  1.00 158.07 ? 920  ASN A CA    1 
ATOM   6169 C  C     . ASN A 1 817 ? -52.391 6.439   -8.923  1.00 163.93 ? 920  ASN A C     1 
ATOM   6170 O  O     . ASN A 1 817 ? -52.037 5.593   -9.751  1.00 168.20 ? 920  ASN A O     1 
ATOM   6171 C  CB    . ASN A 1 817 ? -54.443 5.528   -7.859  1.00 158.51 ? 920  ASN A CB    1 
ATOM   6172 C  CG    . ASN A 1 817 ? -55.008 4.715   -6.716  1.00 179.41 ? 920  ASN A CG    1 
ATOM   6173 O  OD1   . ASN A 1 817 ? -56.190 4.823   -6.388  1.00 196.16 ? 920  ASN A OD1   1 
ATOM   6174 N  ND2   . ASN A 1 817 ? -54.166 3.892   -6.101  1.00 196.54 ? 920  ASN A ND2   1 
ATOM   6175 N  N     . ILE A 1 818 ? -52.261 7.746   -9.135  1.00 152.29 ? 921  ILE A N     1 
ATOM   6176 C  CA    . ILE A 1 818 ? -51.750 8.307   -10.380 1.00 139.11 ? 921  ILE A CA    1 
ATOM   6177 C  C     . ILE A 1 818 ? -50.374 8.896   -10.114 1.00 144.68 ? 921  ILE A C     1 
ATOM   6178 O  O     . ILE A 1 818 ? -50.201 9.693   -9.183  1.00 152.10 ? 921  ILE A O     1 
ATOM   6179 C  CB    . ILE A 1 818 ? -52.704 9.372   -10.949 1.00 140.19 ? 921  ILE A CB    1 
ATOM   6180 C  CG1   . ILE A 1 818 ? -54.111 8.793   -11.114 1.00 121.81 ? 921  ILE A CG1   1 
ATOM   6181 C  CG2   . ILE A 1 818 ? -52.182 9.902   -12.274 1.00 152.25 ? 921  ILE A CG2   1 
ATOM   6182 C  CD1   . ILE A 1 818 ? -55.124 9.789   -11.631 1.00 127.85 ? 921  ILE A CD1   1 
ATOM   6183 N  N     . MET A 1 819 ? -49.398 8.506   -10.929 1.00 137.55 ? 922  MET A N     1 
ATOM   6184 C  CA    . MET A 1 819 ? -48.037 9.007   -10.820 1.00 132.80 ? 922  MET A CA    1 
ATOM   6185 C  C     . MET A 1 819 ? -47.603 9.623   -12.143 1.00 149.99 ? 922  MET A C     1 
ATOM   6186 O  O     . MET A 1 819 ? -48.046 9.206   -13.217 1.00 126.51 ? 922  MET A O     1 
ATOM   6187 C  CB    . MET A 1 819 ? -47.059 7.895   -10.424 1.00 122.17 ? 922  MET A CB    1 
ATOM   6188 C  CG    . MET A 1 819 ? -47.364 7.241   -9.089  1.00 123.39 ? 922  MET A CG    1 
ATOM   6189 S  SD    . MET A 1 819 ? -46.027 6.164   -8.543  1.00 134.02 ? 922  MET A SD    1 
ATOM   6190 C  CE    . MET A 1 819 ? -44.675 7.334   -8.451  1.00 140.80 ? 922  MET A CE    1 
ATOM   6191 N  N     . VAL A 1 820 ? -46.732 10.625  -12.052 1.00 159.75 ? 923  VAL A N     1 
ATOM   6192 C  CA    . VAL A 1 820 ? -46.184 11.298  -13.220 1.00 140.04 ? 923  VAL A CA    1 
ATOM   6193 C  C     . VAL A 1 820 ? -44.667 11.313  -13.112 1.00 138.83 ? 923  VAL A C     1 
ATOM   6194 O  O     . VAL A 1 820 ? -44.101 11.294  -12.014 1.00 154.95 ? 923  VAL A O     1 
ATOM   6195 C  CB    . VAL A 1 820 ? -46.730 12.736  -13.376 1.00 135.29 ? 923  VAL A CB    1 
ATOM   6196 C  CG1   . VAL A 1 820 ? -48.233 12.713  -13.610 1.00 152.52 ? 923  VAL A CG1   1 
ATOM   6197 C  CG2   . VAL A 1 820 ? -46.387 13.572  -12.152 1.00 138.73 ? 923  VAL A CG2   1 
ATOM   6198 N  N     . LYS A 1 821 ? -44.010 11.338  -14.264 1.00 135.01 ? 924  LYS A N     1 
ATOM   6199 C  CA    . LYS A 1 821 ? -42.561 11.425  -14.343 1.00 136.93 ? 924  LYS A CA    1 
ATOM   6200 C  C     . LYS A 1 821 ? -42.138 12.862  -14.621 1.00 163.91 ? 924  LYS A C     1 
ATOM   6201 O  O     . LYS A 1 821 ? -42.944 13.705  -15.023 1.00 152.84 ? 924  LYS A O     1 
ATOM   6202 C  CB    . LYS A 1 821 ? -42.021 10.498  -15.436 1.00 129.83 ? 924  LYS A CB    1 
ATOM   6203 C  CG    . LYS A 1 821 ? -42.372 9.033   -15.241 1.00 131.97 ? 924  LYS A CG    1 
ATOM   6204 C  CD    . LYS A 1 821 ? -42.044 8.217   -16.483 1.00 124.33 ? 924  LYS A CD    1 
ATOM   6205 C  CE    . LYS A 1 821 ? -40.575 8.335   -16.856 1.00 144.91 ? 924  LYS A CE    1 
ATOM   6206 N  NZ    . LYS A 1 821 ? -40.257 7.571   -18.094 1.00 135.97 ? 924  LYS A NZ    1 
ATOM   6207 N  N     . ASP A 1 822 ? -40.851 13.135  -14.394 1.00 172.40 ? 925  ASP A N     1 
ATOM   6208 C  CA    . ASP A 1 822 ? -40.313 14.444  -14.749 1.00 162.35 ? 925  ASP A CA    1 
ATOM   6209 C  C     . ASP A 1 822 ? -40.365 14.667  -16.254 1.00 163.83 ? 925  ASP A C     1 
ATOM   6210 O  O     . ASP A 1 822 ? -40.424 15.814  -16.712 1.00 178.01 ? 925  ASP A O     1 
ATOM   6211 C  CB    . ASP A 1 822 ? -38.882 14.587  -14.233 1.00 158.63 ? 925  ASP A CB    1 
ATOM   6212 C  CG    . ASP A 1 822 ? -37.923 13.620  -14.896 1.00 167.20 ? 925  ASP A CG    1 
ATOM   6213 O  OD1   . ASP A 1 822 ? -38.367 12.528  -15.309 1.00 181.23 ? 925  ASP A OD1   1 
ATOM   6214 O  OD2   . ASP A 1 822 ? -36.724 13.952  -15.006 1.00 169.63 ? 925  ASP A OD2   1 
ATOM   6215 N  N     . ASP A 1 823 ? -40.344 13.585  -17.035 1.00 173.43 ? 926  ASP A N     1 
ATOM   6216 C  CA    . ASP A 1 823 ? -40.538 13.684  -18.475 1.00 159.71 ? 926  ASP A CA    1 
ATOM   6217 C  C     . ASP A 1 823 ? -41.953 14.125  -18.830 1.00 151.75 ? 926  ASP A C     1 
ATOM   6218 O  O     . ASP A 1 823 ? -42.165 14.678  -19.914 1.00 143.50 ? 926  ASP A O     1 
ATOM   6219 C  CB    . ASP A 1 823 ? -40.226 12.338  -19.133 1.00 158.15 ? 926  ASP A CB    1 
ATOM   6220 C  CG    . ASP A 1 823 ? -40.088 12.438  -20.639 1.00 173.76 ? 926  ASP A CG    1 
ATOM   6221 O  OD1   . ASP A 1 823 ? -39.943 13.566  -21.155 1.00 193.34 ? 926  ASP A OD1   1 
ATOM   6222 O  OD2   . ASP A 1 823 ? -40.125 11.383  -21.308 1.00 167.77 ? 926  ASP A OD2   1 
ATOM   6223 N  N     . GLY A 1 824 ? -42.917 13.898  -17.943 1.00 146.67 ? 927  GLY A N     1 
ATOM   6224 C  CA    . GLY A 1 824 ? -44.293 14.278  -18.178 1.00 132.24 ? 927  GLY A CA    1 
ATOM   6225 C  C     . GLY A 1 824 ? -45.239 13.140  -18.495 1.00 139.37 ? 927  GLY A C     1 
ATOM   6226 O  O     . GLY A 1 824 ? -46.374 13.403  -18.909 1.00 126.81 ? 927  GLY A O     1 
ATOM   6227 N  N     . GLN A 1 825 ? -44.820 11.891  -18.311 1.00 147.45 ? 928  GLN A N     1 
ATOM   6228 C  CA    . GLN A 1 825 ? -45.648 10.737  -18.636 1.00 119.39 ? 928  GLN A CA    1 
ATOM   6229 C  C     . GLN A 1 825 ? -46.534 10.378  -17.450 1.00 123.39 ? 928  GLN A C     1 
ATOM   6230 O  O     . GLN A 1 825 ? -46.060 10.301  -16.312 1.00 119.56 ? 928  GLN A O     1 
ATOM   6231 C  CB    . GLN A 1 825 ? -44.776 9.544   -19.027 1.00 134.10 ? 928  GLN A CB    1 
ATOM   6232 C  CG    . GLN A 1 825 ? -45.559 8.296   -19.395 1.00 146.49 ? 928  GLN A CG    1 
ATOM   6233 C  CD    . GLN A 1 825 ? -44.659 7.138   -19.779 1.00 142.53 ? 928  GLN A CD    1 
ATOM   6234 O  OE1   . GLN A 1 825 ? -43.434 7.265   -19.788 1.00 124.05 ? 928  GLN A OE1   1 
ATOM   6235 N  NE2   . GLN A 1 825 ? -45.264 6.000   -20.099 1.00 139.86 ? 928  GLN A NE2   1 
ATOM   6236 N  N     . LEU A 1 826 ? -47.816 10.154  -17.723 1.00 124.54 ? 929  LEU A N     1 
ATOM   6237 C  CA    . LEU A 1 826 ? -48.792 9.800   -16.702 1.00 119.48 ? 929  LEU A CA    1 
ATOM   6238 C  C     . LEU A 1 826 ? -49.062 8.302   -16.741 1.00 135.68 ? 929  LEU A C     1 
ATOM   6239 O  O     . LEU A 1 826 ? -49.188 7.710   -17.818 1.00 140.95 ? 929  LEU A O     1 
ATOM   6240 C  CB    . LEU A 1 826 ? -50.094 10.581  -16.908 1.00 99.74  ? 929  LEU A CB    1 
ATOM   6241 C  CG    . LEU A 1 826 ? -51.201 10.477  -15.854 1.00 112.71 ? 929  LEU A CG    1 
ATOM   6242 C  CD1   . LEU A 1 826 ? -51.941 11.799  -15.741 1.00 122.51 ? 929  LEU A CD1   1 
ATOM   6243 C  CD2   . LEU A 1 826 ? -52.179 9.358   -16.186 1.00 146.42 ? 929  LEU A CD2   1 
ATOM   6244 N  N     . PHE A 1 827 ? -49.151 7.692   -15.561 1.00 131.59 ? 930  PHE A N     1 
ATOM   6245 C  CA    . PHE A 1 827 ? -49.430 6.266   -15.461 1.00 134.23 ? 930  PHE A CA    1 
ATOM   6246 C  C     . PHE A 1 827 ? -50.047 5.973   -14.102 1.00 127.39 ? 930  PHE A C     1 
ATOM   6247 O  O     . PHE A 1 827 ? -49.785 6.675   -13.122 1.00 138.77 ? 930  PHE A O     1 
ATOM   6248 C  CB    . PHE A 1 827 ? -48.164 5.425   -15.674 1.00 134.86 ? 930  PHE A CB    1 
ATOM   6249 C  CG    . PHE A 1 827 ? -47.095 5.652   -14.641 1.00 125.48 ? 930  PHE A CG    1 
ATOM   6250 C  CD1   . PHE A 1 827 ? -46.218 6.719   -14.753 1.00 144.80 ? 930  PHE A CD1   1 
ATOM   6251 C  CD2   . PHE A 1 827 ? -46.956 4.789   -13.567 1.00 120.71 ? 930  PHE A CD2   1 
ATOM   6252 C  CE1   . PHE A 1 827 ? -45.231 6.926   -13.808 1.00 143.07 ? 930  PHE A CE1   1 
ATOM   6253 C  CE2   . PHE A 1 827 ? -45.972 4.991   -12.618 1.00 119.20 ? 930  PHE A CE2   1 
ATOM   6254 C  CZ    . PHE A 1 827 ? -45.108 6.061   -12.740 1.00 124.89 ? 930  PHE A CZ    1 
ATOM   6255 N  N     . HIS A 1 828 ? -50.869 4.929   -14.058 1.00 133.73 ? 931  HIS A N     1 
ATOM   6256 C  CA    . HIS A 1 828 ? -51.552 4.509   -12.844 1.00 125.83 ? 931  HIS A CA    1 
ATOM   6257 C  C     . HIS A 1 828 ? -50.846 3.310   -12.221 1.00 144.47 ? 931  HIS A C     1 
ATOM   6258 O  O     . HIS A 1 828 ? -50.084 2.595   -12.876 1.00 135.53 ? 931  HIS A O     1 
ATOM   6259 C  CB    . HIS A 1 828 ? -53.015 4.163   -13.135 1.00 129.46 ? 931  HIS A CB    1 
ATOM   6260 C  CG    . HIS A 1 828 ? -53.839 5.335   -13.569 1.00 144.50 ? 931  HIS A CG    1 
ATOM   6261 N  ND1   . HIS A 1 828 ? -55.189 5.239   -13.831 1.00 122.54 ? 931  HIS A ND1   1 
ATOM   6262 C  CD2   . HIS A 1 828 ? -53.505 6.629   -13.785 1.00 147.77 ? 931  HIS A CD2   1 
ATOM   6263 C  CE1   . HIS A 1 828 ? -55.650 6.423   -14.191 1.00 145.07 ? 931  HIS A CE1   1 
ATOM   6264 N  NE2   . HIS A 1 828 ? -54.649 7.284   -14.171 1.00 127.26 ? 931  HIS A NE2   1 
ATOM   6265 N  N     . ILE A 1 829 ? -51.114 3.097   -10.931 1.00 135.82 ? 932  ILE A N     1 
ATOM   6266 C  CA    . ILE A 1 829 ? -50.481 2.040   -10.152 1.00 137.39 ? 932  ILE A CA    1 
ATOM   6267 C  C     . ILE A 1 829 ? -51.513 1.428   -9.213  1.00 157.63 ? 932  ILE A C     1 
ATOM   6268 O  O     . ILE A 1 829 ? -52.608 1.960   -9.019  1.00 152.33 ? 932  ILE A O     1 
ATOM   6269 C  CB    . ILE A 1 829 ? -49.263 2.555   -9.353  1.00 143.42 ? 932  ILE A CB    1 
ATOM   6270 C  CG1   . ILE A 1 829 ? -49.645 3.770   -8.502  1.00 134.21 ? 932  ILE A CG1   1 
ATOM   6271 C  CG2   . ILE A 1 829 ? -48.120 2.906   -10.287 1.00 136.85 ? 932  ILE A CG2   1 
ATOM   6272 C  CD1   . ILE A 1 829 ? -49.914 3.452   -7.044  1.00 156.95 ? 932  ILE A CD1   1 
ATOM   6273 N  N     . ASP A 1 830 ? -51.140 0.288   -8.626  1.00 159.26 ? 933  ASP A N     1 
ATOM   6274 C  CA    . ASP A 1 830 ? -51.938 -0.414  -7.619  1.00 155.72 ? 933  ASP A CA    1 
ATOM   6275 C  C     . ASP A 1 830 ? -53.324 -0.772  -8.169  1.00 167.73 ? 933  ASP A C     1 
ATOM   6276 O  O     . ASP A 1 830 ? -54.350 -0.199  -7.798  1.00 158.50 ? 933  ASP A O     1 
ATOM   6277 C  CB    . ASP A 1 830 ? -52.047 0.418   -6.335  1.00 151.41 ? 933  ASP A CB    1 
ATOM   6278 C  CG    . ASP A 1 830 ? -52.664 -0.357  -5.185  1.00 166.97 ? 933  ASP A CG    1 
ATOM   6279 O  OD1   . ASP A 1 830 ? -52.820 -1.590  -5.308  1.00 159.92 ? 933  ASP A OD1   1 
ATOM   6280 O  OD2   . ASP A 1 830 ? -52.994 0.270   -4.156  1.00 194.49 ? 933  ASP A OD2   1 
ATOM   6281 N  N     . PHE A 1 831 ? -53.319 -1.754  -9.070  1.00 172.87 ? 934  PHE A N     1 
ATOM   6282 C  CA    . PHE A 1 831 ? -54.556 -2.267  -9.661  1.00 158.77 ? 934  PHE A CA    1 
ATOM   6283 C  C     . PHE A 1 831 ? -55.054 -3.455  -8.836  1.00 172.44 ? 934  PHE A C     1 
ATOM   6284 O  O     . PHE A 1 831 ? -55.091 -4.604  -9.280  1.00 183.39 ? 934  PHE A O     1 
ATOM   6285 C  CB    . PHE A 1 831 ? -54.334 -2.648  -11.118 1.00 147.28 ? 934  PHE A CB    1 
ATOM   6286 C  CG    . PHE A 1 831 ? -53.815 -1.525  -11.967 1.00 138.94 ? 934  PHE A CG    1 
ATOM   6287 C  CD1   . PHE A 1 831 ? -54.675 -0.559  -12.462 1.00 137.66 ? 934  PHE A CD1   1 
ATOM   6288 C  CD2   . PHE A 1 831 ? -52.469 -1.439  -12.277 1.00 135.94 ? 934  PHE A CD2   1 
ATOM   6289 C  CE1   . PHE A 1 831 ? -54.200 0.475   -13.246 1.00 145.83 ? 934  PHE A CE1   1 
ATOM   6290 C  CE2   . PHE A 1 831 ? -51.987 -0.408  -13.060 1.00 131.75 ? 934  PHE A CE2   1 
ATOM   6291 C  CZ    . PHE A 1 831 ? -52.854 0.550   -13.546 1.00 132.72 ? 934  PHE A CZ    1 
ATOM   6292 N  N     . GLY A 1 832 ? -55.442 -3.149  -7.601  1.00 172.10 ? 935  GLY A N     1 
ATOM   6293 C  CA    . GLY A 1 832 ? -55.921 -4.167  -6.688  1.00 166.35 ? 935  GLY A CA    1 
ATOM   6294 C  C     . GLY A 1 832 ? -57.337 -4.617  -6.978  1.00 164.73 ? 935  GLY A C     1 
ATOM   6295 O  O     . GLY A 1 832 ? -57.658 -5.802  -6.847  1.00 165.42 ? 935  GLY A O     1 
ATOM   6296 N  N     . HIS A 1 833 ? -58.195 -3.681  -7.377  1.00 180.65 ? 936  HIS A N     1 
ATOM   6297 C  CA    . HIS A 1 833 ? -59.601 -3.958  -7.656  1.00 184.46 ? 936  HIS A CA    1 
ATOM   6298 C  C     . HIS A 1 833 ? -59.899 -3.569  -9.099  1.00 182.34 ? 936  HIS A C     1 
ATOM   6299 O  O     . HIS A 1 833 ? -59.859 -2.385  -9.449  1.00 172.94 ? 936  HIS A O     1 
ATOM   6300 C  CB    . HIS A 1 833 ? -60.513 -3.204  -6.688  1.00 182.60 ? 936  HIS A CB    1 
ATOM   6301 C  CG    . HIS A 1 833 ? -60.382 -3.647  -5.264  1.00 187.07 ? 936  HIS A CG    1 
ATOM   6302 N  ND1   . HIS A 1 833 ? -59.225 -3.475  -4.534  1.00 190.89 ? 936  HIS A ND1   1 
ATOM   6303 C  CD2   . HIS A 1 833 ? -61.264 -4.253  -4.435  1.00 201.76 ? 936  HIS A CD2   1 
ATOM   6304 C  CE1   . HIS A 1 833 ? -59.400 -3.958  -3.317  1.00 201.72 ? 936  HIS A CE1   1 
ATOM   6305 N  NE2   . HIS A 1 833 ? -60.628 -4.436  -3.230  1.00 215.64 ? 936  HIS A NE2   1 
ATOM   6306 N  N     . PHE A 1 834 ? -60.197 -4.565  -9.930  1.00 183.16 ? 937  PHE A N     1 
ATOM   6307 C  CA    . PHE A 1 834 ? -60.598 -4.348  -11.311 1.00 165.60 ? 937  PHE A CA    1 
ATOM   6308 C  C     . PHE A 1 834 ? -61.832 -5.191  -11.602 1.00 168.77 ? 937  PHE A C     1 
ATOM   6309 O  O     . PHE A 1 834 ? -62.072 -6.208  -10.946 1.00 200.11 ? 937  PHE A O     1 
ATOM   6310 C  CB    . PHE A 1 834 ? -59.466 -4.690  -12.294 1.00 184.31 ? 937  PHE A CB    1 
ATOM   6311 C  CG    . PHE A 1 834 ? -59.143 -6.157  -12.371 1.00 183.59 ? 937  PHE A CG    1 
ATOM   6312 C  CD1   . PHE A 1 834 ? -58.492 -6.796  -11.330 1.00 177.66 ? 937  PHE A CD1   1 
ATOM   6313 C  CD2   . PHE A 1 834 ? -59.476 -6.891  -13.496 1.00 169.42 ? 937  PHE A CD2   1 
ATOM   6314 C  CE1   . PHE A 1 834 ? -58.194 -8.143  -11.405 1.00 153.77 ? 937  PHE A CE1   1 
ATOM   6315 C  CE2   . PHE A 1 834 ? -59.178 -8.236  -13.577 1.00 150.74 ? 937  PHE A CE2   1 
ATOM   6316 C  CZ    . PHE A 1 834 ? -58.536 -8.862  -12.530 1.00 134.02 ? 937  PHE A CZ    1 
ATOM   6317 N  N     . LEU A 1 835 ? -62.618 -4.749  -12.585 1.00 163.97 ? 938  LEU A N     1 
ATOM   6318 C  CA    . LEU A 1 835 ? -63.920 -5.338  -12.903 1.00 171.11 ? 938  LEU A CA    1 
ATOM   6319 C  C     . LEU A 1 835 ? -64.877 -5.286  -11.716 1.00 204.57 ? 938  LEU A C     1 
ATOM   6320 O  O     . LEU A 1 835 ? -65.834 -6.065  -11.651 1.00 216.57 ? 938  LEU A O     1 
ATOM   6321 C  CB    . LEU A 1 835 ? -63.782 -6.784  -13.399 1.00 166.55 ? 938  LEU A CB    1 
ATOM   6322 C  CG    . LEU A 1 835 ? -63.575 -7.066  -14.890 1.00 161.24 ? 938  LEU A CG    1 
ATOM   6323 C  CD1   . LEU A 1 835 ? -62.338 -6.371  -15.430 1.00 186.58 ? 938  LEU A CD1   1 
ATOM   6324 C  CD2   . LEU A 1 835 ? -63.485 -8.566  -15.125 1.00 146.86 ? 938  LEU A CD2   1 
ATOM   6325 N  N     . ASP A 1 836 ? -64.639 -4.375  -10.776 1.00 201.44 ? 939  ASP A N     1 
ATOM   6326 C  CA    . ASP A 1 836 ? -65.423 -4.311  -9.555  1.00 199.55 ? 939  ASP A CA    1 
ATOM   6327 C  C     . ASP A 1 836 ? -66.694 -3.494  -9.773  1.00 215.46 ? 939  ASP A C     1 
ATOM   6328 O  O     . ASP A 1 836 ? -66.774 -2.640  -10.660 1.00 203.46 ? 939  ASP A O     1 
ATOM   6329 C  CB    . ASP A 1 836 ? -64.594 -3.708  -8.420  1.00 196.76 ? 939  ASP A CB    1 
ATOM   6330 C  CG    . ASP A 1 836 ? -65.087 -4.126  -7.047  1.00 216.95 ? 939  ASP A CG    1 
ATOM   6331 O  OD1   . ASP A 1 836 ? -66.297 -4.396  -6.900  1.00 218.98 ? 939  ASP A OD1   1 
ATOM   6332 O  OD2   . ASP A 1 836 ? -64.260 -4.185  -6.113  1.00 218.73 ? 939  ASP A OD2   1 
ATOM   6333 N  N     . HIS A 1 837 ? -67.698 -3.770  -8.941  1.00 237.55 ? 940  HIS A N     1 
ATOM   6334 C  CA    . HIS A 1 837 ? -68.981 -3.086  -9.039  1.00 239.28 ? 940  HIS A CA    1 
ATOM   6335 C  C     . HIS A 1 837 ? -69.633 -2.950  -7.669  1.00 237.73 ? 940  HIS A C     1 
ATOM   6336 O  O     . HIS A 1 837 ? -70.621 -2.223  -7.518  1.00 228.72 ? 940  HIS A O     1 
ATOM   6337 C  CB    . HIS A 1 837 ? -69.910 -3.832  -9.999  1.00 239.19 ? 940  HIS A CB    1 
ATOM   6338 C  CG    . HIS A 1 837 ? -70.146 -5.262  -9.623  1.00 243.53 ? 940  HIS A CG    1 
ATOM   6339 N  ND1   . HIS A 1 837 ? -69.375 -6.296  -10.108 1.00 226.81 ? 940  HIS A ND1   1 
ATOM   6340 C  CD2   . HIS A 1 837 ? -71.066 -5.829  -8.806  1.00 234.41 ? 940  HIS A CD2   1 
ATOM   6341 C  CE1   . HIS A 1 837 ? -69.810 -7.439  -9.607  1.00 231.91 ? 940  HIS A CE1   1 
ATOM   6342 N  NE2   . HIS A 1 837 ? -70.835 -7.183  -8.815  1.00 229.47 ? 940  HIS A NE2   1 
ATOM   6343 N  N     . LYS A 1 838 ? -69.085 -3.646  -6.674  1.00 224.67 ? 941  LYS A N     1 
ATOM   6344 C  CA    . LYS A 1 838 ? -69.598 -3.620  -5.304  1.00 211.52 ? 941  LYS A CA    1 
ATOM   6345 C  C     . LYS A 1 838 ? -71.076 -3.998  -5.242  1.00 202.25 ? 941  LYS A C     1 
ATOM   6346 O  O     . LYS A 1 838 ? -71.893 -3.258  -4.695  1.00 185.86 ? 941  LYS A O     1 
ATOM   6347 C  CB    . LYS A 1 838 ? -69.382 -2.241  -4.673  1.00 193.69 ? 941  LYS A CB    1 
ATOM   6348 N  N     . VAL A 1 849 ? -65.196 6.505   -15.000 1.00 160.29 ? 952  VAL A N     1 
ATOM   6349 C  CA    . VAL A 1 849 ? -65.494 6.689   -13.583 1.00 179.59 ? 952  VAL A CA    1 
ATOM   6350 C  C     . VAL A 1 849 ? -64.235 6.650   -12.697 1.00 182.76 ? 952  VAL A C     1 
ATOM   6351 O  O     . VAL A 1 849 ? -64.076 7.516   -11.838 1.00 180.47 ? 952  VAL A O     1 
ATOM   6352 C  CB    . VAL A 1 849 ? -66.535 5.654   -13.096 1.00 177.77 ? 952  VAL A CB    1 
ATOM   6353 C  CG1   . VAL A 1 849 ? -66.964 5.963   -11.669 1.00 166.75 ? 952  VAL A CG1   1 
ATOM   6354 C  CG2   . VAL A 1 849 ? -67.735 5.629   -14.029 1.00 169.56 ? 952  VAL A CG2   1 
ATOM   6355 N  N     . PRO A 1 850 ? -63.342 5.664   -12.880 1.00 178.89 ? 953  PRO A N     1 
ATOM   6356 C  CA    . PRO A 1 850 ? -62.121 5.671   -12.055 1.00 176.77 ? 953  PRO A CA    1 
ATOM   6357 C  C     . PRO A 1 850 ? -61.187 6.822   -12.380 1.00 168.91 ? 953  PRO A C     1 
ATOM   6358 O  O     . PRO A 1 850 ? -60.616 7.425   -11.462 1.00 168.92 ? 953  PRO A O     1 
ATOM   6359 C  CB    . PRO A 1 850 ? -61.481 4.309   -12.361 1.00 162.78 ? 953  PRO A CB    1 
ATOM   6360 C  CG    . PRO A 1 850 ? -61.994 3.947   -13.699 1.00 136.26 ? 953  PRO A CG    1 
ATOM   6361 C  CD    . PRO A 1 850 ? -63.400 4.458   -13.731 1.00 154.90 ? 953  PRO A CD    1 
ATOM   6362 N  N     . PHE A 1 851 ? -61.013 7.148   -13.659 1.00 168.28 ? 954  PHE A N     1 
ATOM   6363 C  CA    . PHE A 1 851 ? -60.133 8.237   -14.084 1.00 157.85 ? 954  PHE A CA    1 
ATOM   6364 C  C     . PHE A 1 851 ? -61.001 9.463   -14.349 1.00 175.96 ? 954  PHE A C     1 
ATOM   6365 O  O     . PHE A 1 851 ? -61.515 9.660   -15.450 1.00 190.28 ? 954  PHE A O     1 
ATOM   6366 C  CB    . PHE A 1 851 ? -59.327 7.835   -15.314 1.00 129.73 ? 954  PHE A CB    1 
ATOM   6367 N  N     . VAL A 1 852 ? -61.161 10.294  -13.323 1.00 175.97 ? 955  VAL A N     1 
ATOM   6368 C  CA    . VAL A 1 852 ? -61.955 11.513  -13.422 1.00 175.55 ? 955  VAL A CA    1 
ATOM   6369 C  C     . VAL A 1 852 ? -61.053 12.653  -13.871 1.00 174.68 ? 955  VAL A C     1 
ATOM   6370 O  O     . VAL A 1 852 ? -59.954 12.839  -13.334 1.00 169.18 ? 955  VAL A O     1 
ATOM   6371 C  CB    . VAL A 1 852 ? -62.631 11.841  -12.080 1.00 168.94 ? 955  VAL A CB    1 
ATOM   6372 C  CG1   . VAL A 1 852 ? -63.428 13.133  -12.185 1.00 164.08 ? 955  VAL A CG1   1 
ATOM   6373 C  CG2   . VAL A 1 852 ? -63.526 10.695  -11.642 1.00 173.42 ? 955  VAL A CG2   1 
ATOM   6374 N  N     . LEU A 1 853 ? -61.514 13.417  -14.861 1.00 175.29 ? 956  LEU A N     1 
ATOM   6375 C  CA    . LEU A 1 853 ? -60.770 14.573  -15.345 1.00 180.80 ? 956  LEU A CA    1 
ATOM   6376 C  C     . LEU A 1 853 ? -60.789 15.691  -14.309 1.00 181.55 ? 956  LEU A C     1 
ATOM   6377 O  O     . LEU A 1 853 ? -61.687 16.539  -14.318 1.00 182.94 ? 956  LEU A O     1 
ATOM   6378 C  CB    . LEU A 1 853 ? -61.347 15.069  -16.674 1.00 200.10 ? 956  LEU A CB    1 
ATOM   6379 C  CG    . LEU A 1 853 ? -60.775 14.487  -17.970 1.00 197.52 ? 956  LEU A CG    1 
ATOM   6380 C  CD1   . LEU A 1 853 ? -60.929 12.974  -18.027 1.00 193.25 ? 956  LEU A CD1   1 
ATOM   6381 C  CD2   . LEU A 1 853 ? -61.434 15.137  -19.176 1.00 175.99 ? 956  LEU A CD2   1 
ATOM   6382 N  N     . THR A 1 854 ? -59.804 15.698  -13.414 1.00 179.22 ? 957  THR A N     1 
ATOM   6383 C  CA    . THR A 1 854 ? -59.734 16.722  -12.386 1.00 175.47 ? 957  THR A CA    1 
ATOM   6384 C  C     . THR A 1 854 ? -59.316 18.061  -12.993 1.00 187.03 ? 957  THR A C     1 
ATOM   6385 O  O     . THR A 1 854 ? -58.944 18.158  -14.166 1.00 181.65 ? 957  THR A O     1 
ATOM   6386 C  CB    . THR A 1 854 ? -58.757 16.315  -11.283 1.00 165.67 ? 957  THR A CB    1 
ATOM   6387 O  OG1   . THR A 1 854 ? -57.431 16.237  -11.822 1.00 153.22 ? 957  THR A OG1   1 
ATOM   6388 C  CG2   . THR A 1 854 ? -59.143 14.962  -10.704 1.00 169.75 ? 957  THR A CG2   1 
ATOM   6389 N  N     . GLN A 1 855 ? -59.379 19.107  -12.167 1.00 205.82 ? 958  GLN A N     1 
ATOM   6390 C  CA    . GLN A 1 855 ? -59.026 20.442  -12.640 1.00 196.25 ? 958  GLN A CA    1 
ATOM   6391 C  C     . GLN A 1 855 ? -57.543 20.538  -12.977 1.00 199.27 ? 958  GLN A C     1 
ATOM   6392 O  O     . GLN A 1 855 ? -57.163 21.225  -13.931 1.00 192.17 ? 958  GLN A O     1 
ATOM   6393 C  CB    . GLN A 1 855 ? -59.409 21.488  -11.593 1.00 184.88 ? 958  GLN A CB    1 
ATOM   6394 N  N     . ASP A 1 856 ? -56.692 19.849  -12.211 1.00 198.58 ? 959  ASP A N     1 
ATOM   6395 C  CA    . ASP A 1 856 ? -55.255 19.918  -12.453 1.00 180.94 ? 959  ASP A CA    1 
ATOM   6396 C  C     . ASP A 1 856 ? -54.875 19.318  -13.801 1.00 172.95 ? 959  ASP A C     1 
ATOM   6397 O  O     . ASP A 1 856 ? -53.853 19.700  -14.380 1.00 163.13 ? 959  ASP A O     1 
ATOM   6398 C  CB    . ASP A 1 856 ? -54.497 19.211  -11.329 1.00 170.33 ? 959  ASP A CB    1 
ATOM   6399 C  CG    . ASP A 1 856 ? -54.705 19.870  -9.981  1.00 175.21 ? 959  ASP A CG    1 
ATOM   6400 O  OD1   . ASP A 1 856 ? -55.819 19.761  -9.428  1.00 178.12 ? 959  ASP A OD1   1 
ATOM   6401 O  OD2   . ASP A 1 856 ? -53.752 20.498  -9.472  1.00 196.59 ? 959  ASP A OD2   1 
ATOM   6402 N  N     . PHE A 1 857 ? -55.678 18.384  -14.315 1.00 176.18 ? 960  PHE A N     1 
ATOM   6403 C  CA    . PHE A 1 857 ? -55.365 17.768  -15.600 1.00 167.36 ? 960  PHE A CA    1 
ATOM   6404 C  C     . PHE A 1 857 ? -55.622 18.734  -16.750 1.00 175.64 ? 960  PHE A C     1 
ATOM   6405 O  O     . PHE A 1 857 ? -54.767 18.915  -17.625 1.00 185.37 ? 960  PHE A O     1 
ATOM   6406 C  CB    . PHE A 1 857 ? -56.181 16.487  -15.780 1.00 174.52 ? 960  PHE A CB    1 
ATOM   6407 C  CG    . PHE A 1 857 ? -55.878 15.426  -14.761 1.00 196.14 ? 960  PHE A CG    1 
ATOM   6408 C  CD1   . PHE A 1 857 ? -54.634 15.361  -14.156 1.00 189.05 ? 960  PHE A CD1   1 
ATOM   6409 C  CD2   . PHE A 1 857 ? -56.840 14.495  -14.406 1.00 197.51 ? 960  PHE A CD2   1 
ATOM   6410 C  CE1   . PHE A 1 857 ? -54.354 14.386  -13.217 1.00 171.42 ? 960  PHE A CE1   1 
ATOM   6411 C  CE2   . PHE A 1 857 ? -56.567 13.519  -13.467 1.00 187.07 ? 960  PHE A CE2   1 
ATOM   6412 C  CZ    . PHE A 1 857 ? -55.322 13.464  -12.872 1.00 173.59 ? 960  PHE A CZ    1 
ATOM   6413 N  N     . LEU A 1 858 ? -56.797 19.369  -16.762 1.00 191.95 ? 961  LEU A N     1 
ATOM   6414 C  CA    . LEU A 1 858 ? -57.129 20.285  -17.849 1.00 184.62 ? 961  LEU A CA    1 
ATOM   6415 C  C     . LEU A 1 858 ? -56.270 21.543  -17.812 1.00 172.81 ? 961  LEU A C     1 
ATOM   6416 O  O     . LEU A 1 858 ? -56.060 22.177  -18.853 1.00 185.76 ? 961  LEU A O     1 
ATOM   6417 C  CB    . LEU A 1 858 ? -58.612 20.651  -17.799 1.00 184.54 ? 961  LEU A CB    1 
ATOM   6418 C  CG    . LEU A 1 858 ? -59.608 19.594  -18.288 1.00 187.60 ? 961  LEU A CG    1 
ATOM   6419 C  CD1   . LEU A 1 858 ? -59.092 18.913  -19.549 1.00 176.30 ? 961  LEU A CD1   1 
ATOM   6420 C  CD2   . LEU A 1 858 ? -59.926 18.570  -17.207 1.00 173.15 ? 961  LEU A CD2   1 
ATOM   6421 N  N     . ILE A 1 859 ? -55.772 21.924  -16.633 1.00 174.51 ? 962  ILE A N     1 
ATOM   6422 C  CA    . ILE A 1 859 ? -54.817 23.025  -16.556 1.00 175.52 ? 962  ILE A CA    1 
ATOM   6423 C  C     . ILE A 1 859 ? -53.538 22.667  -17.300 1.00 170.52 ? 962  ILE A C     1 
ATOM   6424 O  O     . ILE A 1 859 ? -52.871 23.540  -17.869 1.00 171.46 ? 962  ILE A O     1 
ATOM   6425 C  CB    . ILE A 1 859 ? -54.547 23.393  -15.081 1.00 169.92 ? 962  ILE A CB    1 
ATOM   6426 C  CG1   . ILE A 1 859 ? -55.798 24.003  -14.446 1.00 151.17 ? 962  ILE A CG1   1 
ATOM   6427 C  CG2   . ILE A 1 859 ? -53.378 24.359  -14.956 1.00 175.05 ? 962  ILE A CG2   1 
ATOM   6428 C  CD1   . ILE A 1 859 ? -56.273 25.269  -15.126 1.00 169.48 ? 962  ILE A CD1   1 
ATOM   6429 N  N     . VAL A 1 860 ? -53.190 21.383  -17.334 1.00 176.07 ? 963  VAL A N     1 
ATOM   6430 C  CA    . VAL A 1 860 ? -52.006 20.930  -18.057 1.00 163.04 ? 963  VAL A CA    1 
ATOM   6431 C  C     . VAL A 1 860 ? -52.349 20.513  -19.483 1.00 157.41 ? 963  VAL A C     1 
ATOM   6432 O  O     . VAL A 1 860 ? -51.604 20.815  -20.418 1.00 134.82 ? 963  VAL A O     1 
ATOM   6433 C  CB    . VAL A 1 860 ? -51.330 19.781  -17.283 1.00 146.77 ? 963  VAL A CB    1 
ATOM   6434 C  CG1   . VAL A 1 860 ? -50.063 19.339  -17.991 1.00 153.81 ? 963  VAL A CG1   1 
ATOM   6435 C  CG2   . VAL A 1 860 ? -51.027 20.206  -15.857 1.00 140.61 ? 963  VAL A CG2   1 
ATOM   6436 N  N     . ILE A 1 861 ? -53.475 19.822  -19.671 1.00 169.26 ? 964  ILE A N     1 
ATOM   6437 C  CA    . ILE A 1 861 ? -53.838 19.324  -20.996 1.00 154.33 ? 964  ILE A CA    1 
ATOM   6438 C  C     . ILE A 1 861 ? -54.169 20.482  -21.930 1.00 162.17 ? 964  ILE A C     1 
ATOM   6439 O  O     . ILE A 1 861 ? -53.587 20.616  -23.013 1.00 165.57 ? 964  ILE A O     1 
ATOM   6440 C  CB    . ILE A 1 861 ? -55.008 18.329  -20.898 1.00 165.79 ? 964  ILE A CB    1 
ATOM   6441 C  CG1   . ILE A 1 861 ? -54.550 17.028  -20.236 1.00 147.14 ? 964  ILE A CG1   1 
ATOM   6442 C  CG2   . ILE A 1 861 ? -55.597 18.059  -22.275 1.00 151.98 ? 964  ILE A CG2   1 
ATOM   6443 C  CD1   . ILE A 1 861 ? -55.643 15.990  -20.107 1.00 135.62 ? 964  ILE A CD1   1 
ATOM   6444 N  N     . SER A 1 862 ? -55.110 21.335  -21.524 1.00 177.70 ? 965  SER A N     1 
ATOM   6445 C  CA    . SER A 1 862 ? -55.539 22.467  -22.345 1.00 140.36 ? 965  SER A CA    1 
ATOM   6446 C  C     . SER A 1 862 ? -54.540 23.623  -22.233 1.00 136.28 ? 965  SER A C     1 
ATOM   6447 O  O     . SER A 1 862 ? -54.858 24.724  -21.785 1.00 150.50 ? 965  SER A O     1 
ATOM   6448 C  CB    . SER A 1 862 ? -56.942 22.905  -21.944 1.00 161.52 ? 965  SER A CB    1 
ATOM   6449 O  OG    . SER A 1 862 ? -57.372 24.011  -22.718 1.00 179.75 ? 965  SER A OG    1 
ATOM   6450 N  N     . LYS A 1 863 ? -53.308 23.341  -22.664 1.00 178.87 ? 966  LYS A N     1 
ATOM   6451 C  CA    . LYS A 1 863 ? -52.211 24.303  -22.634 1.00 178.29 ? 966  LYS A CA    1 
ATOM   6452 C  C     . LYS A 1 863 ? -52.023 24.881  -21.237 1.00 178.95 ? 966  LYS A C     1 
ATOM   6453 O  O     . LYS A 1 863 ? -51.634 24.166  -20.309 1.00 191.72 ? 966  LYS A O     1 
ATOM   6454 C  CB    . LYS A 1 863 ? -52.450 25.425  -23.648 1.00 212.08 ? 966  LYS A CB    1 
ATOM   6455 N  N     . GLY A 1 864 ? -52.299 26.173  -21.081 1.00 173.28 ? 967  GLY A N     1 
ATOM   6456 C  CA    . GLY A 1 864 ? -52.195 26.822  -19.789 1.00 172.04 ? 967  GLY A CA    1 
ATOM   6457 C  C     . GLY A 1 864 ? -53.389 27.699  -19.483 1.00 172.30 ? 967  GLY A C     1 
ATOM   6458 O  O     . GLY A 1 864 ? -53.292 28.642  -18.691 1.00 198.07 ? 967  GLY A O     1 
ATOM   6459 N  N     . ALA A 1 865 ? -54.524 27.397  -20.109 1.00 165.97 ? 968  ALA A N     1 
ATOM   6460 C  CA    . ALA A 1 865 ? -55.741 28.179  -19.919 1.00 175.62 ? 968  ALA A CA    1 
ATOM   6461 C  C     . ALA A 1 865 ? -56.245 27.997  -18.492 1.00 203.61 ? 968  ALA A C     1 
ATOM   6462 O  O     . ALA A 1 865 ? -56.738 26.925  -18.130 1.00 207.99 ? 968  ALA A O     1 
ATOM   6463 C  CB    . ALA A 1 865 ? -56.801 27.759  -20.932 1.00 161.62 ? 968  ALA A CB    1 
ATOM   6464 N  N     . GLN A 1 866 ? -56.122 29.049  -17.681 1.00 225.19 ? 969  GLN A N     1 
ATOM   6465 C  CA    . GLN A 1 866 ? -56.544 28.991  -16.287 1.00 220.03 ? 969  GLN A CA    1 
ATOM   6466 C  C     . GLN A 1 866 ? -58.058 29.035  -16.122 1.00 227.38 ? 969  GLN A C     1 
ATOM   6467 O  O     . GLN A 1 866 ? -58.544 28.842  -15.003 1.00 227.14 ? 969  GLN A O     1 
ATOM   6468 C  CB    . GLN A 1 866 ? -55.909 30.137  -15.495 1.00 215.47 ? 969  GLN A CB    1 
ATOM   6469 C  CG    . GLN A 1 866 ? -56.276 31.531  -15.992 1.00 214.21 ? 969  GLN A CG    1 
ATOM   6470 C  CD    . GLN A 1 866 ? -55.440 31.975  -17.179 1.00 215.91 ? 969  GLN A CD    1 
ATOM   6471 O  OE1   . GLN A 1 866 ? -54.248 31.680  -17.258 1.00 200.76 ? 969  GLN A OE1   1 
ATOM   6472 N  NE2   . GLN A 1 866 ? -56.066 32.683  -18.111 1.00 221.86 ? 969  GLN A NE2   1 
ATOM   6473 N  N     . GLU A 1 867 ? -58.809 29.279  -17.195 1.00 242.48 ? 970  GLU A N     1 
ATOM   6474 C  CA    . GLU A 1 867 ? -60.261 29.360  -17.103 1.00 246.07 ? 970  GLU A CA    1 
ATOM   6475 C  C     . GLU A 1 867 ? -60.928 28.289  -17.957 1.00 241.66 ? 970  GLU A C     1 
ATOM   6476 O  O     . GLU A 1 867 ? -61.196 27.182  -17.479 1.00 229.47 ? 970  GLU A O     1 
ATOM   6477 C  CB    . GLU A 1 867 ? -60.748 30.749  -17.521 1.00 249.48 ? 970  GLU A CB    1 
ATOM   6478 C  CG    . GLU A 1 867 ? -60.261 31.875  -16.625 1.00 247.49 ? 970  GLU A CG    1 
ATOM   6479 C  CD    . GLU A 1 867 ? -60.774 33.232  -17.066 1.00 256.27 ? 970  GLU A CD    1 
ATOM   6480 O  OE1   . GLU A 1 867 ? -61.376 33.316  -18.158 1.00 267.84 ? 970  GLU A OE1   1 
ATOM   6481 O  OE2   . GLU A 1 867 ? -60.578 34.215  -16.321 1.00 255.98 ? 970  GLU A OE2   1 
ATOM   6482 N  N     . CYS A 1 868 ? -61.200 28.612  -19.219 1.00 236.87 ? 971  CYS A N     1 
ATOM   6483 C  CA    . CYS A 1 868 ? -61.882 27.681  -20.110 1.00 230.19 ? 971  CYS A CA    1 
ATOM   6484 C  C     . CYS A 1 868 ? -60.973 26.501  -20.432 1.00 219.61 ? 971  CYS A C     1 
ATOM   6485 O  O     . CYS A 1 868 ? -59.870 26.682  -20.957 1.00 219.54 ? 971  CYS A O     1 
ATOM   6486 C  CB    . CYS A 1 868 ? -62.309 28.393  -21.391 1.00 238.76 ? 971  CYS A CB    1 
ATOM   6487 S  SG    . CYS A 1 868 ? -63.104 27.317  -22.609 1.00 245.61 ? 971  CYS A SG    1 
ATOM   6488 N  N     . THR A 1 869 ? -61.438 25.294  -20.118 1.00 208.44 ? 972  THR A N     1 
ATOM   6489 C  CA    . THR A 1 869 ? -60.673 24.085  -20.390 1.00 182.38 ? 972  THR A CA    1 
ATOM   6490 C  C     . THR A 1 869 ? -61.018 23.453  -21.729 1.00 177.07 ? 972  THR A C     1 
ATOM   6491 O  O     . THR A 1 869 ? -60.189 22.723  -22.286 1.00 181.70 ? 972  THR A O     1 
ATOM   6492 C  CB    . THR A 1 869 ? -60.898 23.056  -19.279 1.00 187.58 ? 972  THR A CB    1 
ATOM   6493 O  OG1   . THR A 1 869 ? -62.248 22.577  -19.338 1.00 195.57 ? 972  THR A OG1   1 
ATOM   6494 C  CG2   . THR A 1 869 ? -60.651 23.686  -17.918 1.00 205.04 ? 972  THR A CG2   1 
ATOM   6495 N  N     . LYS A 1 870 ? -62.212 23.712  -22.256 1.00 183.35 ? 973  LYS A N     1 
ATOM   6496 C  CA    . LYS A 1 870 ? -62.639 23.155  -23.540 1.00 175.63 ? 973  LYS A CA    1 
ATOM   6497 C  C     . LYS A 1 870 ? -62.098 24.042  -24.655 1.00 181.07 ? 973  LYS A C     1 
ATOM   6498 O  O     . LYS A 1 870 ? -62.775 24.943  -25.155 1.00 163.84 ? 973  LYS A O     1 
ATOM   6499 C  CB    . LYS A 1 870 ? -64.156 23.040  -23.600 1.00 175.36 ? 973  LYS A CB    1 
ATOM   6500 C  CG    . LYS A 1 870 ? -64.751 22.120  -22.550 1.00 163.46 ? 973  LYS A CG    1 
ATOM   6501 C  CD    . LYS A 1 870 ? -66.265 22.076  -22.658 1.00 183.45 ? 973  LYS A CD    1 
ATOM   6502 C  CE    . LYS A 1 870 ? -66.857 21.132  -21.627 1.00 204.85 ? 973  LYS A CE    1 
ATOM   6503 N  NZ    . LYS A 1 870 ? -68.344 21.097  -21.700 1.00 235.36 ? 973  LYS A NZ    1 
ATOM   6504 N  N     . THR A 1 871 ? -60.853 23.781  -25.050 1.00 189.18 ? 974  THR A N     1 
ATOM   6505 C  CA    . THR A 1 871 ? -60.220 24.525  -26.132 1.00 173.06 ? 974  THR A CA    1 
ATOM   6506 C  C     . THR A 1 871 ? -59.851 23.587  -27.275 1.00 159.73 ? 974  THR A C     1 
ATOM   6507 O  O     . THR A 1 871 ? -60.380 22.475  -27.365 1.00 160.19 ? 974  THR A O     1 
ATOM   6508 C  CB    . THR A 1 871 ? -58.975 25.260  -25.628 1.00 169.58 ? 974  THR A CB    1 
ATOM   6509 O  OG1   . THR A 1 871 ? -58.032 24.311  -25.115 1.00 171.56 ? 974  THR A OG1   1 
ATOM   6510 C  CG2   . THR A 1 871 ? -59.343 26.246  -24.530 1.00 184.27 ? 974  THR A CG2   1 
ATOM   6511 N  N     . ARG A 1 872 ? -58.946 24.025  -28.154 1.00 169.92 ? 975  ARG A N     1 
ATOM   6512 C  CA    . ARG A 1 872 ? -58.516 23.165  -29.252 1.00 162.73 ? 975  ARG A CA    1 
ATOM   6513 C  C     . ARG A 1 872 ? -57.675 21.996  -28.756 1.00 174.47 ? 975  ARG A C     1 
ATOM   6514 O  O     . ARG A 1 872 ? -57.678 20.927  -29.376 1.00 187.16 ? 975  ARG A O     1 
ATOM   6515 C  CB    . ARG A 1 872 ? -57.735 23.976  -30.287 1.00 158.61 ? 975  ARG A CB    1 
ATOM   6516 C  CG    . ARG A 1 872 ? -58.570 25.004  -31.030 1.00 172.63 ? 975  ARG A CG    1 
ATOM   6517 C  CD    . ARG A 1 872 ? -57.743 25.726  -32.079 1.00 176.71 ? 975  ARG A CD    1 
ATOM   6518 N  NE    . ARG A 1 872 ? -58.536 26.694  -32.828 1.00 220.08 ? 975  ARG A NE    1 
ATOM   6519 C  CZ    . ARG A 1 872 ? -58.054 27.476  -33.785 1.00 216.02 ? 975  ARG A CZ    1 
ATOM   6520 N  NH1   . ARG A 1 872 ? -56.780 27.433  -34.136 1.00 207.36 ? 975  ARG A NH1   1 
ATOM   6521 N  NH2   . ARG A 1 872 ? -58.872 28.323  -34.403 1.00 195.06 ? 975  ARG A NH2   1 
ATOM   6522 N  N     . GLU A 1 873 ? -56.953 22.177  -27.648 1.00 166.06 ? 976  GLU A N     1 
ATOM   6523 C  CA    . GLU A 1 873 ? -56.148 21.089  -27.103 1.00 145.57 ? 976  GLU A CA    1 
ATOM   6524 C  C     . GLU A 1 873 ? -57.033 19.989  -26.530 1.00 160.88 ? 976  GLU A C     1 
ATOM   6525 O  O     . GLU A 1 873 ? -56.797 18.799  -26.771 1.00 160.78 ? 976  GLU A O     1 
ATOM   6526 C  CB    . GLU A 1 873 ? -55.190 21.624  -26.037 1.00 153.98 ? 976  GLU A CB    1 
ATOM   6527 C  CG    . GLU A 1 873 ? -54.061 22.496  -26.576 1.00 146.59 ? 976  GLU A CG    1 
ATOM   6528 C  CD    . GLU A 1 873 ? -54.510 23.903  -26.927 1.00 164.66 ? 976  GLU A CD    1 
ATOM   6529 O  OE1   . GLU A 1 873 ? -55.663 24.261  -26.606 1.00 166.55 ? 976  GLU A OE1   1 
ATOM   6530 O  OE2   . GLU A 1 873 ? -53.708 24.651  -27.523 1.00 147.55 ? 976  GLU A OE2   1 
ATOM   6531 N  N     . PHE A 1 874 ? -58.060 20.368  -25.765 1.00 162.67 ? 977  PHE A N     1 
ATOM   6532 C  CA    . PHE A 1 874 ? -58.978 19.371  -25.225 1.00 151.68 ? 977  PHE A CA    1 
ATOM   6533 C  C     . PHE A 1 874 ? -59.888 18.804  -26.306 1.00 156.45 ? 977  PHE A C     1 
ATOM   6534 O  O     . PHE A 1 874 ? -60.358 17.667  -26.183 1.00 175.09 ? 977  PHE A O     1 
ATOM   6535 C  CB    . PHE A 1 874 ? -59.807 19.976  -24.092 1.00 148.61 ? 977  PHE A CB    1 
ATOM   6536 C  CG    . PHE A 1 874 ? -60.801 19.021  -23.494 1.00 160.46 ? 977  PHE A CG    1 
ATOM   6537 C  CD1   . PHE A 1 874 ? -60.377 17.962  -22.710 1.00 138.83 ? 977  PHE A CD1   1 
ATOM   6538 C  CD2   . PHE A 1 874 ? -62.158 19.183  -23.716 1.00 162.00 ? 977  PHE A CD2   1 
ATOM   6539 C  CE1   . PHE A 1 874 ? -61.288 17.081  -22.159 1.00 144.24 ? 977  PHE A CE1   1 
ATOM   6540 C  CE2   . PHE A 1 874 ? -63.074 18.306  -23.167 1.00 157.54 ? 977  PHE A CE2   1 
ATOM   6541 C  CZ    . PHE A 1 874 ? -62.638 17.254  -22.388 1.00 150.68 ? 977  PHE A CZ    1 
ATOM   6542 N  N     . GLU A 1 875 ? -60.150 19.575  -27.364 1.00 169.01 ? 978  GLU A N     1 
ATOM   6543 C  CA    . GLU A 1 875 ? -60.942 19.058  -28.475 1.00 180.59 ? 978  GLU A CA    1 
ATOM   6544 C  C     . GLU A 1 875 ? -60.235 17.900  -29.166 1.00 170.62 ? 978  GLU A C     1 
ATOM   6545 O  O     . GLU A 1 875 ? -60.890 16.965  -29.640 1.00 160.74 ? 978  GLU A O     1 
ATOM   6546 C  CB    . GLU A 1 875 ? -61.240 20.178  -29.473 1.00 189.64 ? 978  GLU A CB    1 
ATOM   6547 C  CG    . GLU A 1 875 ? -62.204 19.791  -30.582 1.00 197.29 ? 978  GLU A CG    1 
ATOM   6548 C  CD    . GLU A 1 875 ? -62.515 20.948  -31.511 1.00 197.78 ? 978  GLU A CD    1 
ATOM   6549 O  OE1   . GLU A 1 875 ? -61.880 22.014  -31.368 1.00 192.08 ? 978  GLU A OE1   1 
ATOM   6550 O  OE2   . GLU A 1 875 ? -63.395 20.793  -32.384 1.00 203.58 ? 978  GLU A OE2   1 
ATOM   6551 N  N     . ARG A 1 876 ? -58.902 17.942  -29.229 1.00 176.35 ? 979  ARG A N     1 
ATOM   6552 C  CA    . ARG A 1 876 ? -58.134 16.834  -29.778 1.00 167.60 ? 979  ARG A CA    1 
ATOM   6553 C  C     . ARG A 1 876 ? -57.923 15.715  -28.767 1.00 165.06 ? 979  ARG A C     1 
ATOM   6554 O  O     . ARG A 1 876 ? -57.632 14.583  -29.169 1.00 160.54 ? 979  ARG A O     1 
ATOM   6555 C  CB    . ARG A 1 876 ? -56.779 17.334  -30.285 1.00 177.47 ? 979  ARG A CB    1 
ATOM   6556 C  CG    . ARG A 1 876 ? -56.877 18.376  -31.387 1.00 212.28 ? 979  ARG A CG    1 
ATOM   6557 C  CD    . ARG A 1 876 ? -55.504 18.892  -31.783 1.00 222.62 ? 979  ARG A CD    1 
ATOM   6558 N  NE    . ARG A 1 876 ? -54.622 17.817  -32.222 1.00 233.21 ? 979  ARG A NE    1 
ATOM   6559 C  CZ    . ARG A 1 876 ? -53.369 17.990  -32.619 1.00 238.76 ? 979  ARG A CZ    1 
ATOM   6560 N  NH1   . ARG A 1 876 ? -52.813 19.191  -32.647 1.00 242.62 ? 979  ARG A NH1   1 
ATOM   6561 N  NH2   . ARG A 1 876 ? -52.656 16.933  -32.996 1.00 231.52 ? 979  ARG A NH2   1 
ATOM   6562 N  N     . PHE A 1 877 ? -58.059 16.006  -27.471 1.00 152.63 ? 980  PHE A N     1 
ATOM   6563 C  CA    . PHE A 1 877 ? -57.941 14.961  -26.460 1.00 130.08 ? 980  PHE A CA    1 
ATOM   6564 C  C     . PHE A 1 877 ? -59.072 13.949  -26.582 1.00 144.00 ? 980  PHE A C     1 
ATOM   6565 O  O     . PHE A 1 877 ? -58.866 12.748  -26.368 1.00 151.17 ? 980  PHE A O     1 
ATOM   6566 C  CB    . PHE A 1 877 ? -57.922 15.584  -25.064 1.00 136.19 ? 980  PHE A CB    1 
ATOM   6567 C  CG    . PHE A 1 877 ? -57.746 14.587  -23.953 1.00 148.36 ? 980  PHE A CG    1 
ATOM   6568 C  CD1   . PHE A 1 877 ? -56.480 14.177  -23.568 1.00 148.39 ? 980  PHE A CD1   1 
ATOM   6569 C  CD2   . PHE A 1 877 ? -58.845 14.067  -23.287 1.00 136.43 ? 980  PHE A CD2   1 
ATOM   6570 C  CE1   . PHE A 1 877 ? -56.313 13.262  -22.545 1.00 143.13 ? 980  PHE A CE1   1 
ATOM   6571 C  CE2   . PHE A 1 877 ? -58.684 13.151  -22.264 1.00 137.07 ? 980  PHE A CE2   1 
ATOM   6572 C  CZ    . PHE A 1 877 ? -57.417 12.749  -21.893 1.00 150.78 ? 980  PHE A CZ    1 
ATOM   6573 N  N     . GLN A 1 878 ? -60.275 14.416  -26.926 1.00 159.10 ? 981  GLN A N     1 
ATOM   6574 C  CA    . GLN A 1 878 ? -61.401 13.506  -27.109 1.00 146.72 ? 981  GLN A CA    1 
ATOM   6575 C  C     . GLN A 1 878 ? -61.192 12.607  -28.321 1.00 157.40 ? 981  GLN A C     1 
ATOM   6576 O  O     . GLN A 1 878 ? -61.539 11.421  -28.288 1.00 146.14 ? 981  GLN A O     1 
ATOM   6577 C  CB    . GLN A 1 878 ? -62.697 14.301  -27.255 1.00 167.35 ? 981  GLN A CB    1 
ATOM   6578 C  CG    . GLN A 1 878 ? -62.996 15.232  -26.092 1.00 160.49 ? 981  GLN A CG    1 
ATOM   6579 C  CD    . GLN A 1 878 ? -64.070 16.247  -26.428 1.00 168.25 ? 981  GLN A CD    1 
ATOM   6580 O  OE1   . GLN A 1 878 ? -64.263 16.602  -27.591 1.00 152.75 ? 981  GLN A OE1   1 
ATOM   6581 N  NE2   . GLN A 1 878 ? -64.778 16.719  -25.409 1.00 189.88 ? 981  GLN A NE2   1 
ATOM   6582 N  N     . GLU A 1 879 ? -60.624 13.155  -29.399 1.00 157.41 ? 982  GLU A N     1 
ATOM   6583 C  CA    . GLU A 1 879 ? -60.415 12.366  -30.609 1.00 144.58 ? 982  GLU A CA    1 
ATOM   6584 C  C     . GLU A 1 879 ? -59.397 11.255  -30.389 1.00 147.48 ? 982  GLU A C     1 
ATOM   6585 O  O     . GLU A 1 879 ? -59.493 10.197  -31.020 1.00 159.62 ? 982  GLU A O     1 
ATOM   6586 C  CB    . GLU A 1 879 ? -59.977 13.274  -31.758 1.00 144.88 ? 982  GLU A CB    1 
ATOM   6587 C  CG    . GLU A 1 879 ? -60.942 14.415  -32.050 1.00 176.95 ? 982  GLU A CG    1 
ATOM   6588 C  CD    . GLU A 1 879 ? -62.300 13.934  -32.528 1.00 195.86 ? 982  GLU A CD    1 
ATOM   6589 O  OE1   . GLU A 1 879 ? -62.374 12.833  -33.114 1.00 197.89 ? 982  GLU A OE1   1 
ATOM   6590 O  OE2   . GLU A 1 879 ? -63.296 14.657  -32.315 1.00 185.57 ? 982  GLU A OE2   1 
ATOM   6591 N  N     . MET A 1 880 ? -58.418 11.473  -29.508 1.00 129.52 ? 983  MET A N     1 
ATOM   6592 C  CA    . MET A 1 880 ? -57.484 10.402  -29.174 1.00 122.87 ? 983  MET A CA    1 
ATOM   6593 C  C     . MET A 1 880 ? -58.183 9.284   -28.413 1.00 139.93 ? 983  MET A C     1 
ATOM   6594 O  O     . MET A 1 880 ? -57.894 8.101   -28.630 1.00 150.71 ? 983  MET A O     1 
ATOM   6595 C  CB    . MET A 1 880 ? -56.315 10.952  -28.357 1.00 123.10 ? 983  MET A CB    1 
ATOM   6596 C  CG    . MET A 1 880 ? -55.451 11.960  -29.094 1.00 140.57 ? 983  MET A CG    1 
ATOM   6597 S  SD    . MET A 1 880 ? -53.978 12.411  -28.156 1.00 115.19 ? 983  MET A SD    1 
ATOM   6598 C  CE    . MET A 1 880 ? -54.712 13.023  -26.642 1.00 145.48 ? 983  MET A CE    1 
ATOM   6599 N  N     . CYS A 1 881 ? -59.107 9.639   -27.518 1.00 140.57 ? 984  CYS A N     1 
ATOM   6600 C  CA    . CYS A 1 881 ? -59.844 8.623   -26.775 1.00 131.22 ? 984  CYS A CA    1 
ATOM   6601 C  C     . CYS A 1 881 ? -60.805 7.866   -27.682 1.00 120.09 ? 984  CYS A C     1 
ATOM   6602 O  O     . CYS A 1 881 ? -60.978 6.651   -27.534 1.00 128.66 ? 984  CYS A O     1 
ATOM   6603 C  CB    . CYS A 1 881 ? -60.597 9.268   -25.612 1.00 130.98 ? 984  CYS A CB    1 
ATOM   6604 S  SG    . CYS A 1 881 ? -59.543 10.166  -24.450 1.00 132.50 ? 984  CYS A SG    1 
ATOM   6605 N  N     . TYR A 1 882 ? -61.438 8.567   -28.628 1.00 122.31 ? 985  TYR A N     1 
ATOM   6606 C  CA    . TYR A 1 882 ? -62.359 7.906   -29.548 1.00 125.41 ? 985  TYR A CA    1 
ATOM   6607 C  C     . TYR A 1 882 ? -61.635 6.882   -30.412 1.00 128.84 ? 985  TYR A C     1 
ATOM   6608 O  O     . TYR A 1 882 ? -62.126 5.763   -30.606 1.00 112.82 ? 985  TYR A O     1 
ATOM   6609 C  CB    . TYR A 1 882 ? -63.060 8.943   -30.427 1.00 146.98 ? 985  TYR A CB    1 
ATOM   6610 C  CG    . TYR A 1 882 ? -63.879 9.956   -29.660 1.00 154.37 ? 985  TYR A CG    1 
ATOM   6611 C  CD1   . TYR A 1 882 ? -64.449 9.637   -28.435 1.00 155.25 ? 985  TYR A CD1   1 
ATOM   6612 C  CD2   . TYR A 1 882 ? -64.081 11.235  -30.163 1.00 162.68 ? 985  TYR A CD2   1 
ATOM   6613 C  CE1   . TYR A 1 882 ? -65.198 10.562  -27.732 1.00 153.65 ? 985  TYR A CE1   1 
ATOM   6614 C  CE2   . TYR A 1 882 ? -64.828 12.167  -29.468 1.00 161.31 ? 985  TYR A CE2   1 
ATOM   6615 C  CZ    . TYR A 1 882 ? -65.384 11.825  -28.253 1.00 151.18 ? 985  TYR A CZ    1 
ATOM   6616 O  OH    . TYR A 1 882 ? -66.128 12.750  -27.558 1.00 159.82 ? 985  TYR A OH    1 
ATOM   6617 N  N     . LYS A 1 883 ? -60.463 7.246   -30.939 1.00 124.70 ? 986  LYS A N     1 
ATOM   6618 C  CA    . LYS A 1 883 ? -59.698 6.312   -31.757 1.00 108.30 ? 986  LYS A CA    1 
ATOM   6619 C  C     . LYS A 1 883 ? -59.128 5.173   -30.922 1.00 115.03 ? 986  LYS A C     1 
ATOM   6620 O  O     . LYS A 1 883 ? -58.930 4.068   -31.438 1.00 108.99 ? 986  LYS A O     1 
ATOM   6621 C  CB    . LYS A 1 883 ? -58.578 7.049   -32.489 1.00 108.96 ? 986  LYS A CB    1 
ATOM   6622 C  CG    . LYS A 1 883 ? -59.070 8.109   -33.461 1.00 133.56 ? 986  LYS A CG    1 
ATOM   6623 C  CD    . LYS A 1 883 ? -57.915 8.892   -34.063 1.00 137.09 ? 986  LYS A CD    1 
ATOM   6624 C  CE    . LYS A 1 883 ? -58.418 9.980   -34.998 1.00 152.47 ? 986  LYS A CE    1 
ATOM   6625 N  NZ    . LYS A 1 883 ? -57.302 10.783  -35.569 1.00 163.75 ? 986  LYS A NZ    1 
ATOM   6626 N  N     . ALA A 1 884 ? -58.859 5.419   -29.638 1.00 114.33 ? 987  ALA A N     1 
ATOM   6627 C  CA    . ALA A 1 884 ? -58.360 4.362   -28.767 1.00 123.23 ? 987  ALA A CA    1 
ATOM   6628 C  C     . ALA A 1 884 ? -59.484 3.489   -28.227 1.00 136.04 ? 987  ALA A C     1 
ATOM   6629 O  O     . ALA A 1 884 ? -59.288 2.284   -28.034 1.00 131.68 ? 987  ALA A O     1 
ATOM   6630 C  CB    . ALA A 1 884 ? -57.559 4.965   -27.612 1.00 109.81 ? 987  ALA A CB    1 
ATOM   6631 N  N     . TYR A 1 885 ? -60.659 4.072   -27.977 1.00 127.51 ? 988  TYR A N     1 
ATOM   6632 C  CA    . TYR A 1 885 ? -61.798 3.285   -27.514 1.00 108.96 ? 988  TYR A CA    1 
ATOM   6633 C  C     . TYR A 1 885 ? -62.283 2.336   -28.602 1.00 138.80 ? 988  TYR A C     1 
ATOM   6634 O  O     . TYR A 1 885 ? -62.500 1.144   -28.351 1.00 121.82 ? 988  TYR A O     1 
ATOM   6635 C  CB    . TYR A 1 885 ? -62.927 4.216   -27.067 1.00 131.89 ? 988  TYR A CB    1 
ATOM   6636 C  CG    . TYR A 1 885 ? -64.157 3.509   -26.542 1.00 137.30 ? 988  TYR A CG    1 
ATOM   6637 C  CD1   . TYR A 1 885 ? -64.245 3.123   -25.211 1.00 131.08 ? 988  TYR A CD1   1 
ATOM   6638 C  CD2   . TYR A 1 885 ? -65.236 3.239   -27.376 1.00 133.13 ? 988  TYR A CD2   1 
ATOM   6639 C  CE1   . TYR A 1 885 ? -65.369 2.481   -24.727 1.00 132.16 ? 988  TYR A CE1   1 
ATOM   6640 C  CE2   . TYR A 1 885 ? -66.363 2.597   -26.900 1.00 138.64 ? 988  TYR A CE2   1 
ATOM   6641 C  CZ    . TYR A 1 885 ? -66.424 2.221   -25.575 1.00 147.19 ? 988  TYR A CZ    1 
ATOM   6642 O  OH    . TYR A 1 885 ? -67.545 1.583   -25.098 1.00 160.15 ? 988  TYR A OH    1 
ATOM   6643 N  N     . LEU A 1 886 ? -62.457 2.849   -29.822 1.00 133.58 ? 989  LEU A N     1 
ATOM   6644 C  CA    . LEU A 1 886 ? -62.944 2.016   -30.916 1.00 122.74 ? 989  LEU A CA    1 
ATOM   6645 C  C     . LEU A 1 886 ? -61.909 0.982   -31.342 1.00 126.45 ? 989  LEU A C     1 
ATOM   6646 O  O     . LEU A 1 886 ? -62.274 -0.080  -31.858 1.00 127.14 ? 989  LEU A O     1 
ATOM   6647 C  CB    . LEU A 1 886 ? -63.344 2.895   -32.101 1.00 126.50 ? 989  LEU A CB    1 
ATOM   6648 C  CG    . LEU A 1 886 ? -64.018 2.209   -33.290 1.00 163.35 ? 989  LEU A CG    1 
ATOM   6649 C  CD1   . LEU A 1 886 ? -65.282 1.488   -32.848 1.00 152.52 ? 989  LEU A CD1   1 
ATOM   6650 C  CD2   . LEU A 1 886 ? -64.327 3.221   -34.380 1.00 156.89 ? 989  LEU A CD2   1 
ATOM   6651 N  N     . ALA A 1 887 ? -60.621 1.267   -31.131 1.00 119.86 ? 990  ALA A N     1 
ATOM   6652 C  CA    . ALA A 1 887 ? -59.586 0.302   -31.485 1.00 117.75 ? 990  ALA A CA    1 
ATOM   6653 C  C     . ALA A 1 887 ? -59.641 -0.925  -30.583 1.00 132.45 ? 990  ALA A C     1 
ATOM   6654 O  O     . ALA A 1 887 ? -59.526 -2.059  -31.062 1.00 145.03 ? 990  ALA A O     1 
ATOM   6655 C  CB    . ALA A 1 887 ? -58.207 0.957   -31.414 1.00 126.90 ? 990  ALA A CB    1 
ATOM   6656 N  N     . ILE A 1 888 ? -59.813 -0.719  -29.276 1.00 126.54 ? 991  ILE A N     1 
ATOM   6657 C  CA    . ILE A 1 888 ? -59.922 -1.847  -28.356 1.00 107.63 ? 991  ILE A CA    1 
ATOM   6658 C  C     . ILE A 1 888 ? -61.210 -2.619  -28.612 1.00 122.62 ? 991  ILE A C     1 
ATOM   6659 O  O     . ILE A 1 888 ? -61.246 -3.850  -28.502 1.00 121.40 ? 991  ILE A O     1 
ATOM   6660 C  CB    . ILE A 1 888 ? -59.831 -1.357  -26.899 1.00 107.33 ? 991  ILE A CB    1 
ATOM   6661 C  CG1   . ILE A 1 888 ? -58.528 -0.587  -26.679 1.00 134.15 ? 991  ILE A CG1   1 
ATOM   6662 C  CG2   . ILE A 1 888 ? -59.924 -2.527  -25.932 1.00 99.90  ? 991  ILE A CG2   1 
ATOM   6663 C  CD1   . ILE A 1 888 ? -57.284 -1.395  -26.977 1.00 112.17 ? 991  ILE A CD1   1 
ATOM   6664 N  N     . ARG A 1 889 ? -62.286 -1.909  -28.963 1.00 126.63 ? 992  ARG A N     1 
ATOM   6665 C  CA    . ARG A 1 889 ? -63.545 -2.571  -29.288 1.00 115.90 ? 992  ARG A CA    1 
ATOM   6666 C  C     . ARG A 1 889 ? -63.398 -3.494  -30.492 1.00 134.65 ? 992  ARG A C     1 
ATOM   6667 O  O     . ARG A 1 889 ? -64.040 -4.550  -30.546 1.00 126.15 ? 992  ARG A O     1 
ATOM   6668 C  CB    . ARG A 1 889 ? -64.631 -1.521  -29.538 1.00 148.29 ? 992  ARG A CB    1 
ATOM   6669 C  CG    . ARG A 1 889 ? -65.917 -2.057  -30.145 1.00 146.67 ? 992  ARG A CG    1 
ATOM   6670 C  CD    . ARG A 1 889 ? -66.959 -0.957  -30.270 1.00 122.92 ? 992  ARG A CD    1 
ATOM   6671 N  NE    . ARG A 1 889 ? -67.958 -1.262  -31.287 1.00 146.04 ? 992  ARG A NE    1 
ATOM   6672 C  CZ    . ARG A 1 889 ? -69.050 -1.985  -31.075 1.00 138.96 ? 992  ARG A CZ    1 
ATOM   6673 N  NH1   . ARG A 1 889 ? -69.315 -2.503  -29.888 1.00 134.67 ? 992  ARG A NH1   1 
ATOM   6674 N  NH2   . ARG A 1 889 ? -69.895 -2.193  -32.080 1.00 155.27 ? 992  ARG A NH2   1 
ATOM   6675 N  N     . GLN A 1 890 ? -62.551 -3.125  -31.456 1.00 131.13 ? 993  GLN A N     1 
ATOM   6676 C  CA    . GLN A 1 890 ? -62.304 -3.990  -32.604 1.00 126.94 ? 993  GLN A CA    1 
ATOM   6677 C  C     . GLN A 1 890 ? -61.523 -5.242  -32.227 1.00 120.77 ? 993  GLN A C     1 
ATOM   6678 O  O     . GLN A 1 890 ? -61.544 -6.220  -32.983 1.00 125.90 ? 993  GLN A O     1 
ATOM   6679 C  CB    . GLN A 1 890 ? -61.561 -3.217  -33.695 1.00 131.30 ? 993  GLN A CB    1 
ATOM   6680 C  CG    . GLN A 1 890 ? -62.399 -2.145  -34.374 1.00 152.39 ? 993  GLN A CG    1 
ATOM   6681 C  CD    . GLN A 1 890 ? -61.604 -1.325  -35.371 1.00 173.97 ? 993  GLN A CD    1 
ATOM   6682 O  OE1   . GLN A 1 890 ? -60.374 -1.284  -35.318 1.00 165.07 ? 993  GLN A OE1   1 
ATOM   6683 N  NE2   . GLN A 1 890 ? -62.303 -0.668  -36.289 1.00 191.08 ? 993  GLN A NE2   1 
ATOM   6684 N  N     . HIS A 1 891 ? -60.835 -5.235  -31.085 1.00 129.25 ? 994  HIS A N     1 
ATOM   6685 C  CA    . HIS A 1 891 ? -60.131 -6.405  -30.576 1.00 124.17 ? 994  HIS A CA    1 
ATOM   6686 C  C     . HIS A 1 891 ? -60.767 -6.933  -29.293 1.00 123.84 ? 994  HIS A C     1 
ATOM   6687 O  O     . HIS A 1 891 ? -60.072 -7.453  -28.417 1.00 142.06 ? 994  HIS A O     1 
ATOM   6688 C  CB    . HIS A 1 891 ? -58.655 -6.089  -30.340 1.00 114.48 ? 994  HIS A CB    1 
ATOM   6689 C  CG    . HIS A 1 891 ? -57.875 -5.861  -31.597 1.00 120.07 ? 994  HIS A CG    1 
ATOM   6690 N  ND1   . HIS A 1 891 ? -57.757 -4.620  -32.186 1.00 118.81 ? 994  HIS A ND1   1 
ATOM   6691 C  CD2   . HIS A 1 891 ? -57.173 -6.716  -32.377 1.00 112.54 ? 994  HIS A CD2   1 
ATOM   6692 C  CE1   . HIS A 1 891 ? -57.016 -4.721  -33.275 1.00 126.89 ? 994  HIS A CE1   1 
ATOM   6693 N  NE2   . HIS A 1 891 ? -56.649 -5.982  -33.414 1.00 117.03 ? 994  HIS A NE2   1 
ATOM   6694 N  N     . ALA A 1 892 ? -62.092 -6.805  -29.173 1.00 138.58 ? 995  ALA A N     1 
ATOM   6695 C  CA    . ALA A 1 892 ? -62.770 -7.239  -27.956 1.00 119.89 ? 995  ALA A CA    1 
ATOM   6696 C  C     . ALA A 1 892 ? -62.673 -8.745  -27.761 1.00 130.53 ? 995  ALA A C     1 
ATOM   6697 O  O     . ALA A 1 892 ? -62.607 -9.220  -26.622 1.00 129.93 ? 995  ALA A O     1 
ATOM   6698 C  CB    . ALA A 1 892 ? -64.234 -6.800  -27.984 1.00 113.83 ? 995  ALA A CB    1 
ATOM   6699 N  N     . ASN A 1 893 ? -62.661 -9.512  -28.854 1.00 128.76 ? 996  ASN A N     1 
ATOM   6700 C  CA    . ASN A 1 893 ? -62.553 -10.962 -28.735 1.00 122.67 ? 996  ASN A CA    1 
ATOM   6701 C  C     . ASN A 1 893 ? -61.210 -11.380 -28.152 1.00 127.51 ? 996  ASN A C     1 
ATOM   6702 O  O     . ASN A 1 893 ? -61.125 -12.410 -27.474 1.00 124.31 ? 996  ASN A O     1 
ATOM   6703 C  CB    . ASN A 1 893 ? -62.765 -11.619 -30.099 1.00 126.42 ? 996  ASN A CB    1 
ATOM   6704 C  CG    . ASN A 1 893 ? -64.125 -11.309 -30.689 1.00 148.70 ? 996  ASN A CG    1 
ATOM   6705 O  OD1   . ASN A 1 893 ? -64.792 -10.359 -30.278 1.00 165.06 ? 996  ASN A OD1   1 
ATOM   6706 N  ND2   . ASN A 1 893 ? -64.545 -12.112 -31.660 1.00 167.21 ? 996  ASN A ND2   1 
ATOM   6707 N  N     . LEU A 1 894 ? -60.156 -10.599 -28.398 1.00 144.71 ? 997  LEU A N     1 
ATOM   6708 C  CA    . LEU A 1 894 ? -58.837 -10.955 -27.885 1.00 133.30 ? 997  LEU A CA    1 
ATOM   6709 C  C     . LEU A 1 894 ? -58.762 -10.766 -26.375 1.00 120.38 ? 997  LEU A C     1 
ATOM   6710 O  O     . LEU A 1 894 ? -58.242 -11.632 -25.662 1.00 122.82 ? 997  LEU A O     1 
ATOM   6711 C  CB    . LEU A 1 894 ? -57.761 -10.127 -28.592 1.00 149.52 ? 997  LEU A CB    1 
ATOM   6712 C  CG    . LEU A 1 894 ? -56.288 -10.485 -28.367 1.00 127.59 ? 997  LEU A CG    1 
ATOM   6713 C  CD1   . LEU A 1 894 ? -55.487 -10.198 -29.626 1.00 161.58 ? 997  LEU A CD1   1 
ATOM   6714 C  CD2   . LEU A 1 894 ? -55.700 -9.722  -27.189 1.00 103.47 ? 997  LEU A CD2   1 
ATOM   6715 N  N     . PHE A 1 895 ? -59.277 -9.644  -25.868 1.00 117.53 ? 998  PHE A N     1 
ATOM   6716 C  CA    . PHE A 1 895 ? -59.165 -9.362  -24.440 1.00 128.95 ? 998  PHE A CA    1 
ATOM   6717 C  C     . PHE A 1 895 ? -60.106 -10.238 -23.622 1.00 120.57 ? 998  PHE A C     1 
ATOM   6718 O  O     . PHE A 1 895 ? -59.740 -10.698 -22.534 1.00 125.16 ? 998  PHE A O     1 
ATOM   6719 C  CB    . PHE A 1 895 ? -59.437 -7.882  -24.173 1.00 116.41 ? 998  PHE A CB    1 
ATOM   6720 C  CG    . PHE A 1 895 ? -58.377 -6.968  -24.715 1.00 117.41 ? 998  PHE A CG    1 
ATOM   6721 C  CD1   . PHE A 1 895 ? -57.189 -6.781  -24.029 1.00 116.02 ? 998  PHE A CD1   1 
ATOM   6722 C  CD2   . PHE A 1 895 ? -58.568 -6.296  -25.910 1.00 117.90 ? 998  PHE A CD2   1 
ATOM   6723 C  CE1   . PHE A 1 895 ? -56.210 -5.943  -24.525 1.00 112.31 ? 998  PHE A CE1   1 
ATOM   6724 C  CE2   . PHE A 1 895 ? -57.593 -5.456  -26.412 1.00 139.81 ? 998  PHE A CE2   1 
ATOM   6725 C  CZ    . PHE A 1 895 ? -56.413 -5.279  -25.719 1.00 122.94 ? 998  PHE A CZ    1 
ATOM   6726 N  N     . ILE A 1 896 ? -61.319 -10.479 -24.124 1.00 133.83 ? 999  ILE A N     1 
ATOM   6727 C  CA    . ILE A 1 896 ? -62.268 -11.317 -23.394 1.00 136.44 ? 999  ILE A CA    1 
ATOM   6728 C  C     . ILE A 1 896 ? -61.739 -12.741 -23.274 1.00 120.54 ? 999  ILE A C     1 
ATOM   6729 O  O     . ILE A 1 896 ? -61.923 -13.404 -22.245 1.00 133.18 ? 999  ILE A O     1 
ATOM   6730 C  CB    . ILE A 1 896 ? -63.652 -11.271 -24.070 1.00 119.67 ? 999  ILE A CB    1 
ATOM   6731 C  CG1   . ILE A 1 896 ? -64.249 -9.867  -23.957 1.00 108.23 ? 999  ILE A CG1   1 
ATOM   6732 C  CG2   . ILE A 1 896 ? -64.594 -12.290 -23.447 1.00 121.22 ? 999  ILE A CG2   1 
ATOM   6733 C  CD1   . ILE A 1 896 ? -65.631 -9.739  -24.557 1.00 133.10 ? 999  ILE A CD1   1 
ATOM   6734 N  N     . ASN A 1 897 ? -61.058 -13.229 -24.315 1.00 112.45 ? 1000 ASN A N     1 
ATOM   6735 C  CA    . ASN A 1 897 ? -60.434 -14.546 -24.231 1.00 101.49 ? 1000 ASN A CA    1 
ATOM   6736 C  C     . ASN A 1 897 ? -59.330 -14.577 -23.183 1.00 102.24 ? 1000 ASN A C     1 
ATOM   6737 O  O     . ASN A 1 897 ? -59.089 -15.622 -22.568 1.00 118.62 ? 1000 ASN A O     1 
ATOM   6738 C  CB    . ASN A 1 897 ? -59.877 -14.958 -25.595 1.00 105.08 ? 1000 ASN A CB    1 
ATOM   6739 C  CG    . ASN A 1 897 ? -60.964 -15.333 -26.580 1.00 130.14 ? 1000 ASN A CG    1 
ATOM   6740 O  OD1   . ASN A 1 897 ? -62.035 -15.798 -26.191 1.00 144.21 ? 1000 ASN A OD1   1 
ATOM   6741 N  ND2   . ASN A 1 897 ? -60.693 -15.136 -27.865 1.00 136.28 ? 1000 ASN A ND2   1 
ATOM   6742 N  N     . LEU A 1 898 ? -58.652 -13.449 -22.961 1.00 99.86  ? 1001 LEU A N     1 
ATOM   6743 C  CA    . LEU A 1 898 ? -57.593 -13.413 -21.959 1.00 115.06 ? 1001 LEU A CA    1 
ATOM   6744 C  C     . LEU A 1 898 ? -58.153 -13.478 -20.544 1.00 117.55 ? 1001 LEU A C     1 
ATOM   6745 O  O     . LEU A 1 898 ? -57.456 -13.923 -19.625 1.00 120.61 ? 1001 LEU A O     1 
ATOM   6746 C  CB    . LEU A 1 898 ? -56.743 -12.156 -22.139 1.00 117.21 ? 1001 LEU A CB    1 
ATOM   6747 C  CG    . LEU A 1 898 ? -55.950 -12.071 -23.443 1.00 92.09  ? 1001 LEU A CG    1 
ATOM   6748 C  CD1   . LEU A 1 898 ? -55.269 -10.721 -23.561 1.00 104.30 ? 1001 LEU A CD1   1 
ATOM   6749 C  CD2   . LEU A 1 898 ? -54.932 -13.198 -23.532 1.00 89.03  ? 1001 LEU A CD2   1 
ATOM   6750 N  N     . PHE A 1 899 ? -59.398 -13.040 -20.346 1.00 120.86 ? 1002 PHE A N     1 
ATOM   6751 C  CA    . PHE A 1 899 ? -60.018 -13.139 -19.030 1.00 135.55 ? 1002 PHE A CA    1 
ATOM   6752 C  C     . PHE A 1 899 ? -60.621 -14.516 -18.784 1.00 136.11 ? 1002 PHE A C     1 
ATOM   6753 O  O     . PHE A 1 899 ? -60.618 -14.993 -17.644 1.00 130.41 ? 1002 PHE A O     1 
ATOM   6754 C  CB    . PHE A 1 899 ? -61.092 -12.062 -18.866 1.00 132.63 ? 1002 PHE A CB    1 
ATOM   6755 C  CG    . PHE A 1 899 ? -60.541 -10.692 -18.588 1.00 129.09 ? 1002 PHE A CG    1 
ATOM   6756 C  CD1   . PHE A 1 899 ? -60.281 -10.287 -17.289 1.00 153.48 ? 1002 PHE A CD1   1 
ATOM   6757 C  CD2   . PHE A 1 899 ? -60.288 -9.808  -19.622 1.00 124.49 ? 1002 PHE A CD2   1 
ATOM   6758 C  CE1   . PHE A 1 899 ? -59.776 -9.027  -17.029 1.00 136.68 ? 1002 PHE A CE1   1 
ATOM   6759 C  CE2   . PHE A 1 899 ? -59.783 -8.547  -19.368 1.00 128.03 ? 1002 PHE A CE2   1 
ATOM   6760 C  CZ    . PHE A 1 899 ? -59.527 -8.156  -18.070 1.00 130.22 ? 1002 PHE A CZ    1 
ATOM   6761 N  N     . SER A 1 900 ? -61.141 -15.165 -19.830 1.00 120.64 ? 1003 SER A N     1 
ATOM   6762 C  CA    . SER A 1 900 ? -61.715 -16.495 -19.658 1.00 117.04 ? 1003 SER A CA    1 
ATOM   6763 C  C     . SER A 1 900 ? -60.640 -17.542 -19.397 1.00 118.30 ? 1003 SER A C     1 
ATOM   6764 O  O     . SER A 1 900 ? -60.911 -18.558 -18.748 1.00 144.74 ? 1003 SER A O     1 
ATOM   6765 C  CB    . SER A 1 900 ? -62.541 -16.876 -20.887 1.00 130.60 ? 1003 SER A CB    1 
ATOM   6766 O  OG    . SER A 1 900 ? -61.731 -16.945 -22.047 1.00 156.36 ? 1003 SER A OG    1 
ATOM   6767 N  N     . MET A 1 901 ? -59.422 -17.317 -19.892 1.00 111.49 ? 1004 MET A N     1 
ATOM   6768 C  CA    . MET A 1 901 ? -58.312 -18.220 -19.616 1.00 129.69 ? 1004 MET A CA    1 
ATOM   6769 C  C     . MET A 1 901 ? -57.743 -18.042 -18.215 1.00 139.62 ? 1004 MET A C     1 
ATOM   6770 O  O     . MET A 1 901 ? -56.963 -18.891 -17.769 1.00 114.10 ? 1004 MET A O     1 
ATOM   6771 C  CB    . MET A 1 901 ? -57.202 -18.023 -20.653 1.00 105.31 ? 1004 MET A CB    1 
ATOM   6772 C  CG    . MET A 1 901 ? -57.612 -18.381 -22.073 1.00 103.04 ? 1004 MET A CG    1 
ATOM   6773 S  SD    . MET A 1 901 ? -56.362 -17.967 -23.306 1.00 110.65 ? 1004 MET A SD    1 
ATOM   6774 C  CE    . MET A 1 901 ? -55.093 -19.175 -22.936 1.00 102.37 ? 1004 MET A CE    1 
ATOM   6775 N  N     . MET A 1 902 ? -58.111 -16.970 -17.515 1.00 131.93 ? 1005 MET A N     1 
ATOM   6776 C  CA    . MET A 1 902 ? -57.660 -16.724 -16.152 1.00 144.18 ? 1005 MET A CA    1 
ATOM   6777 C  C     . MET A 1 902 ? -58.748 -16.993 -15.120 1.00 157.52 ? 1005 MET A C     1 
ATOM   6778 O  O     . MET A 1 902 ? -58.570 -16.655 -13.945 1.00 163.58 ? 1005 MET A O     1 
ATOM   6779 C  CB    . MET A 1 902 ? -57.153 -15.286 -16.015 1.00 131.47 ? 1005 MET A CB    1 
ATOM   6780 C  CG    . MET A 1 902 ? -55.988 -14.940 -16.930 1.00 117.94 ? 1005 MET A CG    1 
ATOM   6781 S  SD    . MET A 1 902 ? -54.522 -15.941 -16.620 1.00 114.98 ? 1005 MET A SD    1 
ATOM   6782 C  CE    . MET A 1 902 ? -54.227 -15.582 -14.890 1.00 133.25 ? 1005 MET A CE    1 
ATOM   6783 N  N     . LEU A 1 903 ? -59.871 -17.589 -15.529 1.00 146.93 ? 1006 LEU A N     1 
ATOM   6784 C  CA    . LEU A 1 903 ? -60.951 -17.857 -14.584 1.00 144.69 ? 1006 LEU A CA    1 
ATOM   6785 C  C     . LEU A 1 903 ? -60.578 -18.952 -13.594 1.00 176.88 ? 1006 LEU A C     1 
ATOM   6786 O  O     . LEU A 1 903 ? -61.071 -18.952 -12.460 1.00 179.35 ? 1006 LEU A O     1 
ATOM   6787 C  CB    . LEU A 1 903 ? -62.228 -18.234 -15.336 1.00 138.95 ? 1006 LEU A CB    1 
ATOM   6788 C  CG    . LEU A 1 903 ? -62.964 -17.085 -16.026 1.00 149.96 ? 1006 LEU A CG    1 
ATOM   6789 C  CD1   . LEU A 1 903 ? -64.181 -17.599 -16.779 1.00 144.51 ? 1006 LEU A CD1   1 
ATOM   6790 C  CD2   . LEU A 1 903 ? -63.365 -16.030 -15.008 1.00 154.39 ? 1006 LEU A CD2   1 
ATOM   6791 N  N     . GLY A 1 904 ? -59.719 -19.885 -13.995 1.00 198.14 ? 1007 GLY A N     1 
ATOM   6792 C  CA    . GLY A 1 904 ? -59.279 -20.944 -13.112 1.00 204.67 ? 1007 GLY A CA    1 
ATOM   6793 C  C     . GLY A 1 904 ? -58.211 -20.559 -12.116 1.00 190.90 ? 1007 GLY A C     1 
ATOM   6794 O  O     . GLY A 1 904 ? -57.725 -21.421 -11.380 1.00 190.28 ? 1007 GLY A O     1 
ATOM   6795 N  N     . SER A 1 905 ? -57.830 -19.284 -12.069 1.00 139.45 ? 1008 SER A N     1 
ATOM   6796 C  CA    . SER A 1 905 ? -56.794 -18.816 -11.158 1.00 152.82 ? 1008 SER A CA    1 
ATOM   6797 C  C     . SER A 1 905 ? -57.322 -18.491 -9.767  1.00 147.05 ? 1008 SER A C     1 
ATOM   6798 O  O     . SER A 1 905 ? -56.528 -18.127 -8.892  1.00 143.17 ? 1008 SER A O     1 
ATOM   6799 C  CB    . SER A 1 905 ? -56.098 -17.586 -11.747 1.00 147.86 ? 1008 SER A CB    1 
ATOM   6800 O  OG    . SER A 1 905 ? -57.041 -16.601 -12.129 1.00 133.83 ? 1008 SER A OG    1 
ATOM   6801 N  N     . GLY A 1 906 ? -58.628 -18.613 -9.539  1.00 147.80 ? 1009 GLY A N     1 
ATOM   6802 C  CA    . GLY A 1 906 ? -59.181 -18.349 -8.226  1.00 168.95 ? 1009 GLY A CA    1 
ATOM   6803 C  C     . GLY A 1 906 ? -59.109 -16.908 -7.780  1.00 159.18 ? 1009 GLY A C     1 
ATOM   6804 O  O     . GLY A 1 906 ? -59.146 -16.640 -6.577  1.00 195.53 ? 1009 GLY A O     1 
ATOM   6805 N  N     . MET A 1 907 ? -59.005 -15.968 -8.715  1.00 148.68 ? 1010 MET A N     1 
ATOM   6806 C  CA    . MET A 1 907 ? -58.953 -14.563 -8.353  1.00 156.11 ? 1010 MET A CA    1 
ATOM   6807 C  C     . MET A 1 907 ? -60.316 -14.103 -7.833  1.00 165.84 ? 1010 MET A C     1 
ATOM   6808 O  O     . MET A 1 907 ? -61.355 -14.618 -8.254  1.00 163.74 ? 1010 MET A O     1 
ATOM   6809 C  CB    . MET A 1 907 ? -58.531 -13.722 -9.554  1.00 168.16 ? 1010 MET A CB    1 
ATOM   6810 C  CG    . MET A 1 907 ? -57.147 -14.070 -10.083 1.00 175.75 ? 1010 MET A CG    1 
ATOM   6811 S  SD    . MET A 1 907 ? -56.666 -13.099 -11.523 1.00 122.50 ? 1010 MET A SD    1 
ATOM   6812 C  CE    . MET A 1 907 ? -56.779 -11.445 -10.857 1.00 133.45 ? 1010 MET A CE    1 
ATOM   6813 N  N     . PRO A 1 908 ? -60.336 -13.136 -6.909  1.00 166.60 ? 1011 PRO A N     1 
ATOM   6814 C  CA    . PRO A 1 908 ? -61.622 -12.730 -6.315  1.00 168.21 ? 1011 PRO A CA    1 
ATOM   6815 C  C     . PRO A 1 908 ? -62.589 -12.119 -7.313  1.00 176.78 ? 1011 PRO A C     1 
ATOM   6816 O  O     . PRO A 1 908 ? -63.787 -12.429 -7.276  1.00 165.09 ? 1011 PRO A O     1 
ATOM   6817 C  CB    . PRO A 1 908 ? -61.201 -11.722 -5.235  1.00 154.08 ? 1011 PRO A CB    1 
ATOM   6818 C  CG    . PRO A 1 908 ? -59.869 -11.216 -5.684  1.00 157.10 ? 1011 PRO A CG    1 
ATOM   6819 C  CD    . PRO A 1 908 ? -59.202 -12.384 -6.345  1.00 162.63 ? 1011 PRO A CD    1 
ATOM   6820 N  N     . GLU A 1 909 ? -62.109 -11.259 -8.207  1.00 175.63 ? 1012 GLU A N     1 
ATOM   6821 C  CA    . GLU A 1 909 ? -62.962 -10.631 -9.207  1.00 166.15 ? 1012 GLU A CA    1 
ATOM   6822 C  C     . GLU A 1 909 ? -63.050 -11.427 -10.502 1.00 148.77 ? 1012 GLU A C     1 
ATOM   6823 O  O     . GLU A 1 909 ? -63.706 -10.973 -11.445 1.00 149.19 ? 1012 GLU A O     1 
ATOM   6824 C  CB    . GLU A 1 909 ? -62.467 -9.211  -9.507  1.00 170.67 ? 1012 GLU A CB    1 
ATOM   6825 C  CG    . GLU A 1 909 ? -62.837 -8.187  -8.444  1.00 181.81 ? 1012 GLU A CG    1 
ATOM   6826 C  CD    . GLU A 1 909 ? -64.322 -7.875  -8.423  1.00 190.51 ? 1012 GLU A CD    1 
ATOM   6827 O  OE1   . GLU A 1 909 ? -65.006 -8.143  -9.434  1.00 178.04 ? 1012 GLU A OE1   1 
ATOM   6828 O  OE2   . GLU A 1 909 ? -64.807 -7.359  -7.394  1.00 206.37 ? 1012 GLU A OE2   1 
ATOM   6829 N  N     . LEU A 1 910 ? -62.413 -12.590 -10.574 1.00 141.09 ? 1013 LEU A N     1 
ATOM   6830 C  CA    . LEU A 1 910 ? -62.459 -13.457 -11.750 1.00 146.32 ? 1013 LEU A CA    1 
ATOM   6831 C  C     . LEU A 1 910 ? -62.946 -14.838 -11.320 1.00 170.32 ? 1013 LEU A C     1 
ATOM   6832 O  O     . LEU A 1 910 ? -62.200 -15.820 -11.377 1.00 176.48 ? 1013 LEU A O     1 
ATOM   6833 C  CB    . LEU A 1 910 ? -61.086 -13.529 -12.433 1.00 169.55 ? 1013 LEU A CB    1 
ATOM   6834 C  CG    . LEU A 1 910 ? -60.881 -12.652 -13.670 1.00 147.17 ? 1013 LEU A CG    1 
ATOM   6835 C  CD1   . LEU A 1 910 ? -61.079 -11.185 -13.337 1.00 160.37 ? 1013 LEU A CD1   1 
ATOM   6836 C  CD2   . LEU A 1 910 ? -59.503 -12.888 -14.266 1.00 122.35 ? 1013 LEU A CD2   1 
ATOM   6837 N  N     . GLN A 1 911 ? -64.204 -14.910 -10.890 1.00 174.05 ? 1014 GLN A N     1 
ATOM   6838 C  CA    . GLN A 1 911 ? -64.816 -16.157 -10.449 1.00 166.05 ? 1014 GLN A CA    1 
ATOM   6839 C  C     . GLN A 1 911 ? -65.838 -16.694 -11.439 1.00 164.57 ? 1014 GLN A C     1 
ATOM   6840 O  O     . GLN A 1 911 ? -65.785 -17.872 -11.805 1.00 164.61 ? 1014 GLN A O     1 
ATOM   6841 C  CB    . GLN A 1 911 ? -65.476 -15.963 -9.076  1.00 170.18 ? 1014 GLN A CB    1 
ATOM   6842 C  CG    . GLN A 1 911 ? -64.495 -15.700 -7.944  1.00 167.25 ? 1014 GLN A CG    1 
ATOM   6843 C  CD    . GLN A 1 911 ? -63.635 -16.909 -7.621  1.00 181.91 ? 1014 GLN A CD    1 
ATOM   6844 O  OE1   . GLN A 1 911 ? -63.985 -18.042 -7.953  1.00 186.71 ? 1014 GLN A OE1   1 
ATOM   6845 N  NE2   . GLN A 1 911 ? -62.502 -16.671 -6.971  1.00 200.62 ? 1014 GLN A NE2   1 
ATOM   6846 N  N     . SER A 1 912 ? -66.771 -15.858 -11.885 1.00 163.22 ? 1015 SER A N     1 
ATOM   6847 C  CA    . SER A 1 912 ? -67.823 -16.268 -12.804 1.00 180.08 ? 1015 SER A CA    1 
ATOM   6848 C  C     . SER A 1 912 ? -67.820 -15.347 -14.019 1.00 174.87 ? 1015 SER A C     1 
ATOM   6849 O  O     . SER A 1 912 ? -67.071 -14.367 -14.085 1.00 162.10 ? 1015 SER A O     1 
ATOM   6850 C  CB    . SER A 1 912 ? -69.192 -16.265 -12.113 1.00 195.13 ? 1015 SER A CB    1 
ATOM   6851 O  OG    . SER A 1 912 ? -69.440 -15.021 -11.483 1.00 208.73 ? 1015 SER A OG    1 
ATOM   6852 N  N     . PHE A 1 913 ? -68.675 -15.670 -14.989 1.00 180.45 ? 1016 PHE A N     1 
ATOM   6853 C  CA    . PHE A 1 913 ? -68.743 -14.919 -16.236 1.00 161.22 ? 1016 PHE A CA    1 
ATOM   6854 C  C     . PHE A 1 913 ? -69.484 -13.596 -16.102 1.00 167.53 ? 1016 PHE A C     1 
ATOM   6855 O  O     . PHE A 1 913 ? -69.524 -12.830 -17.070 1.00 177.68 ? 1016 PHE A O     1 
ATOM   6856 C  CB    . PHE A 1 913 ? -69.405 -15.768 -17.324 1.00 155.33 ? 1016 PHE A CB    1 
ATOM   6857 C  CG    . PHE A 1 913 ? -68.594 -16.963 -17.736 1.00 158.82 ? 1016 PHE A CG    1 
ATOM   6858 C  CD1   . PHE A 1 913 ? -68.711 -18.165 -17.058 1.00 172.96 ? 1016 PHE A CD1   1 
ATOM   6859 C  CD2   . PHE A 1 913 ? -67.713 -16.884 -18.801 1.00 152.39 ? 1016 PHE A CD2   1 
ATOM   6860 C  CE1   . PHE A 1 913 ? -67.965 -19.266 -17.435 1.00 182.04 ? 1016 PHE A CE1   1 
ATOM   6861 C  CE2   . PHE A 1 913 ? -66.965 -17.980 -19.184 1.00 160.27 ? 1016 PHE A CE2   1 
ATOM   6862 C  CZ    . PHE A 1 913 ? -67.091 -19.173 -18.500 1.00 189.62 ? 1016 PHE A CZ    1 
ATOM   6863 N  N     . ASP A 1 914 ? -70.072 -13.308 -14.938 1.00 197.28 ? 1017 ASP A N     1 
ATOM   6864 C  CA    . ASP A 1 914 ? -70.716 -12.016 -14.740 1.00 198.02 ? 1017 ASP A CA    1 
ATOM   6865 C  C     . ASP A 1 914 ? -69.705 -10.883 -14.625 1.00 197.88 ? 1017 ASP A C     1 
ATOM   6866 O  O     . ASP A 1 914 ? -70.077 -9.717  -14.793 1.00 198.05 ? 1017 ASP A O     1 
ATOM   6867 C  CB    . ASP A 1 914 ? -71.606 -12.050 -13.495 1.00 221.77 ? 1017 ASP A CB    1 
ATOM   6868 C  CG    . ASP A 1 914 ? -70.843 -12.432 -12.239 1.00 228.30 ? 1017 ASP A CG    1 
ATOM   6869 O  OD1   . ASP A 1 914 ? -69.670 -12.846 -12.352 1.00 222.57 ? 1017 ASP A OD1   1 
ATOM   6870 O  OD2   . ASP A 1 914 ? -71.419 -12.318 -11.137 1.00 226.56 ? 1017 ASP A OD2   1 
ATOM   6871 N  N     . ASP A 1 915 ? -68.441 -11.201 -14.342 1.00 180.07 ? 1018 ASP A N     1 
ATOM   6872 C  CA    . ASP A 1 915 ? -67.411 -10.173 -14.252 1.00 167.75 ? 1018 ASP A CA    1 
ATOM   6873 C  C     . ASP A 1 915 ? -66.832 -9.843  -15.621 1.00 163.60 ? 1018 ASP A C     1 
ATOM   6874 O  O     . ASP A 1 915 ? -66.613 -8.668  -15.938 1.00 153.95 ? 1018 ASP A O     1 
ATOM   6875 C  CB    . ASP A 1 915 ? -66.305 -10.623 -13.300 1.00 171.27 ? 1018 ASP A CB    1 
ATOM   6876 C  CG    . ASP A 1 915 ? -66.823 -10.920 -11.907 1.00 177.53 ? 1018 ASP A CG    1 
ATOM   6877 O  OD1   . ASP A 1 915 ? -67.671 -10.151 -11.408 1.00 196.37 ? 1018 ASP A OD1   1 
ATOM   6878 O  OD2   . ASP A 1 915 ? -66.384 -11.927 -11.313 1.00 173.58 ? 1018 ASP A OD2   1 
ATOM   6879 N  N     . ILE A 1 916 ? -66.574 -10.864 -16.443 1.00 145.03 ? 1019 ILE A N     1 
ATOM   6880 C  CA    . ILE A 1 916 ? -66.053 -10.616 -17.783 1.00 132.56 ? 1019 ILE A CA    1 
ATOM   6881 C  C     . ILE A 1 916 ? -67.110 -9.950  -18.653 1.00 142.43 ? 1019 ILE A C     1 
ATOM   6882 O  O     . ILE A 1 916 ? -66.780 -9.232  -19.605 1.00 160.49 ? 1019 ILE A O     1 
ATOM   6883 C  CB    . ILE A 1 916 ? -65.547 -11.928 -18.410 1.00 119.45 ? 1019 ILE A CB    1 
ATOM   6884 C  CG1   . ILE A 1 916 ? -64.709 -12.714 -17.401 1.00 128.49 ? 1019 ILE A CG1   1 
ATOM   6885 C  CG2   . ILE A 1 916 ? -64.720 -11.640 -19.651 1.00 152.55 ? 1019 ILE A CG2   1 
ATOM   6886 C  CD1   . ILE A 1 916 ? -64.138 -13.999 -17.960 1.00 130.44 ? 1019 ILE A CD1   1 
ATOM   6887 N  N     . ALA A 1 917 ? -68.392 -10.162 -18.342 1.00 144.70 ? 1020 ALA A N     1 
ATOM   6888 C  CA    . ALA A 1 917 ? -69.459 -9.490  -19.071 1.00 148.14 ? 1020 ALA A CA    1 
ATOM   6889 C  C     . ALA A 1 917 ? -69.447 -7.984  -18.853 1.00 155.97 ? 1020 ALA A C     1 
ATOM   6890 O  O     . ALA A 1 917 ? -70.037 -7.250  -19.653 1.00 147.78 ? 1020 ALA A O     1 
ATOM   6891 C  CB    . ALA A 1 917 ? -70.818 -10.066 -18.667 1.00 144.14 ? 1020 ALA A CB    1 
ATOM   6892 N  N     . TYR A 1 918 ? -68.793 -7.509  -17.788 1.00 144.41 ? 1021 TYR A N     1 
ATOM   6893 C  CA    . TYR A 1 918 ? -68.659 -6.072  -17.578 1.00 137.30 ? 1021 TYR A CA    1 
ATOM   6894 C  C     . TYR A 1 918 ? -67.852 -5.421  -18.693 1.00 146.97 ? 1021 TYR A C     1 
ATOM   6895 O  O     . TYR A 1 918 ? -68.044 -4.235  -18.987 1.00 148.34 ? 1021 TYR A O     1 
ATOM   6896 C  CB    . TYR A 1 918 ? -68.014 -5.803  -16.217 1.00 137.20 ? 1021 TYR A CB    1 
ATOM   6897 C  CG    . TYR A 1 918 ? -67.751 -4.344  -15.923 1.00 141.36 ? 1021 TYR A CG    1 
ATOM   6898 C  CD1   . TYR A 1 918 ? -68.795 -3.472  -15.643 1.00 165.45 ? 1021 TYR A CD1   1 
ATOM   6899 C  CD2   . TYR A 1 918 ? -66.456 -3.841  -15.911 1.00 141.56 ? 1021 TYR A CD2   1 
ATOM   6900 C  CE1   . TYR A 1 918 ? -68.558 -2.137  -15.370 1.00 163.51 ? 1021 TYR A CE1   1 
ATOM   6901 C  CE2   . TYR A 1 918 ? -66.209 -2.509  -15.638 1.00 150.42 ? 1021 TYR A CE2   1 
ATOM   6902 C  CZ    . TYR A 1 918 ? -67.263 -1.662  -15.368 1.00 154.15 ? 1021 TYR A CZ    1 
ATOM   6903 O  OH    . TYR A 1 918 ? -67.023 -0.334  -15.096 1.00 146.64 ? 1021 TYR A OH    1 
ATOM   6904 N  N     . ILE A 1 919 ? -66.953 -6.177  -19.325 1.00 147.49 ? 1022 ILE A N     1 
ATOM   6905 C  CA    . ILE A 1 919 ? -66.213 -5.656  -20.469 1.00 122.15 ? 1022 ILE A CA    1 
ATOM   6906 C  C     . ILE A 1 919 ? -67.144 -5.463  -21.660 1.00 132.91 ? 1022 ILE A C     1 
ATOM   6907 O  O     . ILE A 1 919 ? -67.009 -4.498  -22.422 1.00 122.19 ? 1022 ILE A O     1 
ATOM   6908 C  CB    . ILE A 1 919 ? -65.031 -6.585  -20.810 1.00 123.21 ? 1022 ILE A CB    1 
ATOM   6909 C  CG1   . ILE A 1 919 ? -63.934 -6.483  -19.746 1.00 134.32 ? 1022 ILE A CG1   1 
ATOM   6910 C  CG2   . ILE A 1 919 ? -64.459 -6.262  -22.182 1.00 124.09 ? 1022 ILE A CG2   1 
ATOM   6911 C  CD1   . ILE A 1 919 ? -64.107 -7.434  -18.580 1.00 150.10 ? 1022 ILE A CD1   1 
ATOM   6912 N  N     . ARG A 1 920 ? -68.115 -6.366  -21.828 1.00 139.25 ? 1023 ARG A N     1 
ATOM   6913 C  CA    . ARG A 1 920 ? -69.048 -6.253  -22.944 1.00 141.10 ? 1023 ARG A CA    1 
ATOM   6914 C  C     . ARG A 1 920 ? -69.899 -4.994  -22.847 1.00 135.12 ? 1023 ARG A C     1 
ATOM   6915 O  O     . ARG A 1 920 ? -70.250 -4.403  -23.875 1.00 132.86 ? 1023 ARG A O     1 
ATOM   6916 C  CB    . ARG A 1 920 ? -69.946 -7.489  -23.006 1.00 149.50 ? 1023 ARG A CB    1 
ATOM   6917 C  CG    . ARG A 1 920 ? -69.204 -8.793  -23.235 1.00 131.64 ? 1023 ARG A CG    1 
ATOM   6918 C  CD    . ARG A 1 920 ? -70.170 -9.963  -23.297 1.00 136.86 ? 1023 ARG A CD    1 
ATOM   6919 N  NE    . ARG A 1 920 ? -71.164 -9.797  -24.352 1.00 109.76 ? 1023 ARG A NE    1 
ATOM   6920 N  N     . LYS A 1 921 ? -70.241 -4.568  -21.629 1.00 140.56 ? 1024 LYS A N     1 
ATOM   6921 C  CA    . LYS A 1 921 ? -71.083 -3.387  -21.471 1.00 156.19 ? 1024 LYS A CA    1 
ATOM   6922 C  C     . LYS A 1 921 ? -70.277 -2.099  -21.589 1.00 154.90 ? 1024 LYS A C     1 
ATOM   6923 O  O     . LYS A 1 921 ? -70.747 -1.123  -22.185 1.00 137.44 ? 1024 LYS A O     1 
ATOM   6924 C  CB    . LYS A 1 921 ? -71.817 -3.439  -20.131 1.00 150.43 ? 1024 LYS A CB    1 
ATOM   6925 C  CG    . LYS A 1 921 ? -72.766 -4.618  -19.992 1.00 159.72 ? 1024 LYS A CG    1 
ATOM   6926 C  CD    . LYS A 1 921 ? -73.654 -4.472  -18.768 1.00 169.94 ? 1024 LYS A CD    1 
ATOM   6927 C  CE    . LYS A 1 921 ? -74.530 -3.233  -18.871 1.00 183.26 ? 1024 LYS A CE    1 
ATOM   6928 N  NZ    . LYS A 1 921 ? -75.435 -3.090  -17.697 1.00 199.11 ? 1024 LYS A NZ    1 
ATOM   6929 N  N     . THR A 1 922 ? -69.064 -2.072  -21.029 1.00 155.85 ? 1025 THR A N     1 
ATOM   6930 C  CA    . THR A 1 922 ? -68.231 -0.880  -21.135 1.00 155.38 ? 1025 THR A CA    1 
ATOM   6931 C  C     . THR A 1 922 ? -67.671 -0.692  -22.539 1.00 141.07 ? 1025 THR A C     1 
ATOM   6932 O  O     . THR A 1 922 ? -67.265 0.422   -22.887 1.00 121.05 ? 1025 THR A O     1 
ATOM   6933 C  CB    . THR A 1 922 ? -67.089 -0.936  -20.119 1.00 137.46 ? 1025 THR A CB    1 
ATOM   6934 O  OG1   . THR A 1 922 ? -66.369 0.303   -20.137 1.00 157.56 ? 1025 THR A OG1   1 
ATOM   6935 C  CG2   . THR A 1 922 ? -66.139 -2.065  -20.454 1.00 124.44 ? 1025 THR A CG2   1 
ATOM   6936 N  N     . LEU A 1 923 ? -67.636 -1.751  -23.347 1.00 125.83 ? 1026 LEU A N     1 
ATOM   6937 C  CA    . LEU A 1 923 ? -67.266 -1.644  -24.751 1.00 119.15 ? 1026 LEU A CA    1 
ATOM   6938 C  C     . LEU A 1 923 ? -68.471 -1.503  -25.669 1.00 146.66 ? 1026 LEU A C     1 
ATOM   6939 O  O     . LEU A 1 923 ? -68.291 -1.232  -26.862 1.00 151.03 ? 1026 LEU A O     1 
ATOM   6940 C  CB    . LEU A 1 923 ? -66.443 -2.864  -25.182 1.00 133.42 ? 1026 LEU A CB    1 
ATOM   6941 C  CG    . LEU A 1 923 ? -64.989 -2.916  -24.711 1.00 140.26 ? 1026 LEU A CG    1 
ATOM   6942 C  CD1   . LEU A 1 923 ? -64.307 -4.177  -25.216 1.00 95.58  ? 1026 LEU A CD1   1 
ATOM   6943 C  CD2   . LEU A 1 923 ? -64.244 -1.679  -25.180 1.00 148.45 ? 1026 LEU A CD2   1 
ATOM   6944 N  N     . ALA A 1 924 ? -69.682 -1.676  -25.141 1.00 136.23 ? 1027 ALA A N     1 
ATOM   6945 C  CA    . ALA A 1 924 ? -70.922 -1.589  -25.909 1.00 144.81 ? 1027 ALA A CA    1 
ATOM   6946 C  C     . ALA A 1 924 ? -70.889 -2.541  -27.105 1.00 158.65 ? 1027 ALA A C     1 
ATOM   6947 O  O     . ALA A 1 924 ? -71.069 -2.150  -28.260 1.00 174.83 ? 1027 ALA A O     1 
ATOM   6948 C  CB    . ALA A 1 924 ? -71.195 -0.149  -26.350 1.00 152.79 ? 1027 ALA A CB    1 
ATOM   6949 N  N     . LEU A 1 925 ? -70.652 -3.816  -26.801 1.00 143.10 ? 1028 LEU A N     1 
ATOM   6950 C  CA    . LEU A 1 925 ? -70.568 -4.851  -27.823 1.00 147.40 ? 1028 LEU A CA    1 
ATOM   6951 C  C     . LEU A 1 925 ? -71.928 -5.258  -28.374 1.00 160.43 ? 1028 LEU A C     1 
ATOM   6952 O  O     . LEU A 1 925 ? -71.983 -6.083  -29.292 1.00 165.08 ? 1028 LEU A O     1 
ATOM   6953 C  CB    . LEU A 1 925 ? -69.845 -6.080  -27.265 1.00 148.97 ? 1028 LEU A CB    1 
ATOM   6954 C  CG    . LEU A 1 925 ? -68.413 -5.842  -26.778 1.00 134.59 ? 1028 LEU A CG    1 
ATOM   6955 C  CD1   . LEU A 1 925 ? -67.769 -7.145  -26.331 1.00 140.64 ? 1028 LEU A CD1   1 
ATOM   6956 C  CD2   . LEU A 1 925 ? -67.582 -5.172  -27.862 1.00 142.21 ? 1028 LEU A CD2   1 
ATOM   6957 N  N     . ASP A 1 926 ? -73.018 -4.709  -27.842 1.00 164.81 ? 1029 ASP A N     1 
ATOM   6958 C  CA    . ASP A 1 926 ? -74.358 -4.982  -28.342 1.00 162.84 ? 1029 ASP A CA    1 
ATOM   6959 C  C     . ASP A 1 926 ? -74.881 -3.885  -29.258 1.00 155.04 ? 1029 ASP A C     1 
ATOM   6960 O  O     . ASP A 1 926 ? -76.020 -3.977  -29.726 1.00 167.66 ? 1029 ASP A O     1 
ATOM   6961 C  CB    . ASP A 1 926 ? -75.328 -5.183  -27.172 1.00 166.52 ? 1029 ASP A CB    1 
ATOM   6962 C  CG    . ASP A 1 926 ? -74.961 -6.375  -26.309 1.00 169.00 ? 1029 ASP A CG    1 
ATOM   6963 O  OD1   . ASP A 1 926 ? -74.428 -7.364  -26.855 1.00 167.46 ? 1029 ASP A OD1   1 
ATOM   6964 O  OD2   . ASP A 1 926 ? -75.206 -6.323  -25.085 1.00 169.47 ? 1029 ASP A OD2   1 
ATOM   6965 N  N     . LYS A 1 927 ? -74.083 -2.858  -29.523 1.00 138.92 ? 1030 LYS A N     1 
ATOM   6966 C  CA    . LYS A 1 927 ? -74.461 -1.741  -30.377 1.00 163.31 ? 1030 LYS A CA    1 
ATOM   6967 C  C     . LYS A 1 927 ? -73.530 -1.689  -31.585 1.00 141.83 ? 1030 LYS A C     1 
ATOM   6968 O  O     . LYS A 1 927 ? -72.578 -2.465  -31.699 1.00 136.37 ? 1030 LYS A O     1 
ATOM   6969 C  CB    . LYS A 1 927 ? -74.427 -0.426  -29.592 1.00 167.11 ? 1030 LYS A CB    1 
ATOM   6970 C  CG    . LYS A 1 927 ? -75.332 -0.418  -28.369 1.00 173.01 ? 1030 LYS A CG    1 
ATOM   6971 C  CD    . LYS A 1 927 ? -75.154 0.849   -27.549 1.00 169.41 ? 1030 LYS A CD    1 
ATOM   6972 C  CE    . LYS A 1 927 ? -76.135 0.897   -26.388 1.00 175.13 ? 1030 LYS A CE    1 
ATOM   6973 N  NZ    . LYS A 1 927 ? -76.013 2.159   -25.607 1.00 161.70 ? 1030 LYS A NZ    1 
ATOM   6974 N  N     . THR A 1 928 ? -73.814 -0.762  -32.497 1.00 176.27 ? 1031 THR A N     1 
ATOM   6975 C  CA    . THR A 1 928 ? -73.006 -0.608  -33.699 1.00 198.06 ? 1031 THR A CA    1 
ATOM   6976 C  C     . THR A 1 928 ? -71.798 0.276   -33.391 1.00 189.78 ? 1031 THR A C     1 
ATOM   6977 O  O     . THR A 1 928 ? -71.522 0.615   -32.237 1.00 198.43 ? 1031 THR A O     1 
ATOM   6978 C  CB    . THR A 1 928 ? -73.850 -0.049  -34.843 1.00 201.07 ? 1031 THR A CB    1 
ATOM   6979 O  OG1   . THR A 1 928 ? -73.053 0.028   -36.032 1.00 220.17 ? 1031 THR A OG1   1 
ATOM   6980 C  CG2   . THR A 1 928 ? -74.366 1.338   -34.501 1.00 181.53 ? 1031 THR A CG2   1 
ATOM   6981 N  N     . GLU A 1 929 ? -71.059 0.660   -34.433 1.00 173.38 ? 1032 GLU A N     1 
ATOM   6982 C  CA    . GLU A 1 929 ? -69.849 1.452   -34.235 1.00 183.67 ? 1032 GLU A CA    1 
ATOM   6983 C  C     . GLU A 1 929 ? -70.182 2.858   -33.747 1.00 177.40 ? 1032 GLU A C     1 
ATOM   6984 O  O     . GLU A 1 929 ? -69.554 3.365   -32.810 1.00 161.03 ? 1032 GLU A O     1 
ATOM   6985 C  CB    . GLU A 1 929 ? -69.043 1.504   -35.534 1.00 199.28 ? 1032 GLU A CB    1 
ATOM   6986 C  CG    . GLU A 1 929 ? -67.788 2.359   -35.464 1.00 191.46 ? 1032 GLU A CG    1 
ATOM   6987 C  CD    . GLU A 1 929 ? -66.960 2.279   -36.733 1.00 207.40 ? 1032 GLU A CD    1 
ATOM   6988 O  OE1   . GLU A 1 929 ? -67.061 1.259   -37.446 1.00 218.72 ? 1032 GLU A OE1   1 
ATOM   6989 O  OE2   . GLU A 1 929 ? -66.212 3.237   -37.020 1.00 205.61 ? 1032 GLU A OE2   1 
ATOM   6990 N  N     . GLN A 1 930 ? -71.171 3.502   -34.368 1.00 169.65 ? 1033 GLN A N     1 
ATOM   6991 C  CA    . GLN A 1 930 ? -71.531 4.860   -33.974 1.00 158.87 ? 1033 GLN A CA    1 
ATOM   6992 C  C     . GLN A 1 930 ? -72.312 4.878   -32.665 1.00 164.42 ? 1033 GLN A C     1 
ATOM   6993 O  O     . GLN A 1 930 ? -72.135 5.788   -31.848 1.00 170.96 ? 1033 GLN A O     1 
ATOM   6994 C  CB    . GLN A 1 930 ? -72.334 5.536   -35.086 1.00 168.05 ? 1033 GLN A CB    1 
ATOM   6995 C  CG    . GLN A 1 930 ? -72.774 6.957   -34.765 1.00 176.79 ? 1033 GLN A CG    1 
ATOM   6996 C  CD    . GLN A 1 930 ? -71.606 7.899   -34.539 1.00 162.75 ? 1033 GLN A CD    1 
ATOM   6997 O  OE1   . GLN A 1 930 ? -70.521 7.707   -35.089 1.00 182.67 ? 1033 GLN A OE1   1 
ATOM   6998 N  NE2   . GLN A 1 930 ? -71.822 8.923   -33.722 1.00 165.70 ? 1033 GLN A NE2   1 
ATOM   6999 N  N     . GLU A 1 931 ? -73.178 3.885   -32.449 1.00 172.40 ? 1034 GLU A N     1 
ATOM   7000 C  CA    . GLU A 1 931 ? -73.947 3.839   -31.209 1.00 173.10 ? 1034 GLU A CA    1 
ATOM   7001 C  C     . GLU A 1 931 ? -73.054 3.559   -30.008 1.00 171.55 ? 1034 GLU A C     1 
ATOM   7002 O  O     . GLU A 1 931 ? -73.332 4.043   -28.904 1.00 157.35 ? 1034 GLU A O     1 
ATOM   7003 C  CB    . GLU A 1 931 ? -75.050 2.786   -31.314 1.00 176.44 ? 1034 GLU A CB    1 
ATOM   7004 C  CG    . GLU A 1 931 ? -76.147 2.922   -30.274 1.00 183.24 ? 1034 GLU A CG    1 
ATOM   7005 C  CD    . GLU A 1 931 ? -77.210 1.848   -30.409 1.00 196.35 ? 1034 GLU A CD    1 
ATOM   7006 O  OE1   . GLU A 1 931 ? -77.102 1.017   -31.334 1.00 202.39 ? 1034 GLU A OE1   1 
ATOM   7007 O  OE2   . GLU A 1 931 ? -78.152 1.835   -29.589 1.00 198.36 ? 1034 GLU A OE2   1 
ATOM   7008 N  N     . ALA A 1 932 ? -71.982 2.786   -30.198 1.00 181.18 ? 1035 ALA A N     1 
ATOM   7009 C  CA    . ALA A 1 932 ? -71.011 2.583   -29.130 1.00 172.26 ? 1035 ALA A CA    1 
ATOM   7010 C  C     . ALA A 1 932 ? -70.174 3.828   -28.874 1.00 168.36 ? 1035 ALA A C     1 
ATOM   7011 O  O     . ALA A 1 932 ? -69.649 3.990   -27.767 1.00 163.95 ? 1035 ALA A O     1 
ATOM   7012 C  CB    . ALA A 1 932 ? -70.097 1.402   -29.460 1.00 159.59 ? 1035 ALA A CB    1 
ATOM   7013 N  N     . LEU A 1 933 ? -70.036 4.704   -29.872 1.00 149.47 ? 1036 LEU A N     1 
ATOM   7014 C  CA    . LEU A 1 933 ? -69.291 5.943   -29.673 1.00 145.77 ? 1036 LEU A CA    1 
ATOM   7015 C  C     . LEU A 1 933 ? -70.042 6.894   -28.750 1.00 169.61 ? 1036 LEU A C     1 
ATOM   7016 O  O     . LEU A 1 933 ? -69.446 7.489   -27.844 1.00 171.56 ? 1036 LEU A O     1 
ATOM   7017 C  CB    . LEU A 1 933 ? -69.016 6.608   -31.021 1.00 162.69 ? 1036 LEU A CB    1 
ATOM   7018 C  CG    . LEU A 1 933 ? -68.243 7.928   -30.989 1.00 168.27 ? 1036 LEU A CG    1 
ATOM   7019 C  CD1   . LEU A 1 933 ? -66.820 7.706   -30.501 1.00 128.08 ? 1036 LEU A CD1   1 
ATOM   7020 C  CD2   . LEU A 1 933 ? -68.250 8.591   -32.359 1.00 164.78 ? 1036 LEU A CD2   1 
ATOM   7021 N  N     . GLU A 1 934 ? -71.351 7.049   -28.963 1.00 167.82 ? 1037 GLU A N     1 
ATOM   7022 C  CA    . GLU A 1 934 ? -72.139 7.930   -28.109 1.00 166.25 ? 1037 GLU A CA    1 
ATOM   7023 C  C     . GLU A 1 934 ? -72.262 7.382   -26.693 1.00 160.94 ? 1037 GLU A C     1 
ATOM   7024 O  O     . GLU A 1 934 ? -72.461 8.154   -25.749 1.00 169.20 ? 1037 GLU A O     1 
ATOM   7025 C  CB    . GLU A 1 934 ? -73.523 8.152   -28.718 1.00 172.56 ? 1037 GLU A CB    1 
ATOM   7026 C  CG    . GLU A 1 934 ? -73.509 8.990   -29.986 1.00 183.20 ? 1037 GLU A CG    1 
ATOM   7027 C  CD    . GLU A 1 934 ? -74.251 8.329   -31.130 1.00 186.33 ? 1037 GLU A CD    1 
ATOM   7028 O  OE1   . GLU A 1 934 ? -74.731 7.190   -30.951 1.00 200.25 ? 1037 GLU A OE1   1 
ATOM   7029 O  OE2   . GLU A 1 934 ? -74.352 8.949   -32.210 1.00 179.69 ? 1037 GLU A OE2   1 
ATOM   7030 N  N     . TYR A 1 935 ? -72.149 6.062   -26.525 1.00 145.87 ? 1038 TYR A N     1 
ATOM   7031 C  CA    . TYR A 1 935 ? -72.165 5.484   -25.185 1.00 155.36 ? 1038 TYR A CA    1 
ATOM   7032 C  C     . TYR A 1 935 ? -70.978 5.975   -24.367 1.00 150.66 ? 1038 TYR A C     1 
ATOM   7033 O  O     . TYR A 1 935 ? -71.131 6.380   -23.209 1.00 174.15 ? 1038 TYR A O     1 
ATOM   7034 C  CB    . TYR A 1 935 ? -72.165 3.956   -25.268 1.00 159.75 ? 1038 TYR A CB    1 
ATOM   7035 C  CG    . TYR A 1 935 ? -71.856 3.278   -23.951 1.00 133.40 ? 1038 TYR A CG    1 
ATOM   7036 C  CD1   . TYR A 1 935 ? -72.827 3.154   -22.966 1.00 152.51 ? 1038 TYR A CD1   1 
ATOM   7037 C  CD2   . TYR A 1 935 ? -70.592 2.763   -23.692 1.00 153.64 ? 1038 TYR A CD2   1 
ATOM   7038 C  CE1   . TYR A 1 935 ? -72.548 2.537   -21.760 1.00 136.44 ? 1038 TYR A CE1   1 
ATOM   7039 C  CE2   . TYR A 1 935 ? -70.304 2.145   -22.490 1.00 162.81 ? 1038 TYR A CE2   1 
ATOM   7040 C  CZ    . TYR A 1 935 ? -71.285 2.035   -21.528 1.00 138.06 ? 1038 TYR A CZ    1 
ATOM   7041 O  OH    . TYR A 1 935 ? -71.003 1.420   -20.330 1.00 175.81 ? 1038 TYR A OH    1 
ATOM   7042 N  N     . PHE A 1 936 ? -69.781 5.946   -24.957 1.00 148.14 ? 1039 PHE A N     1 
ATOM   7043 C  CA    . PHE A 1 936 ? -68.601 6.433   -24.253 1.00 143.20 ? 1039 PHE A CA    1 
ATOM   7044 C  C     . PHE A 1 936 ? -68.697 7.930   -23.990 1.00 170.86 ? 1039 PHE A C     1 
ATOM   7045 O  O     . PHE A 1 936 ? -68.363 8.395   -22.895 1.00 179.36 ? 1039 PHE A O     1 
ATOM   7046 C  CB    . PHE A 1 936 ? -67.340 6.101   -25.051 1.00 139.83 ? 1039 PHE A CB    1 
ATOM   7047 C  CG    . PHE A 1 936 ? -66.063 6.437   -24.335 1.00 154.50 ? 1039 PHE A CG    1 
ATOM   7048 C  CD1   . PHE A 1 936 ? -65.639 5.679   -23.256 1.00 168.31 ? 1039 PHE A CD1   1 
ATOM   7049 C  CD2   . PHE A 1 936 ? -65.281 7.503   -24.747 1.00 142.62 ? 1039 PHE A CD2   1 
ATOM   7050 C  CE1   . PHE A 1 936 ? -64.463 5.982   -22.596 1.00 147.17 ? 1039 PHE A CE1   1 
ATOM   7051 C  CE2   . PHE A 1 936 ? -64.102 7.811   -24.092 1.00 148.56 ? 1039 PHE A CE2   1 
ATOM   7052 C  CZ    . PHE A 1 936 ? -63.693 7.049   -23.015 1.00 141.74 ? 1039 PHE A CZ    1 
ATOM   7053 N  N     . MET A 1 937 ? -69.159 8.700   -24.980 1.00 155.62 ? 1040 MET A N     1 
ATOM   7054 C  CA    . MET A 1 937 ? -69.340 10.133  -24.777 1.00 149.86 ? 1040 MET A CA    1 
ATOM   7055 C  C     . MET A 1 937 ? -70.389 10.418  -23.712 1.00 175.29 ? 1040 MET A C     1 
ATOM   7056 O  O     . MET A 1 937 ? -70.275 11.405  -22.975 1.00 189.16 ? 1040 MET A O     1 
ATOM   7057 C  CB    . MET A 1 937 ? -69.726 10.806  -26.095 1.00 157.62 ? 1040 MET A CB    1 
ATOM   7058 C  CG    . MET A 1 937 ? -68.719 10.601  -27.213 1.00 159.39 ? 1040 MET A CG    1 
ATOM   7059 S  SD    . MET A 1 937 ? -69.240 11.353  -28.766 1.00 170.89 ? 1040 MET A SD    1 
ATOM   7060 C  CE    . MET A 1 937 ? -69.341 13.076  -28.289 1.00 180.32 ? 1040 MET A CE    1 
ATOM   7061 N  N     . LYS A 1 938 ? -71.416 9.571   -23.615 1.00 202.82 ? 1041 LYS A N     1 
ATOM   7062 C  CA    . LYS A 1 938 ? -72.428 9.743   -22.578 1.00 213.65 ? 1041 LYS A CA    1 
ATOM   7063 C  C     . LYS A 1 938 ? -71.847 9.468   -21.196 1.00 210.24 ? 1041 LYS A C     1 
ATOM   7064 O  O     . LYS A 1 938 ? -71.991 10.283  -20.278 1.00 218.16 ? 1041 LYS A O     1 
ATOM   7065 C  CB    . LYS A 1 938 ? -73.621 8.827   -22.857 1.00 220.83 ? 1041 LYS A CB    1 
ATOM   7066 C  CG    . LYS A 1 938 ? -74.658 8.770   -21.745 1.00 219.98 ? 1041 LYS A CG    1 
ATOM   7067 C  CD    . LYS A 1 938 ? -75.302 10.125  -21.503 1.00 213.25 ? 1041 LYS A CD    1 
ATOM   7068 C  CE    . LYS A 1 938 ? -76.538 9.995   -20.625 1.00 229.95 ? 1041 LYS A CE    1 
ATOM   7069 N  NZ    . LYS A 1 938 ? -76.253 9.274   -19.355 1.00 223.92 ? 1041 LYS A NZ    1 
ATOM   7070 N  N     . GLN A 1 939 ? -71.177 8.324   -21.033 1.00 185.33 ? 1042 GLN A N     1 
ATOM   7071 C  CA    . GLN A 1 939 ? -70.630 7.968   -19.727 1.00 188.60 ? 1042 GLN A CA    1 
ATOM   7072 C  C     . GLN A 1 939 ? -69.480 8.884   -19.325 1.00 179.53 ? 1042 GLN A C     1 
ATOM   7073 O  O     . GLN A 1 939 ? -69.234 9.076   -18.129 1.00 177.97 ? 1042 GLN A O     1 
ATOM   7074 C  CB    . GLN A 1 939 ? -70.174 6.509   -19.729 1.00 172.76 ? 1042 GLN A CB    1 
ATOM   7075 C  CG    . GLN A 1 939 ? -71.264 5.516   -20.107 1.00 169.01 ? 1042 GLN A CG    1 
ATOM   7076 C  CD    . GLN A 1 939 ? -72.428 5.520   -19.135 1.00 194.57 ? 1042 GLN A CD    1 
ATOM   7077 O  OE1   . GLN A 1 939 ? -72.257 5.777   -17.943 1.00 219.23 ? 1042 GLN A OE1   1 
ATOM   7078 N  NE2   . GLN A 1 939 ? -73.623 5.237   -19.642 1.00 191.43 ? 1042 GLN A NE2   1 
ATOM   7079 N  N     . MET A 1 940 ? -68.765 9.453   -20.299 1.00 178.95 ? 1043 MET A N     1 
ATOM   7080 C  CA    . MET A 1 940 ? -67.723 10.420  -19.970 1.00 173.80 ? 1043 MET A CA    1 
ATOM   7081 C  C     . MET A 1 940 ? -68.325 11.751  -19.537 1.00 189.39 ? 1043 MET A C     1 
ATOM   7082 O  O     . MET A 1 940 ? -67.808 12.404  -18.623 1.00 179.05 ? 1043 MET A O     1 
ATOM   7083 C  CB    . MET A 1 940 ? -66.786 10.617  -21.162 1.00 164.04 ? 1043 MET A CB    1 
ATOM   7084 C  CG    . MET A 1 940 ? -65.805 9.475   -21.407 1.00 171.08 ? 1043 MET A CG    1 
ATOM   7085 S  SD    . MET A 1 940 ? -64.375 9.476   -20.305 1.00 173.89 ? 1043 MET A SD    1 
ATOM   7086 C  CE    . MET A 1 940 ? -64.936 8.402   -18.985 1.00 180.25 ? 1043 MET A CE    1 
ATOM   7087 N  N     . ASN A 1 941 ? -69.418 12.168  -20.180 1.00 198.60 ? 1044 ASN A N     1 
ATOM   7088 C  CA    . ASN A 1 941 ? -70.087 13.403  -19.788 1.00 184.02 ? 1044 ASN A CA    1 
ATOM   7089 C  C     . ASN A 1 941 ? -70.878 13.243  -18.496 1.00 187.93 ? 1044 ASN A C     1 
ATOM   7090 O  O     . ASN A 1 941 ? -71.251 14.248  -17.883 1.00 200.86 ? 1044 ASN A O     1 
ATOM   7091 C  CB    . ASN A 1 941 ? -71.007 13.883  -20.914 1.00 194.09 ? 1044 ASN A CB    1 
ATOM   7092 C  CG    . ASN A 1 941 ? -71.545 15.281  -20.674 1.00 202.16 ? 1044 ASN A CG    1 
ATOM   7093 O  OD1   . ASN A 1 941 ? -70.888 16.274  -20.988 1.00 204.95 ? 1044 ASN A OD1   1 
ATOM   7094 N  ND2   . ASN A 1 941 ? -72.747 15.365  -20.116 1.00 197.81 ? 1044 ASN A ND2   1 
ATOM   7095 N  N     . ASP A 1 942 ? -71.144 12.007  -18.072 1.00 201.26 ? 1045 ASP A N     1 
ATOM   7096 C  CA    . ASP A 1 942 ? -71.798 11.767  -16.792 1.00 212.85 ? 1045 ASP A CA    1 
ATOM   7097 C  C     . ASP A 1 942 ? -70.802 11.736  -15.640 1.00 219.09 ? 1045 ASP A C     1 
ATOM   7098 O  O     . ASP A 1 942 ? -71.073 12.298  -14.573 1.00 230.14 ? 1045 ASP A O     1 
ATOM   7099 C  CB    . ASP A 1 942 ? -72.586 10.455  -16.836 1.00 207.83 ? 1045 ASP A CB    1 
ATOM   7100 C  CG    . ASP A 1 942 ? -73.728 10.494  -17.831 1.00 208.98 ? 1045 ASP A CG    1 
ATOM   7101 O  OD1   . ASP A 1 942 ? -74.225 11.602  -18.126 1.00 227.90 ? 1045 ASP A OD1   1 
ATOM   7102 O  OD2   . ASP A 1 942 ? -74.129 9.417   -18.319 1.00 208.36 ? 1045 ASP A OD2   1 
ATOM   7103 N  N     . ALA A 1 943 ? -69.652 11.086  -15.835 1.00 199.43 ? 1046 ALA A N     1 
ATOM   7104 C  CA    . ALA A 1 943 ? -68.612 11.103  -14.811 1.00 189.13 ? 1046 ALA A CA    1 
ATOM   7105 C  C     . ALA A 1 943 ? -68.050 12.506  -14.626 1.00 192.15 ? 1046 ALA A C     1 
ATOM   7106 O  O     . ALA A 1 943 ? -67.850 12.958  -13.493 1.00 184.52 ? 1046 ALA A O     1 
ATOM   7107 C  CB    . ALA A 1 943 ? -67.501 10.119  -15.173 1.00 188.48 ? 1046 ALA A CB    1 
ATOM   7108 N  N     . HIS A 1 944 ? -67.791 13.209  -15.726 1.00 198.39 ? 1047 HIS A N     1 
ATOM   7109 C  CA    . HIS A 1 944 ? -67.358 14.604  -15.695 1.00 197.45 ? 1047 HIS A CA    1 
ATOM   7110 C  C     . HIS A 1 944 ? -68.574 15.459  -16.032 1.00 208.45 ? 1047 HIS A C     1 
ATOM   7111 O  O     . HIS A 1 944 ? -68.932 15.611  -17.203 1.00 203.09 ? 1047 HIS A O     1 
ATOM   7112 C  CB    . HIS A 1 944 ? -66.215 14.845  -16.675 1.00 192.38 ? 1047 HIS A CB    1 
ATOM   7113 C  CG    . HIS A 1 944 ? -65.311 13.666  -16.849 1.00 191.50 ? 1047 HIS A CG    1 
ATOM   7114 N  ND1   . HIS A 1 944 ? -65.282 12.916  -18.006 1.00 191.62 ? 1047 HIS A ND1   1 
ATOM   7115 C  CD2   . HIS A 1 944 ? -64.409 13.101  -16.012 1.00 200.55 ? 1047 HIS A CD2   1 
ATOM   7116 C  CE1   . HIS A 1 944 ? -64.398 11.944  -17.875 1.00 203.87 ? 1047 HIS A CE1   1 
ATOM   7117 N  NE2   . HIS A 1 944 ? -63.855 12.033  -16.675 1.00 215.43 ? 1047 HIS A NE2   1 
ATOM   7118 N  N     . HIS A 1 945 ? -69.211 16.011  -14.998 1.00 214.03 ? 1048 HIS A N     1 
ATOM   7119 C  CA    . HIS A 1 945 ? -70.442 16.779  -15.156 1.00 214.44 ? 1048 HIS A CA    1 
ATOM   7120 C  C     . HIS A 1 945 ? -70.259 17.927  -16.140 1.00 222.81 ? 1048 HIS A C     1 
ATOM   7121 O  O     . HIS A 1 945 ? -69.661 18.955  -15.805 1.00 214.70 ? 1048 HIS A O     1 
ATOM   7122 C  CB    . HIS A 1 945 ? -70.913 17.309  -13.801 1.00 196.74 ? 1048 HIS A CB    1 
ATOM   7123 C  CG    . HIS A 1 945 ? -71.128 16.239  -12.777 1.00 193.48 ? 1048 HIS A CG    1 
ATOM   7124 N  ND1   . HIS A 1 945 ? -72.328 15.578  -12.631 1.00 224.22 ? 1048 HIS A ND1   1 
ATOM   7125 C  CD2   . HIS A 1 945 ? -70.294 15.712  -11.850 1.00 188.62 ? 1048 HIS A CD2   1 
ATOM   7126 C  CE1   . HIS A 1 945 ? -72.225 14.691  -11.657 1.00 215.50 ? 1048 HIS A CE1   1 
ATOM   7127 N  NE2   . HIS A 1 945 ? -71.001 14.752  -11.166 1.00 208.17 ? 1048 HIS A NE2   1 
ATOM   7128 N  N     . GLY A 1 946 ? -70.772 17.757  -17.356 1.00 244.89 ? 1049 GLY A N     1 
ATOM   7129 C  CA    . GLY A 1 946 ? -70.599 18.762  -18.387 1.00 238.95 ? 1049 GLY A CA    1 
ATOM   7130 C  C     . GLY A 1 946 ? -69.196 18.839  -18.944 1.00 230.72 ? 1049 GLY A C     1 
ATOM   7131 O  O     . GLY A 1 946 ? -68.744 19.926  -19.314 1.00 246.75 ? 1049 GLY A O     1 
ATOM   7132 N  N     . GLY A 1 947 ? -68.493 17.712  -19.013 1.00 212.94 ? 1050 GLY A N     1 
ATOM   7133 C  CA    . GLY A 1 947 ? -67.124 17.704  -19.490 1.00 217.89 ? 1050 GLY A CA    1 
ATOM   7134 C  C     . GLY A 1 947 ? -66.969 17.173  -20.900 1.00 229.19 ? 1050 GLY A C     1 
ATOM   7135 O  O     . GLY A 1 947 ? -66.157 17.686  -21.676 1.00 216.09 ? 1050 GLY A O     1 
ATOM   7136 N  N     . TRP A 1 948 ? -67.743 16.145  -21.245 1.00 234.22 ? 1051 TRP A N     1 
ATOM   7137 C  CA    . TRP A 1 948 ? -67.652 15.536  -22.566 1.00 216.71 ? 1051 TRP A CA    1 
ATOM   7138 C  C     . TRP A 1 948 ? -68.939 15.732  -23.356 1.00 206.96 ? 1051 TRP A C     1 
ATOM   7139 O  O     . TRP A 1 948 ? -69.597 14.757  -23.735 1.00 198.02 ? 1051 TRP A O     1 
ATOM   7140 C  CB    . TRP A 1 948 ? -67.324 14.046  -22.445 1.00 192.12 ? 1051 TRP A CB    1 
ATOM   7141 C  CG    . TRP A 1 948 ? -65.884 13.775  -22.134 1.00 179.79 ? 1051 TRP A CG    1 
ATOM   7142 C  CD1   . TRP A 1 948 ? -65.205 14.136  -21.008 1.00 177.43 ? 1051 TRP A CD1   1 
ATOM   7143 C  CD2   . TRP A 1 948 ? -64.948 13.070  -22.959 1.00 180.40 ? 1051 TRP A CD2   1 
ATOM   7144 N  NE1   . TRP A 1 948 ? -63.902 13.707  -21.082 1.00 173.74 ? 1051 TRP A NE1   1 
ATOM   7145 C  CE2   . TRP A 1 948 ? -63.719 13.049  -22.270 1.00 176.27 ? 1051 TRP A CE2   1 
ATOM   7146 C  CE3   . TRP A 1 948 ? -65.029 12.458  -24.213 1.00 172.09 ? 1051 TRP A CE3   1 
ATOM   7147 C  CZ2   . TRP A 1 948 ? -62.581 12.440  -22.793 1.00 174.40 ? 1051 TRP A CZ2   1 
ATOM   7148 C  CZ3   . TRP A 1 948 ? -63.898 11.854  -24.731 1.00 180.81 ? 1051 TRP A CZ3   1 
ATOM   7149 C  CH2   . TRP A 1 948 ? -62.690 11.849  -24.022 1.00 186.76 ? 1051 TRP A CH2   1 
ATOM   7150 N  N     . THR A 1 949 ? -69.303 16.986  -23.608 1.00 225.78 ? 1052 THR A N     1 
ATOM   7151 C  CA    . THR A 1 949 ? -70.488 17.280  -24.396 1.00 241.23 ? 1052 THR A CA    1 
ATOM   7152 C  C     . THR A 1 949 ? -70.271 16.866  -25.851 1.00 236.82 ? 1052 THR A C     1 
ATOM   7153 O  O     . THR A 1 949 ? -69.141 16.777  -26.339 1.00 227.82 ? 1052 THR A O     1 
ATOM   7154 C  CB    . THR A 1 949 ? -70.830 18.770  -24.310 1.00 250.62 ? 1052 THR A CB    1 
ATOM   7155 O  OG1   . THR A 1 949 ? -70.595 19.236  -22.976 1.00 249.51 ? 1052 THR A OG1   1 
ATOM   7156 C  CG2   . THR A 1 949 ? -72.293 19.010  -24.661 1.00 218.75 ? 1052 THR A CG2   1 
ATOM   7157 N  N     . THR A 1 950 ? -71.377 16.600  -26.541 1.00 221.93 ? 1053 THR A N     1 
ATOM   7158 C  CA    . THR A 1 950 ? -71.340 16.171  -27.936 1.00 205.28 ? 1053 THR A CA    1 
ATOM   7159 C  C     . THR A 1 950 ? -70.658 17.203  -28.829 1.00 209.41 ? 1053 THR A C     1 
ATOM   7160 O  O     . THR A 1 950 ? -71.243 18.234  -29.163 1.00 231.06 ? 1053 THR A O     1 
ATOM   7161 C  CB    . THR A 1 950 ? -72.756 15.902  -28.478 1.00 191.90 ? 1053 THR A CB    1 
ATOM   7162 O  OG1   . THR A 1 950 ? -73.525 17.111  -28.433 1.00 188.98 ? 1053 THR A OG1   1 
ATOM   7163 C  CG2   . THR A 1 950 ? -73.451 14.834  -27.647 1.00 194.35 ? 1053 THR A CG2   1 
ATOM   7164 N  N     . GLN B 2 13  ? -7.939  8.403   -11.205 1.00 205.44 ? 12   GLN B N     1 
ATOM   7165 C  CA    . GLN B 2 13  ? -6.526  8.763   -11.172 1.00 220.11 ? 12   GLN B CA    1 
ATOM   7166 C  C     . GLN B 2 13  ? -6.341  10.249  -11.467 1.00 223.44 ? 12   GLN B C     1 
ATOM   7167 O  O     . GLN B 2 13  ? -6.158  11.054  -10.554 1.00 219.92 ? 12   GLN B O     1 
ATOM   7168 C  CB    . GLN B 2 13  ? -5.735  7.919   -12.173 1.00 211.75 ? 12   GLN B CB    1 
ATOM   7169 C  CG    . GLN B 2 13  ? -4.226  8.059   -12.053 1.00 206.19 ? 12   GLN B CG    1 
ATOM   7170 C  CD    . GLN B 2 13  ? -3.481  7.196   -13.054 1.00 211.07 ? 12   GLN B CD    1 
ATOM   7171 O  OE1   . GLN B 2 13  ? -3.962  6.953   -14.160 1.00 182.44 ? 12   GLN B OE1   1 
ATOM   7172 N  NE2   . GLN B 2 13  ? -2.303  6.723   -12.665 1.00 218.42 ? 12   GLN B NE2   1 
ATOM   7173 N  N     . GLU B 2 14  ? -6.390  10.604  -12.753 1.00 226.65 ? 13   GLU B N     1 
ATOM   7174 C  CA    . GLU B 2 14  ? -6.266  11.995  -13.204 1.00 204.11 ? 13   GLU B CA    1 
ATOM   7175 C  C     . GLU B 2 14  ? -7.264  12.195  -14.344 1.00 205.24 ? 13   GLU B C     1 
ATOM   7176 O  O     . GLU B 2 14  ? -6.933  11.996  -15.515 1.00 193.80 ? 13   GLU B O     1 
ATOM   7177 C  CB    . GLU B 2 14  ? -4.840  12.316  -13.635 1.00 201.41 ? 13   GLU B CB    1 
ATOM   7178 C  CG    . GLU B 2 14  ? -3.844  12.425  -12.489 1.00 230.69 ? 13   GLU B CG    1 
ATOM   7179 C  CD    . GLU B 2 14  ? -4.024  13.692  -11.672 1.00 230.42 ? 13   GLU B CD    1 
ATOM   7180 O  OE1   . GLU B 2 14  ? -4.677  14.635  -12.167 1.00 223.32 ? 13   GLU B OE1   1 
ATOM   7181 O  OE2   . GLU B 2 14  ? -3.510  13.746  -10.535 1.00 228.68 ? 13   GLU B OE2   1 
ATOM   7182 N  N     . LYS B 2 15  ? -8.483  12.595  -13.989 1.00 204.29 ? 14   LYS B N     1 
ATOM   7183 C  CA    . LYS B 2 15  ? -9.545  12.765  -14.974 1.00 189.35 ? 14   LYS B CA    1 
ATOM   7184 C  C     . LYS B 2 15  ? -9.243  13.955  -15.878 1.00 174.83 ? 14   LYS B C     1 
ATOM   7185 O  O     . LYS B 2 15  ? -9.096  15.086  -15.403 1.00 188.46 ? 14   LYS B O     1 
ATOM   7186 C  CB    . LYS B 2 15  ? -10.887 12.954  -14.272 1.00 191.08 ? 14   LYS B CB    1 
ATOM   7187 C  CG    . LYS B 2 15  ? -12.040 13.279  -15.209 1.00 183.84 ? 14   LYS B CG    1 
ATOM   7188 C  CD    . LYS B 2 15  ? -12.311 12.136  -16.173 1.00 181.52 ? 14   LYS B CD    1 
ATOM   7189 C  CE    . LYS B 2 15  ? -12.748 10.883  -15.433 1.00 207.17 ? 14   LYS B CE    1 
ATOM   7190 N  NZ    . LYS B 2 15  ? -13.989 11.111  -14.643 1.00 219.94 ? 14   LYS B NZ    1 
ATOM   7191 N  N     . TYR B 2 16  ? -9.153  13.699  -17.183 1.00 180.93 ? 15   TYR B N     1 
ATOM   7192 C  CA    . TYR B 2 16  ? -8.944  14.749  -18.181 1.00 160.43 ? 15   TYR B CA    1 
ATOM   7193 C  C     . TYR B 2 16  ? -9.725  14.363  -19.434 1.00 178.19 ? 15   TYR B C     1 
ATOM   7194 O  O     . TYR B 2 16  ? -9.228  13.606  -20.273 1.00 175.91 ? 15   TYR B O     1 
ATOM   7195 C  CB    . TYR B 2 16  ? -7.464  14.943  -18.491 1.00 162.56 ? 15   TYR B CB    1 
ATOM   7196 C  CG    . TYR B 2 16  ? -6.669  15.555  -17.361 1.00 176.80 ? 15   TYR B CG    1 
ATOM   7197 C  CD1   . TYR B 2 16  ? -6.894  16.865  -16.958 1.00 159.50 ? 15   TYR B CD1   1 
ATOM   7198 C  CD2   . TYR B 2 16  ? -5.683  14.829  -16.706 1.00 187.82 ? 15   TYR B CD2   1 
ATOM   7199 C  CE1   . TYR B 2 16  ? -6.166  17.431  -15.928 1.00 155.75 ? 15   TYR B CE1   1 
ATOM   7200 C  CE2   . TYR B 2 16  ? -4.950  15.387  -15.675 1.00 179.92 ? 15   TYR B CE2   1 
ATOM   7201 C  CZ    . TYR B 2 16  ? -5.195  16.688  -15.291 1.00 156.36 ? 15   TYR B CZ    1 
ATOM   7202 O  OH    . TYR B 2 16  ? -4.468  17.247  -14.266 1.00 169.84 ? 15   TYR B OH    1 
ATOM   7203 N  N     . ARG B 2 17  ? -10.944 14.883  -19.555 1.00 192.49 ? 16   ARG B N     1 
ATOM   7204 C  CA    . ARG B 2 17  ? -11.788 14.635  -20.723 1.00 174.21 ? 16   ARG B CA    1 
ATOM   7205 C  C     . ARG B 2 17  ? -11.491 15.711  -21.760 1.00 177.34 ? 16   ARG B C     1 
ATOM   7206 O  O     . ARG B 2 17  ? -12.004 16.830  -21.677 1.00 165.46 ? 16   ARG B O     1 
ATOM   7207 C  CB    . ARG B 2 17  ? -13.263 14.626  -20.336 1.00 171.72 ? 16   ARG B CB    1 
ATOM   7208 C  CG    . ARG B 2 17  ? -13.651 13.513  -19.378 1.00 194.31 ? 16   ARG B CG    1 
ATOM   7209 C  CD    . ARG B 2 17  ? -15.145 13.529  -19.100 1.00 195.95 ? 16   ARG B CD    1 
ATOM   7210 N  NE    . ARG B 2 17  ? -15.549 12.440  -18.219 1.00 223.05 ? 16   ARG B NE    1 
ATOM   7211 C  CZ    . ARG B 2 17  ? -16.799 12.206  -17.843 1.00 218.68 ? 16   ARG B CZ    1 
ATOM   7212 N  NH1   . ARG B 2 17  ? -17.799 12.968  -18.256 1.00 199.39 ? 16   ARG B NH1   1 
ATOM   7213 N  NH2   . ARG B 2 17  ? -17.053 11.182  -17.034 1.00 206.97 ? 16   ARG B NH2   1 
ATOM   7214 N  N     . LEU B 2 18  ? -10.658 15.374  -22.740 1.00 165.01 ? 17   LEU B N     1 
ATOM   7215 C  CA    . LEU B 2 18  ? -10.294 16.306  -23.796 1.00 119.50 ? 17   LEU B CA    1 
ATOM   7216 C  C     . LEU B 2 18  ? -11.298 16.221  -24.937 1.00 132.01 ? 17   LEU B C     1 
ATOM   7217 O  O     . LEU B 2 18  ? -11.777 15.137  -25.281 1.00 153.09 ? 17   LEU B O     1 
ATOM   7218 C  CB    . LEU B 2 18  ? -8.883  16.015  -24.311 1.00 134.55 ? 17   LEU B CB    1 
ATOM   7219 C  CG    . LEU B 2 18  ? -7.775  15.944  -23.258 1.00 129.24 ? 17   LEU B CG    1 
ATOM   7220 C  CD1   . LEU B 2 18  ? -6.408  15.866  -23.921 1.00 127.43 ? 17   LEU B CD1   1 
ATOM   7221 C  CD2   . LEU B 2 18  ? -7.847  17.127  -22.302 1.00 127.58 ? 17   LEU B CD2   1 
ATOM   7222 N  N     . VAL B 2 19  ? -11.618 17.374  -25.518 1.00 119.90 ? 18   VAL B N     1 
ATOM   7223 C  CA    . VAL B 2 19  ? -12.592 17.470  -26.597 1.00 125.34 ? 18   VAL B CA    1 
ATOM   7224 C  C     . VAL B 2 19  ? -11.952 18.208  -27.765 1.00 119.45 ? 18   VAL B C     1 
ATOM   7225 O  O     . VAL B 2 19  ? -11.266 19.218  -27.572 1.00 112.95 ? 18   VAL B O     1 
ATOM   7226 C  CB    . VAL B 2 19  ? -13.881 18.185  -26.137 1.00 118.00 ? 18   VAL B CB    1 
ATOM   7227 C  CG1   . VAL B 2 19  ? -14.899 18.218  -27.257 1.00 129.94 ? 18   VAL B CG1   1 
ATOM   7228 C  CG2   . VAL B 2 19  ? -14.462 17.503  -24.908 1.00 107.73 ? 18   VAL B CG2   1 
ATOM   7229 N  N     . VAL B 2 20  ? -12.172 17.700  -28.974 1.00 104.80 ? 19   VAL B N     1 
ATOM   7230 C  CA    . VAL B 2 20  ? -11.634 18.292  -30.193 1.00 119.05 ? 19   VAL B CA    1 
ATOM   7231 C  C     . VAL B 2 20  ? -12.820 18.800  -31.004 1.00 114.13 ? 19   VAL B C     1 
ATOM   7232 O  O     . VAL B 2 20  ? -13.508 18.023  -31.675 1.00 106.79 ? 19   VAL B O     1 
ATOM   7233 C  CB    . VAL B 2 20  ? -10.790 17.295  -30.995 1.00 125.27 ? 19   VAL B CB    1 
ATOM   7234 C  CG1   . VAL B 2 20  ? -10.198 17.971  -32.223 1.00 105.80 ? 19   VAL B CG1   1 
ATOM   7235 C  CG2   . VAL B 2 20  ? -9.693  16.705  -30.122 1.00 107.45 ? 19   VAL B CG2   1 
ATOM   7236 N  N     . VAL B 2 21  ? -13.062 20.106  -30.945 1.00 127.35 ? 20   VAL B N     1 
ATOM   7237 C  CA    . VAL B 2 21  ? -14.151 20.728  -31.676 1.00 114.51 ? 20   VAL B CA    1 
ATOM   7238 C  C     . VAL B 2 21  ? -13.581 21.470  -32.876 1.00 107.74 ? 20   VAL B C     1 
ATOM   7239 O  O     . VAL B 2 21  ? -12.403 21.838  -32.917 1.00 119.20 ? 20   VAL B O     1 
ATOM   7240 C  CB    . VAL B 2 21  ? -14.978 21.679  -30.781 1.00 103.61 ? 20   VAL B CB    1 
ATOM   7241 C  CG1   . VAL B 2 21  ? -15.535 20.931  -29.585 1.00 101.79 ? 20   VAL B CG1   1 
ATOM   7242 C  CG2   . VAL B 2 21  ? -14.129 22.855  -30.332 1.00 106.38 ? 20   VAL B CG2   1 
ATOM   7243 N  N     . GLY B 2 22  ? -14.427 21.696  -33.867 1.00 106.53 ? 21   GLY B N     1 
ATOM   7244 C  CA    . GLY B 2 22  ? -14.012 22.404  -35.058 1.00 111.25 ? 21   GLY B CA    1 
ATOM   7245 C  C     . GLY B 2 22  ? -14.981 22.164  -36.194 1.00 104.44 ? 21   GLY B C     1 
ATOM   7246 O  O     . GLY B 2 22  ? -15.971 21.443  -36.062 1.00 98.26  ? 21   GLY B O     1 
ATOM   7247 N  N     . GLY B 2 23  ? -14.668 22.790  -37.323 1.00 100.22 ? 22   GLY B N     1 
ATOM   7248 C  CA    . GLY B 2 23  ? -15.486 22.670  -38.507 1.00 99.01  ? 22   GLY B CA    1 
ATOM   7249 C  C     . GLY B 2 23  ? -15.337 21.309  -39.168 1.00 121.69 ? 22   GLY B C     1 
ATOM   7250 O  O     . GLY B 2 23  ? -14.782 20.357  -38.618 1.00 109.18 ? 22   GLY B O     1 
ATOM   7251 N  N     . GLY B 2 24  ? -15.856 21.231  -40.392 1.00 133.53 ? 23   GLY B N     1 
ATOM   7252 C  CA    . GLY B 2 24  ? -15.810 20.001  -41.158 1.00 126.36 ? 23   GLY B CA    1 
ATOM   7253 C  C     . GLY B 2 24  ? -14.544 19.912  -41.987 1.00 135.82 ? 23   GLY B C     1 
ATOM   7254 O  O     . GLY B 2 24  ? -14.174 20.865  -42.677 1.00 138.37 ? 23   GLY B O     1 
ATOM   7255 N  N     . GLY B 2 25  ? -13.880 18.761  -41.911 1.00 148.34 ? 24   GLY B N     1 
ATOM   7256 C  CA    . GLY B 2 25  ? -12.691 18.528  -42.706 1.00 133.35 ? 24   GLY B CA    1 
ATOM   7257 C  C     . GLY B 2 25  ? -11.482 19.341  -42.312 1.00 133.31 ? 24   GLY B C     1 
ATOM   7258 O  O     . GLY B 2 25  ? -10.537 19.444  -43.097 1.00 137.47 ? 24   GLY B O     1 
ATOM   7259 N  N     . VAL B 2 26  ? -11.479 19.924  -41.112 1.00 117.99 ? 25   VAL B N     1 
ATOM   7260 C  CA    . VAL B 2 26  ? -10.330 20.712  -40.679 1.00 129.40 ? 25   VAL B CA    1 
ATOM   7261 C  C     . VAL B 2 26  ? -9.196  19.837  -40.165 1.00 105.40 ? 25   VAL B C     1 
ATOM   7262 O  O     . VAL B 2 26  ? -8.057  20.309  -40.064 1.00 107.32 ? 25   VAL B O     1 
ATOM   7263 C  CB    . VAL B 2 26  ? -10.741 21.727  -39.600 1.00 104.09 ? 25   VAL B CB    1 
ATOM   7264 C  CG1   . VAL B 2 26  ? -11.880 22.590  -40.102 1.00 110.45 ? 25   VAL B CG1   1 
ATOM   7265 C  CG2   . VAL B 2 26  ? -11.136 21.012  -38.320 1.00 107.57 ? 25   VAL B CG2   1 
ATOM   7266 N  N     . GLY B 2 27  ? -9.471  18.583  -39.842 1.00 104.59 ? 26   GLY B N     1 
ATOM   7267 C  CA    . GLY B 2 27  ? -8.467  17.668  -39.359 1.00 105.91 ? 26   GLY B CA    1 
ATOM   7268 C  C     . GLY B 2 27  ? -8.633  17.184  -37.931 1.00 107.52 ? 26   GLY B C     1 
ATOM   7269 O  O     . GLY B 2 27  ? -7.646  16.734  -37.336 1.00 114.34 ? 26   GLY B O     1 
ATOM   7270 N  N     . LYS B 2 28  ? -9.839  17.264  -37.363 1.00 104.03 ? 27   LYS B N     1 
ATOM   7271 C  CA    . LYS B 2 28  ? -10.050 16.768  -36.007 1.00 103.93 ? 27   LYS B CA    1 
ATOM   7272 C  C     . LYS B 2 28  ? -9.803  15.267  -35.927 1.00 144.14 ? 27   LYS B C     1 
ATOM   7273 O  O     . LYS B 2 28  ? -9.235  14.774  -34.946 1.00 120.18 ? 27   LYS B O     1 
ATOM   7274 C  CB    . LYS B 2 28  ? -11.468 17.098  -35.543 1.00 118.95 ? 27   LYS B CB    1 
ATOM   7275 C  CG    . LYS B 2 28  ? -11.833 18.559  -35.665 1.00 102.07 ? 27   LYS B CG    1 
ATOM   7276 C  CD    . LYS B 2 28  ? -13.307 18.787  -35.412 1.00 100.24 ? 27   LYS B CD    1 
ATOM   7277 C  CE    . LYS B 2 28  ? -14.147 18.044  -36.432 1.00 119.19 ? 27   LYS B CE    1 
ATOM   7278 N  NZ    . LYS B 2 28  ? -15.588 18.366  -36.295 1.00 119.76 ? 27   LYS B NZ    1 
ATOM   7279 N  N     . SER B 2 29  ? -10.219 14.526  -36.956 1.00 140.06 ? 28   SER B N     1 
ATOM   7280 C  CA    . SER B 2 29  ? -10.061 13.076  -36.934 1.00 128.71 ? 28   SER B CA    1 
ATOM   7281 C  C     . SER B 2 29  ? -8.610  12.672  -37.164 1.00 138.71 ? 28   SER B C     1 
ATOM   7282 O  O     . SER B 2 29  ? -8.110  11.744  -36.519 1.00 124.69 ? 28   SER B O     1 
ATOM   7283 C  CB    . SER B 2 29  ? -10.972 12.438  -37.982 1.00 125.62 ? 28   SER B CB    1 
ATOM   7284 O  OG    . SER B 2 29  ? -12.328 12.783  -37.756 1.00 101.09 ? 28   SER B OG    1 
ATOM   7285 N  N     . ALA B 2 30  ? -7.917  13.358  -38.076 1.00 123.39 ? 29   ALA B N     1 
ATOM   7286 C  CA    . ALA B 2 30  ? -6.529  13.011  -38.361 1.00 125.59 ? 29   ALA B CA    1 
ATOM   7287 C  C     . ALA B 2 30  ? -5.621  13.349  -37.185 1.00 125.26 ? 29   ALA B C     1 
ATOM   7288 O  O     . ALA B 2 30  ? -4.680  12.605  -36.888 1.00 129.50 ? 29   ALA B O     1 
ATOM   7289 C  CB    . ALA B 2 30  ? -6.058  13.723  -39.628 1.00 109.27 ? 29   ALA B CB    1 
ATOM   7290 N  N     . LEU B 2 31  ? -5.887  14.466  -36.504 1.00 118.32 ? 30   LEU B N     1 
ATOM   7291 C  CA    . LEU B 2 31  ? -5.069  14.842  -35.355 1.00 137.96 ? 30   LEU B CA    1 
ATOM   7292 C  C     . LEU B 2 31  ? -5.347  13.956  -34.148 1.00 123.96 ? 30   LEU B C     1 
ATOM   7293 O  O     . LEU B 2 31  ? -4.436  13.689  -33.356 1.00 119.82 ? 30   LEU B O     1 
ATOM   7294 C  CB    . LEU B 2 31  ? -5.307  16.308  -34.994 1.00 140.29 ? 30   LEU B CB    1 
ATOM   7295 C  CG    . LEU B 2 31  ? -4.766  17.372  -35.949 1.00 120.70 ? 30   LEU B CG    1 
ATOM   7296 C  CD1   . LEU B 2 31  ? -5.232  18.752  -35.517 1.00 128.88 ? 30   LEU B CD1   1 
ATOM   7297 C  CD2   . LEU B 2 31  ? -3.249  17.314  -36.009 1.00 116.34 ? 30   LEU B CD2   1 
ATOM   7298 N  N     . THR B 2 32  ? -6.589  13.495  -33.990 1.00 109.85 ? 31   THR B N     1 
ATOM   7299 C  CA    . THR B 2 32  ? -6.940  12.695  -32.821 1.00 132.40 ? 31   THR B CA    1 
ATOM   7300 C  C     . THR B 2 32  ? -6.264  11.330  -32.862 1.00 122.88 ? 31   THR B C     1 
ATOM   7301 O  O     . THR B 2 32  ? -5.597  10.928  -31.902 1.00 118.78 ? 31   THR B O     1 
ATOM   7302 C  CB    . THR B 2 32  ? -8.458  12.540  -32.726 1.00 145.09 ? 31   THR B CB    1 
ATOM   7303 O  OG1   . THR B 2 32  ? -9.063  13.831  -32.581 1.00 134.43 ? 31   THR B OG1   1 
ATOM   7304 C  CG2   . THR B 2 32  ? -8.829  11.674  -31.533 1.00 108.33 ? 31   THR B CG2   1 
ATOM   7305 N  N     . ILE B 2 33  ? -6.424  10.599  -33.969 1.00 123.95 ? 32   ILE B N     1 
ATOM   7306 C  CA    . ILE B 2 33  ? -5.804  9.284   -34.076 1.00 121.34 ? 32   ILE B CA    1 
ATOM   7307 C  C     . ILE B 2 33  ? -4.290  9.387   -34.196 1.00 124.76 ? 32   ILE B C     1 
ATOM   7308 O  O     . ILE B 2 33  ? -3.584  8.412   -33.915 1.00 158.24 ? 32   ILE B O     1 
ATOM   7309 C  CB    . ILE B 2 33  ? -6.390  8.498   -35.264 1.00 113.29 ? 32   ILE B CB    1 
ATOM   7310 C  CG1   . ILE B 2 33  ? -6.043  9.181   -36.587 1.00 151.67 ? 32   ILE B CG1   1 
ATOM   7311 C  CG2   . ILE B 2 33  ? -7.898  8.355   -35.116 1.00 106.84 ? 32   ILE B CG2   1 
ATOM   7312 C  CD1   . ILE B 2 33  ? -6.581  8.458   -37.798 1.00 119.48 ? 32   ILE B CD1   1 
ATOM   7313 N  N     . GLN B 2 34  ? -3.769  10.546  -34.606 1.00 139.44 ? 33   GLN B N     1 
ATOM   7314 C  CA    . GLN B 2 34  ? -2.322  10.735  -34.629 1.00 133.73 ? 33   GLN B CA    1 
ATOM   7315 C  C     . GLN B 2 34  ? -1.741  10.746  -33.223 1.00 136.21 ? 33   GLN B C     1 
ATOM   7316 O  O     . GLN B 2 34  ? -0.569  10.398  -33.033 1.00 151.83 ? 33   GLN B O     1 
ATOM   7317 C  CB    . GLN B 2 34  ? -1.973  12.036  -35.353 1.00 154.78 ? 33   GLN B CB    1 
ATOM   7318 C  CG    . GLN B 2 34  ? -0.499  12.185  -35.699 1.00 167.31 ? 33   GLN B CG    1 
ATOM   7319 C  CD    . GLN B 2 34  ? -0.090  11.313  -36.867 1.00 164.51 ? 33   GLN B CD    1 
ATOM   7320 O  OE1   . GLN B 2 34  ? -0.917  10.958  -37.705 1.00 172.26 ? 33   GLN B OE1   1 
ATOM   7321 N  NE2   . GLN B 2 34  ? 1.188   10.960  -36.929 1.00 130.63 ? 33   GLN B NE2   1 
ATOM   7322 N  N     . PHE B 2 35  ? -2.539  11.137  -32.228 1.00 143.18 ? 34   PHE B N     1 
ATOM   7323 C  CA    . PHE B 2 35  ? -2.051  11.200  -30.855 1.00 157.50 ? 34   PHE B CA    1 
ATOM   7324 C  C     . PHE B 2 35  ? -1.986  9.822   -30.209 1.00 161.98 ? 34   PHE B C     1 
ATOM   7325 O  O     . PHE B 2 35  ? -1.161  9.600   -29.316 1.00 184.00 ? 34   PHE B O     1 
ATOM   7326 C  CB    . PHE B 2 35  ? -2.939  12.137  -30.029 1.00 132.94 ? 34   PHE B CB    1 
ATOM   7327 C  CG    . PHE B 2 35  ? -2.447  12.356  -28.628 1.00 130.05 ? 34   PHE B CG    1 
ATOM   7328 C  CD1   . PHE B 2 35  ? -1.297  13.089  -28.392 1.00 146.95 ? 34   PHE B CD1   1 
ATOM   7329 C  CD2   . PHE B 2 35  ? -3.137  11.835  -27.547 1.00 134.10 ? 34   PHE B CD2   1 
ATOM   7330 C  CE1   . PHE B 2 35  ? -0.839  13.293  -27.106 1.00 155.58 ? 34   PHE B CE1   1 
ATOM   7331 C  CE2   . PHE B 2 35  ? -2.686  12.037  -26.257 1.00 151.89 ? 34   PHE B CE2   1 
ATOM   7332 C  CZ    . PHE B 2 35  ? -1.535  12.767  -26.037 1.00 161.89 ? 34   PHE B CZ    1 
ATOM   7333 N  N     . ILE B 2 36  ? -2.827  8.888   -30.650 1.00 165.45 ? 35   ILE B N     1 
ATOM   7334 C  CA    . ILE B 2 36  ? -2.853  7.527   -30.120 1.00 177.82 ? 35   ILE B CA    1 
ATOM   7335 C  C     . ILE B 2 36  ? -2.219  6.544   -31.100 1.00 162.42 ? 35   ILE B C     1 
ATOM   7336 O  O     . ILE B 2 36  ? -1.178  5.949   -30.809 1.00 146.39 ? 35   ILE B O     1 
ATOM   7337 C  CB    . ILE B 2 36  ? -4.290  7.095   -29.746 1.00 180.54 ? 35   ILE B CB    1 
ATOM   7338 C  CG1   . ILE B 2 36  ? -4.870  7.980   -28.641 1.00 147.39 ? 35   ILE B CG1   1 
ATOM   7339 C  CG2   . ILE B 2 36  ? -4.324  5.626   -29.324 1.00 202.10 ? 35   ILE B CG2   1 
ATOM   7340 C  CD1   . ILE B 2 36  ? -5.684  9.153   -29.148 1.00 131.98 ? 35   ILE B CD1   1 
ATOM   7341 N  N     . ALA B 2 37  ? -2.835  6.362   -32.274 1.00 171.23 ? 36   ALA B N     1 
ATOM   7342 C  CA    . ALA B 2 37  ? -2.330  5.402   -33.249 1.00 164.98 ? 36   ALA B CA    1 
ATOM   7343 C  C     . ALA B 2 37  ? -1.030  5.857   -33.898 1.00 143.14 ? 36   ALA B C     1 
ATOM   7344 O  O     . ALA B 2 37  ? -0.289  5.016   -34.421 1.00 161.40 ? 36   ALA B O     1 
ATOM   7345 C  CB    . ALA B 2 37  ? -3.373  5.128   -34.334 1.00 137.54 ? 36   ALA B CB    1 
ATOM   7346 N  N     . SER B 2 38  ? -0.745  7.161   -33.882 1.00 161.22 ? 37   SER B N     1 
ATOM   7347 C  CA    . SER B 2 38  ? 0.488   7.718   -34.445 1.00 154.00 ? 37   SER B CA    1 
ATOM   7348 C  C     . SER B 2 38  ? 0.627   7.388   -35.930 1.00 145.04 ? 37   SER B C     1 
ATOM   7349 O  O     . SER B 2 38  ? 1.722   7.111   -36.424 1.00 133.36 ? 37   SER B O     1 
ATOM   7350 C  CB    . SER B 2 38  ? 1.717   7.248   -33.663 1.00 151.19 ? 37   SER B CB    1 
ATOM   7351 O  OG    . SER B 2 38  ? 1.642   7.650   -32.306 1.00 146.62 ? 37   SER B OG    1 
ATOM   7352 N  N     . TYR B 2 39  ? -0.492  7.419   -36.651 1.00 151.29 ? 38   TYR B N     1 
ATOM   7353 C  CA    . TYR B 2 39  ? -0.485  7.203   -38.092 1.00 143.24 ? 38   TYR B CA    1 
ATOM   7354 C  C     . TYR B 2 39  ? -1.472  8.165   -38.737 1.00 142.93 ? 38   TYR B C     1 
ATOM   7355 O  O     . TYR B 2 39  ? -2.592  8.336   -38.245 1.00 146.79 ? 38   TYR B O     1 
ATOM   7356 C  CB    . TYR B 2 39  ? -0.816  5.741   -38.439 1.00 123.23 ? 38   TYR B CB    1 
ATOM   7357 C  CG    . TYR B 2 39  ? -2.209  5.484   -38.979 1.00 126.57 ? 38   TYR B CG    1 
ATOM   7358 C  CD1   . TYR B 2 39  ? -3.263  5.184   -38.125 1.00 116.20 ? 38   TYR B CD1   1 
ATOM   7359 C  CD2   . TYR B 2 39  ? -2.463  5.518   -40.345 1.00 117.53 ? 38   TYR B CD2   1 
ATOM   7360 C  CE1   . TYR B 2 39  ? -4.534  4.941   -38.617 1.00 156.11 ? 38   TYR B CE1   1 
ATOM   7361 C  CE2   . TYR B 2 39  ? -3.729  5.277   -40.845 1.00 129.84 ? 38   TYR B CE2   1 
ATOM   7362 C  CZ    . TYR B 2 39  ? -4.761  4.989   -39.977 1.00 157.30 ? 38   TYR B CZ    1 
ATOM   7363 O  OH    . TYR B 2 39  ? -6.024  4.748   -40.471 1.00 129.55 ? 38   TYR B OH    1 
ATOM   7364 N  N     . PHE B 2 40  ? -1.043  8.806   -39.821 1.00 134.78 ? 39   PHE B N     1 
ATOM   7365 C  CA    . PHE B 2 40  ? -1.873  9.781   -40.513 1.00 158.15 ? 39   PHE B CA    1 
ATOM   7366 C  C     . PHE B 2 40  ? -2.841  9.083   -41.459 1.00 135.86 ? 39   PHE B C     1 
ATOM   7367 O  O     . PHE B 2 40  ? -2.467  8.157   -42.184 1.00 153.10 ? 39   PHE B O     1 
ATOM   7368 C  CB    . PHE B 2 40  ? -1.000  10.771  -41.286 1.00 144.50 ? 39   PHE B CB    1 
ATOM   7369 C  CG    . PHE B 2 40  ? -1.779  11.758  -42.109 1.00 124.21 ? 39   PHE B CG    1 
ATOM   7370 C  CD1   . PHE B 2 40  ? -2.524  12.754  -41.501 1.00 140.94 ? 39   PHE B CD1   1 
ATOM   7371 C  CD2   . PHE B 2 40  ? -1.757  11.698  -43.493 1.00 140.09 ? 39   PHE B CD2   1 
ATOM   7372 C  CE1   . PHE B 2 40  ? -3.238  13.668  -42.256 1.00 132.84 ? 39   PHE B CE1   1 
ATOM   7373 C  CE2   . PHE B 2 40  ? -2.469  12.608  -44.254 1.00 143.78 ? 39   PHE B CE2   1 
ATOM   7374 C  CZ    . PHE B 2 40  ? -3.210  13.594  -43.634 1.00 114.57 ? 39   PHE B CZ    1 
ATOM   7375 N  N     . VAL B 2 41  ? -4.090  9.533   -41.446 1.00 113.11 ? 40   VAL B N     1 
ATOM   7376 C  CA    . VAL B 2 41  ? -5.140  8.942   -42.264 1.00 146.30 ? 40   VAL B CA    1 
ATOM   7377 C  C     . VAL B 2 41  ? -5.465  9.893   -43.407 1.00 118.36 ? 40   VAL B C     1 
ATOM   7378 O  O     . VAL B 2 41  ? -5.252  11.107  -43.315 1.00 170.01 ? 40   VAL B O     1 
ATOM   7379 C  CB    . VAL B 2 41  ? -6.396  8.621   -41.425 1.00 147.30 ? 40   VAL B CB    1 
ATOM   7380 C  CG1   . VAL B 2 41  ? -7.278  9.854   -41.271 1.00 133.45 ? 40   VAL B CG1   1 
ATOM   7381 C  CG2   . VAL B 2 41  ? -7.162  7.459   -42.034 1.00 148.43 ? 40   VAL B CG2   1 
ATOM   7382 N  N     . THR B 2 42  ? -5.975  9.328   -44.500 1.00 115.01 ? 41   THR B N     1 
ATOM   7383 C  CA    . THR B 2 42  ? -6.287  10.098  -45.694 1.00 121.82 ? 41   THR B CA    1 
ATOM   7384 C  C     . THR B 2 42  ? -7.753  10.030  -46.093 1.00 149.04 ? 41   THR B C     1 
ATOM   7385 O  O     . THR B 2 42  ? -8.150  10.716  -47.043 1.00 152.92 ? 41   THR B O     1 
ATOM   7386 C  CB    . THR B 2 42  ? -5.422  9.630   -46.874 1.00 163.62 ? 41   THR B CB    1 
ATOM   7387 O  OG1   . THR B 2 42  ? -5.750  10.393  -48.041 1.00 168.68 ? 41   THR B OG1   1 
ATOM   7388 C  CG2   . THR B 2 42  ? -5.658  8.154   -47.156 1.00 154.81 ? 41   THR B CG2   1 
ATOM   7389 N  N     . ASP B 2 43  ? -8.566  9.231   -45.409 1.00 171.16 ? 42   ASP B N     1 
ATOM   7390 C  CA    . ASP B 2 43  ? -9.975  9.153   -45.757 1.00 151.11 ? 42   ASP B CA    1 
ATOM   7391 C  C     . ASP B 2 43  ? -10.740 10.327  -45.153 1.00 147.16 ? 42   ASP B C     1 
ATOM   7392 O  O     . ASP B 2 43  ? -10.284 10.991  -44.218 1.00 150.77 ? 42   ASP B O     1 
ATOM   7393 C  CB    . ASP B 2 43  ? -10.581 7.824   -45.294 1.00 145.58 ? 42   ASP B CB    1 
ATOM   7394 C  CG    . ASP B 2 43  ? -10.563 7.657   -43.783 1.00 163.10 ? 42   ASP B CG    1 
ATOM   7395 O  OD1   . ASP B 2 43  ? -9.930  8.475   -43.085 1.00 156.51 ? 42   ASP B OD1   1 
ATOM   7396 O  OD2   . ASP B 2 43  ? -11.191 6.697   -43.290 1.00 193.30 ? 42   ASP B OD2   1 
ATOM   7397 N  N     . TYR B 2 44  ? -11.920 10.581  -45.709 1.00 161.43 ? 43   TYR B N     1 
ATOM   7398 C  CA    . TYR B 2 44  ? -12.806 11.641  -45.240 1.00 136.55 ? 43   TYR B CA    1 
ATOM   7399 C  C     . TYR B 2 44  ? -14.045 10.968  -44.659 1.00 143.39 ? 43   TYR B C     1 
ATOM   7400 O  O     . TYR B 2 44  ? -15.104 10.917  -45.285 1.00 129.42 ? 43   TYR B O     1 
ATOM   7401 C  CB    . TYR B 2 44  ? -13.152 12.594  -46.371 1.00 142.78 ? 43   TYR B CB    1 
ATOM   7402 C  CG    . TYR B 2 44  ? -13.640 13.965  -45.947 1.00 163.07 ? 43   TYR B CG    1 
ATOM   7403 C  CD1   . TYR B 2 44  ? -14.325 14.151  -44.753 1.00 144.21 ? 43   TYR B CD1   1 
ATOM   7404 C  CD2   . TYR B 2 44  ? -13.414 15.076  -46.750 1.00 140.86 ? 43   TYR B CD2   1 
ATOM   7405 C  CE1   . TYR B 2 44  ? -14.770 15.402  -44.373 1.00 140.27 ? 43   TYR B CE1   1 
ATOM   7406 C  CE2   . TYR B 2 44  ? -13.855 16.330  -46.378 1.00 109.52 ? 43   TYR B CE2   1 
ATOM   7407 C  CZ    . TYR B 2 44  ? -14.532 16.488  -45.189 1.00 140.50 ? 43   TYR B CZ    1 
ATOM   7408 O  OH    . TYR B 2 44  ? -14.975 17.735  -44.814 1.00 155.51 ? 43   TYR B OH    1 
ATOM   7409 N  N     . ASP B 2 45  ? -13.894 10.433  -43.449 1.00 149.87 ? 44   ASP B N     1 
ATOM   7410 C  CA    . ASP B 2 45  ? -15.009 9.838   -42.728 1.00 143.34 ? 44   ASP B CA    1 
ATOM   7411 C  C     . ASP B 2 45  ? -15.664 10.920  -41.881 1.00 142.97 ? 44   ASP B C     1 
ATOM   7412 O  O     . ASP B 2 45  ? -15.075 11.340  -40.872 1.00 125.39 ? 44   ASP B O     1 
ATOM   7413 C  CB    . ASP B 2 45  ? -14.529 8.688   -41.851 1.00 125.77 ? 44   ASP B CB    1 
ATOM   7414 C  CG    . ASP B 2 45  ? -15.671 7.917   -41.215 1.00 155.87 ? 44   ASP B CG    1 
ATOM   7415 O  OD1   . ASP B 2 45  ? -16.841 8.173   -41.569 1.00 156.29 ? 44   ASP B OD1   1 
ATOM   7416 O  OD2   . ASP B 2 45  ? -15.395 7.050   -40.358 1.00 143.13 ? 44   ASP B OD2   1 
ATOM   7417 N  N     . PRO B 2 46  ? -16.852 11.416  -42.249 1.00 102.88 ? 45   PRO B N     1 
ATOM   7418 C  CA    . PRO B 2 46  ? -17.509 12.441  -41.427 1.00 101.82 ? 45   PRO B CA    1 
ATOM   7419 C  C     . PRO B 2 46  ? -17.803 11.941  -40.022 1.00 119.76 ? 45   PRO B C     1 
ATOM   7420 O  O     . PRO B 2 46  ? -18.718 11.138  -39.814 1.00 127.51 ? 45   PRO B O     1 
ATOM   7421 C  CB    . PRO B 2 46  ? -18.799 12.742  -42.204 1.00 145.17 ? 45   PRO B CB    1 
ATOM   7422 C  CG    . PRO B 2 46  ? -18.513 12.300  -43.606 1.00 135.12 ? 45   PRO B CG    1 
ATOM   7423 C  CD    . PRO B 2 46  ? -17.623 11.105  -43.463 1.00 141.72 ? 45   PRO B CD    1 
ATOM   7424 N  N     . THR B 2 47  ? -17.019 12.410  -39.055 1.00 134.46 ? 46   THR B N     1 
ATOM   7425 C  CA    . THR B 2 47  ? -17.156 11.951  -37.680 1.00 108.73 ? 46   THR B CA    1 
ATOM   7426 C  C     . THR B 2 47  ? -18.468 12.440  -37.077 1.00 91.30  ? 46   THR B C     1 
ATOM   7427 O  O     . THR B 2 47  ? -18.949 13.531  -37.391 1.00 110.05 ? 46   THR B O     1 
ATOM   7428 C  CB    . THR B 2 47  ? -15.974 12.441  -36.839 1.00 94.26  ? 46   THR B CB    1 
ATOM   7429 O  OG1   . THR B 2 47  ? -14.749 12.158  -37.528 1.00 118.74 ? 46   THR B OG1   1 
ATOM   7430 C  CG2   . THR B 2 47  ? -15.949 11.752  -35.477 1.00 94.38  ? 46   THR B CG2   1 
ATOM   7431 N  N     . ILE B 2 48  ? -19.058 11.613  -36.216 1.00 112.37 ? 47   ILE B N     1 
ATOM   7432 C  CA    . ILE B 2 48  ? -20.233 12.011  -35.450 1.00 112.31 ? 47   ILE B CA    1 
ATOM   7433 C  C     . ILE B 2 48  ? -19.803 12.228  -34.005 1.00 105.59 ? 47   ILE B C     1 
ATOM   7434 O  O     . ILE B 2 48  ? -19.870 13.349  -33.485 1.00 122.67 ? 47   ILE B O     1 
ATOM   7435 C  CB    . ILE B 2 48  ? -21.359 10.966  -35.558 1.00 96.19  ? 47   ILE B CB    1 
ATOM   7436 C  CG1   . ILE B 2 48  ? -21.821 10.827  -37.014 1.00 87.45  ? 47   ILE B CG1   1 
ATOM   7437 C  CG2   . ILE B 2 48  ? -22.529 11.349  -34.664 1.00 91.26  ? 47   ILE B CG2   1 
ATOM   7438 C  CD1   . ILE B 2 48  ? -22.917 9.808   -37.211 1.00 90.29  ? 47   ILE B CD1   1 
ATOM   7439 N  N     . GLU B 2 49  ? -19.351 11.159  -33.350 1.00 95.49  ? 48   GLU B N     1 
ATOM   7440 C  CA    . GLU B 2 49  ? -18.744 11.275  -32.024 1.00 114.08 ? 48   GLU B CA    1 
ATOM   7441 C  C     . GLU B 2 49  ? -17.998 9.980   -31.727 1.00 114.46 ? 48   GLU B C     1 
ATOM   7442 O  O     . GLU B 2 49  ? -18.628 8.938   -31.514 1.00 117.49 ? 48   GLU B O     1 
ATOM   7443 C  CB    . GLU B 2 49  ? -19.794 11.561  -30.957 1.00 132.55 ? 48   GLU B CB    1 
ATOM   7444 C  CG    . GLU B 2 49  ? -19.197 11.978  -29.619 1.00 138.22 ? 48   GLU B CG    1 
ATOM   7445 C  CD    . GLU B 2 49  ? -20.246 12.275  -28.563 1.00 164.73 ? 48   GLU B CD    1 
ATOM   7446 O  OE1   . GLU B 2 49  ? -21.377 11.759  -28.683 1.00 198.87 ? 48   GLU B OE1   1 
ATOM   7447 O  OE2   . GLU B 2 49  ? -19.938 13.026  -27.613 1.00 129.55 ? 48   GLU B OE2   1 
ATOM   7448 N  N     . ASP B 2 50  ? -16.669 10.049  -31.708 1.00 122.46 ? 49   ASP B N     1 
ATOM   7449 C  CA    . ASP B 2 50  ? -15.817 8.914   -31.386 1.00 103.81 ? 49   ASP B CA    1 
ATOM   7450 C  C     . ASP B 2 50  ? -14.982 9.243   -30.157 1.00 111.17 ? 49   ASP B C     1 
ATOM   7451 O  O     . ASP B 2 50  ? -14.531 10.381  -29.989 1.00 124.68 ? 49   ASP B O     1 
ATOM   7452 C  CB    . ASP B 2 50  ? -14.904 8.555   -32.564 1.00 105.44 ? 49   ASP B CB    1 
ATOM   7453 C  CG    . ASP B 2 50  ? -15.676 8.308   -33.845 1.00 125.23 ? 49   ASP B CG    1 
ATOM   7454 O  OD1   . ASP B 2 50  ? -16.847 7.883   -33.762 1.00 130.35 ? 49   ASP B OD1   1 
ATOM   7455 O  OD2   . ASP B 2 50  ? -15.112 8.540   -34.936 1.00 128.85 ? 49   ASP B OD2   1 
ATOM   7456 N  N     . SER B 2 51  ? -14.779 8.246   -29.300 1.00 125.25 ? 50   SER B N     1 
ATOM   7457 C  CA    . SER B 2 51  ? -14.027 8.411   -28.065 1.00 122.89 ? 50   SER B CA    1 
ATOM   7458 C  C     . SER B 2 51  ? -12.722 7.632   -28.136 1.00 139.00 ? 50   SER B C     1 
ATOM   7459 O  O     . SER B 2 51  ? -12.685 6.504   -28.639 1.00 137.16 ? 50   SER B O     1 
ATOM   7460 C  CB    . SER B 2 51  ? -14.844 7.947   -26.855 1.00 121.77 ? 50   SER B CB    1 
ATOM   7461 O  OG    . SER B 2 51  ? -14.096 8.064   -25.656 1.00 132.30 ? 50   SER B OG    1 
ATOM   7462 N  N     . TYR B 2 52  ? -11.653 8.241   -27.630 1.00 145.66 ? 51   TYR B N     1 
ATOM   7463 C  CA    . TYR B 2 52  ? -10.344 7.612   -27.562 1.00 127.60 ? 51   TYR B CA    1 
ATOM   7464 C  C     . TYR B 2 52  ? -9.736  7.864   -26.190 1.00 139.10 ? 51   TYR B C     1 
ATOM   7465 O  O     . TYR B 2 52  ? -9.956  8.913   -25.578 1.00 128.73 ? 51   TYR B O     1 
ATOM   7466 C  CB    . TYR B 2 52  ? -9.402  8.138   -28.655 1.00 124.18 ? 51   TYR B CB    1 
ATOM   7467 C  CG    . TYR B 2 52  ? -9.845  7.812   -30.064 1.00 129.00 ? 51   TYR B CG    1 
ATOM   7468 C  CD1   . TYR B 2 52  ? -9.466  6.623   -30.674 1.00 131.87 ? 51   TYR B CD1   1 
ATOM   7469 C  CD2   . TYR B 2 52  ? -10.637 8.695   -30.787 1.00 141.60 ? 51   TYR B CD2   1 
ATOM   7470 C  CE1   . TYR B 2 52  ? -9.866  6.321   -31.963 1.00 138.58 ? 51   TYR B CE1   1 
ATOM   7471 C  CE2   . TYR B 2 52  ? -11.041 8.402   -32.076 1.00 120.01 ? 51   TYR B CE2   1 
ATOM   7472 C  CZ    . TYR B 2 52  ? -10.653 7.214   -32.659 1.00 121.68 ? 51   TYR B CZ    1 
ATOM   7473 O  OH    . TYR B 2 52  ? -11.053 6.918   -33.941 1.00 148.92 ? 51   TYR B OH    1 
ATOM   7474 N  N     . THR B 2 53  ? -8.970  6.887   -25.711 1.00 148.91 ? 52   THR B N     1 
ATOM   7475 C  CA    . THR B 2 53  ? -8.320  6.966   -24.411 1.00 163.44 ? 52   THR B CA    1 
ATOM   7476 C  C     . THR B 2 53  ? -6.847  6.615   -24.555 1.00 169.63 ? 52   THR B C     1 
ATOM   7477 O  O     . THR B 2 53  ? -6.492  5.661   -25.254 1.00 149.26 ? 52   THR B O     1 
ATOM   7478 C  CB    . THR B 2 53  ? -8.980  6.026   -23.394 1.00 146.01 ? 52   THR B CB    1 
ATOM   7479 O  OG1   . THR B 2 53  ? -9.078  4.709   -23.951 1.00 145.46 ? 52   THR B OG1   1 
ATOM   7480 C  CG2   . THR B 2 53  ? -10.370 6.524   -23.026 1.00 150.18 ? 52   THR B CG2   1 
ATOM   7481 N  N     . LYS B 2 54  ? -5.993  7.390   -23.889 1.00 152.66 ? 53   LYS B N     1 
ATOM   7482 C  CA    . LYS B 2 54  ? -4.558  7.145   -23.918 1.00 176.60 ? 53   LYS B CA    1 
ATOM   7483 C  C     . LYS B 2 54  ? -3.941  7.623   -22.613 1.00 183.57 ? 53   LYS B C     1 
ATOM   7484 O  O     . LYS B 2 54  ? -4.122  8.781   -22.226 1.00 137.33 ? 53   LYS B O     1 
ATOM   7485 C  CB    . LYS B 2 54  ? -3.895  7.850   -25.107 1.00 173.70 ? 53   LYS B CB    1 
ATOM   7486 C  CG    . LYS B 2 54  ? -2.401  7.594   -25.212 1.00 182.46 ? 53   LYS B CG    1 
ATOM   7487 C  CD    . LYS B 2 54  ? -1.814  8.204   -26.472 1.00 147.82 ? 53   LYS B CD    1 
ATOM   7488 C  CE    . LYS B 2 54  ? -0.338  7.865   -26.608 1.00 180.13 ? 53   LYS B CE    1 
ATOM   7489 N  NZ    . LYS B 2 54  ? 0.252   8.408   -27.863 1.00 185.62 ? 53   LYS B NZ    1 
ATOM   7490 N  N     . GLN B 2 55  ? -3.217  6.728   -21.944 1.00 186.41 ? 54   GLN B N     1 
ATOM   7491 C  CA    . GLN B 2 55  ? -2.510  7.071   -20.717 1.00 173.79 ? 54   GLN B CA    1 
ATOM   7492 C  C     . GLN B 2 55  ? -1.187  7.739   -21.070 1.00 156.54 ? 54   GLN B C     1 
ATOM   7493 O  O     . GLN B 2 55  ? -0.371  7.165   -21.799 1.00 137.41 ? 54   GLN B O     1 
ATOM   7494 C  CB    . GLN B 2 55  ? -2.278  5.822   -19.869 1.00 170.28 ? 54   GLN B CB    1 
ATOM   7495 C  CG    . GLN B 2 55  ? -1.451  6.062   -18.616 1.00 196.33 ? 54   GLN B CG    1 
ATOM   7496 C  CD    . GLN B 2 55  ? -2.175  6.909   -17.588 1.00 193.62 ? 54   GLN B CD    1 
ATOM   7497 O  OE1   . GLN B 2 55  ? -1.563  7.719   -16.891 1.00 206.69 ? 54   GLN B OE1   1 
ATOM   7498 N  NE2   . GLN B 2 55  ? -3.485  6.719   -17.482 1.00 191.54 ? 54   GLN B NE2   1 
ATOM   7499 N  N     . CYS B 2 56  ? -0.975  8.947   -20.556 1.00 168.71 ? 55   CYS B N     1 
ATOM   7500 C  CA    . CYS B 2 56  ? 0.229   9.716   -20.832 1.00 181.21 ? 55   CYS B CA    1 
ATOM   7501 C  C     . CYS B 2 56  ? 0.914   10.100  -19.529 1.00 168.73 ? 55   CYS B C     1 
ATOM   7502 O  O     . CYS B 2 56  ? 0.261   10.325  -18.505 1.00 158.21 ? 55   CYS B O     1 
ATOM   7503 C  CB    . CYS B 2 56  ? -0.089  10.977  -21.645 1.00 164.73 ? 55   CYS B CB    1 
ATOM   7504 S  SG    . CYS B 2 56  ? -0.779  10.650  -23.282 1.00 215.25 ? 55   CYS B SG    1 
ATOM   7505 N  N     . VAL B 2 57  ? 2.243   10.172  -19.579 1.00 189.62 ? 56   VAL B N     1 
ATOM   7506 C  CA    . VAL B 2 57  ? 3.044   10.541  -18.417 1.00 202.70 ? 56   VAL B CA    1 
ATOM   7507 C  C     . VAL B 2 57  ? 3.968   11.693  -18.788 1.00 201.76 ? 56   VAL B C     1 
ATOM   7508 O  O     . VAL B 2 57  ? 4.920   11.998  -18.061 1.00 225.59 ? 56   VAL B O     1 
ATOM   7509 C  CB    . VAL B 2 57  ? 3.847   9.340   -17.884 1.00 211.57 ? 56   VAL B CB    1 
ATOM   7510 C  CG1   . VAL B 2 57  ? 2.908   8.254   -17.376 1.00 219.66 ? 56   VAL B CG1   1 
ATOM   7511 C  CG2   . VAL B 2 57  ? 4.768   8.795   -18.965 1.00 184.70 ? 56   VAL B CG2   1 
ATOM   7512 N  N     . ILE B 2 58  ? 3.695   12.338  -19.925 1.00 189.84 ? 57   ILE B N     1 
ATOM   7513 C  CA    . ILE B 2 58  ? 4.490   13.495  -20.327 1.00 216.06 ? 57   ILE B CA    1 
ATOM   7514 C  C     . ILE B 2 58  ? 4.286   14.647  -19.353 1.00 227.71 ? 57   ILE B C     1 
ATOM   7515 O  O     . ILE B 2 58  ? 5.221   15.408  -19.072 1.00 213.56 ? 57   ILE B O     1 
ATOM   7516 C  CB    . ILE B 2 58  ? 4.145   13.901  -21.772 1.00 209.29 ? 57   ILE B CB    1 
ATOM   7517 C  CG1   . ILE B 2 58  ? 4.344   12.714  -22.717 1.00 191.94 ? 57   ILE B CG1   1 
ATOM   7518 C  CG2   . ILE B 2 58  ? 4.993   15.083  -22.218 1.00 208.80 ? 57   ILE B CG2   1 
ATOM   7519 C  CD1   . ILE B 2 58  ? 5.763   12.189  -22.748 1.00 195.38 ? 57   ILE B CD1   1 
ATOM   7520 N  N     . ASP B 2 59  ? 3.077   14.791  -18.816 1.00 217.05 ? 58   ASP B N     1 
ATOM   7521 C  CA    . ASP B 2 59  ? 2.818   15.766  -17.769 1.00 226.18 ? 58   ASP B CA    1 
ATOM   7522 C  C     . ASP B 2 59  ? 3.590   15.388  -16.504 1.00 244.00 ? 58   ASP B C     1 
ATOM   7523 O  O     . ASP B 2 59  ? 4.158   14.297  -16.391 1.00 247.74 ? 58   ASP B O     1 
ATOM   7524 C  CB    . ASP B 2 59  ? 1.315   15.851  -17.492 1.00 206.02 ? 58   ASP B CB    1 
ATOM   7525 C  CG    . ASP B 2 59  ? 0.923   17.119  -16.759 1.00 207.77 ? 58   ASP B CG    1 
ATOM   7526 O  OD1   . ASP B 2 59  ? 1.274   18.218  -17.237 1.00 211.02 ? 58   ASP B OD1   1 
ATOM   7527 O  OD2   . ASP B 2 59  ? 0.250   17.016  -15.712 1.00 209.41 ? 58   ASP B OD2   1 
ATOM   7528 N  N     . ASP B 2 60  ? 3.611   16.308  -15.537 1.00 274.19 ? 59   ASP B N     1 
ATOM   7529 C  CA    . ASP B 2 60  ? 4.358   16.073  -14.307 1.00 264.38 ? 59   ASP B CA    1 
ATOM   7530 C  C     . ASP B 2 60  ? 3.805   14.913  -13.487 1.00 265.02 ? 59   ASP B C     1 
ATOM   7531 O  O     . ASP B 2 60  ? 4.478   14.464  -12.554 1.00 271.03 ? 59   ASP B O     1 
ATOM   7532 C  CB    . ASP B 2 60  ? 4.388   17.344  -13.453 1.00 271.40 ? 59   ASP B CB    1 
ATOM   7533 C  CG    . ASP B 2 60  ? 3.021   17.723  -12.919 1.00 289.66 ? 59   ASP B CG    1 
ATOM   7534 O  OD1   . ASP B 2 60  ? 2.014   17.439  -13.597 1.00 279.04 ? 59   ASP B OD1   1 
ATOM   7535 O  OD2   . ASP B 2 60  ? 2.956   18.307  -11.817 1.00 309.10 ? 59   ASP B OD2   1 
ATOM   7536 N  N     . ARG B 2 61  ? 2.611   14.426  -13.805 1.00 239.96 ? 60   ARG B N     1 
ATOM   7537 C  CA    . ARG B 2 61  ? 2.023   13.278  -13.121 1.00 230.64 ? 60   ARG B CA    1 
ATOM   7538 C  C     . ARG B 2 61  ? 1.365   12.395  -14.176 1.00 193.03 ? 60   ARG B C     1 
ATOM   7539 O  O     . ARG B 2 61  ? 1.651   12.499  -15.374 1.00 187.12 ? 60   ARG B O     1 
ATOM   7540 C  CB    . ARG B 2 61  ? 1.042   13.739  -12.031 1.00 236.17 ? 60   ARG B CB    1 
ATOM   7541 C  CG    . ARG B 2 61  ? 1.694   14.495  -10.886 1.00 248.05 ? 60   ARG B CG    1 
ATOM   7542 C  CD    . ARG B 2 61  ? 0.664   15.026  -9.907  1.00 248.16 ? 60   ARG B CD    1 
ATOM   7543 N  NE    . ARG B 2 61  ? 1.288   15.802  -8.841  1.00 258.83 ? 60   ARG B NE    1 
ATOM   7544 C  CZ    . ARG B 2 61  ? 0.624   16.407  -7.867  1.00 257.18 ? 60   ARG B CZ    1 
ATOM   7545 N  NH1   . ARG B 2 61  ? -0.695  16.348  -7.788  1.00 245.25 ? 60   ARG B NH1   1 
ATOM   7546 N  NH2   . ARG B 2 61  ? 1.301   17.090  -6.947  1.00 257.89 ? 60   ARG B NH2   1 
ATOM   7547 N  N     . ALA B 2 62  ? 0.475   11.510  -13.736 1.00 172.45 ? 61   ALA B N     1 
ATOM   7548 C  CA    . ALA B 2 62  ? -0.275  10.673  -14.657 1.00 181.11 ? 61   ALA B CA    1 
ATOM   7549 C  C     . ALA B 2 62  ? -1.404  11.475  -15.301 1.00 196.94 ? 61   ALA B C     1 
ATOM   7550 O  O     . ALA B 2 62  ? -1.673  12.624  -14.939 1.00 191.16 ? 61   ALA B O     1 
ATOM   7551 C  CB    . ALA B 2 62  ? -0.831  9.445   -13.937 1.00 162.74 ? 61   ALA B CB    1 
ATOM   7552 N  N     . ALA B 2 63  ? -2.073  10.855  -16.270 1.00 165.42 ? 62   ALA B N     1 
ATOM   7553 C  CA    . ALA B 2 63  ? -3.148  11.531  -16.992 1.00 170.17 ? 62   ALA B CA    1 
ATOM   7554 C  C     . ALA B 2 63  ? -4.050  10.492  -17.635 1.00 182.49 ? 62   ALA B C     1 
ATOM   7555 O  O     . ALA B 2 63  ? -3.575  9.655   -18.410 1.00 179.00 ? 62   ALA B O     1 
ATOM   7556 C  CB    . ALA B 2 63  ? -2.581  12.481  -18.047 1.00 158.16 ? 62   ALA B CB    1 
ATOM   7557 N  N     . ARG B 2 64  ? -5.342  10.545  -17.318 1.00 182.21 ? 63   ARG B N     1 
ATOM   7558 C  CA    . ARG B 2 64  ? -6.357  9.717   -17.968 1.00 178.96 ? 63   ARG B CA    1 
ATOM   7559 C  C     . ARG B 2 64  ? -7.027  10.584  -19.029 1.00 183.91 ? 63   ARG B C     1 
ATOM   7560 O  O     . ARG B 2 64  ? -8.063  11.205  -18.789 1.00 195.85 ? 63   ARG B O     1 
ATOM   7561 C  CB    . ARG B 2 64  ? -7.363  9.182   -16.955 1.00 188.35 ? 63   ARG B CB    1 
ATOM   7562 C  CG    . ARG B 2 64  ? -6.839  8.057   -16.079 1.00 216.14 ? 63   ARG B CG    1 
ATOM   7563 C  CD    . ARG B 2 64  ? -6.770  6.749   -16.849 1.00 203.92 ? 63   ARG B CD    1 
ATOM   7564 N  NE    . ARG B 2 64  ? -8.063  6.388   -17.418 1.00 199.74 ? 63   ARG B NE    1 
ATOM   7565 C  CZ    . ARG B 2 64  ? -9.005  5.716   -16.771 1.00 199.56 ? 63   ARG B CZ    1 
ATOM   7566 N  NH1   . ARG B 2 64  ? -8.833  5.312   -15.523 1.00 194.22 ? 63   ARG B NH1   1 
ATOM   7567 N  NH2   . ARG B 2 64  ? -10.150 5.444   -17.391 1.00 213.67 ? 63   ARG B NH2   1 
ATOM   7568 N  N     . LEU B 2 65  ? -6.422  10.627  -20.213 1.00 175.30 ? 64   LEU B N     1 
ATOM   7569 C  CA    . LEU B 2 65  ? -6.906  11.480  -21.294 1.00 183.67 ? 64   LEU B CA    1 
ATOM   7570 C  C     . LEU B 2 65  ? -8.080  10.800  -21.988 1.00 172.57 ? 64   LEU B C     1 
ATOM   7571 O  O     . LEU B 2 65  ? -7.915  9.755   -22.626 1.00 164.39 ? 64   LEU B O     1 
ATOM   7572 C  CB    . LEU B 2 65  ? -5.783  11.781  -22.281 1.00 182.12 ? 64   LEU B CB    1 
ATOM   7573 C  CG    . LEU B 2 65  ? -4.549  12.490  -21.717 1.00 152.91 ? 64   LEU B CG    1 
ATOM   7574 C  CD1   . LEU B 2 65  ? -3.603  12.888  -22.838 1.00 127.69 ? 64   LEU B CD1   1 
ATOM   7575 C  CD2   . LEU B 2 65  ? -4.950  13.704  -20.894 1.00 152.39 ? 64   LEU B CD2   1 
ATOM   7576 N  N     . ASP B 2 66  ? -9.266  11.392  -21.865 1.00 164.94 ? 65   ASP B N     1 
ATOM   7577 C  CA    . ASP B 2 66  ? -10.469 10.915  -22.544 1.00 174.19 ? 65   ASP B CA    1 
ATOM   7578 C  C     . ASP B 2 66  ? -10.748 11.866  -23.702 1.00 167.44 ? 65   ASP B C     1 
ATOM   7579 O  O     . ASP B 2 66  ? -11.363 12.920  -23.521 1.00 172.91 ? 65   ASP B O     1 
ATOM   7580 C  CB    . ASP B 2 66  ? -11.648 10.841  -21.579 1.00 200.34 ? 65   ASP B CB    1 
ATOM   7581 C  CG    . ASP B 2 66  ? -11.395 9.897   -20.420 1.00 188.13 ? 65   ASP B CG    1 
ATOM   7582 O  OD1   . ASP B 2 66  ? -10.730 8.861   -20.630 1.00 201.78 ? 65   ASP B OD1   1 
ATOM   7583 O  OD2   . ASP B 2 66  ? -11.860 10.192  -19.299 1.00 176.75 ? 65   ASP B OD2   1 
ATOM   7584 N  N     . ILE B 2 67  ? -10.293 11.493  -24.892 1.00 142.75 ? 66   ILE B N     1 
ATOM   7585 C  CA    . ILE B 2 67  ? -10.397 12.343  -26.073 1.00 152.38 ? 66   ILE B CA    1 
ATOM   7586 C  C     . ILE B 2 67  ? -11.709 12.054  -26.788 1.00 150.50 ? 66   ILE B C     1 
ATOM   7587 O  O     . ILE B 2 67  ? -12.103 10.893  -26.952 1.00 132.37 ? 66   ILE B O     1 
ATOM   7588 C  CB    . ILE B 2 67  ? -9.191  12.128  -27.005 1.00 142.57 ? 66   ILE B CB    1 
ATOM   7589 C  CG1   . ILE B 2 67  ? -7.886  12.276  -26.223 1.00 123.69 ? 66   ILE B CG1   1 
ATOM   7590 C  CG2   . ILE B 2 67  ? -9.227  13.113  -28.163 1.00 147.21 ? 66   ILE B CG2   1 
ATOM   7591 C  CD1   . ILE B 2 67  ? -6.648  12.071  -27.061 1.00 126.67 ? 66   ILE B CD1   1 
ATOM   7592 N  N     . LEU B 2 68  ? -12.390 13.116  -27.217 1.00 125.92 ? 67   LEU B N     1 
ATOM   7593 C  CA    . LEU B 2 68  ? -13.657 13.015  -27.935 1.00 140.74 ? 67   LEU B CA    1 
ATOM   7594 C  C     . LEU B 2 68  ? -13.521 13.744  -29.266 1.00 109.78 ? 67   LEU B C     1 
ATOM   7595 O  O     . LEU B 2 68  ? -13.439 14.977  -29.298 1.00 124.36 ? 67   LEU B O     1 
ATOM   7596 C  CB    . LEU B 2 68  ? -14.810 13.596  -27.115 1.00 117.58 ? 67   LEU B CB    1 
ATOM   7597 C  CG    . LEU B 2 68  ? -15.325 12.810  -25.905 1.00 126.77 ? 67   LEU B CG    1 
ATOM   7598 C  CD1   . LEU B 2 68  ? -14.421 12.985  -24.692 1.00 132.35 ? 67   LEU B CD1   1 
ATOM   7599 C  CD2   . LEU B 2 68  ? -16.753 13.220  -25.577 1.00 105.49 ? 67   LEU B CD2   1 
ATOM   7600 N  N     . ASP B 2 69  ? -13.497 12.985  -30.358 1.00 100.13 ? 68   ASP B N     1 
ATOM   7601 C  CA    . ASP B 2 69  ? -13.476 13.556  -31.703 1.00 103.29 ? 68   ASP B CA    1 
ATOM   7602 C  C     . ASP B 2 69  ? -14.909 13.905  -32.086 1.00 132.95 ? 68   ASP B C     1 
ATOM   7603 O  O     . ASP B 2 69  ? -15.709 13.026  -32.417 1.00 110.67 ? 68   ASP B O     1 
ATOM   7604 C  CB    . ASP B 2 69  ? -12.853 12.577  -32.692 1.00 101.49 ? 68   ASP B CB    1 
ATOM   7605 C  CG    . ASP B 2 69  ? -12.747 13.148  -34.095 1.00 128.01 ? 68   ASP B CG    1 
ATOM   7606 O  OD1   . ASP B 2 69  ? -12.889 14.379  -34.259 1.00 111.37 ? 68   ASP B OD1   1 
ATOM   7607 O  OD2   . ASP B 2 69  ? -12.526 12.361  -35.038 1.00 128.61 ? 68   ASP B OD2   1 
ATOM   7608 N  N     . THR B 2 70  ? -15.236 15.193  -32.046 1.00 118.23 ? 69   THR B N     1 
ATOM   7609 C  CA    . THR B 2 70  ? -16.601 15.649  -32.250 1.00 106.90 ? 69   THR B CA    1 
ATOM   7610 C  C     . THR B 2 70  ? -16.890 15.888  -33.730 1.00 105.04 ? 69   THR B C     1 
ATOM   7611 O  O     . THR B 2 70  ? -15.999 15.868  -34.582 1.00 121.45 ? 69   THR B O     1 
ATOM   7612 C  CB    . THR B 2 70  ? -16.863 16.923  -31.446 1.00 105.77 ? 69   THR B CB    1 
ATOM   7613 O  OG1   . THR B 2 70  ? -15.950 17.947  -31.860 1.00 107.76 ? 69   THR B OG1   1 
ATOM   7614 C  CG2   . THR B 2 70  ? -16.678 16.655  -29.964 1.00 102.52 ? 69   THR B CG2   1 
ATOM   7615 N  N     . ALA B 2 71  ? -18.165 16.123  -34.026 1.00 96.43  ? 70   ALA B N     1 
ATOM   7616 C  CA    . ALA B 2 71  ? -18.636 16.319  -35.387 1.00 93.14  ? 70   ALA B CA    1 
ATOM   7617 C  C     . ALA B 2 71  ? -18.539 17.785  -35.795 1.00 99.51  ? 70   ALA B C     1 
ATOM   7618 O  O     . ALA B 2 71  ? -18.468 18.690  -34.960 1.00 94.43  ? 70   ALA B O     1 
ATOM   7619 C  CB    . ALA B 2 71  ? -20.079 15.835  -35.531 1.00 107.91 ? 70   ALA B CB    1 
ATOM   7620 N  N     . GLY B 2 72  ? -18.538 18.008  -37.106 1.00 93.42  ? 71   GLY B N     1 
ATOM   7621 C  CA    . GLY B 2 72  ? -18.499 19.348  -37.655 1.00 94.10  ? 71   GLY B CA    1 
ATOM   7622 C  C     . GLY B 2 72  ? -19.367 19.486  -38.888 1.00 126.67 ? 71   GLY B C     1 
ATOM   7623 O  O     . GLY B 2 72  ? -19.067 20.279  -39.785 1.00 150.20 ? 71   GLY B O     1 
ATOM   7624 N  N     . GLN B 2 73  ? -20.449 18.713  -38.940 1.00 110.73 ? 72   GLN B N     1 
ATOM   7625 C  CA    . GLN B 2 73  ? -21.366 18.719  -40.071 1.00 121.48 ? 72   GLN B CA    1 
ATOM   7626 C  C     . GLN B 2 73  ? -22.547 19.658  -39.872 1.00 141.59 ? 72   GLN B C     1 
ATOM   7627 O  O     . GLN B 2 73  ? -23.377 19.781  -40.780 1.00 167.36 ? 72   GLN B O     1 
ATOM   7628 C  CB    . GLN B 2 73  ? -21.882 17.299  -40.335 1.00 140.45 ? 72   GLN B CB    1 
ATOM   7629 C  CG    . GLN B 2 73  ? -20.791 16.254  -40.506 1.00 134.48 ? 72   GLN B CG    1 
ATOM   7630 C  CD    . GLN B 2 73  ? -20.009 16.426  -41.794 1.00 179.52 ? 72   GLN B CD    1 
ATOM   7631 O  OE1   . GLN B 2 73  ? -18.839 16.052  -41.877 1.00 182.13 ? 72   GLN B OE1   1 
ATOM   7632 N  NE2   . GLN B 2 73  ? -20.655 16.986  -42.810 1.00 189.99 ? 72   GLN B NE2   1 
ATOM   7633 N  N     . GLU B 2 74  ? -22.653 20.297  -38.703 1.00 138.20 ? 73   GLU B N     1 
ATOM   7634 C  CA    . GLU B 2 74  ? -23.735 21.219  -38.361 1.00 155.71 ? 73   GLU B CA    1 
ATOM   7635 C  C     . GLU B 2 74  ? -25.095 20.530  -38.289 1.00 143.67 ? 73   GLU B C     1 
ATOM   7636 O  O     . GLU B 2 74  ? -26.077 21.142  -37.856 1.00 171.69 ? 73   GLU B O     1 
ATOM   7637 C  CB    . GLU B 2 74  ? -23.788 22.390  -39.349 1.00 149.61 ? 73   GLU B CB    1 
ATOM   7638 C  CG    . GLU B 2 74  ? -22.733 23.461  -39.106 1.00 173.20 ? 73   GLU B CG    1 
ATOM   7639 C  CD    . GLU B 2 74  ? -22.991 24.267  -37.844 1.00 168.18 ? 73   GLU B CD    1 
ATOM   7640 O  OE1   . GLU B 2 74  ? -24.127 24.222  -37.324 1.00 152.50 ? 73   GLU B OE1   1 
ATOM   7641 O  OE2   . GLU B 2 74  ? -22.056 24.947  -37.371 1.00 182.08 ? 73   GLU B OE2   1 
ATOM   7642 N  N     . GLU B 2 75  ? -25.171 19.266  -38.706 1.00 130.81 ? 74   GLU B N     1 
ATOM   7643 C  CA    . GLU B 2 75  ? -26.389 18.486  -38.532 1.00 130.89 ? 74   GLU B CA    1 
ATOM   7644 C  C     . GLU B 2 75  ? -26.432 17.765  -37.194 1.00 123.36 ? 74   GLU B C     1 
ATOM   7645 O  O     . GLU B 2 75  ? -27.504 17.303  -36.787 1.00 141.06 ? 74   GLU B O     1 
ATOM   7646 C  CB    . GLU B 2 75  ? -26.541 17.464  -39.664 1.00 125.15 ? 74   GLU B CB    1 
ATOM   7647 C  CG    . GLU B 2 75  ? -25.443 16.419  -39.716 1.00 133.05 ? 74   GLU B CG    1 
ATOM   7648 C  CD    . GLU B 2 75  ? -25.780 15.265  -40.642 1.00 162.79 ? 74   GLU B CD    1 
ATOM   7649 O  OE1   . GLU B 2 75  ? -26.980 15.045  -40.907 1.00 170.61 ? 74   GLU B OE1   1 
ATOM   7650 O  OE2   . GLU B 2 75  ? -24.844 14.580  -41.106 1.00 181.48 ? 74   GLU B OE2   1 
ATOM   7651 N  N     . PHE B 2 76  ? -25.295 17.657  -36.507 1.00 125.82 ? 75   PHE B N     1 
ATOM   7652 C  CA    . PHE B 2 76  ? -25.225 17.092  -35.167 1.00 132.08 ? 75   PHE B CA    1 
ATOM   7653 C  C     . PHE B 2 76  ? -24.940 18.168  -34.123 1.00 132.60 ? 75   PHE B C     1 
ATOM   7654 O  O     . PHE B 2 76  ? -24.359 17.886  -33.073 1.00 115.32 ? 75   PHE B O     1 
ATOM   7655 C  CB    . PHE B 2 76  ? -24.167 15.992  -35.101 1.00 105.30 ? 75   PHE B CB    1 
ATOM   7656 C  CG    . PHE B 2 76  ? -24.266 14.987  -36.212 1.00 104.02 ? 75   PHE B CG    1 
ATOM   7657 C  CD1   . PHE B 2 76  ? -25.330 14.103  -36.272 1.00 106.82 ? 75   PHE B CD1   1 
ATOM   7658 C  CD2   . PHE B 2 76  ? -23.290 14.921  -37.193 1.00 116.08 ? 75   PHE B CD2   1 
ATOM   7659 C  CE1   . PHE B 2 76  ? -25.423 13.176  -37.294 1.00 127.07 ? 75   PHE B CE1   1 
ATOM   7660 C  CE2   . PHE B 2 76  ? -23.376 13.995  -38.215 1.00 142.16 ? 75   PHE B CE2   1 
ATOM   7661 C  CZ    . PHE B 2 76  ? -24.444 13.122  -38.266 1.00 151.28 ? 75   PHE B CZ    1 
ATOM   7662 N  N     . GLY B 2 77  ? -25.341 19.409  -34.409 1.00 123.78 ? 76   GLY B N     1 
ATOM   7663 C  CA    . GLY B 2 77  ? -25.107 20.508  -33.489 1.00 133.44 ? 76   GLY B CA    1 
ATOM   7664 C  C     . GLY B 2 77  ? -25.819 20.364  -32.161 1.00 139.74 ? 76   GLY B C     1 
ATOM   7665 O  O     . GLY B 2 77  ? -25.382 20.953  -31.167 1.00 124.62 ? 76   GLY B O     1 
ATOM   7666 N  N     . ALA B 2 78  ? -26.911 19.597  -32.120 1.00 117.55 ? 77   ALA B N     1 
ATOM   7667 C  CA    . ALA B 2 78  ? -27.581 19.333  -30.853 1.00 120.33 ? 77   ALA B CA    1 
ATOM   7668 C  C     . ALA B 2 78  ? -26.697 18.544  -29.898 1.00 137.66 ? 77   ALA B C     1 
ATOM   7669 O  O     . ALA B 2 78  ? -26.908 18.602  -28.681 1.00 155.26 ? 77   ALA B O     1 
ATOM   7670 C  CB    . ALA B 2 78  ? -28.892 18.583  -31.095 1.00 123.03 ? 77   ALA B CB    1 
ATOM   7671 N  N     . MET B 2 79  ? -25.714 17.811  -30.421 1.00 131.01 ? 78   MET B N     1 
ATOM   7672 C  CA    . MET B 2 79  ? -24.766 17.090  -29.585 1.00 113.70 ? 78   MET B CA    1 
ATOM   7673 C  C     . MET B 2 79  ? -23.683 17.993  -29.009 1.00 121.38 ? 78   MET B C     1 
ATOM   7674 O  O     . MET B 2 79  ? -22.971 17.565  -28.094 1.00 126.71 ? 78   MET B O     1 
ATOM   7675 C  CB    . MET B 2 79  ? -24.122 15.954  -30.385 1.00 118.13 ? 78   MET B CB    1 
ATOM   7676 C  CG    . MET B 2 79  ? -25.125 15.070  -31.112 1.00 130.43 ? 78   MET B CG    1 
ATOM   7677 S  SD    . MET B 2 79  ? -24.359 13.712  -32.017 1.00 102.02 ? 78   MET B SD    1 
ATOM   7678 C  CE    . MET B 2 79  ? -23.718 12.723  -30.670 1.00 108.76 ? 78   MET B CE    1 
ATOM   7679 N  N     . ARG B 2 80  ? -23.541 19.220  -29.520 1.00 151.31 ? 79   ARG B N     1 
ATOM   7680 C  CA    . ARG B 2 80  ? -22.562 20.149  -28.963 1.00 137.20 ? 79   ARG B CA    1 
ATOM   7681 C  C     . ARG B 2 80  ? -22.886 20.486  -27.514 1.00 134.14 ? 79   ARG B C     1 
ATOM   7682 O  O     . ARG B 2 80  ? -22.000 20.471  -26.652 1.00 116.08 ? 79   ARG B O     1 
ATOM   7683 C  CB    . ARG B 2 80  ? -22.505 21.427  -29.801 1.00 115.80 ? 79   ARG B CB    1 
ATOM   7684 C  CG    . ARG B 2 80  ? -21.947 21.256  -31.203 1.00 118.54 ? 79   ARG B CG    1 
ATOM   7685 C  CD    . ARG B 2 80  ? -21.642 22.612  -31.819 1.00 121.88 ? 79   ARG B CD    1 
ATOM   7686 N  NE    . ARG B 2 80  ? -20.986 22.497  -33.115 1.00 118.29 ? 79   ARG B NE    1 
ATOM   7687 C  CZ    . ARG B 2 80  ? -21.599 22.639  -34.282 1.00 135.09 ? 79   ARG B CZ    1 
ATOM   7688 N  NH1   . ARG B 2 80  ? -22.893 22.903  -34.355 1.00 155.13 ? 79   ARG B NH1   1 
ATOM   7689 N  NH2   . ARG B 2 80  ? -20.895 22.516  -35.404 1.00 116.31 ? 79   ARG B NH2   1 
ATOM   7690 N  N     . GLU B 2 81  ? -24.154 20.775  -27.225 1.00 142.93 ? 80   GLU B N     1 
ATOM   7691 C  CA    . GLU B 2 81  ? -24.579 21.148  -25.881 1.00 142.22 ? 80   GLU B CA    1 
ATOM   7692 C  C     . GLU B 2 81  ? -24.385 20.033  -24.859 1.00 143.60 ? 80   GLU B C     1 
ATOM   7693 O  O     . GLU B 2 81  ? -24.639 20.262  -23.671 1.00 156.55 ? 80   GLU B O     1 
ATOM   7694 C  CB    . GLU B 2 81  ? -26.048 21.581  -25.906 1.00 155.94 ? 80   GLU B CB    1 
ATOM   7695 C  CG    . GLU B 2 81  ? -26.312 22.825  -26.735 1.00 145.97 ? 80   GLU B CG    1 
ATOM   7696 C  CD    . GLU B 2 81  ? -25.810 24.086  -26.062 1.00 174.25 ? 80   GLU B CD    1 
ATOM   7697 O  OE1   . GLU B 2 81  ? -25.865 24.158  -24.816 1.00 175.71 ? 80   GLU B OE1   1 
ATOM   7698 O  OE2   . GLU B 2 81  ? -25.360 25.006  -26.776 1.00 168.79 ? 80   GLU B OE2   1 
ATOM   7699 N  N     . GLN B 2 82  ? -23.951 18.843  -25.276 1.00 151.85 ? 81   GLN B N     1 
ATOM   7700 C  CA    . GLN B 2 82  ? -23.727 17.741  -24.345 1.00 143.64 ? 81   GLN B CA    1 
ATOM   7701 C  C     . GLN B 2 82  ? -22.268 17.660  -23.904 1.00 132.79 ? 81   GLN B C     1 
ATOM   7702 O  O     . GLN B 2 82  ? -21.968 17.775  -22.711 1.00 135.29 ? 81   GLN B O     1 
ATOM   7703 C  CB    . GLN B 2 82  ? -24.173 16.417  -24.978 1.00 150.74 ? 81   GLN B CB    1 
ATOM   7704 C  CG    . GLN B 2 82  ? -23.909 15.200  -24.104 1.00 170.12 ? 81   GLN B CG    1 
ATOM   7705 C  CD    . GLN B 2 82  ? -24.469 15.364  -22.709 1.00 173.01 ? 81   GLN B CD    1 
ATOM   7706 O  OE1   . GLN B 2 82  ? -23.725 15.393  -21.730 1.00 174.76 ? 81   GLN B OE1   1 
ATOM   7707 N  NE2   . GLN B 2 82  ? -25.789 15.479  -22.611 1.00 185.36 ? 81   GLN B NE2   1 
ATOM   7708 N  N     . TYR B 2 83  ? -21.349 17.457  -24.853 1.00 127.56 ? 82   TYR B N     1 
ATOM   7709 C  CA    . TYR B 2 83  ? -19.945 17.309  -24.487 1.00 136.30 ? 82   TYR B CA    1 
ATOM   7710 C  C     . TYR B 2 83  ? -19.333 18.611  -23.986 1.00 145.78 ? 82   TYR B C     1 
ATOM   7711 O  O     . TYR B 2 83  ? -18.270 18.578  -23.357 1.00 164.04 ? 82   TYR B O     1 
ATOM   7712 C  CB    . TYR B 2 83  ? -19.131 16.757  -25.664 1.00 140.57 ? 82   TYR B CB    1 
ATOM   7713 C  CG    . TYR B 2 83  ? -19.157 17.583  -26.935 1.00 119.15 ? 82   TYR B CG    1 
ATOM   7714 C  CD1   . TYR B 2 83  ? -18.422 18.757  -27.043 1.00 122.33 ? 82   TYR B CD1   1 
ATOM   7715 C  CD2   . TYR B 2 83  ? -19.885 17.164  -28.040 1.00 128.44 ? 82   TYR B CD2   1 
ATOM   7716 C  CE1   . TYR B 2 83  ? -18.435 19.504  -28.204 1.00 122.69 ? 82   TYR B CE1   1 
ATOM   7717 C  CE2   . TYR B 2 83  ? -19.901 17.903  -29.207 1.00 120.69 ? 82   TYR B CE2   1 
ATOM   7718 C  CZ    . TYR B 2 83  ? -19.175 19.072  -29.284 1.00 124.94 ? 82   TYR B CZ    1 
ATOM   7719 O  OH    . TYR B 2 83  ? -19.186 19.813  -30.443 1.00 127.11 ? 82   TYR B OH    1 
ATOM   7720 N  N     . MET B 2 84  ? -19.972 19.751  -24.246 1.00 130.92 ? 83   MET B N     1 
ATOM   7721 C  CA    . MET B 2 84  ? -19.516 21.016  -23.686 1.00 130.34 ? 83   MET B CA    1 
ATOM   7722 C  C     . MET B 2 84  ? -19.884 21.174  -22.216 1.00 133.17 ? 83   MET B C     1 
ATOM   7723 O  O     . MET B 2 84  ? -19.551 22.202  -21.619 1.00 139.85 ? 83   MET B O     1 
ATOM   7724 C  CB    . MET B 2 84  ? -20.081 22.191  -24.492 1.00 138.87 ? 83   MET B CB    1 
ATOM   7725 C  CG    . MET B 2 84  ? -19.517 22.304  -25.902 1.00 129.09 ? 83   MET B CG    1 
ATOM   7726 S  SD    . MET B 2 84  ? -20.013 23.817  -26.752 1.00 124.92 ? 83   MET B SD    1 
ATOM   7727 C  CE    . MET B 2 84  ? -21.798 23.707  -26.644 1.00 145.91 ? 83   MET B CE    1 
ATOM   7728 N  N     . ARG B 2 85  ? -20.562 20.191  -21.626 1.00 139.81 ? 84   ARG B N     1 
ATOM   7729 C  CA    . ARG B 2 85  ? -20.867 20.194  -20.201 1.00 142.73 ? 84   ARG B CA    1 
ATOM   7730 C  C     . ARG B 2 85  ? -19.994 19.237  -19.404 1.00 149.49 ? 84   ARG B C     1 
ATOM   7731 O  O     . ARG B 2 85  ? -19.757 19.475  -18.216 1.00 157.18 ? 84   ARG B O     1 
ATOM   7732 C  CB    . ARG B 2 85  ? -22.338 19.830  -19.967 1.00 147.39 ? 84   ARG B CB    1 
ATOM   7733 C  CG    . ARG B 2 85  ? -23.323 20.664  -20.763 1.00 144.93 ? 84   ARG B CG    1 
ATOM   7734 C  CD    . ARG B 2 85  ? -24.760 20.240  -20.500 1.00 157.43 ? 84   ARG B CD    1 
ATOM   7735 N  NE    . ARG B 2 85  ? -25.188 20.539  -19.140 1.00 163.98 ? 84   ARG B NE    1 
ATOM   7736 C  CZ    . ARG B 2 85  ? -26.421 20.355  -18.687 1.00 178.62 ? 84   ARG B CZ    1 
ATOM   7737 N  NH1   . ARG B 2 85  ? -27.377 19.873  -19.464 1.00 185.98 ? 84   ARG B NH1   1 
ATOM   7738 N  NH2   . ARG B 2 85  ? -26.702 20.662  -17.424 1.00 182.40 ? 84   ARG B NH2   1 
ATOM   7739 N  N     . THR B 2 86  ? -19.512 18.164  -20.032 1.00 142.33 ? 85   THR B N     1 
ATOM   7740 C  CA    . THR B 2 86  ? -18.727 17.148  -19.345 1.00 142.11 ? 85   THR B CA    1 
ATOM   7741 C  C     . THR B 2 86  ? -17.228 17.282  -19.570 1.00 163.19 ? 85   THR B C     1 
ATOM   7742 O  O     . THR B 2 86  ? -16.450 16.762  -18.763 1.00 171.71 ? 85   THR B O     1 
ATOM   7743 C  CB    . THR B 2 86  ? -19.170 15.748  -19.788 1.00 162.76 ? 85   THR B CB    1 
ATOM   7744 O  OG1   . THR B 2 86  ? -18.964 15.606  -21.200 1.00 136.03 ? 85   THR B OG1   1 
ATOM   7745 C  CG2   . THR B 2 86  ? -20.642 15.530  -19.473 1.00 174.36 ? 85   THR B CG2   1 
ATOM   7746 N  N     . GLY B 2 87  ? -16.806 17.956  -20.637 1.00 144.15 ? 86   GLY B N     1 
ATOM   7747 C  CA    . GLY B 2 87  ? -15.387 18.070  -20.927 1.00 143.49 ? 86   GLY B CA    1 
ATOM   7748 C  C     . GLY B 2 87  ? -14.740 19.211  -20.157 1.00 148.42 ? 86   GLY B C     1 
ATOM   7749 O  O     . GLY B 2 87  ? -15.343 20.259  -19.927 1.00 164.39 ? 86   GLY B O     1 
ATOM   7750 N  N     . GLU B 2 88  ? -13.487 18.992  -19.758 1.00 150.97 ? 87   GLU B N     1 
ATOM   7751 C  CA    . GLU B 2 88  ? -12.701 19.997  -19.055 1.00 153.87 ? 87   GLU B CA    1 
ATOM   7752 C  C     . GLU B 2 88  ? -11.539 20.518  -19.892 1.00 152.35 ? 87   GLU B C     1 
ATOM   7753 O  O     . GLU B 2 88  ? -10.659 21.200  -19.356 1.00 153.66 ? 87   GLU B O     1 
ATOM   7754 C  CB    . GLU B 2 88  ? -12.184 19.440  -17.726 1.00 162.81 ? 87   GLU B CB    1 
ATOM   7755 C  CG    . GLU B 2 88  ? -11.493 18.089  -17.824 1.00 166.63 ? 87   GLU B CG    1 
ATOM   7756 C  CD    . GLU B 2 88  ? -12.452 16.928  -17.641 1.00 181.77 ? 87   GLU B CD    1 
ATOM   7757 O  OE1   . GLU B 2 88  ? -13.678 17.164  -17.612 1.00 204.91 ? 87   GLU B OE1   1 
ATOM   7758 O  OE2   . GLU B 2 88  ? -11.979 15.778  -17.521 1.00 171.34 ? 87   GLU B OE2   1 
ATOM   7759 N  N     . GLY B 2 89  ? -11.516 20.218  -21.188 1.00 146.75 ? 88   GLY B N     1 
ATOM   7760 C  CA    . GLY B 2 89  ? -10.467 20.695  -22.067 1.00 128.24 ? 88   GLY B CA    1 
ATOM   7761 C  C     . GLY B 2 89  ? -10.860 20.613  -23.527 1.00 127.41 ? 88   GLY B C     1 
ATOM   7762 O  O     . GLY B 2 89  ? -11.215 19.538  -24.019 1.00 142.53 ? 88   GLY B O     1 
ATOM   7763 N  N     . PHE B 2 90  ? -10.801 21.740  -24.232 1.00 113.56 ? 89   PHE B N     1 
ATOM   7764 C  CA    . PHE B 2 90  ? -11.232 21.815  -25.618 1.00 131.17 ? 89   PHE B CA    1 
ATOM   7765 C  C     . PHE B 2 90  ? -10.074 22.235  -26.513 1.00 131.69 ? 89   PHE B C     1 
ATOM   7766 O  O     . PHE B 2 90  ? -9.073  22.792  -26.055 1.00 123.67 ? 89   PHE B O     1 
ATOM   7767 C  CB    . PHE B 2 90  ? -12.401 22.795  -25.782 1.00 121.11 ? 89   PHE B CB    1 
ATOM   7768 C  CG    . PHE B 2 90  ? -13.614 22.428  -24.978 1.00 125.08 ? 89   PHE B CG    1 
ATOM   7769 C  CD1   . PHE B 2 90  ? -14.595 21.610  -25.515 1.00 110.86 ? 89   PHE B CD1   1 
ATOM   7770 C  CD2   . PHE B 2 90  ? -13.774 22.898  -23.686 1.00 110.65 ? 89   PHE B CD2   1 
ATOM   7771 C  CE1   . PHE B 2 90  ? -15.712 21.268  -24.777 1.00 130.29 ? 89   PHE B CE1   1 
ATOM   7772 C  CE2   . PHE B 2 90  ? -14.889 22.560  -22.943 1.00 126.73 ? 89   PHE B CE2   1 
ATOM   7773 C  CZ    . PHE B 2 90  ? -15.859 21.744  -23.490 1.00 142.73 ? 89   PHE B CZ    1 
ATOM   7774 N  N     . LEU B 2 91  ? -10.223 21.955  -27.806 1.00 122.85 ? 90   LEU B N     1 
ATOM   7775 C  CA    . LEU B 2 91  ? -9.234  22.321  -28.818 1.00 122.00 ? 90   LEU B CA    1 
ATOM   7776 C  C     . LEU B 2 91  ? -9.973  22.952  -29.994 1.00 141.36 ? 90   LEU B C     1 
ATOM   7777 O  O     . LEU B 2 91  ? -10.510 22.243  -30.850 1.00 123.88 ? 90   LEU B O     1 
ATOM   7778 C  CB    . LEU B 2 91  ? -8.418  21.111  -29.264 1.00 112.18 ? 90   LEU B CB    1 
ATOM   7779 C  CG    . LEU B 2 91  ? -7.425  20.535  -28.255 1.00 114.42 ? 90   LEU B CG    1 
ATOM   7780 C  CD1   . LEU B 2 91  ? -6.658  19.374  -28.866 1.00 125.35 ? 90   LEU B CD1   1 
ATOM   7781 C  CD2   . LEU B 2 91  ? -6.471  21.612  -27.770 1.00 117.10 ? 90   LEU B CD2   1 
ATOM   7782 N  N     . LEU B 2 92  ? -10.007 24.281  -30.028 1.00 122.68 ? 91   LEU B N     1 
ATOM   7783 C  CA    . LEU B 2 92  ? -10.569 25.006  -31.164 1.00 123.78 ? 91   LEU B CA    1 
ATOM   7784 C  C     . LEU B 2 92  ? -9.620  24.845  -32.343 1.00 115.73 ? 91   LEU B C     1 
ATOM   7785 O  O     . LEU B 2 92  ? -8.627  25.566  -32.459 1.00 127.18 ? 91   LEU B O     1 
ATOM   7786 C  CB    . LEU B 2 92  ? -10.771 26.476  -30.816 1.00 141.85 ? 91   LEU B CB    1 
ATOM   7787 C  CG    . LEU B 2 92  ? -11.606 26.799  -29.575 1.00 142.09 ? 91   LEU B CG    1 
ATOM   7788 C  CD1   . LEU B 2 92  ? -11.626 28.299  -29.329 1.00 142.21 ? 91   LEU B CD1   1 
ATOM   7789 C  CD2   . LEU B 2 92  ? -13.018 26.261  -29.718 1.00 144.05 ? 91   LEU B CD2   1 
ATOM   7790 N  N     . VAL B 2 93  ? -9.911  23.891  -33.222 1.00 113.10 ? 92   VAL B N     1 
ATOM   7791 C  CA    . VAL B 2 93  ? -9.034  23.589  -34.345 1.00 136.93 ? 92   VAL B CA    1 
ATOM   7792 C  C     . VAL B 2 93  ? -9.695  24.051  -35.636 1.00 126.12 ? 92   VAL B C     1 
ATOM   7793 O  O     . VAL B 2 93  ? -10.922 24.008  -35.789 1.00 120.95 ? 92   VAL B O     1 
ATOM   7794 C  CB    . VAL B 2 93  ? -8.678  22.088  -34.411 1.00 117.18 ? 92   VAL B CB    1 
ATOM   7795 C  CG1   . VAL B 2 93  ? -8.209  21.589  -33.053 1.00 120.20 ? 92   VAL B CG1   1 
ATOM   7796 C  CG2   . VAL B 2 93  ? -9.856  21.280  -34.889 1.00 111.24 ? 92   VAL B CG2   1 
ATOM   7797 N  N     . PHE B 2 94  ? -8.864  24.512  -36.566 1.00 110.53 ? 93   PHE B N     1 
ATOM   7798 C  CA    . PHE B 2 94  ? -9.325  24.930  -37.881 1.00 111.89 ? 93   PHE B CA    1 
ATOM   7799 C  C     . PHE B 2 94  ? -8.221  24.646  -38.888 1.00 117.15 ? 93   PHE B C     1 
ATOM   7800 O  O     . PHE B 2 94  ? -7.068  24.398  -38.526 1.00 111.03 ? 93   PHE B O     1 
ATOM   7801 C  CB    . PHE B 2 94  ? -9.719  26.412  -37.900 1.00 114.92 ? 93   PHE B CB    1 
ATOM   7802 C  CG    . PHE B 2 94  ? -8.565  27.353  -37.686 1.00 110.91 ? 93   PHE B CG    1 
ATOM   7803 C  CD1   . PHE B 2 94  ? -8.149  27.681  -36.406 1.00 122.60 ? 93   PHE B CD1   1 
ATOM   7804 C  CD2   . PHE B 2 94  ? -7.902  27.915  -38.765 1.00 124.01 ? 93   PHE B CD2   1 
ATOM   7805 C  CE1   . PHE B 2 94  ? -7.088  28.546  -36.206 1.00 114.53 ? 93   PHE B CE1   1 
ATOM   7806 C  CE2   . PHE B 2 94  ? -6.841  28.781  -38.571 1.00 124.94 ? 93   PHE B CE2   1 
ATOM   7807 C  CZ    . PHE B 2 94  ? -6.434  29.097  -37.290 1.00 115.43 ? 93   PHE B CZ    1 
ATOM   7808 N  N     . SER B 2 95  ? -8.588  24.685  -40.164 1.00 112.64 ? 94   SER B N     1 
ATOM   7809 C  CA    . SER B 2 95  ? -7.648  24.466  -41.253 1.00 110.70 ? 94   SER B CA    1 
ATOM   7810 C  C     . SER B 2 95  ? -7.187  25.808  -41.805 1.00 118.54 ? 94   SER B C     1 
ATOM   7811 O  O     . SER B 2 95  ? -8.014  26.664  -42.138 1.00 110.30 ? 94   SER B O     1 
ATOM   7812 C  CB    . SER B 2 95  ? -8.284  23.628  -42.363 1.00 108.30 ? 94   SER B CB    1 
ATOM   7813 O  OG    . SER B 2 95  ? -7.431  23.551  -43.492 1.00 115.59 ? 94   SER B OG    1 
ATOM   7814 N  N     . VAL B 2 96  ? -5.867  25.988  -41.899 1.00 120.74 ? 95   VAL B N     1 
ATOM   7815 C  CA    . VAL B 2 96  ? -5.315  27.200  -42.494 1.00 114.57 ? 95   VAL B CA    1 
ATOM   7816 C  C     . VAL B 2 96  ? -5.605  27.298  -43.982 1.00 118.25 ? 95   VAL B C     1 
ATOM   7817 O  O     . VAL B 2 96  ? -5.404  28.364  -44.575 1.00 136.71 ? 95   VAL B O     1 
ATOM   7818 C  CB    . VAL B 2 96  ? -3.794  27.283  -42.254 1.00 117.07 ? 95   VAL B CB    1 
ATOM   7819 C  CG1   . VAL B 2 96  ? -3.492  27.275  -40.763 1.00 120.76 ? 95   VAL B CG1   1 
ATOM   7820 C  CG2   . VAL B 2 96  ? -3.082  26.140  -42.957 1.00 117.59 ? 95   VAL B CG2   1 
ATOM   7821 N  N     . THR B 2 97  ? -6.065  26.213  -44.599 1.00 112.85 ? 96   THR B N     1 
ATOM   7822 C  CA    . THR B 2 97  ? -6.488  26.217  -45.991 1.00 112.39 ? 96   THR B CA    1 
ATOM   7823 C  C     . THR B 2 97  ? -7.979  26.484  -46.148 1.00 110.47 ? 96   THR B C     1 
ATOM   7824 O  O     . THR B 2 97  ? -8.485  26.449  -47.274 1.00 160.15 ? 96   THR B O     1 
ATOM   7825 C  CB    . THR B 2 97  ? -6.136  24.882  -46.656 1.00 126.87 ? 96   THR B CB    1 
ATOM   7826 O  OG1   . THR B 2 97  ? -6.843  23.820  -46.003 1.00 132.28 ? 96   THR B OG1   1 
ATOM   7827 C  CG2   . THR B 2 97  ? -4.642  24.617  -46.562 1.00 114.54 ? 96   THR B CG2   1 
ATOM   7828 N  N     . ASP B 2 98  ? -8.690  26.749  -45.051 1.00 109.50 ? 97   ASP B N     1 
ATOM   7829 C  CA    . ASP B 2 98  ? -10.137 26.966  -45.080 1.00 115.90 ? 97   ASP B CA    1 
ATOM   7830 C  C     . ASP B 2 98  ? -10.454 28.150  -44.171 1.00 141.47 ? 97   ASP B C     1 
ATOM   7831 O  O     . ASP B 2 98  ? -10.500 28.002  -42.946 1.00 131.15 ? 97   ASP B O     1 
ATOM   7832 C  CB    . ASP B 2 98  ? -10.885 25.712  -44.641 1.00 106.06 ? 97   ASP B CB    1 
ATOM   7833 C  CG    . ASP B 2 98  ? -12.393 25.865  -44.728 1.00 110.30 ? 97   ASP B CG    1 
ATOM   7834 O  OD1   . ASP B 2 98  ? -12.868 26.870  -45.299 1.00 122.00 ? 97   ASP B OD1   1 
ATOM   7835 O  OD2   . ASP B 2 98  ? -13.107 24.974  -44.222 1.00 125.53 ? 97   ASP B OD2   1 
ATOM   7836 N  N     . ARG B 2 99  ? -10.676 29.321  -44.774 1.00 133.36 ? 98   ARG B N     1 
ATOM   7837 C  CA    . ARG B 2 99  ? -11.076 30.488  -43.997 1.00 116.29 ? 98   ARG B CA    1 
ATOM   7838 C  C     . ARG B 2 99  ? -12.467 30.334  -43.401 1.00 118.33 ? 98   ARG B C     1 
ATOM   7839 O  O     . ARG B 2 99  ? -12.772 30.987  -42.397 1.00 124.50 ? 98   ARG B O     1 
ATOM   7840 C  CB    . ARG B 2 99  ? -11.029 31.751  -44.857 1.00 113.30 ? 98   ARG B CB    1 
ATOM   7841 C  CG    . ARG B 2 99  ? -9.646  32.115  -45.355 1.00 149.80 ? 98   ARG B CG    1 
ATOM   7842 C  CD    . ARG B 2 99  ? -9.602  33.553  -45.837 1.00 131.33 ? 98   ARG B CD    1 
ATOM   7843 N  NE    . ARG B 2 99  ? -9.885  34.490  -44.757 1.00 132.75 ? 98   ARG B NE    1 
ATOM   7844 C  CZ    . ARG B 2 99  ? -8.967  34.999  -43.947 1.00 130.83 ? 98   ARG B CZ    1 
ATOM   7845 N  NH1   . ARG B 2 99  ? -7.688  34.682  -44.068 1.00 136.48 ? 98   ARG B NH1   1 
ATOM   7846 N  NH2   . ARG B 2 99  ? -9.341  35.846  -42.993 1.00 133.60 ? 98   ARG B NH2   1 
ATOM   7847 N  N     . GLY B 2 100 ? -13.318 29.499  -44.002 1.00 110.94 ? 99   GLY B N     1 
ATOM   7848 C  CA    . GLY B 2 100 ? -14.638 29.273  -43.439 1.00 116.78 ? 99   GLY B CA    1 
ATOM   7849 C  C     . GLY B 2 100 ? -14.577 28.750  -42.018 1.00 123.51 ? 99   GLY B C     1 
ATOM   7850 O  O     . GLY B 2 100 ? -15.313 29.212  -41.144 1.00 149.19 ? 99   GLY B O     1 
ATOM   7851 N  N     . SER B 2 101 ? -13.691 27.784  -41.765 1.00 145.18 ? 100  SER B N     1 
ATOM   7852 C  CA    . SER B 2 101 ? -13.502 27.297  -40.404 1.00 127.05 ? 100  SER B CA    1 
ATOM   7853 C  C     . SER B 2 101 ? -12.880 28.360  -39.510 1.00 127.89 ? 100  SER B C     1 
ATOM   7854 O  O     . SER B 2 101 ? -13.180 28.413  -38.313 1.00 111.51 ? 100  SER B O     1 
ATOM   7855 C  CB    . SER B 2 101 ? -12.632 26.042  -40.413 1.00 126.61 ? 100  SER B CB    1 
ATOM   7856 O  OG    . SER B 2 101 ? -11.348 26.315  -40.950 1.00 105.81 ? 100  SER B OG    1 
ATOM   7857 N  N     . PHE B 2 102 ? -12.021 29.213  -40.072 1.00 114.76 ? 101  PHE B N     1 
ATOM   7858 C  CA    . PHE B 2 102 ? -11.372 30.250  -39.277 1.00 116.18 ? 101  PHE B CA    1 
ATOM   7859 C  C     . PHE B 2 102 ? -12.381 31.274  -38.770 1.00 125.95 ? 101  PHE B C     1 
ATOM   7860 O  O     . PHE B 2 102 ? -12.296 31.720  -37.620 1.00 133.29 ? 101  PHE B O     1 
ATOM   7861 C  CB    . PHE B 2 102 ? -10.279 30.929  -40.101 1.00 110.76 ? 101  PHE B CB    1 
ATOM   7862 C  CG    . PHE B 2 102 ? -9.629  32.091  -39.409 1.00 112.74 ? 101  PHE B CG    1 
ATOM   7863 C  CD1   . PHE B 2 102 ? -8.672  31.885  -38.430 1.00 127.07 ? 101  PHE B CD1   1 
ATOM   7864 C  CD2   . PHE B 2 102 ? -9.968  33.392  -39.745 1.00 118.95 ? 101  PHE B CD2   1 
ATOM   7865 C  CE1   . PHE B 2 102 ? -8.069  32.954  -37.794 1.00 142.40 ? 101  PHE B CE1   1 
ATOM   7866 C  CE2   . PHE B 2 102 ? -9.369  34.464  -39.113 1.00 143.43 ? 101  PHE B CE2   1 
ATOM   7867 C  CZ    . PHE B 2 102 ? -8.418  34.245  -38.137 1.00 151.80 ? 101  PHE B CZ    1 
ATOM   7868 N  N     . GLU B 2 103 ? -13.341 31.659  -39.608 1.00 118.11 ? 102  GLU B N     1 
ATOM   7869 C  CA    . GLU B 2 103 ? -14.367 32.615  -39.217 1.00 122.66 ? 102  GLU B CA    1 
ATOM   7870 C  C     . GLU B 2 103 ? -15.539 31.963  -38.493 1.00 121.97 ? 102  GLU B C     1 
ATOM   7871 O  O     . GLU B 2 103 ? -16.535 32.640  -38.221 1.00 164.65 ? 102  GLU B O     1 
ATOM   7872 C  CB    . GLU B 2 103 ? -14.872 33.378  -40.445 1.00 128.34 ? 102  GLU B CB    1 
ATOM   7873 C  CG    . GLU B 2 103 ? -15.575 32.511  -41.474 1.00 149.76 ? 102  GLU B CG    1 
ATOM   7874 C  CD    . GLU B 2 103 ? -15.946 33.280  -42.726 1.00 148.43 ? 102  GLU B CD    1 
ATOM   7875 O  OE1   . GLU B 2 103 ? -15.379 34.372  -42.943 1.00 134.41 ? 102  GLU B OE1   1 
ATOM   7876 O  OE2   . GLU B 2 103 ? -16.805 32.795  -43.491 1.00 154.34 ? 102  GLU B OE2   1 
ATOM   7877 N  N     . GLU B 2 104 ? -15.445 30.670  -38.182 1.00 120.68 ? 103  GLU B N     1 
ATOM   7878 C  CA    . GLU B 2 104 ? -16.470 29.967  -37.421 1.00 134.20 ? 103  GLU B CA    1 
ATOM   7879 C  C     . GLU B 2 104 ? -15.918 29.356  -36.139 1.00 130.05 ? 103  GLU B C     1 
ATOM   7880 O  O     . GLU B 2 104 ? -16.646 28.642  -35.440 1.00 112.04 ? 103  GLU B O     1 
ATOM   7881 C  CB    . GLU B 2 104 ? -17.125 28.882  -38.281 1.00 132.15 ? 103  GLU B CB    1 
ATOM   7882 C  CG    . GLU B 2 104 ? -17.915 29.419  -39.467 1.00 127.52 ? 103  GLU B CG    1 
ATOM   7883 C  CD    . GLU B 2 104 ? -19.232 30.045  -39.060 1.00 162.52 ? 103  GLU B CD    1 
ATOM   7884 O  OE1   . GLU B 2 104 ? -19.987 29.400  -38.304 1.00 178.67 ? 103  GLU B OE1   1 
ATOM   7885 O  OE2   . GLU B 2 104 ? -19.512 31.183  -39.495 1.00 162.31 ? 103  GLU B OE2   1 
ATOM   7886 N  N     . ILE B 2 105 ? -14.650 29.616  -35.815 1.00 140.58 ? 104  ILE B N     1 
ATOM   7887 C  CA    . ILE B 2 105 ? -14.072 29.089  -34.583 1.00 134.11 ? 104  ILE B CA    1 
ATOM   7888 C  C     . ILE B 2 105 ? -14.687 29.769  -33.368 1.00 145.06 ? 104  ILE B C     1 
ATOM   7889 O  O     . ILE B 2 105 ? -14.982 29.117  -32.358 1.00 143.20 ? 104  ILE B O     1 
ATOM   7890 C  CB    . ILE B 2 105 ? -12.539 29.243  -34.604 1.00 134.56 ? 104  ILE B CB    1 
ATOM   7891 C  CG1   . ILE B 2 105 ? -11.908 28.138  -35.448 1.00 135.71 ? 104  ILE B CG1   1 
ATOM   7892 C  CG2   . ILE B 2 105 ? -11.969 29.225  -33.193 1.00 137.44 ? 104  ILE B CG2   1 
ATOM   7893 C  CD1   . ILE B 2 105 ? -12.291 26.749  -34.997 1.00 139.89 ? 104  ILE B CD1   1 
ATOM   7894 N  N     . TYR B 2 106 ? -14.902 31.087  -33.447 1.00 149.06 ? 105  TYR B N     1 
ATOM   7895 C  CA    . TYR B 2 106 ? -15.417 31.823  -32.297 1.00 130.10 ? 105  TYR B CA    1 
ATOM   7896 C  C     . TYR B 2 106 ? -16.787 31.315  -31.870 1.00 135.41 ? 105  TYR B C     1 
ATOM   7897 O  O     . TYR B 2 106 ? -17.117 31.358  -30.680 1.00 132.29 ? 105  TYR B O     1 
ATOM   7898 C  CB    . TYR B 2 106 ? -15.474 33.321  -32.610 1.00 146.06 ? 105  TYR B CB    1 
ATOM   7899 C  CG    . TYR B 2 106 ? -16.647 33.739  -33.470 1.00 160.33 ? 105  TYR B CG    1 
ATOM   7900 C  CD1   . TYR B 2 106 ? -16.627 33.553  -34.846 1.00 173.52 ? 105  TYR B CD1   1 
ATOM   7901 C  CD2   . TYR B 2 106 ? -17.771 34.330  -32.906 1.00 157.16 ? 105  TYR B CD2   1 
ATOM   7902 C  CE1   . TYR B 2 106 ? -17.697 33.937  -35.634 1.00 176.67 ? 105  TYR B CE1   1 
ATOM   7903 C  CE2   . TYR B 2 106 ? -18.844 34.717  -33.686 1.00 166.23 ? 105  TYR B CE2   1 
ATOM   7904 C  CZ    . TYR B 2 106 ? -18.802 34.518  -35.050 1.00 169.36 ? 105  TYR B CZ    1 
ATOM   7905 O  OH    . TYR B 2 106 ? -19.867 34.902  -35.832 1.00 164.70 ? 105  TYR B OH    1 
ATOM   7906 N  N     . LYS B 2 107 ? -17.591 30.820  -32.816 1.00 135.14 ? 106  LYS B N     1 
ATOM   7907 C  CA    . LYS B 2 107 ? -18.897 30.274  -32.459 1.00 140.17 ? 106  LYS B CA    1 
ATOM   7908 C  C     . LYS B 2 107 ? -18.758 29.091  -31.510 1.00 147.30 ? 106  LYS B C     1 
ATOM   7909 O  O     . LYS B 2 107 ? -19.582 28.910  -30.606 1.00 155.43 ? 106  LYS B O     1 
ATOM   7910 C  CB    . LYS B 2 107 ? -19.662 29.867  -33.718 1.00 144.63 ? 106  LYS B CB    1 
ATOM   7911 C  CG    . LYS B 2 107 ? -20.057 31.035  -34.607 1.00 152.20 ? 106  LYS B CG    1 
ATOM   7912 C  CD    . LYS B 2 107 ? -21.119 30.620  -35.612 1.00 170.37 ? 106  LYS B CD    1 
ATOM   7913 C  CE    . LYS B 2 107 ? -21.544 31.787  -36.487 1.00 159.44 ? 106  LYS B CE    1 
ATOM   7914 N  NZ    . LYS B 2 107 ? -22.587 31.386  -37.471 1.00 156.93 ? 106  LYS B NZ    1 
ATOM   7915 N  N     . PHE B 2 108 ? -17.719 28.274  -31.696 1.00 150.92 ? 107  PHE B N     1 
ATOM   7916 C  CA    . PHE B 2 108 ? -17.443 27.209  -30.738 1.00 142.76 ? 107  PHE B CA    1 
ATOM   7917 C  C     . PHE B 2 108 ? -16.972 27.780  -29.407 1.00 122.19 ? 107  PHE B C     1 
ATOM   7918 O  O     . PHE B 2 108 ? -17.303 27.245  -28.343 1.00 134.35 ? 107  PHE B O     1 
ATOM   7919 C  CB    . PHE B 2 108 ? -16.402 26.244  -31.304 1.00 144.27 ? 107  PHE B CB    1 
ATOM   7920 C  CG    . PHE B 2 108 ? -16.929 25.345  -32.383 1.00 109.27 ? 107  PHE B CG    1 
ATOM   7921 C  CD1   . PHE B 2 108 ? -16.922 25.750  -33.707 1.00 109.35 ? 107  PHE B CD1   1 
ATOM   7922 C  CD2   . PHE B 2 108 ? -17.429 24.091  -32.074 1.00 106.94 ? 107  PHE B CD2   1 
ATOM   7923 C  CE1   . PHE B 2 108 ? -17.407 24.923  -34.702 1.00 108.21 ? 107  PHE B CE1   1 
ATOM   7924 C  CE2   . PHE B 2 108 ? -17.913 23.259  -33.063 1.00 111.59 ? 107  PHE B CE2   1 
ATOM   7925 C  CZ    . PHE B 2 108 ? -17.904 23.675  -34.379 1.00 110.24 ? 107  PHE B CZ    1 
ATOM   7926 N  N     . GLN B 2 109 ? -16.203 28.870  -29.447 1.00 120.85 ? 108  GLN B N     1 
ATOM   7927 C  CA    . GLN B 2 109 ? -15.685 29.459  -28.217 1.00 127.91 ? 108  GLN B CA    1 
ATOM   7928 C  C     . GLN B 2 109 ? -16.781 30.158  -27.422 1.00 133.82 ? 108  GLN B C     1 
ATOM   7929 O  O     . GLN B 2 109 ? -16.677 30.271  -26.195 1.00 128.69 ? 108  GLN B O     1 
ATOM   7930 C  CB    . GLN B 2 109 ? -14.551 30.431  -28.547 1.00 129.78 ? 108  GLN B CB    1 
ATOM   7931 C  CG    . GLN B 2 109 ? -13.706 30.855  -27.355 1.00 122.67 ? 108  GLN B CG    1 
ATOM   7932 C  CD    . GLN B 2 109 ? -14.186 32.147  -26.724 1.00 137.39 ? 108  GLN B CD    1 
ATOM   7933 O  OE1   . GLN B 2 109 ? -15.186 32.726  -27.147 1.00 151.77 ? 108  GLN B OE1   1 
ATOM   7934 N  NE2   . GLN B 2 109 ? -13.468 32.609  -25.707 1.00 145.72 ? 108  GLN B NE2   1 
ATOM   7935 N  N     . ARG B 2 110 ? -17.836 30.628  -28.092 1.00 132.81 ? 109  ARG B N     1 
ATOM   7936 C  CA    . ARG B 2 110 ? -18.927 31.287  -27.383 1.00 133.50 ? 109  ARG B CA    1 
ATOM   7937 C  C     . ARG B 2 110 ? -19.872 30.275  -26.746 1.00 120.15 ? 109  ARG B C     1 
ATOM   7938 O  O     . ARG B 2 110 ? -20.399 30.517  -25.654 1.00 118.89 ? 109  ARG B O     1 
ATOM   7939 C  CB    . ARG B 2 110 ? -19.697 32.208  -28.330 1.00 127.59 ? 109  ARG B CB    1 
ATOM   7940 C  CG    . ARG B 2 110 ? -18.843 33.269  -29.003 1.00 135.76 ? 109  ARG B CG    1 
ATOM   7941 C  CD    . ARG B 2 110 ? -18.145 34.160  -27.991 1.00 134.93 ? 109  ARG B CD    1 
ATOM   7942 N  NE    . ARG B 2 110 ? -17.064 34.927  -28.599 1.00 120.22 ? 109  ARG B NE    1 
ATOM   7943 C  CZ    . ARG B 2 110 ? -17.234 36.043  -29.293 1.00 138.39 ? 109  ARG B CZ    1 
ATOM   7944 N  NH1   . ARG B 2 110 ? -18.438 36.551  -29.500 1.00 147.26 ? 109  ARG B NH1   1 
ATOM   7945 N  NH2   . ARG B 2 110 ? -16.171 36.664  -29.796 1.00 139.01 ? 109  ARG B NH2   1 
ATOM   7946 N  N     . GLN B 2 111 ? -20.100 29.140  -27.410 1.00 119.56 ? 110  GLN B N     1 
ATOM   7947 C  CA    . GLN B 2 111 ? -21.000 28.133  -26.858 1.00 118.37 ? 110  GLN B CA    1 
ATOM   7948 C  C     . GLN B 2 111 ? -20.410 27.464  -25.623 1.00 117.03 ? 110  GLN B C     1 
ATOM   7949 O  O     . GLN B 2 111 ? -21.153 27.105  -24.703 1.00 125.18 ? 110  GLN B O     1 
ATOM   7950 C  CB    . GLN B 2 111 ? -21.332 27.082  -27.917 1.00 121.52 ? 110  GLN B CB    1 
ATOM   7951 C  CG    . GLN B 2 111 ? -22.111 27.614  -29.106 1.00 135.78 ? 110  GLN B CG    1 
ATOM   7952 C  CD    . GLN B 2 111 ? -22.472 26.524  -30.095 1.00 167.53 ? 110  GLN B CD    1 
ATOM   7953 O  OE1   . GLN B 2 111 ? -22.441 25.338  -29.767 1.00 142.10 ? 110  GLN B OE1   1 
ATOM   7954 N  NE2   . GLN B 2 111 ? -22.815 26.921  -31.315 1.00 180.74 ? 110  GLN B NE2   1 
ATOM   7955 N  N     . ILE B 2 112 ? -19.088 27.288  -25.582 1.00 139.34 ? 111  ILE B N     1 
ATOM   7956 C  CA    . ILE B 2 112 ? -18.460 26.642  -24.433 1.00 141.65 ? 111  ILE B CA    1 
ATOM   7957 C  C     . ILE B 2 112 ? -18.598 27.512  -23.190 1.00 152.25 ? 111  ILE B C     1 
ATOM   7958 O  O     . ILE B 2 112 ? -19.006 27.040  -22.123 1.00 129.12 ? 111  ILE B O     1 
ATOM   7959 C  CB    . ILE B 2 112 ? -16.985 26.322  -24.737 1.00 133.48 ? 111  ILE B CB    1 
ATOM   7960 C  CG1   . ILE B 2 112 ? -16.882 25.297  -25.868 1.00 112.50 ? 111  ILE B CG1   1 
ATOM   7961 C  CG2   . ILE B 2 112 ? -16.286 25.810  -23.488 1.00 135.64 ? 111  ILE B CG2   1 
ATOM   7962 C  CD1   . ILE B 2 112 ? -15.468 25.056  -26.345 1.00 108.15 ? 111  ILE B CD1   1 
ATOM   7963 N  N     . LEU B 2 113 ? -18.262 28.799  -23.310 1.00 148.59 ? 112  LEU B N     1 
ATOM   7964 C  CA    . LEU B 2 113 ? -18.345 29.694  -22.160 1.00 123.50 ? 112  LEU B CA    1 
ATOM   7965 C  C     . LEU B 2 113 ? -19.789 29.960  -21.753 1.00 134.29 ? 112  LEU B C     1 
ATOM   7966 O  O     . LEU B 2 113 ? -20.064 30.191  -20.571 1.00 146.96 ? 112  LEU B O     1 
ATOM   7967 C  CB    . LEU B 2 113 ? -17.627 31.008  -22.465 1.00 115.55 ? 112  LEU B CB    1 
ATOM   7968 C  CG    . LEU B 2 113 ? -16.151 30.887  -22.850 1.00 116.46 ? 112  LEU B CG    1 
ATOM   7969 C  CD1   . LEU B 2 113 ? -15.541 32.260  -23.074 1.00 141.48 ? 112  LEU B CD1   1 
ATOM   7970 C  CD2   . LEU B 2 113 ? -15.379 30.119  -21.789 1.00 123.98 ? 112  LEU B CD2   1 
ATOM   7971 N  N     . ARG B 2 114 ? -20.720 29.933  -22.710 1.00 129.05 ? 113  ARG B N     1 
ATOM   7972 C  CA    . ARG B 2 114 ? -22.126 30.137  -22.376 1.00 138.02 ? 113  ARG B CA    1 
ATOM   7973 C  C     . ARG B 2 114 ? -22.689 28.942  -21.617 1.00 146.96 ? 113  ARG B C     1 
ATOM   7974 O  O     . ARG B 2 114 ? -23.532 29.105  -20.727 1.00 145.83 ? 113  ARG B O     1 
ATOM   7975 C  CB    . ARG B 2 114 ? -22.931 30.402  -23.650 1.00 133.76 ? 113  ARG B CB    1 
ATOM   7976 C  CG    . ARG B 2 114 ? -24.407 30.717  -23.429 1.00 145.61 ? 113  ARG B CG    1 
ATOM   7977 C  CD    . ARG B 2 114 ? -25.279 29.479  -23.591 1.00 138.99 ? 113  ARG B CD    1 
ATOM   7978 N  NE    . ARG B 2 114 ? -25.005 28.784  -24.843 1.00 150.86 ? 113  ARG B NE    1 
ATOM   7979 C  CZ    . ARG B 2 114 ? -25.613 29.044  -25.992 1.00 186.12 ? 113  ARG B CZ    1 
ATOM   7980 N  NH1   . ARG B 2 114 ? -26.542 29.981  -26.085 1.00 195.16 ? 113  ARG B NH1   1 
ATOM   7981 N  NH2   . ARG B 2 114 ? -25.279 28.347  -27.075 1.00 180.03 ? 113  ARG B NH2   1 
ATOM   7982 N  N     . VAL B 2 115 ? -22.236 27.734  -21.955 1.00 147.19 ? 114  VAL B N     1 
ATOM   7983 C  CA    . VAL B 2 115 ? -22.734 26.535  -21.288 1.00 145.39 ? 114  VAL B CA    1 
ATOM   7984 C  C     . VAL B 2 115 ? -22.263 26.495  -19.839 1.00 154.50 ? 114  VAL B C     1 
ATOM   7985 O  O     . VAL B 2 115 ? -23.057 26.280  -18.916 1.00 175.86 ? 114  VAL B O     1 
ATOM   7986 C  CB    . VAL B 2 115 ? -22.298 25.276  -22.058 1.00 127.52 ? 114  VAL B CB    1 
ATOM   7987 C  CG1   . VAL B 2 115 ? -22.360 24.058  -21.158 1.00 121.98 ? 114  VAL B CG1   1 
ATOM   7988 C  CG2   . VAL B 2 115 ? -23.176 25.075  -23.281 1.00 140.11 ? 114  VAL B CG2   1 
ATOM   7989 N  N     . LYS B 2 116 ? -20.967 26.707  -19.618 1.00 154.67 ? 115  LYS B N     1 
ATOM   7990 C  CA    . LYS B 2 116 ? -20.393 26.596  -18.284 1.00 152.48 ? 115  LYS B CA    1 
ATOM   7991 C  C     . LYS B 2 116 ? -20.535 27.869  -17.461 1.00 160.73 ? 115  LYS B C     1 
ATOM   7992 O  O     . LYS B 2 116 ? -20.264 27.835  -16.255 1.00 182.98 ? 115  LYS B O     1 
ATOM   7993 C  CB    . LYS B 2 116 ? -18.917 26.208  -18.387 1.00 152.05 ? 115  LYS B CB    1 
ATOM   7994 C  CG    . LYS B 2 116 ? -18.684 24.940  -19.189 1.00 161.61 ? 115  LYS B CG    1 
ATOM   7995 C  CD    . LYS B 2 116 ? -17.207 24.637  -19.339 1.00 155.71 ? 115  LYS B CD    1 
ATOM   7996 C  CE    . LYS B 2 116 ? -16.992 23.365  -20.139 1.00 173.90 ? 115  LYS B CE    1 
ATOM   7997 N  NZ    . LYS B 2 116 ? -17.659 22.192  -19.507 1.00 171.66 ? 115  LYS B NZ    1 
ATOM   7998 N  N     . ASP B 2 117 ? -20.952 28.977  -18.077 1.00 158.61 ? 116  ASP B N     1 
ATOM   7999 C  CA    . ASP B 2 117 ? -21.138 30.256  -17.391 1.00 159.92 ? 116  ASP B CA    1 
ATOM   8000 C  C     . ASP B 2 117 ? -19.853 30.681  -16.674 1.00 166.05 ? 116  ASP B C     1 
ATOM   8001 O  O     . ASP B 2 117 ? -19.827 30.922  -15.466 1.00 174.33 ? 116  ASP B O     1 
ATOM   8002 C  CB    . ASP B 2 117 ? -22.324 30.189  -16.422 1.00 161.39 ? 116  ASP B CB    1 
ATOM   8003 C  CG    . ASP B 2 117 ? -22.791 31.560  -15.971 1.00 194.59 ? 116  ASP B CG    1 
ATOM   8004 O  OD1   . ASP B 2 117 ? -22.272 32.571  -16.490 1.00 197.20 ? 116  ASP B OD1   1 
ATOM   8005 O  OD2   . ASP B 2 117 ? -23.681 31.627  -15.096 1.00 204.21 ? 116  ASP B OD2   1 
ATOM   8006 N  N     . ARG B 2 118 ? -18.776 30.760  -17.452 1.00 163.87 ? 117  ARG B N     1 
ATOM   8007 C  CA    . ARG B 2 118 ? -17.463 31.128  -16.945 1.00 154.09 ? 117  ARG B CA    1 
ATOM   8008 C  C     . ARG B 2 118 ? -16.828 32.153  -17.875 1.00 161.59 ? 117  ARG B C     1 
ATOM   8009 O  O     . ARG B 2 118 ? -17.161 32.240  -19.060 1.00 150.23 ? 117  ARG B O     1 
ATOM   8010 C  CB    . ARG B 2 118 ? -16.546 29.902  -16.810 1.00 161.74 ? 117  ARG B CB    1 
ATOM   8011 C  CG    . ARG B 2 118 ? -17.065 28.830  -15.863 1.00 174.99 ? 117  ARG B CG    1 
ATOM   8012 C  CD    . ARG B 2 118 ? -16.845 29.210  -14.408 1.00 174.07 ? 117  ARG B CD    1 
ATOM   8013 N  NE    . ARG B 2 118 ? -15.433 29.172  -14.044 1.00 190.99 ? 117  ARG B NE    1 
ATOM   8014 C  CZ    . ARG B 2 118 ? -14.966 29.398  -12.824 1.00 202.18 ? 117  ARG B CZ    1 
ATOM   8015 N  NH1   . ARG B 2 118 ? -15.774 29.687  -11.817 1.00 200.86 ? 117  ARG B NH1   1 
ATOM   8016 N  NH2   . ARG B 2 118 ? -13.656 29.331  -12.608 1.00 207.41 ? 117  ARG B NH2   1 
ATOM   8017 N  N     . ASP B 2 119 ? -15.900 32.935  -17.318 1.00 171.34 ? 118  ASP B N     1 
ATOM   8018 C  CA    . ASP B 2 119 ? -15.200 33.932  -18.123 1.00 160.10 ? 118  ASP B CA    1 
ATOM   8019 C  C     . ASP B 2 119 ? -14.214 33.275  -19.079 1.00 150.87 ? 118  ASP B C     1 
ATOM   8020 O  O     . ASP B 2 119 ? -14.035 33.739  -20.211 1.00 159.32 ? 118  ASP B O     1 
ATOM   8021 C  CB    . ASP B 2 119 ? -14.482 34.930  -17.216 1.00 155.85 ? 118  ASP B CB    1 
ATOM   8022 C  CG    . ASP B 2 119 ? -15.435 35.689  -16.315 1.00 175.06 ? 118  ASP B CG    1 
ATOM   8023 O  OD1   . ASP B 2 119 ? -16.608 35.868  -16.706 1.00 179.85 ? 118  ASP B OD1   1 
ATOM   8024 O  OD2   . ASP B 2 119 ? -15.011 36.107  -15.218 1.00 198.19 ? 118  ASP B OD2   1 
ATOM   8025 N  N     . GLU B 2 120 ? -13.566 32.197  -18.644 1.00 164.20 ? 119  GLU B N     1 
ATOM   8026 C  CA    . GLU B 2 120 ? -12.602 31.491  -19.474 1.00 176.16 ? 119  GLU B CA    1 
ATOM   8027 C  C     . GLU B 2 120 ? -12.658 30.008  -19.142 1.00 168.03 ? 119  GLU B C     1 
ATOM   8028 O  O     . GLU B 2 120 ? -13.257 29.593  -18.146 1.00 164.97 ? 119  GLU B O     1 
ATOM   8029 C  CB    . GLU B 2 120 ? -11.184 32.038  -19.278 1.00 184.56 ? 119  GLU B CB    1 
ATOM   8030 C  CG    . GLU B 2 120 ? -10.654 31.887  -17.861 1.00 185.81 ? 119  GLU B CG    1 
ATOM   8031 C  CD    . GLU B 2 120 ? -9.216  32.349  -17.724 1.00 220.11 ? 119  GLU B CD    1 
ATOM   8032 O  OE1   . GLU B 2 120 ? -8.579  32.630  -18.761 1.00 215.58 ? 119  GLU B OE1   1 
ATOM   8033 O  OE2   . GLU B 2 120 ? -8.723  32.431  -16.579 1.00 228.48 ? 119  GLU B OE2   1 
ATOM   8034 N  N     . PHE B 2 121 ? -12.019 29.206  -19.997 1.00 171.51 ? 120  PHE B N     1 
ATOM   8035 C  CA    . PHE B 2 121 ? -11.949 27.766  -19.798 1.00 163.41 ? 120  PHE B CA    1 
ATOM   8036 C  C     . PHE B 2 121 ? -10.764 27.244  -20.589 1.00 158.45 ? 120  PHE B C     1 
ATOM   8037 O  O     . PHE B 2 121 ? -10.491 27.766  -21.679 1.00 168.36 ? 120  PHE B O     1 
ATOM   8038 C  CB    . PHE B 2 121 ? -13.243 27.075  -20.243 1.00 166.12 ? 120  PHE B CB    1 
ATOM   8039 C  CG    . PHE B 2 121 ? -13.504 25.772  -19.544 1.00 162.03 ? 120  PHE B CG    1 
ATOM   8040 C  CD1   . PHE B 2 121 ? -13.934 25.755  -18.227 1.00 158.73 ? 120  PHE B CD1   1 
ATOM   8041 C  CD2   . PHE B 2 121 ? -13.319 24.567  -20.200 1.00 163.32 ? 120  PHE B CD2   1 
ATOM   8042 C  CE1   . PHE B 2 121 ? -14.172 24.559  -17.576 1.00 158.47 ? 120  PHE B CE1   1 
ATOM   8043 C  CE2   . PHE B 2 121 ? -13.555 23.369  -19.554 1.00 160.40 ? 120  PHE B CE2   1 
ATOM   8044 C  CZ    . PHE B 2 121 ? -13.983 23.365  -18.241 1.00 159.89 ? 120  PHE B CZ    1 
ATOM   8045 N  N     . PRO B 2 122 ? -10.034 26.239  -20.083 1.00 155.89 ? 121  PRO B N     1 
ATOM   8046 C  CA    . PRO B 2 122 ? -8.836  25.761  -20.789 1.00 164.70 ? 121  PRO B CA    1 
ATOM   8047 C  C     . PRO B 2 122 ? -9.117  25.258  -22.197 1.00 166.79 ? 121  PRO B C     1 
ATOM   8048 O  O     . PRO B 2 122 ? -9.758  24.219  -22.384 1.00 158.63 ? 121  PRO B O     1 
ATOM   8049 C  CB    . PRO B 2 122 ? -8.322  24.630  -19.885 1.00 161.78 ? 121  PRO B CB    1 
ATOM   8050 C  CG    . PRO B 2 122 ? -9.484  24.261  -19.016 1.00 162.44 ? 121  PRO B CG    1 
ATOM   8051 C  CD    . PRO B 2 122 ? -10.237 25.533  -18.808 1.00 159.71 ? 121  PRO B CD    1 
ATOM   8052 N  N     . MET B 2 123 ? -8.634  25.999  -23.192 1.00 161.67 ? 122  MET B N     1 
ATOM   8053 C  CA    . MET B 2 123 ? -8.768  25.615  -24.589 1.00 136.44 ? 122  MET B CA    1 
ATOM   8054 C  C     . MET B 2 123 ? -7.607  26.211  -25.371 1.00 138.03 ? 122  MET B C     1 
ATOM   8055 O  O     . MET B 2 123 ? -7.109  27.291  -25.043 1.00 139.77 ? 122  MET B O     1 
ATOM   8056 C  CB    . MET B 2 123 ? -10.110 26.072  -25.176 1.00 124.18 ? 122  MET B CB    1 
ATOM   8057 C  CG    . MET B 2 123 ? -10.358 27.566  -25.073 1.00 153.53 ? 122  MET B CG    1 
ATOM   8058 S  SD    . MET B 2 123 ? -11.991 28.053  -25.661 1.00 148.07 ? 122  MET B SD    1 
ATOM   8059 C  CE    . MET B 2 123 ? -13.039 27.210  -24.480 1.00 122.75 ? 122  MET B CE    1 
ATOM   8060 N  N     . ILE B 2 124 ? -7.175  25.492  -26.405 1.00 144.25 ? 123  ILE B N     1 
ATOM   8061 C  CA    . ILE B 2 124 ? -6.023  25.875  -27.213 1.00 127.33 ? 123  ILE B CA    1 
ATOM   8062 C  C     . ILE B 2 124 ? -6.464  25.988  -28.665 1.00 123.08 ? 123  ILE B C     1 
ATOM   8063 O  O     . ILE B 2 124 ? -7.098  25.070  -29.199 1.00 132.10 ? 123  ILE B O     1 
ATOM   8064 C  CB    . ILE B 2 124 ? -4.869  24.865  -27.070 1.00 133.72 ? 123  ILE B CB    1 
ATOM   8065 C  CG1   . ILE B 2 124 ? -4.516  24.656  -25.596 1.00 131.95 ? 123  ILE B CG1   1 
ATOM   8066 C  CG2   . ILE B 2 124 ? -3.648  25.335  -27.843 1.00 134.09 ? 123  ILE B CG2   1 
ATOM   8067 C  CD1   . ILE B 2 124 ? -4.050  25.913  -24.895 1.00 168.46 ? 123  ILE B CD1   1 
ATOM   8068 N  N     . LEU B 2 125 ? -6.129  27.110  -29.298 1.00 119.78 ? 124  LEU B N     1 
ATOM   8069 C  CA    . LEU B 2 125 ? -6.451  27.328  -30.703 1.00 118.19 ? 124  LEU B CA    1 
ATOM   8070 C  C     . LEU B 2 125 ? -5.395  26.657  -31.574 1.00 135.93 ? 124  LEU B C     1 
ATOM   8071 O  O     . LEU B 2 125 ? -4.214  27.015  -31.513 1.00 121.12 ? 124  LEU B O     1 
ATOM   8072 C  CB    . LEU B 2 125 ? -6.533  28.823  -31.004 1.00 133.88 ? 124  LEU B CB    1 
ATOM   8073 C  CG    . LEU B 2 125 ? -6.925  29.232  -32.426 1.00 117.92 ? 124  LEU B CG    1 
ATOM   8074 C  CD1   . LEU B 2 125 ? -8.332  28.761  -32.751 1.00 135.66 ? 124  LEU B CD1   1 
ATOM   8075 C  CD2   . LEU B 2 125 ? -6.810  30.737  -32.602 1.00 118.89 ? 124  LEU B CD2   1 
ATOM   8076 N  N     . ILE B 2 126 ? -5.818  25.691  -32.386 1.00 121.13 ? 125  ILE B N     1 
ATOM   8077 C  CA    . ILE B 2 126 ? -4.917  24.887  -33.202 1.00 117.34 ? 125  ILE B CA    1 
ATOM   8078 C  C     . ILE B 2 126 ? -5.157  25.214  -34.669 1.00 129.02 ? 125  ILE B C     1 
ATOM   8079 O  O     . ILE B 2 126 ? -6.305  25.230  -35.130 1.00 115.61 ? 125  ILE B O     1 
ATOM   8080 C  CB    . ILE B 2 126 ? -5.110  23.383  -32.939 1.00 116.34 ? 125  ILE B CB    1 
ATOM   8081 C  CG1   . ILE B 2 126 ? -4.963  23.076  -31.448 1.00 117.48 ? 125  ILE B CG1   1 
ATOM   8082 C  CG2   . ILE B 2 126 ? -4.118  22.567  -33.753 1.00 117.21 ? 125  ILE B CG2   1 
ATOM   8083 C  CD1   . ILE B 2 126 ? -3.573  23.316  -30.908 1.00 120.57 ? 125  ILE B CD1   1 
ATOM   8084 N  N     . GLY B 2 127 ? -4.074  25.473  -35.400 1.00 117.84 ? 126  GLY B N     1 
ATOM   8085 C  CA    . GLY B 2 127 ? -4.147  25.666  -36.835 1.00 117.12 ? 126  GLY B CA    1 
ATOM   8086 C  C     . GLY B 2 127 ? -3.588  24.476  -37.587 1.00 117.16 ? 126  GLY B C     1 
ATOM   8087 O  O     . GLY B 2 127 ? -2.370  24.287  -37.642 1.00 145.85 ? 126  GLY B O     1 
ATOM   8088 N  N     . ASN B 2 128 ? -4.466  23.668  -38.172 1.00 115.03 ? 127  ASN B N     1 
ATOM   8089 C  CA    . ASN B 2 128 ? -4.063  22.413  -38.784 1.00 115.00 ? 127  ASN B CA    1 
ATOM   8090 C  C     . ASN B 2 128 ? -3.772  22.596  -40.273 1.00 126.43 ? 127  ASN B C     1 
ATOM   8091 O  O     . ASN B 2 128 ? -3.972  23.669  -40.848 1.00 132.10 ? 127  ASN B O     1 
ATOM   8092 C  CB    . ASN B 2 128 ? -5.145  21.353  -38.572 1.00 116.90 ? 127  ASN B CB    1 
ATOM   8093 C  CG    . ASN B 2 128 ? -4.620  19.942  -38.742 1.00 121.30 ? 127  ASN B CG    1 
ATOM   8094 O  OD1   . ASN B 2 128 ? -3.416  19.702  -38.655 1.00 136.06 ? 127  ASN B OD1   1 
ATOM   8095 N  ND2   . ASN B 2 128 ? -5.522  19.001  -38.989 1.00 122.76 ? 127  ASN B ND2   1 
ATOM   8096 N  N     . LYS B 2 129 ? -3.285  21.518  -40.894 1.00 115.61 ? 128  LYS B N     1 
ATOM   8097 C  CA    . LYS B 2 129 ? -2.947  21.491  -42.319 1.00 116.06 ? 128  LYS B CA    1 
ATOM   8098 C  C     . LYS B 2 129 ? -1.901  22.549  -42.662 1.00 118.27 ? 128  LYS B C     1 
ATOM   8099 O  O     . LYS B 2 129 ? -1.944  23.171  -43.726 1.00 118.35 ? 128  LYS B O     1 
ATOM   8100 C  CB    . LYS B 2 129 ? -4.193  21.651  -43.194 1.00 114.26 ? 128  LYS B CB    1 
ATOM   8101 C  CG    . LYS B 2 129 ? -5.213  20.536  -43.025 1.00 111.81 ? 128  LYS B CG    1 
ATOM   8102 C  CD    . LYS B 2 129 ? -6.322  20.642  -44.056 1.00 132.99 ? 128  LYS B CD    1 
ATOM   8103 C  CE    . LYS B 2 129 ? -7.375  19.569  -43.847 1.00 109.19 ? 128  LYS B CE    1 
ATOM   8104 N  NZ    . LYS B 2 129 ? -8.508  19.717  -44.801 1.00 116.89 ? 128  LYS B NZ    1 
ATOM   8105 N  N     . ALA B 2 130 ? -0.946  22.750  -41.752 1.00 120.22 ? 129  ALA B N     1 
ATOM   8106 C  CA    . ALA B 2 130 ? 0.110   23.727  -41.985 1.00 122.54 ? 129  ALA B CA    1 
ATOM   8107 C  C     . ALA B 2 130 ? 1.103   23.270  -43.044 1.00 124.24 ? 129  ALA B C     1 
ATOM   8108 O  O     . ALA B 2 130 ? 1.863   24.096  -43.558 1.00 125.97 ? 129  ALA B O     1 
ATOM   8109 C  CB    . ALA B 2 130 ? 0.843   24.031  -40.679 1.00 124.63 ? 129  ALA B CB    1 
ATOM   8110 N  N     . ASP B 2 131 ? 1.117   21.978  -43.381 1.00 123.91 ? 130  ASP B N     1 
ATOM   8111 C  CA    . ASP B 2 131 ? 2.011   21.506  -44.432 1.00 125.62 ? 130  ASP B CA    1 
ATOM   8112 C  C     . ASP B 2 131 ? 1.563   21.988  -45.806 1.00 124.85 ? 130  ASP B C     1 
ATOM   8113 O  O     . ASP B 2 131 ? 2.400   22.183  -46.695 1.00 158.85 ? 130  ASP B O     1 
ATOM   8114 C  CB    . ASP B 2 131 ? 2.097   19.981  -44.412 1.00 125.57 ? 130  ASP B CB    1 
ATOM   8115 C  CG    . ASP B 2 131 ? 0.776   19.319  -44.750 1.00 127.78 ? 130  ASP B CG    1 
ATOM   8116 O  OD1   . ASP B 2 131 ? -0.202  19.511  -43.996 1.00 121.56 ? 130  ASP B OD1   1 
ATOM   8117 O  OD2   . ASP B 2 131 ? 0.713   18.618  -45.780 1.00 131.26 ? 130  ASP B OD2   1 
ATOM   8118 N  N     . LEU B 2 132 ? 0.259   22.187  -45.998 1.00 122.33 ? 131  LEU B N     1 
ATOM   8119 C  CA    . LEU B 2 132 ? -0.278  22.666  -47.271 1.00 121.61 ? 131  LEU B CA    1 
ATOM   8120 C  C     . LEU B 2 132 ? -0.097  24.182  -47.387 1.00 139.91 ? 131  LEU B C     1 
ATOM   8121 O  O     . LEU B 2 132 ? -1.051  24.958  -47.446 1.00 157.74 ? 131  LEU B O     1 
ATOM   8122 C  CB    . LEU B 2 132 ? -1.742  22.267  -47.407 1.00 120.77 ? 131  LEU B CB    1 
ATOM   8123 C  CG    . LEU B 2 132 ? -2.055  20.769  -47.373 1.00 117.95 ? 131  LEU B CG    1 
ATOM   8124 C  CD1   . LEU B 2 132 ? -3.554  20.532  -47.444 1.00 116.02 ? 131  LEU B CD1   1 
ATOM   8125 C  CD2   . LEU B 2 132 ? -1.344  20.046  -48.505 1.00 148.68 ? 131  LEU B CD2   1 
ATOM   8126 N  N     . ASP B 2 133 ? 1.172   24.596  -47.417 1.00 162.18 ? 132  ASP B N     1 
ATOM   8127 C  CA    . ASP B 2 133 ? 1.488   26.018  -47.515 1.00 164.40 ? 132  ASP B CA    1 
ATOM   8128 C  C     . ASP B 2 133 ? 1.080   26.595  -48.864 1.00 150.44 ? 132  ASP B C     1 
ATOM   8129 O  O     . ASP B 2 133 ? 0.755   27.784  -48.954 1.00 167.35 ? 132  ASP B O     1 
ATOM   8130 C  CB    . ASP B 2 133 ? 2.980   26.242  -47.273 1.00 187.62 ? 132  ASP B CB    1 
ATOM   8131 C  CG    . ASP B 2 133 ? 3.385   25.968  -45.838 1.00 194.43 ? 132  ASP B CG    1 
ATOM   8132 O  OD1   . ASP B 2 133 ? 2.685   26.447  -44.921 1.00 166.53 ? 132  ASP B OD1   1 
ATOM   8133 O  OD2   . ASP B 2 133 ? 4.400   25.271  -45.627 1.00 198.17 ? 132  ASP B OD2   1 
ATOM   8134 N  N     . HIS B 2 134 ? 1.088   25.776  -49.916 1.00 138.06 ? 133  HIS B N     1 
ATOM   8135 C  CA    . HIS B 2 134 ? 0.693   26.242  -51.239 1.00 125.58 ? 133  HIS B CA    1 
ATOM   8136 C  C     . HIS B 2 134 ? -0.801  26.511  -51.348 1.00 123.07 ? 133  HIS B C     1 
ATOM   8137 O  O     . HIS B 2 134 ? -1.237  27.086  -52.351 1.00 122.99 ? 133  HIS B O     1 
ATOM   8138 C  CB    . HIS B 2 134 ? 1.118   25.223  -52.299 1.00 150.41 ? 133  HIS B CB    1 
ATOM   8139 C  CG    . HIS B 2 134 ? 0.532   23.860  -52.099 1.00 125.02 ? 133  HIS B CG    1 
ATOM   8140 N  ND1   . HIS B 2 134 ? 1.007   22.977  -51.154 1.00 126.59 ? 133  HIS B ND1   1 
ATOM   8141 C  CD2   . HIS B 2 134 ? -0.486  23.226  -52.728 1.00 123.35 ? 133  HIS B CD2   1 
ATOM   8142 C  CE1   . HIS B 2 134 ? 0.304   21.859  -51.206 1.00 152.16 ? 133  HIS B CE1   1 
ATOM   8143 N  NE2   . HIS B 2 134 ? -0.608  21.985  -52.152 1.00 166.23 ? 133  HIS B NE2   1 
ATOM   8144 N  N     . GLN B 2 135 ? -1.593  26.114  -50.348 1.00 136.62 ? 134  GLN B N     1 
ATOM   8145 C  CA    . GLN B 2 135 ? -3.031  26.355  -50.347 1.00 133.01 ? 134  GLN B CA    1 
ATOM   8146 C  C     . GLN B 2 135 ? -3.486  27.059  -49.073 1.00 118.93 ? 134  GLN B C     1 
ATOM   8147 O  O     . GLN B 2 135 ? -4.685  27.075  -48.775 1.00 116.12 ? 134  GLN B O     1 
ATOM   8148 C  CB    . GLN B 2 135 ? -3.799  25.043  -50.532 1.00 119.40 ? 134  GLN B CB    1 
ATOM   8149 C  CG    . GLN B 2 135 ? -3.596  24.398  -51.893 1.00 117.98 ? 134  GLN B CG    1 
ATOM   8150 C  CD    . GLN B 2 135 ? -4.145  22.987  -51.960 1.00 129.68 ? 134  GLN B CD    1 
ATOM   8151 O  OE1   . GLN B 2 135 ? -4.554  22.419  -50.948 1.00 159.07 ? 134  GLN B OE1   1 
ATOM   8152 N  NE2   . GLN B 2 135 ? -4.154  22.413  -53.158 1.00 155.24 ? 134  GLN B NE2   1 
ATOM   8153 N  N     . ARG B 2 136 ? -2.557  27.639  -48.317 1.00 119.61 ? 135  ARG B N     1 
ATOM   8154 C  CA    . ARG B 2 136 ? -2.914  28.318  -47.079 1.00 119.13 ? 135  ARG B CA    1 
ATOM   8155 C  C     . ARG B 2 136 ? -3.637  29.625  -47.377 1.00 146.21 ? 135  ARG B C     1 
ATOM   8156 O  O     . ARG B 2 136 ? -3.157  30.451  -48.160 1.00 125.40 ? 135  ARG B O     1 
ATOM   8157 C  CB    . ARG B 2 136 ? -1.665  28.588  -46.241 1.00 121.24 ? 135  ARG B CB    1 
ATOM   8158 C  CG    . ARG B 2 136 ? -1.915  29.505  -45.052 1.00 136.00 ? 135  ARG B CG    1 
ATOM   8159 C  CD    . ARG B 2 136 ? -0.616  29.948  -44.396 1.00 145.50 ? 135  ARG B CD    1 
ATOM   8160 N  NE    . ARG B 2 136 ? -0.018  28.897  -43.582 1.00 126.33 ? 135  ARG B NE    1 
ATOM   8161 C  CZ    . ARG B 2 136 ? -0.197  28.771  -42.274 1.00 124.14 ? 135  ARG B CZ    1 
ATOM   8162 N  NH1   . ARG B 2 136 ? -0.957  29.615  -41.596 1.00 123.39 ? 135  ARG B NH1   1 
ATOM   8163 N  NH2   . ARG B 2 136 ? 0.404   27.775  -41.630 1.00 152.94 ? 135  ARG B NH2   1 
ATOM   8164 N  N     . GLN B 2 137 ? -4.798  29.811  -46.749 1.00 134.38 ? 136  GLN B N     1 
ATOM   8165 C  CA    . GLN B 2 137 ? -5.564  31.041  -46.874 1.00 125.73 ? 136  GLN B CA    1 
ATOM   8166 C  C     . GLN B 2 137 ? -5.595  31.862  -45.594 1.00 130.08 ? 136  GLN B C     1 
ATOM   8167 O  O     . GLN B 2 137 ? -5.968  33.040  -45.643 1.00 140.39 ? 136  GLN B O     1 
ATOM   8168 C  CB    . GLN B 2 137 ? -7.002  30.732  -47.315 1.00 126.62 ? 136  GLN B CB    1 
ATOM   8169 C  CG    . GLN B 2 137 ? -7.119  30.213  -48.738 1.00 141.40 ? 136  GLN B CG    1 
ATOM   8170 C  CD    . GLN B 2 137 ? -8.552  29.910  -49.130 1.00 170.98 ? 136  GLN B CD    1 
ATOM   8171 O  OE1   . GLN B 2 137 ? -9.414  29.712  -48.273 1.00 152.12 ? 136  GLN B OE1   1 
ATOM   8172 N  NE2   . GLN B 2 137 ? -8.815  29.876  -50.431 1.00 163.73 ? 136  GLN B NE2   1 
ATOM   8173 N  N     . VAL B 2 138 ? -5.220  31.280  -44.458 1.00 125.90 ? 137  VAL B N     1 
ATOM   8174 C  CA    . VAL B 2 138 ? -5.143  31.986  -43.184 1.00 117.97 ? 137  VAL B CA    1 
ATOM   8175 C  C     . VAL B 2 138 ? -3.684  31.972  -42.752 1.00 129.84 ? 137  VAL B C     1 
ATOM   8176 O  O     . VAL B 2 138 ? -3.161  30.926  -42.348 1.00 148.41 ? 137  VAL B O     1 
ATOM   8177 C  CB    . VAL B 2 138 ? -6.040  31.350  -42.113 1.00 116.97 ? 137  VAL B CB    1 
ATOM   8178 C  CG1   . VAL B 2 138 ? -6.071  32.220  -40.865 1.00 117.21 ? 137  VAL B CG1   1 
ATOM   8179 C  CG2   . VAL B 2 138 ? -7.442  31.125  -42.654 1.00 114.14 ? 137  VAL B CG2   1 
ATOM   8180 N  N     . THR B 2 139 ? -3.026  33.126  -42.835 1.00 138.42 ? 138  THR B N     1 
ATOM   8181 C  CA    . THR B 2 139 ? -1.621  33.205  -42.473 1.00 149.48 ? 138  THR B CA    1 
ATOM   8182 C  C     . THR B 2 139 ? -1.451  33.084  -40.958 1.00 155.48 ? 138  THR B C     1 
ATOM   8183 O  O     . THR B 2 139 ? -2.419  33.056  -40.192 1.00 132.73 ? 138  THR B O     1 
ATOM   8184 C  CB    . THR B 2 139 ? -1.005  34.510  -42.976 1.00 128.39 ? 138  THR B CB    1 
ATOM   8185 O  OG1   . THR B 2 139 ? 0.403   34.509  -42.710 1.00 159.02 ? 138  THR B OG1   1 
ATOM   8186 C  CG2   . THR B 2 139 ? -1.642  35.701  -42.283 1.00 126.52 ? 138  THR B CG2   1 
ATOM   8187 N  N     . GLN B 2 140 ? -0.189  33.014  -40.529 1.00 161.15 ? 139  GLN B N     1 
ATOM   8188 C  CA    . GLN B 2 140 ? 0.100   32.816  -39.112 1.00 147.90 ? 139  GLN B CA    1 
ATOM   8189 C  C     . GLN B 2 140 ? -0.298  34.033  -38.286 1.00 172.14 ? 139  GLN B C     1 
ATOM   8190 O  O     . GLN B 2 140 ? -0.774  33.889  -37.154 1.00 156.82 ? 139  GLN B O     1 
ATOM   8191 C  CB    . GLN B 2 140 ? 1.583   32.501  -38.917 1.00 154.26 ? 139  GLN B CB    1 
ATOM   8192 C  CG    . GLN B 2 140 ? 2.086   31.337  -39.752 1.00 172.16 ? 139  GLN B CG    1 
ATOM   8193 C  CD    . GLN B 2 140 ? 3.480   30.896  -39.354 1.00 162.62 ? 139  GLN B CD    1 
ATOM   8194 O  OE1   . GLN B 2 140 ? 4.037   31.375  -38.367 1.00 159.86 ? 139  GLN B OE1   1 
ATOM   8195 N  NE2   . GLN B 2 140 ? 4.052   29.977  -40.123 1.00 167.72 ? 139  GLN B NE2   1 
ATOM   8196 N  N     . GLU B 2 141 ? -0.111  35.237  -38.834 1.00 175.10 ? 140  GLU B N     1 
ATOM   8197 C  CA    . GLU B 2 141 ? -0.423  36.451  -38.084 1.00 148.79 ? 140  GLU B CA    1 
ATOM   8198 C  C     . GLU B 2 141 ? -1.908  36.530  -37.749 1.00 152.18 ? 140  GLU B C     1 
ATOM   8199 O  O     . GLU B 2 141 ? -2.284  37.019  -36.678 1.00 168.20 ? 140  GLU B O     1 
ATOM   8200 C  CB    . GLU B 2 141 ? 0.018   37.685  -38.871 1.00 164.12 ? 140  GLU B CB    1 
ATOM   8201 C  CG    . GLU B 2 141 ? 1.519   37.948  -38.844 1.00 196.24 ? 140  GLU B CG    1 
ATOM   8202 C  CD    . GLU B 2 141 ? 2.315   36.927  -39.636 1.00 193.92 ? 140  GLU B CD    1 
ATOM   8203 O  OE1   . GLU B 2 141 ? 1.724   36.250  -40.504 1.00 192.98 ? 140  GLU B OE1   1 
ATOM   8204 O  OE2   . GLU B 2 141 ? 3.533   36.801  -39.389 1.00 205.06 ? 140  GLU B OE2   1 
ATOM   8205 N  N     . GLU B 2 142 ? -2.767  36.053  -38.652 1.00 126.33 ? 141  GLU B N     1 
ATOM   8206 C  CA    . GLU B 2 142 ? -4.192  35.995  -38.354 1.00 124.21 ? 141  GLU B CA    1 
ATOM   8207 C  C     . GLU B 2 142 ? -4.515  34.939  -37.306 1.00 144.47 ? 141  GLU B C     1 
ATOM   8208 O  O     . GLU B 2 142 ? -5.562  35.028  -36.656 1.00 158.74 ? 141  GLU B O     1 
ATOM   8209 C  CB    . GLU B 2 142 ? -4.989  35.721  -39.630 1.00 122.24 ? 141  GLU B CB    1 
ATOM   8210 C  CG    . GLU B 2 142 ? -4.739  36.721  -40.742 1.00 123.19 ? 141  GLU B CG    1 
ATOM   8211 C  CD    . GLU B 2 142 ? -5.497  36.382  -42.009 1.00 121.46 ? 141  GLU B CD    1 
ATOM   8212 O  OE1   . GLU B 2 142 ? -6.617  35.840  -41.905 1.00 137.76 ? 141  GLU B OE1   1 
ATOM   8213 O  OE2   . GLU B 2 142 ? -4.971  36.652  -43.109 1.00 160.86 ? 141  GLU B OE2   1 
ATOM   8214 N  N     . GLY B 2 143 ? -3.642  33.945  -37.130 1.00 131.40 ? 142  GLY B N     1 
ATOM   8215 C  CA    . GLY B 2 143 ? -3.883  32.936  -36.112 1.00 132.58 ? 142  GLY B CA    1 
ATOM   8216 C  C     . GLY B 2 143 ? -3.708  33.481  -34.707 1.00 136.21 ? 142  GLY B C     1 
ATOM   8217 O  O     . GLY B 2 143 ? -4.594  33.342  -33.859 1.00 123.74 ? 142  GLY B O     1 
ATOM   8218 N  N     . GLN B 2 144 ? -2.560  34.111  -34.441 1.00 132.67 ? 143  GLN B N     1 
ATOM   8219 C  CA    . GLN B 2 144 ? -2.342  34.732  -33.141 1.00 133.88 ? 143  GLN B CA    1 
ATOM   8220 C  C     . GLN B 2 144 ? -3.274  35.912  -32.905 1.00 156.01 ? 143  GLN B C     1 
ATOM   8221 O  O     . GLN B 2 144 ? -3.446  36.330  -31.754 1.00 158.49 ? 143  GLN B O     1 
ATOM   8222 C  CB    . GLN B 2 144 ? -0.886  35.181  -33.002 1.00 137.74 ? 143  GLN B CB    1 
ATOM   8223 C  CG    . GLN B 2 144 ? 0.130   34.060  -33.151 1.00 154.96 ? 143  GLN B CG    1 
ATOM   8224 C  CD    . GLN B 2 144 ? 0.804   34.062  -34.507 1.00 157.32 ? 143  GLN B CD    1 
ATOM   8225 O  OE1   . GLN B 2 144 ? 0.844   35.085  -35.191 1.00 173.06 ? 143  GLN B OE1   1 
ATOM   8226 N  NE2   . GLN B 2 144 ? 1.339   32.914  -34.905 1.00 158.21 ? 143  GLN B NE2   1 
ATOM   8227 N  N     . GLN B 2 145 ? -3.870  36.461  -33.966 1.00 150.79 ? 144  GLN B N     1 
ATOM   8228 C  CA    . GLN B 2 145 ? -4.884  37.497  -33.799 1.00 141.57 ? 144  GLN B CA    1 
ATOM   8229 C  C     . GLN B 2 145 ? -6.094  36.957  -33.048 1.00 148.52 ? 144  GLN B C     1 
ATOM   8230 O  O     . GLN B 2 145 ? -6.602  37.596  -32.119 1.00 159.75 ? 144  GLN B O     1 
ATOM   8231 C  CB    . GLN B 2 145 ? -5.295  38.049  -35.165 1.00 146.65 ? 144  GLN B CB    1 
ATOM   8232 C  CG    . GLN B 2 145 ? -6.569  38.882  -35.151 1.00 176.85 ? 144  GLN B CG    1 
ATOM   8233 C  CD    . GLN B 2 145 ? -6.407  40.199  -34.417 1.00 164.84 ? 144  GLN B CD    1 
ATOM   8234 O  OE1   . GLN B 2 145 ? -5.291  40.661  -34.180 1.00 163.26 ? 144  GLN B OE1   1 
ATOM   8235 N  NE2   . GLN B 2 145 ? -7.527  40.813  -34.054 1.00 164.00 ? 144  GLN B NE2   1 
ATOM   8236 N  N     . LEU B 2 146 ? -6.570  35.772  -33.438 1.00 144.83 ? 145  LEU B N     1 
ATOM   8237 C  CA    . LEU B 2 146 ? -7.669  35.137  -32.721 1.00 135.27 ? 145  LEU B CA    1 
ATOM   8238 C  C     . LEU B 2 146 ? -7.232  34.587  -31.370 1.00 141.44 ? 145  LEU B C     1 
ATOM   8239 O  O     . LEU B 2 146 ? -8.083  34.363  -30.503 1.00 140.19 ? 145  LEU B O     1 
ATOM   8240 C  CB    . LEU B 2 146 ? -8.277  34.019  -33.569 1.00 128.44 ? 145  LEU B CB    1 
ATOM   8241 C  CG    . LEU B 2 146 ? -9.600  34.339  -34.268 1.00 156.65 ? 145  LEU B CG    1 
ATOM   8242 C  CD1   . LEU B 2 146 ? -10.729 34.428  -33.254 1.00 141.99 ? 145  LEU B CD1   1 
ATOM   8243 C  CD2   . LEU B 2 146 ? -9.492  35.632  -35.063 1.00 170.32 ? 145  LEU B CD2   1 
ATOM   8244 N  N     . ALA B 2 147 ? -5.931  34.361  -31.174 1.00 139.90 ? 146  ALA B N     1 
ATOM   8245 C  CA    . ALA B 2 147 ? -5.447  33.912  -29.873 1.00 140.66 ? 146  ALA B CA    1 
ATOM   8246 C  C     . ALA B 2 147 ? -5.612  35.004  -28.824 1.00 160.59 ? 146  ALA B C     1 
ATOM   8247 O  O     . ALA B 2 147 ? -6.087  34.745  -27.713 1.00 167.06 ? 146  ALA B O     1 
ATOM   8248 C  CB    . ALA B 2 147 ? -3.985  33.479  -29.978 1.00 137.63 ? 146  ALA B CB    1 
ATOM   8249 N  N     . ARG B 2 148 ? -5.221  36.235  -29.161 1.00 166.39 ? 147  ARG B N     1 
ATOM   8250 C  CA    . ARG B 2 148 ? -5.403  37.345  -28.233 1.00 147.98 ? 147  ARG B CA    1 
ATOM   8251 C  C     . ARG B 2 148 ? -6.868  37.741  -28.115 1.00 143.04 ? 147  ARG B C     1 
ATOM   8252 O  O     . ARG B 2 148 ? -7.305  38.188  -27.048 1.00 139.23 ? 147  ARG B O     1 
ATOM   8253 C  CB    . ARG B 2 148 ? -4.564  38.544  -28.677 1.00 154.70 ? 147  ARG B CB    1 
ATOM   8254 C  CG    . ARG B 2 148 ? -3.105  38.215  -28.951 1.00 157.89 ? 147  ARG B CG    1 
ATOM   8255 C  CD    . ARG B 2 148 ? -2.308  39.471  -29.266 1.00 166.21 ? 147  ARG B CD    1 
ATOM   8256 N  NE    . ARG B 2 148 ? -2.883  40.223  -30.374 1.00 193.72 ? 147  ARG B NE    1 
ATOM   8257 C  CZ    . ARG B 2 148 ? -2.513  40.095  -31.641 1.00 182.27 ? 147  ARG B CZ    1 
ATOM   8258 N  NH1   . ARG B 2 148 ? -1.563  39.248  -32.002 1.00 158.96 ? 147  ARG B NH1   1 
ATOM   8259 N  NH2   . ARG B 2 148 ? -3.111  40.836  -32.570 1.00 170.52 ? 147  ARG B NH2   1 
ATOM   8260 N  N     . GLN B 2 149 ? -7.639  37.585  -29.194 1.00 145.53 ? 148  GLN B N     1 
ATOM   8261 C  CA    . GLN B 2 149 ? -9.059  37.918  -29.150 1.00 142.92 ? 148  GLN B CA    1 
ATOM   8262 C  C     . GLN B 2 149 ? -9.823  36.949  -28.256 1.00 151.55 ? 148  GLN B C     1 
ATOM   8263 O  O     . GLN B 2 149 ? -10.643 37.365  -27.429 1.00 155.16 ? 148  GLN B O     1 
ATOM   8264 C  CB    . GLN B 2 149 ? -9.638  37.920  -30.565 1.00 143.82 ? 148  GLN B CB    1 
ATOM   8265 C  CG    . GLN B 2 149 ? -11.150 38.045  -30.620 1.00 166.29 ? 148  GLN B CG    1 
ATOM   8266 C  CD    . GLN B 2 149 ? -11.689 37.957  -32.034 1.00 174.74 ? 148  GLN B CD    1 
ATOM   8267 O  OE1   . GLN B 2 149 ? -11.078 38.461  -32.976 1.00 175.63 ? 148  GLN B OE1   1 
ATOM   8268 N  NE2   . GLN B 2 149 ? -12.836 37.306  -32.190 1.00 153.59 ? 148  GLN B NE2   1 
ATOM   8269 N  N     . LEU B 2 150 ? -9.569  35.652  -28.408 1.00 149.88 ? 149  LEU B N     1 
ATOM   8270 C  CA    . LEU B 2 150 ? -10.210 34.633  -27.589 1.00 170.45 ? 149  LEU B CA    1 
ATOM   8271 C  C     . LEU B 2 150 ? -9.479  34.382  -26.277 1.00 155.69 ? 149  LEU B C     1 
ATOM   8272 O  O     . LEU B 2 150 ? -9.934  33.552  -25.483 1.00 154.19 ? 149  LEU B O     1 
ATOM   8273 C  CB    . LEU B 2 150 ? -10.326 33.320  -28.373 1.00 146.92 ? 149  LEU B CB    1 
ATOM   8274 C  CG    . LEU B 2 150 ? -11.127 33.373  -29.676 1.00 138.66 ? 149  LEU B CG    1 
ATOM   8275 C  CD1   . LEU B 2 150 ? -11.136 32.014  -30.357 1.00 141.83 ? 149  LEU B CD1   1 
ATOM   8276 C  CD2   . LEU B 2 150 ? -12.546 33.858  -29.419 1.00 145.04 ? 149  LEU B CD2   1 
ATOM   8277 N  N     . LYS B 2 151 ? -8.366  35.079  -26.034 1.00 148.65 ? 150  LYS B N     1 
ATOM   8278 C  CA    . LYS B 2 151 ? -7.576  34.924  -24.810 1.00 160.20 ? 150  LYS B CA    1 
ATOM   8279 C  C     . LYS B 2 151 ? -7.120  33.478  -24.622 1.00 143.84 ? 150  LYS B C     1 
ATOM   8280 O  O     . LYS B 2 151 ? -7.111  32.949  -23.509 1.00 151.35 ? 150  LYS B O     1 
ATOM   8281 C  CB    . LYS B 2 151 ? -8.348  35.419  -23.584 1.00 159.32 ? 150  LYS B CB    1 
ATOM   8282 C  CG    . LYS B 2 151 ? -8.708  36.895  -23.637 1.00 155.58 ? 150  LYS B CG    1 
ATOM   8283 C  CD    . LYS B 2 151 ? -9.463  37.328  -22.391 1.00 146.89 ? 150  LYS B CD    1 
ATOM   8284 C  CE    . LYS B 2 151 ? -9.822  38.804  -22.452 1.00 192.51 ? 150  LYS B CE    1 
ATOM   8285 N  NZ    . LYS B 2 151 ? -10.564 39.248  -21.240 1.00 204.19 ? 150  LYS B NZ    1 
ATOM   8286 N  N     . VAL B 2 152 ? -6.737  32.834  -25.724 1.00 127.60 ? 151  VAL B N     1 
ATOM   8287 C  CA    . VAL B 2 152 ? -6.268  31.454  -25.691 1.00 127.02 ? 151  VAL B CA    1 
ATOM   8288 C  C     . VAL B 2 152 ? -4.849  31.394  -26.237 1.00 128.69 ? 151  VAL B C     1 
ATOM   8289 O  O     . VAL B 2 152 ? -4.268  32.420  -26.607 1.00 136.32 ? 151  VAL B O     1 
ATOM   8290 C  CB    . VAL B 2 152 ? -7.203  30.525  -26.487 1.00 123.72 ? 151  VAL B CB    1 
ATOM   8291 C  CG1   . VAL B 2 152 ? -8.620  30.605  -25.944 1.00 132.90 ? 151  VAL B CG1   1 
ATOM   8292 C  CG2   . VAL B 2 152 ? -7.170  30.881  -27.965 1.00 154.02 ? 151  VAL B CG2   1 
ATOM   8293 N  N     . THR B 2 153 ? -4.283  30.192  -26.290 1.00 151.22 ? 152  THR B N     1 
ATOM   8294 C  CA    . THR B 2 153 ? -2.946  29.974  -26.825 1.00 151.91 ? 152  THR B CA    1 
ATOM   8295 C  C     . THR B 2 153 ? -3.056  29.429  -28.243 1.00 143.58 ? 152  THR B C     1 
ATOM   8296 O  O     . THR B 2 153 ? -3.845  28.514  -28.502 1.00 158.60 ? 152  THR B O     1 
ATOM   8297 C  CB    . THR B 2 153 ? -2.155  29.003  -25.946 1.00 152.42 ? 152  THR B CB    1 
ATOM   8298 O  OG1   . THR B 2 153 ? -2.097  29.508  -24.606 1.00 164.30 ? 152  THR B OG1   1 
ATOM   8299 C  CG2   . THR B 2 153 ? -0.739  28.829  -26.477 1.00 136.12 ? 152  THR B CG2   1 
ATOM   8300 N  N     . TYR B 2 154 ? -2.274  29.995  -29.156 1.00 130.82 ? 153  TYR B N     1 
ATOM   8301 C  CA    . TYR B 2 154 ? -2.262  29.567  -30.546 1.00 130.54 ? 153  TYR B CA    1 
ATOM   8302 C  C     . TYR B 2 154 ? -1.106  28.606  -30.786 1.00 151.83 ? 153  TYR B C     1 
ATOM   8303 O  O     . TYR B 2 154 ? -0.031  28.749  -30.196 1.00 146.90 ? 153  TYR B O     1 
ATOM   8304 C  CB    . TYR B 2 154 ? -2.150  30.766  -31.489 1.00 156.38 ? 153  TYR B CB    1 
ATOM   8305 C  CG    . TYR B 2 154 ? -2.243  30.400  -32.953 1.00 140.20 ? 153  TYR B CG    1 
ATOM   8306 C  CD1   . TYR B 2 154 ? -3.448  29.995  -33.511 1.00 135.87 ? 153  TYR B CD1   1 
ATOM   8307 C  CD2   . TYR B 2 154 ? -1.127  30.465  -33.778 1.00 133.80 ? 153  TYR B CD2   1 
ATOM   8308 C  CE1   . TYR B 2 154 ? -3.540  29.659  -34.847 1.00 134.16 ? 153  TYR B CE1   1 
ATOM   8309 C  CE2   . TYR B 2 154 ? -1.210  30.132  -35.117 1.00 126.10 ? 153  TYR B CE2   1 
ATOM   8310 C  CZ    . TYR B 2 154 ? -2.419  29.730  -35.646 1.00 123.31 ? 153  TYR B CZ    1 
ATOM   8311 O  OH    . TYR B 2 154 ? -2.509  29.398  -36.978 1.00 123.04 ? 153  TYR B OH    1 
ATOM   8312 N  N     . MET B 2 155 ? -1.337  27.626  -31.657 1.00 139.93 ? 154  MET B N     1 
ATOM   8313 C  CA    . MET B 2 155 ? -0.319  26.630  -31.980 1.00 131.25 ? 154  MET B CA    1 
ATOM   8314 C  C     . MET B 2 155 ? -0.695  25.973  -33.296 1.00 127.81 ? 154  MET B C     1 
ATOM   8315 O  O     . MET B 2 155 ? -1.756  25.349  -33.392 1.00 141.59 ? 154  MET B O     1 
ATOM   8316 C  CB    . MET B 2 155 ? -0.203  25.585  -30.870 1.00 140.87 ? 154  MET B CB    1 
ATOM   8317 C  CG    . MET B 2 155 ? 0.812   24.492  -31.154 1.00 164.59 ? 154  MET B CG    1 
ATOM   8318 S  SD    . MET B 2 155 ? 0.694   23.116  -29.995 1.00 133.48 ? 154  MET B SD    1 
ATOM   8319 C  CE    . MET B 2 155 ? 0.835   23.978  -28.432 1.00 133.14 ? 154  MET B CE    1 
ATOM   8320 N  N     . GLU B 2 156 ? 0.161   26.112  -34.303 1.00 126.81 ? 155  GLU B N     1 
ATOM   8321 C  CA    . GLU B 2 156 ? -0.080  25.453  -35.577 1.00 137.55 ? 155  GLU B CA    1 
ATOM   8322 C  C     . GLU B 2 156 ? 0.304   23.980  -35.499 1.00 125.37 ? 155  GLU B C     1 
ATOM   8323 O  O     . GLU B 2 156 ? 1.141   23.573  -34.688 1.00 152.70 ? 155  GLU B O     1 
ATOM   8324 C  CB    . GLU B 2 156 ? 0.695   26.142  -36.700 1.00 126.48 ? 155  GLU B CB    1 
ATOM   8325 C  CG    . GLU B 2 156 ? 0.143   27.506  -37.073 1.00 125.90 ? 155  GLU B CG    1 
ATOM   8326 C  CD    . GLU B 2 156 ? 0.726   28.041  -38.364 1.00 148.11 ? 155  GLU B CD    1 
ATOM   8327 O  OE1   . GLU B 2 156 ? 1.778   27.531  -38.804 1.00 160.60 ? 155  GLU B OE1   1 
ATOM   8328 O  OE2   . GLU B 2 156 ? 0.125   28.971  -38.942 1.00 138.39 ? 155  GLU B OE2   1 
ATOM   8329 N  N     . ALA B 2 157 ? -0.327  23.178  -36.351 1.00 123.31 ? 156  ALA B N     1 
ATOM   8330 C  CA    . ALA B 2 157 ? -0.099  21.742  -36.355 1.00 134.38 ? 156  ALA B CA    1 
ATOM   8331 C  C     . ALA B 2 157 ? -0.282  21.214  -37.770 1.00 144.92 ? 156  ALA B C     1 
ATOM   8332 O  O     . ALA B 2 157 ? -0.773  21.912  -38.661 1.00 145.67 ? 156  ALA B O     1 
ATOM   8333 C  CB    . ALA B 2 157 ? -1.039  21.024  -35.380 1.00 129.52 ? 156  ALA B CB    1 
ATOM   8334 N  N     . SER B 2 158 ? 0.126   19.961  -37.967 1.00 129.78 ? 157  SER B N     1 
ATOM   8335 C  CA    . SER B 2 158 ? -0.025  19.303  -39.263 1.00 140.24 ? 157  SER B CA    1 
ATOM   8336 C  C     . SER B 2 158 ? -0.013  17.800  -39.024 1.00 122.27 ? 157  SER B C     1 
ATOM   8337 O  O     . SER B 2 158 ? 1.034   17.237  -38.692 1.00 138.05 ? 157  SER B O     1 
ATOM   8338 C  CB    . SER B 2 158 ? 1.085   19.719  -40.221 1.00 144.30 ? 157  SER B CB    1 
ATOM   8339 O  OG    . SER B 2 158 ? 0.980   19.022  -41.452 1.00 123.29 ? 157  SER B OG    1 
ATOM   8340 N  N     . ALA B 2 159 ? -1.172  17.160  -39.188 1.00 132.07 ? 158  ALA B N     1 
ATOM   8341 C  CA    . ALA B 2 159 ? -1.256  15.717  -38.999 1.00 147.33 ? 158  ALA B CA    1 
ATOM   8342 C  C     . ALA B 2 159 ? -0.494  14.948  -40.069 1.00 139.16 ? 158  ALA B C     1 
ATOM   8343 O  O     . ALA B 2 159 ? -0.097  13.804  -39.826 1.00 161.69 ? 158  ALA B O     1 
ATOM   8344 C  CB    . ALA B 2 159 ? -2.719  15.272  -38.982 1.00 129.52 ? 158  ALA B CB    1 
ATOM   8345 N  N     . LYS B 2 160 ? -0.282  15.549  -41.243 1.00 122.83 ? 159  LYS B N     1 
ATOM   8346 C  CA    . LYS B 2 160 ? 0.415   14.852  -42.319 1.00 133.35 ? 159  LYS B CA    1 
ATOM   8347 C  C     . LYS B 2 160 ? 1.884   14.622  -41.982 1.00 143.99 ? 159  LYS B C     1 
ATOM   8348 O  O     . LYS B 2 160 ? 2.465   13.616  -42.404 1.00 129.36 ? 159  LYS B O     1 
ATOM   8349 C  CB    . LYS B 2 160 ? 0.275   15.639  -43.623 1.00 121.51 ? 159  LYS B CB    1 
ATOM   8350 C  CG    . LYS B 2 160 ? 0.851   14.943  -44.843 1.00 122.86 ? 159  LYS B CG    1 
ATOM   8351 C  CD    . LYS B 2 160 ? 0.289   15.525  -46.130 1.00 121.84 ? 159  LYS B CD    1 
ATOM   8352 C  CE    . LYS B 2 160 ? 0.901   14.864  -47.354 1.00 134.20 ? 159  LYS B CE    1 
ATOM   8353 N  NZ    . LYS B 2 160 ? 0.321   15.394  -48.619 1.00 154.30 ? 159  LYS B NZ    1 
ATOM   8354 N  N     . ILE B 2 161 ? 2.495   15.529  -41.221 1.00 132.97 ? 160  ILE B N     1 
ATOM   8355 C  CA    . ILE B 2 161 ? 3.882   15.397  -40.797 1.00 129.76 ? 160  ILE B CA    1 
ATOM   8356 C  C     . ILE B 2 161 ? 4.022   15.249  -39.291 1.00 130.45 ? 160  ILE B C     1 
ATOM   8357 O  O     . ILE B 2 161 ? 5.149   15.193  -38.789 1.00 172.74 ? 160  ILE B O     1 
ATOM   8358 C  CB    . ILE B 2 161 ? 4.736   16.581  -41.296 1.00 136.69 ? 160  ILE B CB    1 
ATOM   8359 C  CG1   . ILE B 2 161 ? 4.219   17.897  -40.711 1.00 130.52 ? 160  ILE B CG1   1 
ATOM   8360 C  CG2   . ILE B 2 161 ? 4.738   16.635  -42.817 1.00 131.44 ? 160  ILE B CG2   1 
ATOM   8361 C  CD1   . ILE B 2 161 ? 4.987   19.116  -41.173 1.00 132.27 ? 160  ILE B CD1   1 
ATOM   8362 N  N     . ARG B 2 162 ? 2.911   15.179  -38.558 1.00 128.05 ? 161  ARG B N     1 
ATOM   8363 C  CA    . ARG B 2 162 ? 2.896   15.056  -37.099 1.00 141.66 ? 161  ARG B CA    1 
ATOM   8364 C  C     . ARG B 2 162 ? 3.719   16.169  -36.445 1.00 130.76 ? 161  ARG B C     1 
ATOM   8365 O  O     . ARG B 2 162 ? 4.754   15.945  -35.818 1.00 176.17 ? 161  ARG B O     1 
ATOM   8366 C  CB    . ARG B 2 162 ? 3.390   13.675  -36.656 1.00 131.81 ? 161  ARG B CB    1 
ATOM   8367 C  CG    . ARG B 2 162 ? 2.953   13.301  -35.250 1.00 146.23 ? 161  ARG B CG    1 
ATOM   8368 C  CD    . ARG B 2 162 ? 3.468   11.934  -34.839 1.00 161.08 ? 161  ARG B CD    1 
ATOM   8369 N  NE    . ARG B 2 162 ? 2.563   11.284  -33.897 1.00 130.55 ? 161  ARG B NE    1 
ATOM   8370 C  CZ    . ARG B 2 162 ? 2.531   11.532  -32.595 1.00 130.21 ? 161  ARG B CZ    1 
ATOM   8371 N  NH1   . ARG B 2 162 ? 3.344   12.415  -32.040 1.00 132.51 ? 161  ARG B NH1   1 
ATOM   8372 N  NH2   . ARG B 2 162 ? 1.659   10.879  -31.832 1.00 141.77 ? 161  ARG B NH2   1 
ATOM   8373 N  N     . MET B 2 163 ? 3.216   17.388  -36.613 1.00 143.11 ? 162  MET B N     1 
ATOM   8374 C  CA    . MET B 2 163 ? 3.825   18.582  -36.041 1.00 138.93 ? 162  MET B CA    1 
ATOM   8375 C  C     . MET B 2 163 ? 2.950   19.078  -34.899 1.00 150.40 ? 162  MET B C     1 
ATOM   8376 O  O     . MET B 2 163 ? 1.767   19.372  -35.105 1.00 152.48 ? 162  MET B O     1 
ATOM   8377 C  CB    . MET B 2 163 ? 4.001   19.671  -37.100 1.00 132.84 ? 162  MET B CB    1 
ATOM   8378 C  CG    . MET B 2 163 ? 4.630   20.948  -36.571 1.00 134.80 ? 162  MET B CG    1 
ATOM   8379 S  SD    . MET B 2 163 ? 4.772   22.230  -37.829 1.00 153.17 ? 162  MET B SD    1 
ATOM   8380 C  CE    . MET B 2 163 ? 3.049   22.491  -38.236 1.00 157.41 ? 162  MET B CE    1 
ATOM   8381 N  N     . ASN B 2 164 ? 3.532   19.161  -33.701 1.00 139.89 ? 163  ASN B N     1 
ATOM   8382 C  CA    . ASN B 2 164 ? 2.843   19.659  -32.510 1.00 146.10 ? 163  ASN B CA    1 
ATOM   8383 C  C     . ASN B 2 164 ? 1.575   18.865  -32.206 1.00 146.70 ? 163  ASN B C     1 
ATOM   8384 O  O     . ASN B 2 164 ? 0.585   19.420  -31.724 1.00 127.90 ? 163  ASN B O     1 
ATOM   8385 C  CB    . ASN B 2 164 ? 2.519   21.151  -32.639 1.00 136.91 ? 163  ASN B CB    1 
ATOM   8386 C  CG    . ASN B 2 164 ? 3.759   22.001  -32.826 1.00 146.23 ? 163  ASN B CG    1 
ATOM   8387 O  OD1   . ASN B 2 164 ? 4.827   21.686  -32.301 1.00 173.98 ? 163  ASN B OD1   1 
ATOM   8388 N  ND2   . ASN B 2 164 ? 3.625   23.085  -33.581 1.00 161.68 ? 163  ASN B ND2   1 
ATOM   8389 N  N     . VAL B 2 165 ? 1.591   17.562  -32.484 1.00 166.38 ? 164  VAL B N     1 
ATOM   8390 C  CA    . VAL B 2 165 ? 0.439   16.722  -32.172 1.00 128.40 ? 164  VAL B CA    1 
ATOM   8391 C  C     . VAL B 2 165 ? 0.415   16.376  -30.689 1.00 145.51 ? 164  VAL B C     1 
ATOM   8392 O  O     . VAL B 2 165 ? -0.622  16.491  -30.026 1.00 124.92 ? 164  VAL B O     1 
ATOM   8393 C  CB    . VAL B 2 165 ? 0.443   15.457  -33.050 1.00 128.50 ? 164  VAL B CB    1 
ATOM   8394 C  CG1   . VAL B 2 165 ? -0.673  14.515  -32.629 1.00 129.07 ? 164  VAL B CG1   1 
ATOM   8395 C  CG2   . VAL B 2 165 ? 0.300   15.832  -34.516 1.00 123.84 ? 164  VAL B CG2   1 
ATOM   8396 N  N     . ASP B 2 166 ? 1.557   15.948  -30.145 1.00 159.14 ? 165  ASP B N     1 
ATOM   8397 C  CA    . ASP B 2 166 ? 1.636   15.694  -28.710 1.00 151.05 ? 165  ASP B CA    1 
ATOM   8398 C  C     . ASP B 2 166 ? 1.590   16.994  -27.919 1.00 139.75 ? 165  ASP B C     1 
ATOM   8399 O  O     . ASP B 2 166 ? 0.988   17.050  -26.841 1.00 134.78 ? 165  ASP B O     1 
ATOM   8400 C  CB    . ASP B 2 166 ? 2.908   14.913  -28.380 1.00 165.40 ? 165  ASP B CB    1 
ATOM   8401 C  CG    . ASP B 2 166 ? 2.794   13.441  -28.722 1.00 155.82 ? 165  ASP B CG    1 
ATOM   8402 O  OD1   . ASP B 2 166 ? 2.708   13.113  -29.923 1.00 139.48 ? 165  ASP B OD1   1 
ATOM   8403 O  OD2   . ASP B 2 166 ? 2.792   12.612  -27.787 1.00 164.73 ? 165  ASP B OD2   1 
ATOM   8404 N  N     . GLN B 2 167 ? 2.216   18.052  -28.441 1.00 140.82 ? 166  GLN B N     1 
ATOM   8405 C  CA    . GLN B 2 167 ? 2.241   19.323  -27.727 1.00 144.96 ? 166  GLN B CA    1 
ATOM   8406 C  C     . GLN B 2 167 ? 0.860   19.963  -27.660 1.00 141.71 ? 166  GLN B C     1 
ATOM   8407 O  O     . GLN B 2 167 ? 0.576   20.716  -26.723 1.00 150.68 ? 166  GLN B O     1 
ATOM   8408 C  CB    . GLN B 2 167 ? 3.236   20.281  -28.387 1.00 143.35 ? 166  GLN B CB    1 
ATOM   8409 C  CG    . GLN B 2 167 ? 4.702   19.891  -28.223 1.00 140.08 ? 166  GLN B CG    1 
ATOM   8410 C  CD    . GLN B 2 167 ? 5.124   18.757  -29.140 1.00 155.81 ? 166  GLN B CD    1 
ATOM   8411 O  OE1   . GLN B 2 167 ? 4.319   18.226  -29.906 1.00 161.03 ? 166  GLN B OE1   1 
ATOM   8412 N  NE2   . GLN B 2 167 ? 6.396   18.381  -29.067 1.00 161.36 ? 166  GLN B NE2   1 
ATOM   8413 N  N     . ALA B 2 168 ? -0.007  19.678  -28.633 1.00 128.31 ? 167  ALA B N     1 
ATOM   8414 C  CA    . ALA B 2 168 ? -1.346  20.258  -28.621 1.00 125.64 ? 167  ALA B CA    1 
ATOM   8415 C  C     . ALA B 2 168 ? -2.162  19.734  -27.446 1.00 144.24 ? 167  ALA B C     1 
ATOM   8416 O  O     . ALA B 2 168 ? -2.798  20.510  -26.722 1.00 149.58 ? 167  ALA B O     1 
ATOM   8417 C  CB    . ALA B 2 168 ? -2.057  19.970  -29.943 1.00 122.89 ? 167  ALA B CB    1 
ATOM   8418 N  N     . PHE B 2 169 ? -2.154  18.416  -27.237 1.00 138.03 ? 168  PHE B N     1 
ATOM   8419 C  CA    . PHE B 2 169 ? -2.902  17.836  -26.129 1.00 136.56 ? 168  PHE B CA    1 
ATOM   8420 C  C     . PHE B 2 169 ? -2.194  18.029  -24.794 1.00 157.70 ? 168  PHE B C     1 
ATOM   8421 O  O     . PHE B 2 169 ? -2.857  18.117  -23.755 1.00 179.80 ? 168  PHE B O     1 
ATOM   8422 C  CB    . PHE B 2 169 ? -3.148  16.348  -26.381 1.00 142.01 ? 168  PHE B CB    1 
ATOM   8423 C  CG    . PHE B 2 169 ? -4.019  16.071  -27.573 1.00 136.48 ? 168  PHE B CG    1 
ATOM   8424 C  CD1   . PHE B 2 169 ? -5.396  16.017  -27.442 1.00 117.10 ? 168  PHE B CD1   1 
ATOM   8425 C  CD2   . PHE B 2 169 ? -3.461  15.866  -28.823 1.00 122.45 ? 168  PHE B CD2   1 
ATOM   8426 C  CE1   . PHE B 2 169 ? -6.201  15.764  -28.537 1.00 114.53 ? 168  PHE B CE1   1 
ATOM   8427 C  CE2   . PHE B 2 169 ? -4.260  15.612  -29.922 1.00 119.66 ? 168  PHE B CE2   1 
ATOM   8428 C  CZ    . PHE B 2 169 ? -5.632  15.561  -29.778 1.00 114.62 ? 168  PHE B CZ    1 
ATOM   8429 N  N     . HIS B 2 170 ? -0.861  18.097  -24.799 1.00 142.39 ? 169  HIS B N     1 
ATOM   8430 C  CA    . HIS B 2 170 ? -0.133  18.275  -23.547 1.00 149.16 ? 169  HIS B CA    1 
ATOM   8431 C  C     . HIS B 2 170 ? -0.236  19.709  -23.045 1.00 146.24 ? 169  HIS B C     1 
ATOM   8432 O  O     . HIS B 2 170 ? -0.322  19.943  -21.834 1.00 144.50 ? 169  HIS B O     1 
ATOM   8433 C  CB    . HIS B 2 170 ? 1.328   17.863  -23.724 1.00 166.99 ? 169  HIS B CB    1 
ATOM   8434 C  CG    . HIS B 2 170 ? 1.516   16.391  -23.916 1.00 173.75 ? 169  HIS B CG    1 
ATOM   8435 N  ND1   . HIS B 2 170 ? 2.351   15.867  -24.879 1.00 160.98 ? 169  HIS B ND1   1 
ATOM   8436 C  CD2   . HIS B 2 170 ? 0.977   15.331  -23.269 1.00 160.86 ? 169  HIS B CD2   1 
ATOM   8437 C  CE1   . HIS B 2 170 ? 2.317   14.548  -24.818 1.00 165.44 ? 169  HIS B CE1   1 
ATOM   8438 N  NE2   . HIS B 2 170 ? 1.491   14.197  -23.849 1.00 175.90 ? 169  HIS B NE2   1 
ATOM   8439 N  N     . GLU B 2 171 ? -0.227  20.686  -23.954 1.00 155.26 ? 170  GLU B N     1 
ATOM   8440 C  CA    . GLU B 2 171 ? -0.462  22.064  -23.539 1.00 164.42 ? 170  GLU B CA    1 
ATOM   8441 C  C     . GLU B 2 171 ? -1.900  22.288  -23.096 1.00 165.15 ? 170  GLU B C     1 
ATOM   8442 O  O     . GLU B 2 171 ? -2.169  23.252  -22.373 1.00 155.30 ? 170  GLU B O     1 
ATOM   8443 C  CB    . GLU B 2 171 ? -0.105  23.034  -24.666 1.00 147.90 ? 170  GLU B CB    1 
ATOM   8444 C  CG    . GLU B 2 171 ? 1.391   23.226  -24.869 1.00 165.45 ? 170  GLU B CG    1 
ATOM   8445 C  CD    . GLU B 2 171 ? 2.055   23.943  -23.707 1.00 171.12 ? 170  GLU B CD    1 
ATOM   8446 O  OE1   . GLU B 2 171 ? 1.350   24.656  -22.962 1.00 168.00 ? 170  GLU B OE1   1 
ATOM   8447 O  OE2   . GLU B 2 171 ? 3.283   23.792  -23.539 1.00 194.17 ? 170  GLU B OE2   1 
ATOM   8448 N  N     . LEU B 2 172 ? -2.825  21.419  -23.509 1.00 144.66 ? 171  LEU B N     1 
ATOM   8449 C  CA    . LEU B 2 172 ? -4.202  21.536  -23.044 1.00 137.82 ? 171  LEU B CA    1 
ATOM   8450 C  C     . LEU B 2 172 ? -4.336  21.063  -21.603 1.00 145.68 ? 171  LEU B C     1 
ATOM   8451 O  O     . LEU B 2 172 ? -5.062  21.673  -20.809 1.00 158.78 ? 171  LEU B O     1 
ATOM   8452 C  CB    . LEU B 2 172 ? -5.136  20.747  -23.962 1.00 135.41 ? 171  LEU B CB    1 
ATOM   8453 C  CG    . LEU B 2 172 ? -6.619  20.755  -23.586 1.00 133.08 ? 171  LEU B CG    1 
ATOM   8454 C  CD1   . LEU B 2 172 ? -7.138  22.180  -23.488 1.00 133.25 ? 171  LEU B CD1   1 
ATOM   8455 C  CD2   . LEU B 2 172 ? -7.431  19.954  -24.591 1.00 117.75 ? 171  LEU B CD2   1 
ATOM   8456 N  N     . VAL B 2 173 ? -3.639  19.982  -21.242 1.00 167.78 ? 172  VAL B N     1 
ATOM   8457 C  CA    . VAL B 2 173 ? -3.698  19.488  -19.873 1.00 159.28 ? 172  VAL B CA    1 
ATOM   8458 C  C     . VAL B 2 173 ? -2.914  20.386  -18.924 1.00 160.88 ? 172  VAL B C     1 
ATOM   8459 O  O     . VAL B 2 173 ? -3.113  20.318  -17.705 1.00 182.32 ? 172  VAL B O     1 
ATOM   8460 C  CB    . VAL B 2 173 ? -3.194  18.032  -19.803 1.00 153.39 ? 172  VAL B CB    1 
ATOM   8461 C  CG1   . VAL B 2 173 ? -1.676  17.983  -19.775 1.00 162.14 ? 172  VAL B CG1   1 
ATOM   8462 C  CG2   . VAL B 2 173 ? -3.779  17.321  -18.594 1.00 174.30 ? 172  VAL B CG2   1 
ATOM   8463 N  N     . ARG B 2 174 ? -2.030  21.238  -19.449 1.00 155.66 ? 173  ARG B N     1 
ATOM   8464 C  CA    . ARG B 2 174 ? -1.313  22.191  -18.611 1.00 162.20 ? 173  ARG B CA    1 
ATOM   8465 C  C     . ARG B 2 174 ? -2.158  23.406  -18.252 1.00 181.51 ? 173  ARG B C     1 
ATOM   8466 O  O     . ARG B 2 174 ? -1.886  24.056  -17.237 1.00 197.07 ? 173  ARG B O     1 
ATOM   8467 C  CB    . ARG B 2 174 ? -0.030  22.654  -19.306 1.00 161.18 ? 173  ARG B CB    1 
ATOM   8468 C  CG    . ARG B 2 174 ? 1.031   21.579  -19.459 1.00 162.56 ? 173  ARG B CG    1 
ATOM   8469 C  CD    . ARG B 2 174 ? 2.321   22.164  -20.010 1.00 175.19 ? 173  ARG B CD    1 
ATOM   8470 N  NE    . ARG B 2 174 ? 3.328   21.141  -20.264 1.00 192.02 ? 173  ARG B NE    1 
ATOM   8471 C  CZ    . ARG B 2 174 ? 3.540   20.575  -21.444 1.00 175.34 ? 173  ARG B CZ    1 
ATOM   8472 N  NH1   . ARG B 2 174 ? 2.830   20.909  -22.509 1.00 163.04 ? 173  ARG B NH1   1 
ATOM   8473 N  NH2   . ARG B 2 174 ? 4.491   19.652  -21.560 1.00 182.88 ? 173  ARG B NH2   1 
ATOM   8474 N  N     . VAL B 2 175 ? -3.164  23.736  -19.063 1.00 168.04 ? 174  VAL B N     1 
ATOM   8475 C  CA    . VAL B 2 175 ? -4.052  24.836  -18.706 1.00 151.41 ? 174  VAL B CA    1 
ATOM   8476 C  C     . VAL B 2 175 ? -5.136  24.358  -17.747 1.00 168.46 ? 174  VAL B C     1 
ATOM   8477 O  O     . VAL B 2 175 ? -5.671  25.151  -16.963 1.00 173.94 ? 174  VAL B O     1 
ATOM   8478 C  CB    . VAL B 2 175 ? -4.653  25.472  -19.972 1.00 143.11 ? 174  VAL B CB    1 
ATOM   8479 C  CG1   . VAL B 2 175 ? -5.388  26.763  -19.632 1.00 158.05 ? 174  VAL B CG1   1 
ATOM   8480 C  CG2   . VAL B 2 175 ? -3.565  25.741  -20.996 1.00 141.90 ? 174  VAL B CG2   1 
ATOM   8481 N  N     . ILE B 2 176 ? -5.469  23.065  -17.780 1.00 156.52 ? 175  ILE B N     1 
ATOM   8482 C  CA    . ILE B 2 176 ? -6.461  22.529  -16.854 1.00 164.68 ? 175  ILE B CA    1 
ATOM   8483 C  C     . ILE B 2 176 ? -5.931  22.564  -15.425 1.00 179.32 ? 175  ILE B C     1 
ATOM   8484 O  O     . ILE B 2 176 ? -6.660  22.904  -14.486 1.00 186.79 ? 175  ILE B O     1 
ATOM   8485 C  CB    . ILE B 2 176 ? -6.869  21.105  -17.275 1.00 148.96 ? 175  ILE B CB    1 
ATOM   8486 C  CG1   . ILE B 2 176 ? -7.401  21.105  -18.708 1.00 141.39 ? 175  ILE B CG1   1 
ATOM   8487 C  CG2   . ILE B 2 176 ? -7.915  20.547  -16.324 1.00 149.08 ? 175  ILE B CG2   1 
ATOM   8488 C  CD1   . ILE B 2 176 ? -7.728  19.726  -19.238 1.00 144.77 ? 175  ILE B CD1   1 
ATOM   8489 N  N     . ARG B 2 177 ? -4.654  22.217  -15.237 1.00 191.83 ? 176  ARG B N     1 
ATOM   8490 C  CA    . ARG B 2 177 ? -4.068  22.271  -13.901 1.00 186.81 ? 176  ARG B CA    1 
ATOM   8491 C  C     . ARG B 2 177 ? -3.883  23.712  -13.438 1.00 194.48 ? 176  ARG B C     1 
ATOM   8492 O  O     . ARG B 2 177 ? -4.076  24.019  -12.256 1.00 203.19 ? 176  ARG B O     1 
ATOM   8493 C  CB    . ARG B 2 177 ? -2.735  21.519  -13.879 1.00 183.93 ? 176  ARG B CB    1 
ATOM   8494 C  CG    . ARG B 2 177 ? -1.716  22.044  -14.876 1.00 209.09 ? 176  ARG B CG    1 
ATOM   8495 C  CD    . ARG B 2 177 ? -0.361  21.371  -14.741 1.00 232.69 ? 176  ARG B CD    1 
ATOM   8496 N  NE    . ARG B 2 177 ? 0.625   21.995  -15.617 1.00 243.55 ? 176  ARG B NE    1 
ATOM   8497 C  CZ    . ARG B 2 177 ? 1.884   21.599  -15.736 1.00 239.49 ? 176  ARG B CZ    1 
ATOM   8498 N  NH1   . ARG B 2 177 ? 2.353   20.568  -15.051 1.00 237.73 ? 176  ARG B NH1   1 
ATOM   8499 N  NH2   . ARG B 2 177 ? 2.695   22.253  -16.563 1.00 215.27 ? 176  ARG B NH2   1 
ATOM   8500 N  N     . LYS B 2 178 ? -3.518  24.609  -14.354 1.00 181.05 ? 177  LYS B N     1 
ATOM   8501 C  CA    . LYS B 2 178 ? -3.348  26.022  -14.040 1.00 172.05 ? 177  LYS B CA    1 
ATOM   8502 C  C     . LYS B 2 178 ? -4.665  26.786  -14.036 1.00 177.86 ? 177  LYS B C     1 
ATOM   8503 O  O     . LYS B 2 178 ? -4.653  28.016  -13.916 1.00 176.90 ? 177  LYS B O     1 
ATOM   8504 C  CB    . LYS B 2 178 ? -2.375  26.668  -15.030 1.00 164.88 ? 177  LYS B CB    1 
ATOM   8505 N  N     . PHE B 2 179 ? -5.792  26.088  -14.172 1.00 185.15 ? 178  PHE B N     1 
ATOM   8506 C  CA    . PHE B 2 179 ? -7.104  26.717  -14.108 1.00 192.04 ? 178  PHE B CA    1 
ATOM   8507 C  C     . PHE B 2 179 ? -7.562  26.810  -12.658 1.00 199.56 ? 178  PHE B C     1 
ATOM   8508 O  O     . PHE B 2 179 ? -7.521  27.889  -12.058 1.00 204.28 ? 178  PHE B O     1 
ATOM   8509 C  CB    . PHE B 2 179 ? -8.114  25.932  -14.950 1.00 184.01 ? 178  PHE B CB    1 
ATOM   8510 C  CG    . PHE B 2 179 ? -9.476  26.562  -15.014 1.00 192.03 ? 178  PHE B CG    1 
ATOM   8511 C  CD1   . PHE B 2 179 ? -9.731  27.604  -15.889 1.00 189.77 ? 178  PHE B CD1   1 
ATOM   8512 C  CD2   . PHE B 2 179 ? -10.505 26.104  -14.207 1.00 212.20 ? 178  PHE B CD2   1 
ATOM   8513 C  CE1   . PHE B 2 179 ? -10.985 28.184  -15.953 1.00 198.79 ? 178  PHE B CE1   1 
ATOM   8514 C  CE2   . PHE B 2 179 ? -11.760 26.679  -14.266 1.00 203.37 ? 178  PHE B CE2   1 
ATOM   8515 C  CZ    . PHE B 2 179 ? -12.001 27.720  -15.141 1.00 183.72 ? 178  PHE B CZ    1 
ATOM   8516 N  N     . GLN B 2 180 ? -7.991  25.682  -12.096 1.00 215.06 ? 179  GLN B N     1 
ATOM   8517 C  CA    . GLN B 2 180 ? -8.389  25.590  -10.691 1.00 224.54 ? 179  GLN B CA    1 
ATOM   8518 C  C     . GLN B 2 180 ? -9.457  26.618  -10.326 1.00 221.24 ? 179  GLN B C     1 
ATOM   8519 O  O     . GLN B 2 180 ? -10.534 26.646  -10.920 1.00 215.61 ? 179  GLN B O     1 
ATOM   8520 C  CB    . GLN B 2 180 ? -7.164  25.749  -9.783  1.00 233.22 ? 179  GLN B CB    1 
ATOM   8521 C  CG    . GLN B 2 180 ? -7.473  25.719  -8.293  1.00 230.13 ? 179  GLN B CG    1 
ATOM   8522 C  CD    . GLN B 2 180 ? -7.596  27.107  -7.694  1.00 220.17 ? 179  GLN B CD    1 
ATOM   8523 O  OE1   . GLN B 2 180 ? -7.166  28.094  -8.291  1.00 220.12 ? 179  GLN B OE1   1 
ATOM   8524 N  NE2   . GLN B 2 180 ? -8.186  27.189  -6.508  1.00 232.02 ? 179  GLN B NE2   1 
HETATM 8525 C  C2    . 5H5 C 3 .   ? -42.353 7.731   -4.635  1.00 144.56 ? 1101 5H5 A C2    1 
HETATM 8526 C  C4    . 5H5 C 3 .   ? -41.390 6.632   -4.978  1.00 135.39 ? 1101 5H5 A C4    1 
HETATM 8527 C  C6    . 5H5 C 3 .   ? -39.960 7.123   -4.783  1.00 136.46 ? 1101 5H5 A C6    1 
HETATM 8528 C  C8    . 5H5 C 3 .   ? -42.419 5.192   -6.660  1.00 142.49 ? 1101 5H5 A C8    1 
HETATM 8529 C  C12   . 5H5 C 3 .   ? -43.371 1.780   -9.963  1.00 141.49 ? 1101 5H5 A C12   1 
HETATM 8530 C  C15   . 5H5 C 3 .   ? -46.375 0.342   -8.521  1.00 138.36 ? 1101 5H5 A C15   1 
HETATM 8531 C  C16   . 5H5 C 3 .   ? -46.653 0.407   -7.180  1.00 147.64 ? 1101 5H5 A C16   1 
HETATM 8532 C  C18   . 5H5 C 3 .   ? -45.172 1.919   -7.544  1.00 132.01 ? 1101 5H5 A C18   1 
HETATM 8533 C  C19   . 5H5 C 3 .   ? -44.206 3.045   -7.284  1.00 125.89 ? 1101 5H5 A C19   1 
HETATM 8534 C  C21   . 5H5 C 3 .   ? -43.307 4.690   -5.701  1.00 154.40 ? 1101 5H5 A C21   1 
HETATM 8535 C  C24   . 5H5 C 3 .   ? -49.086 -2.077  -6.260  1.00 161.48 ? 1101 5H5 A C24   1 
HETATM 8536 C  C27   . 5H5 C 3 .   ? -47.705 0.436   -4.045  1.00 134.02 ? 1101 5H5 A C27   1 
HETATM 8537 N  N1    . 5H5 C 3 .   ? -42.956 7.741   -3.347  1.00 141.32 ? 1101 5H5 A N1    1 
HETATM 8538 O  O3    . 5H5 C 3 .   ? -42.606 8.597   -5.462  1.00 152.66 ? 1101 5H5 A O3    1 
HETATM 8539 O  O7    . 5H5 C 3 .   ? -41.573 6.222   -6.336  1.00 143.15 ? 1101 5H5 A O7    1 
HETATM 8540 C  C9    . 5H5 C 3 .   ? -42.390 4.648   -7.950  1.00 134.58 ? 1101 5H5 A C9    1 
HETATM 8541 C  C10   . 5H5 C 3 .   ? -43.246 3.595   -8.309  1.00 136.46 ? 1101 5H5 A C10   1 
HETATM 8542 O  O11   . 5H5 C 3 .   ? -43.137 3.132   -9.597  1.00 141.75 ? 1101 5H5 A O11   1 
HETATM 8543 C  C13   . 5H5 C 3 .   ? -44.873 1.561   -10.044 1.00 135.90 ? 1101 5H5 A C13   1 
HETATM 8544 N  N14   . 5H5 C 3 .   ? -45.448 1.292   -8.725  1.00 126.95 ? 1101 5H5 A N14   1 
HETATM 8545 N  N17   . 5H5 C 3 .   ? -45.936 1.354   -6.570  1.00 148.70 ? 1101 5H5 A N17   1 
HETATM 8546 C  C20   . 5H5 C 3 .   ? -44.183 3.640   -6.005  1.00 142.29 ? 1101 5H5 A C20   1 
HETATM 8547 C  C22   . 5H5 C 3 .   ? -47.646 -0.488  -6.504  1.00 148.62 ? 1101 5H5 A C22   1 
HETATM 8548 N  N23   . 5H5 C 3 .   ? -48.265 -1.482  -7.168  1.00 150.18 ? 1101 5H5 A N23   1 
HETATM 8549 N  N25   . 5H5 C 3 .   ? -48.965 -1.450  -5.057  1.00 149.15 ? 1101 5H5 A N25   1 
HETATM 8550 N  N26   . 5H5 C 3 .   ? -48.029 -0.419  -5.231  1.00 141.69 ? 1101 5H5 A N26   1 
HETATM 8551 C  C28   . 5H5 C 3 .   ? -46.770 -0.339  -3.123  1.00 157.05 ? 1101 5H5 A C28   1 
HETATM 8552 C  C29   . 5H5 C 3 .   ? -48.946 0.909   -3.288  1.00 145.45 ? 1101 5H5 A C29   1 
HETATM 8553 P  PG    . GNP D 4 .   ? -15.287 15.830  -40.090 1.00 109.80 ? 201  GNP B PG    1 
HETATM 8554 O  O1G   . GNP D 4 .   ? -15.853 15.978  -41.504 1.00 103.72 ? 201  GNP B O1G   1 
HETATM 8555 O  O2G   . GNP D 4 .   ? -15.617 14.504  -39.407 1.00 112.44 ? 201  GNP B O2G   1 
HETATM 8556 O  O3G   . GNP D 4 .   ? -15.527 17.049  -39.195 1.00 127.35 ? 201  GNP B O3G   1 
HETATM 8557 N  N3B   . GNP D 4 .   ? -13.510 15.768  -40.398 1.00 112.37 ? 201  GNP B N3B   1 
HETATM 8558 P  PB    . GNP D 4 .   ? -12.405 16.186  -39.203 1.00 119.42 ? 201  GNP B PB    1 
HETATM 8559 O  O1B   . GNP D 4 .   ? -12.178 17.674  -39.116 1.00 101.05 ? 201  GNP B O1B   1 
HETATM 8560 O  O2B   . GNP D 4 .   ? -12.713 15.411  -37.950 1.00 115.15 ? 201  GNP B O2B   1 
HETATM 8561 O  O3A   . GNP D 4 .   ? -10.920 15.624  -39.784 1.00 136.44 ? 201  GNP B O3A   1 
HETATM 8562 P  PA    . GNP D 4 .   ? -10.585 14.596  -41.002 1.00 116.60 ? 201  GNP B PA    1 
HETATM 8563 O  O1A   . GNP D 4 .   ? -9.271  13.921  -40.768 1.00 103.79 ? 201  GNP B O1A   1 
HETATM 8564 O  O2A   . GNP D 4 .   ? -11.798 13.825  -41.430 1.00 144.98 ? 201  GNP B O2A   1 
HETATM 8565 O  "O5'" . GNP D 4 .   ? -10.211 15.718  -42.165 1.00 116.66 ? 201  GNP B "O5'" 1 
HETATM 8566 C  "C5'" . GNP D 4 .   ? -10.670 15.570  -43.482 1.00 136.01 ? 201  GNP B "C5'" 1 
HETATM 8567 C  "C4'" . GNP D 4 .   ? -9.510  15.543  -44.457 1.00 140.75 ? 201  GNP B "C4'" 1 
HETATM 8568 O  "O4'" . GNP D 4 .   ? -8.457  16.425  -44.045 1.00 136.28 ? 201  GNP B "O4'" 1 
HETATM 8569 C  "C3'" . GNP D 4 .   ? -8.868  14.170  -44.677 1.00 128.78 ? 201  GNP B "C3'" 1 
HETATM 8570 O  "O3'" . GNP D 4 .   ? -8.681  14.006  -46.063 1.00 121.28 ? 201  GNP B "O3'" 1 
HETATM 8571 C  "C2'" . GNP D 4 .   ? -7.528  14.294  -43.957 1.00 131.87 ? 201  GNP B "C2'" 1 
HETATM 8572 O  "O2'" . GNP D 4 .   ? -6.566  13.442  -44.507 1.00 111.24 ? 201  GNP B "O2'" 1 
HETATM 8573 C  "C1'" . GNP D 4 .   ? -7.224  15.782  -44.163 1.00 120.70 ? 201  GNP B "C1'" 1 
HETATM 8574 N  N9    . GNP D 4 .   ? -6.283  16.313  -43.203 1.00 109.16 ? 201  GNP B N9    1 
HETATM 8575 C  C8    . GNP D 4 .   ? -6.436  16.381  -41.840 1.00 125.69 ? 201  GNP B C8    1 
HETATM 8576 N  N7    . GNP D 4 .   ? -5.409  16.907  -41.244 1.00 114.28 ? 201  GNP B N7    1 
HETATM 8577 C  C5    . GNP D 4 .   ? -4.530  17.201  -42.255 1.00 112.25 ? 201  GNP B C5    1 
HETATM 8578 C  C6    . GNP D 4 .   ? -3.233  17.793  -42.215 1.00 129.19 ? 201  GNP B C6    1 
HETATM 8579 O  O6    . GNP D 4 .   ? -2.594  18.182  -41.252 1.00 118.60 ? 201  GNP B O6    1 
HETATM 8580 N  N1    . GNP D 4 .   ? -2.701  17.901  -43.509 1.00 115.73 ? 201  GNP B N1    1 
HETATM 8581 C  C2    . GNP D 4 .   ? -3.310  17.506  -44.666 1.00 121.58 ? 201  GNP B C2    1 
HETATM 8582 N  N2    . GNP D 4 .   ? -2.635  17.693  -45.811 1.00 116.10 ? 201  GNP B N2    1 
HETATM 8583 N  N3    . GNP D 4 .   ? -4.502  16.964  -44.694 1.00 115.73 ? 201  GNP B N3    1 
HETATM 8584 C  C4    . GNP D 4 .   ? -5.057  16.836  -43.480 1.00 111.31 ? 201  GNP B C4    1 
HETATM 8585 MG MG    . MG  E 5 .   ? -14.037 13.993  -37.834 1.00 105.23 ? 202  MG  B MG    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . ASN A 4   ? 2.5436 2.1507 3.8208 -0.1153 -0.5781 0.6137  107  ASN A N     
2    C  CA    . ASN A 4   ? 2.4539 2.0425 3.6280 -0.1351 -0.6059 0.6137  107  ASN A CA    
3    C  C     . ASN A 4   ? 2.2356 1.8438 3.3900 -0.1475 -0.6502 0.6314  107  ASN A C     
4    O  O     . ASN A 4   ? 2.2206 1.8156 3.2891 -0.1645 -0.6737 0.6309  107  ASN A O     
5    C  CB    . ASN A 4   ? 2.5119 2.0712 3.6466 -0.1459 -0.6139 0.6232  107  ASN A CB    
6    C  CG    . ASN A 4   ? 2.5701 2.1159 3.6996 -0.1389 -0.5661 0.5952  107  ASN A CG    
7    O  OD1   . ASN A 4   ? 2.6728 2.2327 3.8438 -0.1244 -0.5258 0.5715  107  ASN A OD1   
8    N  ND2   . ASN A 4   ? 2.2691 1.7884 3.3440 -0.1507 -0.5690 0.5960  107  ASN A ND2   
9    N  N     . ARG A 5   ? 2.1118 1.7509 3.3458 -0.1406 -0.6598 0.6463  108  ARG A N     
10   C  CA    . ARG A 5   ? 2.0166 1.6743 3.2378 -0.1554 -0.7013 0.6630  108  ARG A CA    
11   C  C     . ARG A 5   ? 2.2412 1.9062 3.4202 -0.1570 -0.7007 0.6461  108  ARG A C     
12   O  O     . ARG A 5   ? 2.2778 1.9417 3.3979 -0.1753 -0.7335 0.6525  108  ARG A O     
13   C  CB    . ARG A 5   ? 2.1444 1.8331 3.4670 -0.1493 -0.7100 0.6837  108  ARG A CB    
14   C  CG    . ARG A 5   ? 2.2023 1.9110 3.6128 -0.1256 -0.6695 0.6711  108  ARG A CG    
15   C  CD    . ARG A 5   ? 2.4133 2.1523 3.9242 -0.1217 -0.6787 0.6937  108  ARG A CD    
16   N  NE    . ARG A 5   ? 2.2960 2.0519 3.8912 -0.0994 -0.6363 0.6811  108  ARG A NE    
17   C  CZ    . ARG A 5   ? 1.9369 1.6863 3.5881 -0.0834 -0.6012 0.6772  108  ARG A CZ    
18   N  NH1   . ARG A 5   ? 1.7029 1.4300 3.3382 -0.0859 -0.6033 0.6854  108  ARG A NH1   
19   N  NH2   . ARG A 5   ? 1.7073 1.4712 3.4304 -0.0651 -0.5616 0.6640  108  ARG A NH2   
20   N  N     . GLU A 6   ? 2.4708 2.1416 3.6776 -0.1391 -0.6630 0.6243  109  GLU A N     
21   C  CA    . GLU A 6   ? 2.1244 1.8018 3.2897 -0.1396 -0.6599 0.6073  109  GLU A CA    
22   C  C     . GLU A 6   ? 2.1044 1.7688 3.1539 -0.1530 -0.6519 0.5807  109  GLU A C     
23   O  O     . GLU A 6   ? 2.2156 1.8856 3.2041 -0.1630 -0.6638 0.5714  109  GLU A O     
24   C  CB    . GLU A 6   ? 2.0747 1.7750 3.2954 -0.1194 -0.6138 0.5816  109  GLU A CB    
25   C  CG    . GLU A 6   ? 1.8557 1.5785 3.1869 -0.1067 -0.6147 0.6001  109  GLU A CG    
26   C  CD    . GLU A 6   ? 2.2484 1.9699 3.6501 -0.0974 -0.5978 0.6093  109  GLU A CD    
27   O  OE1   . GLU A 6   ? 2.6276 2.3222 3.9981 -0.0985 -0.5867 0.6049  109  GLU A OE1   
28   O  OE2   . GLU A 6   ? 2.2226 1.9693 3.7114 -0.0894 -0.5944 0.6209  109  GLU A OE2   
29   N  N     . GLU A 7   ? 2.1040 1.7510 3.1238 -0.1534 -0.6308 0.5684  110  GLU A N     
30   C  CA    . GLU A 7   ? 2.2058 1.8413 3.1204 -0.1660 -0.6220 0.5443  110  GLU A CA    
31   C  C     . GLU A 7   ? 2.0996 1.7144 2.9472 -0.1880 -0.6666 0.5655  110  GLU A C     
32   O  O     . GLU A 7   ? 1.9343 1.5440 2.6943 -0.1997 -0.6657 0.5477  110  GLU A O     
33   C  CB    . GLU A 7   ? 2.3385 1.9601 3.2430 -0.1624 -0.5902 0.5283  110  GLU A CB    
34   C  CG    . GLU A 7   ? 2.2778 1.9151 3.2420 -0.1435 -0.5440 0.5058  110  GLU A CG    
35   C  CD    . GLU A 7   ? 2.4094 2.0295 3.3664 -0.1423 -0.5148 0.4926  110  GLU A CD    
36   O  OE1   . GLU A 7   ? 2.5679 2.1661 3.4681 -0.1558 -0.5288 0.4982  110  GLU A OE1   
37   O  OE2   . GLU A 7   ? 2.5468 2.1735 3.5533 -0.1290 -0.4769 0.4761  110  GLU A OE2   
38   N  N     . LYS A 8   ? 2.2508 1.8526 3.1379 -0.1946 -0.7054 0.6040  111  LYS A N     
39   C  CA    . LYS A 8   ? 2.1840 1.7646 3.0077 -0.2180 -0.7506 0.6264  111  LYS A CA    
40   C  C     . LYS A 8   ? 2.1434 1.7358 2.9351 -0.2270 -0.7697 0.6243  111  LYS A C     
41   O  O     . LYS A 8   ? 2.4417 2.0156 3.1559 -0.2486 -0.7971 0.6306  111  LYS A O     
42   C  CB    . LYS A 8   ? 2.0504 1.6354 2.9241 -0.2244 -0.7779 0.6551  111  LYS A CB    
43   C  CG    . LYS A 8   ? 2.0740 1.6443 2.9754 -0.2170 -0.7618 0.6598  111  LYS A CG    
44   C  CD    . LYS A 8   ? 2.2261 1.8103 3.1946 -0.2192 -0.7838 0.6868  111  LYS A CD    
45   C  CE    . LYS A 8   ? 1.9192 1.4896 2.9231 -0.2089 -0.7636 0.6908  111  LYS A CE    
46   N  NZ    . LYS A 8   ? 2.5972 2.1829 3.6737 -0.2091 -0.7832 0.7184  111  LYS A NZ    
47   N  N     . ILE A 9   ? 2.0710 1.6922 2.9184 -0.2119 -0.7541 0.6145  112  ILE A N     
48   C  CA    . ILE A 9   ? 2.2986 1.9313 3.1197 -0.2193 -0.7692 0.6112  112  ILE A CA    
49   C  C     . ILE A 9   ? 2.0179 1.6592 2.7725 -0.2157 -0.7331 0.5708  112  ILE A C     
50   O  O     . ILE A 9   ? 2.0777 1.7113 2.7595 -0.2302 -0.7453 0.5639  112  ILE A O     
51   C  CB    . ILE A 9   ? 2.2658 1.9295 3.1855 -0.2073 -0.7724 0.6226  112  ILE A CB    
52   C  CG1   . ILE A 9   ? 2.1319 1.8055 3.1118 -0.2145 -0.7950 0.6479  112  ILE A CG1   
53   C  CG2   . ILE A 9   ? 2.0744 1.7492 2.9673 -0.2161 -0.7875 0.6189  112  ILE A CG2   
54   C  CD1   . ILE A 9   ? 1.6136 1.3215 2.6929 -0.2047 -0.7938 0.6568  112  ILE A CD1   
55   N  N     . LEU A 10  ? 2.0359 1.6923 2.8143 -0.1974 -0.6883 0.5441  113  LEU A N     
56   C  CA    . LEU A 10  ? 2.1734 1.8414 2.8953 -0.1931 -0.6544 0.5076  113  LEU A CA    
57   C  C     . LEU A 10  ? 1.8878 1.5341 2.5108 -0.2078 -0.6525 0.4950  113  LEU A C     
58   O  O     . LEU A 10  ? 1.8396 1.4878 2.3972 -0.2134 -0.6448 0.4765  113  LEU A O     
59   C  CB    . LEU A 10  ? 2.1725 1.8609 2.9437 -0.1723 -0.6087 0.4840  113  LEU A CB    
60   C  CG    . LEU A 10  ? 2.3018 2.0131 3.1681 -0.1560 -0.6005 0.4899  113  LEU A CG    
61   C  CD1   . LEU A 10  ? 2.1985 1.9245 3.0981 -0.1387 -0.5521 0.4632  113  LEU A CD1   
62   C  CD2   . LEU A 10  ? 2.1380 1.8648 2.9966 -0.1578 -0.6123 0.4887  113  LEU A CD2   
63   N  N     . ASN A 11  ? 1.9000 1.5247 2.5124 -0.2142 -0.6583 0.5052  114  ASN A N     
64   C  CA    . ASN A 11  ? 1.9469 1.5502 2.4684 -0.2285 -0.6547 0.4937  114  ASN A CA    
65   C  C     . ASN A 11  ? 2.1272 1.7092 2.5782 -0.2503 -0.6891 0.5064  114  ASN A C     
66   O  O     . ASN A 11  ? 1.7679 1.3357 2.1365 -0.2615 -0.6809 0.4912  114  ASN A O     
67   C  CB    . ASN A 11  ? 1.9794 1.5627 2.5097 -0.2311 -0.6545 0.5041  114  ASN A CB    
68   C  CG    . ASN A 11  ? 2.1091 1.7076 2.6825 -0.2134 -0.6125 0.4830  114  ASN A CG    
69   O  OD1   . ASN A 11  ? 2.0257 1.6232 2.5517 -0.2143 -0.5850 0.4587  114  ASN A OD1   
70   N  ND2   . ASN A 11  ? 1.9711 1.5831 2.6350 -0.1980 -0.6068 0.4921  114  ASN A ND2   
71   N  N     . ARG A 12  ? 2.2647 1.8437 2.7460 -0.2577 -0.7264 0.5339  115  ARG A N     
72   C  CA    . ARG A 12  ? 2.1462 1.7029 2.5580 -0.2811 -0.7594 0.5455  115  ARG A CA    
73   C  C     . ARG A 12  ? 2.0839 1.6516 2.4490 -0.2804 -0.7419 0.5201  115  ARG A C     
74   O  O     . ARG A 12  ? 1.9905 1.5394 2.2692 -0.2940 -0.7375 0.5071  115  ARG A O     
75   C  CB    . ARG A 12  ? 2.1278 1.6811 2.5890 -0.2902 -0.8051 0.5826  115  ARG A CB    
76   C  CG    . ARG A 12  ? 2.3305 1.8674 2.8274 -0.2950 -0.8297 0.6134  115  ARG A CG    
77   C  CD    . ARG A 12  ? 2.7721 2.2703 3.1788 -0.3204 -0.8510 0.6225  115  ARG A CD    
78   N  NE    . ARG A 12  ? 2.7854 2.2741 3.1359 -0.3452 -0.8793 0.6270  115  ARG A NE    
79   C  CZ    . ARG A 12  ? 2.5893 2.0479 2.8620 -0.3719 -0.8991 0.6325  115  ARG A CZ    
80   N  NH1   . ARG A 12  ? 2.5342 1.9705 2.7750 -0.3770 -0.8953 0.6353  115  ARG A NH1   
81   N  NH2   . ARG A 12  ? 2.3398 1.7880 2.5642 -0.3951 -0.9219 0.6347  115  ARG A NH2   
82   N  N     . GLU A 13  ? 2.1463 1.7436 2.5690 -0.2645 -0.7302 0.5131  116  GLU A N     
83   C  CA    . GLU A 13  ? 1.9306 1.5388 2.3156 -0.2628 -0.7144 0.4913  116  GLU A CA    
84   C  C     . GLU A 13  ? 1.9757 1.5927 2.3171 -0.2529 -0.6711 0.4576  116  GLU A C     
85   O  O     . GLU A 13  ? 1.9042 1.5212 2.1910 -0.2560 -0.6593 0.4404  116  GLU A O     
86   C  CB    . GLU A 13  ? 2.1508 1.7885 2.6128 -0.2480 -0.7123 0.4936  116  GLU A CB    
87   C  CG    . GLU A 13  ? 2.1283 1.7904 2.6786 -0.2256 -0.6893 0.4911  116  GLU A CG    
88   C  CD    . GLU A 13  ? 2.1551 1.8437 2.7828 -0.2127 -0.6888 0.4958  116  GLU A CD    
89   O  OE1   . GLU A 13  ? 2.2208 1.9138 2.8269 -0.2179 -0.6963 0.4924  116  GLU A OE1   
90   O  OE2   . GLU A 13  ? 1.8672 1.5707 2.5777 -0.1978 -0.6794 0.5028  116  GLU A OE2   
91   N  N     . ILE A 14  ? 2.1605 1.7849 2.5256 -0.2415 -0.6473 0.4485  117  ILE A N     
92   C  CA    . ILE A 14  ? 1.7245 1.3583 2.0475 -0.2345 -0.6088 0.4184  117  ILE A CA    
93   C  C     . ILE A 14  ? 1.7809 1.3867 2.0119 -0.2529 -0.6137 0.4147  117  ILE A C     
94   O  O     . ILE A 14  ? 2.0808 1.6910 2.2590 -0.2526 -0.5922 0.3935  117  ILE A O     
95   C  CB    . ILE A 14  ? 1.5384 1.1849 1.9090 -0.2207 -0.5834 0.4102  117  ILE A CB    
96   C  CG1   . ILE A 14  ? 1.7383 1.4146 2.1899 -0.2011 -0.5668 0.4051  117  ILE A CG1   
97   C  CG2   . ILE A 14  ? 1.4589 1.1095 1.7763 -0.2195 -0.5507 0.3837  117  ILE A CG2   
98   C  CD1   . ILE A 14  ? 1.6160 1.3029 2.1124 -0.1884 -0.5378 0.3943  117  ILE A CD1   
99   N  N     . GLY A 15  ? 1.8886 1.4646 2.0996 -0.2693 -0.6415 0.4360  118  GLY A N     
100  C  CA    . GLY A 15  ? 1.8620 1.4073 1.9841 -0.2887 -0.6466 0.4338  118  GLY A CA    
101  C  C     . GLY A 15  ? 1.9352 1.4653 1.9977 -0.3030 -0.6596 0.4332  118  GLY A C     
102  O  O     . GLY A 15  ? 1.7637 1.2739 1.7492 -0.3149 -0.6501 0.4218  118  GLY A O     
103  N  N     . PHE A 16  ? 1.8969 1.4346 1.9935 -0.3026 -0.6799 0.4448  119  PHE A N     
104  C  CA    . PHE A 16  ? 1.9239 1.4458 1.9646 -0.3169 -0.6911 0.4432  119  PHE A CA    
105  C  C     . PHE A 16  ? 2.1393 1.6792 2.1535 -0.3043 -0.6532 0.4133  119  PHE A C     
106  O  O     . PHE A 16  ? 1.9666 1.4858 1.9065 -0.3164 -0.6462 0.4031  119  PHE A O     
107  C  CB    . PHE A 16  ? 2.0321 1.5597 2.1217 -0.3201 -0.7231 0.4641  119  PHE A CB    
108  C  CG    . PHE A 16  ? 2.2522 1.7535 2.2795 -0.3423 -0.7449 0.4693  119  PHE A CG    
109  C  CD1   . PHE A 16  ? 2.2373 1.7050 2.1697 -0.3608 -0.7402 0.4602  119  PHE A CD1   
110  C  CD2   . PHE A 16  ? 2.1578 1.6670 2.2216 -0.3455 -0.7687 0.4829  119  PHE A CD2   
111  C  CE1   . PHE A 16  ? 2.2825 1.7222 2.1545 -0.3828 -0.7579 0.4636  119  PHE A CE1   
112  C  CE2   . PHE A 16  ? 2.2426 1.7257 2.2469 -0.3680 -0.7884 0.4869  119  PHE A CE2   
113  C  CZ    . PHE A 16  ? 2.1561 1.6031 2.0629 -0.3869 -0.7825 0.4768  119  PHE A CZ    
114  N  N     . ALA A 17  ? 2.1261 1.7036 2.2002 -0.2806 -0.6275 0.3997  120  ALA A N     
115  C  CA    . ALA A 17  ? 1.7708 1.3684 1.8254 -0.2678 -0.5929 0.3737  120  ALA A CA    
116  C  C     . ALA A 17  ? 2.0052 1.5996 2.0082 -0.2676 -0.5649 0.3555  120  ALA A C     
117  O  O     . ALA A 17  ? 1.6086 1.2037 1.5648 -0.2668 -0.5441 0.3390  120  ALA A O     
118  C  CB    . ALA A 17  ? 1.6115 1.2488 1.7425 -0.2444 -0.5741 0.3654  120  ALA A CB    
119  N  N     . ILE A 18  ? 1.7677 1.3587 1.7806 -0.2684 -0.5632 0.3588  121  ILE A N     
120  C  CA    . ILE A 18  ? 1.7270 1.3165 1.6945 -0.2691 -0.5371 0.3422  121  ILE A CA    
121  C  C     . ILE A 18  ? 1.9138 1.4636 1.7990 -0.2914 -0.5480 0.3466  121  ILE A C     
122  O  O     . ILE A 18  ? 1.7822 1.3297 1.6171 -0.2929 -0.5238 0.3303  121  ILE A O     
123  C  CB    . ILE A 18  ? 1.6680 1.2664 1.6744 -0.2631 -0.5298 0.3432  121  ILE A CB    
124  C  CG1   . ILE A 18  ? 1.7237 1.3574 1.8096 -0.2425 -0.5170 0.3381  121  ILE A CG1   
125  C  CG2   . ILE A 18  ? 1.8672 1.4678 1.8307 -0.2640 -0.5018 0.3254  121  ILE A CG2   
126  C  CD1   . ILE A 18  ? 1.9132 1.5537 2.0394 -0.2366 -0.5068 0.3376  121  ILE A CD1   
127  N  N     . GLY A 19  ? 1.7946 1.3129 1.6648 -0.3097 -0.5839 0.3688  122  GLY A N     
128  C  CA    . GLY A 19  ? 1.9995 1.4755 1.7887 -0.3338 -0.5959 0.3742  122  GLY A CA    
129  C  C     . GLY A 19  ? 2.1255 1.5792 1.8959 -0.3457 -0.6047 0.3845  122  GLY A C     
130  O  O     . GLY A 19  ? 2.3820 1.7981 2.0813 -0.3672 -0.6134 0.3889  122  GLY A O     
131  N  N     . MET A 20  ? 2.1647 1.6381 1.9947 -0.3331 -0.6014 0.3880  123  MET A N     
132  C  CA    . MET A 20  ? 2.2428 1.6959 2.0626 -0.3429 -0.6091 0.3986  123  MET A CA    
133  C  C     . MET A 20  ? 2.3697 1.8378 2.2725 -0.3318 -0.6235 0.4148  123  MET A C     
134  O  O     . MET A 20  ? 1.9657 1.4676 1.9328 -0.3119 -0.6113 0.4076  123  MET A O     
135  C  CB    . MET A 20  ? 1.9738 1.4351 1.7656 -0.3381 -0.5727 0.3764  123  MET A CB    
136  C  CG    . MET A 20  ? 1.8435 1.3498 1.6804 -0.3142 -0.5386 0.3538  123  MET A CG    
137  S  SD    . MET A 20  ? 1.8850 1.4021 1.6914 -0.3117 -0.5003 0.3311  123  MET A SD    
138  C  CE    . MET A 20  ? 2.3052 1.8728 2.1478 -0.2881 -0.4667 0.3067  123  MET A CE    
139  N  N     . PRO A 21  ? 2.4956 1.9382 2.3997 -0.3441 -0.6484 0.4372  124  PRO A N     
140  C  CA    . PRO A 21  ? 2.2415 1.6960 2.2287 -0.3332 -0.6618 0.4550  124  PRO A CA    
141  C  C     . PRO A 21  ? 2.3965 1.8780 2.4295 -0.3134 -0.6265 0.4365  124  PRO A C     
142  O  O     . PRO A 21  ? 2.4403 1.9248 2.4352 -0.3129 -0.5977 0.4153  124  PRO A O     
143  C  CB    . PRO A 21  ? 2.2710 1.6874 2.2334 -0.3535 -0.6943 0.4825  124  PRO A CB    
144  C  CG    . PRO A 21  ? 2.2409 1.6303 2.1099 -0.3707 -0.6827 0.4701  124  PRO A CG    
145  C  CD    . PRO A 21  ? 2.2846 1.6842 2.1138 -0.3693 -0.6654 0.4485  124  PRO A CD    
146  N  N     . VAL A 22  ? 2.4544 1.9555 2.5719 -0.2978 -0.6287 0.4451  125  VAL A N     
147  C  CA    . VAL A 22  ? 2.3045 1.8291 2.4699 -0.2801 -0.5954 0.4281  125  VAL A CA    
148  C  C     . VAL A 22  ? 2.4167 1.9203 2.5704 -0.2871 -0.5913 0.4326  125  VAL A C     
149  O  O     . VAL A 22  ? 2.3510 1.8681 2.5134 -0.2787 -0.5592 0.4125  125  VAL A O     
150  C  CB    . VAL A 22  ? 2.0208 1.5679 2.2799 -0.2626 -0.5974 0.4367  125  VAL A CB    
151  C  CG1   . VAL A 22  ? 1.9674 1.5404 2.2681 -0.2449 -0.5576 0.4132  125  VAL A CG1   
152  C  CG2   . VAL A 22  ? 1.9858 1.5477 2.2552 -0.2594 -0.6097 0.4387  125  VAL A CG2   
153  N  N     . CYS A 23  ? 2.3619 1.8320 2.4935 -0.3037 -0.6235 0.4588  126  CYS A N     
154  C  CA    . CYS A 23  ? 2.2591 1.7064 2.3801 -0.3110 -0.6214 0.4656  126  CYS A CA    
155  C  C     . CYS A 23  ? 2.3174 1.7582 2.3656 -0.3196 -0.5950 0.4420  126  CYS A C     
156  O  O     . CYS A 23  ? 2.5668 1.9968 2.6119 -0.3220 -0.5820 0.4393  126  CYS A O     
157  C  CB    . CYS A 23  ? 2.3201 1.7320 2.4279 -0.3287 -0.6644 0.5009  126  CYS A CB    
158  S  SG    . CYS A 23  ? 2.6969 2.1162 2.9042 -0.3187 -0.6963 0.5346  126  CYS A SG    
159  N  N     . GLU A 24  ? 2.2431 1.6900 2.2351 -0.3241 -0.5858 0.4252  127  GLU A N     
160  C  CA    . GLU A 24  ? 2.3575 1.8018 2.2861 -0.3309 -0.5588 0.4029  127  GLU A CA    
161  C  C     . GLU A 24  ? 2.3082 1.7857 2.2686 -0.3150 -0.5199 0.3769  127  GLU A C     
162  O  O     . GLU A 24  ? 2.2893 1.7681 2.2069 -0.3201 -0.4965 0.3594  127  GLU A O     
163  C  CB    . GLU A 24  ? 2.3444 1.7866 2.2103 -0.3386 -0.5575 0.3928  127  GLU A CB    
164  C  CG    . GLU A 24  ? 2.6025 2.0063 2.4191 -0.3596 -0.5934 0.4155  127  GLU A CG    
165  C  CD    . GLU A 24  ? 2.6666 2.0613 2.4110 -0.3697 -0.5857 0.4024  127  GLU A CD    
166  O  OE1   . GLU A 24  ? 2.6123 2.0301 2.3438 -0.3602 -0.5520 0.3771  127  GLU A OE1   
167  O  OE2   . GLU A 24  ? 2.7408 2.1046 2.4415 -0.3878 -0.6131 0.4180  127  GLU A OE2   
168  N  N     . PHE A 25  ? 2.2283 1.7321 2.2615 -0.2971 -0.5121 0.3740  128  PHE A N     
169  C  CA    . PHE A 25  ? 2.0714 1.6043 2.1351 -0.2842 -0.4764 0.3502  128  PHE A CA    
170  C  C     . PHE A 25  ? 2.1771 1.7023 2.2925 -0.2802 -0.4714 0.3568  128  PHE A C     
171  O  O     . PHE A 25  ? 2.3743 1.9123 2.4953 -0.2769 -0.4420 0.3374  128  PHE A O     
172  C  CB    . PHE A 25  ? 1.9838 1.5526 2.0873 -0.2672 -0.4636 0.3371  128  PHE A CB    
173  C  CG    . PHE A 25  ? 2.2191 1.7976 2.2763 -0.2690 -0.4636 0.3284  128  PHE A CG    
174  C  CD1   . PHE A 25  ? 2.0179 1.6046 2.0204 -0.2737 -0.4417 0.3092  128  PHE A CD1   
175  C  CD2   . PHE A 25  ? 2.2738 1.8533 2.3446 -0.2660 -0.4847 0.3400  128  PHE A CD2   
176  C  CE1   . PHE A 25  ? 2.0919 1.6860 2.0547 -0.2742 -0.4394 0.3018  128  PHE A CE1   
177  C  CE2   . PHE A 25  ? 1.9138 1.4993 1.9415 -0.2678 -0.4828 0.3316  128  PHE A CE2   
178  C  CZ    . PHE A 25  ? 2.0729 1.6650 2.0470 -0.2714 -0.4594 0.3126  128  PHE A CZ    
179  N  N     . ASP A 26  ? 2.2153 1.7197 2.3692 -0.2810 -0.4990 0.3841  129  ASP A N     
180  C  CA    . ASP A 26  ? 2.0232 1.5159 2.2266 -0.2773 -0.4940 0.3927  129  ASP A CA    
181  C  C     . ASP A 26  ? 1.9791 1.4429 2.1350 -0.2928 -0.4928 0.3956  129  ASP A C     
182  O  O     . ASP A 26  ? 2.0216 1.4783 2.2067 -0.2905 -0.4773 0.3934  129  ASP A O     
183  C  CB    . ASP A 26  ? 1.8463 1.3270 2.1105 -0.2726 -0.5248 0.4240  129  ASP A CB    
184  C  CG    . ASP A 26  ? 2.0524 1.5615 2.3712 -0.2570 -0.5246 0.4220  129  ASP A CG    
185  O  OD1   . ASP A 26  ? 2.4582 1.9758 2.7479 -0.2598 -0.5382 0.4218  129  ASP A OD1   
186  O  OD2   . ASP A 26  ? 2.0773 1.5986 2.4675 -0.2423 -0.5092 0.4201  129  ASP A OD2   
187  N  N     . MET A 27  ? 1.9846 1.4298 2.0673 -0.3092 -0.5072 0.3998  130  MET A N     
188  C  CA    . MET A 27  ? 2.3099 1.7261 2.3409 -0.3257 -0.5060 0.4025  130  MET A CA    
189  C  C     . MET A 27  ? 2.1038 1.5355 2.0859 -0.3295 -0.4727 0.3723  130  MET A C     
190  O  O     . MET A 27  ? 2.2193 1.6294 2.1404 -0.3454 -0.4721 0.3719  130  MET A O     
191  C  CB    . MET A 27  ? 2.4341 1.8159 2.4120 -0.3439 -0.5417 0.4270  130  MET A CB    
192  C  CG    . MET A 27  ? 2.2369 1.6253 2.1632 -0.3493 -0.5478 0.4195  130  MET A CG    
193  S  SD    . MET A 27  ? 2.4892 1.8309 2.3420 -0.3753 -0.5870 0.4461  130  MET A SD    
194  C  CE    . MET A 27  ? 2.4651 1.7795 2.2556 -0.3918 -0.5692 0.4386  130  MET A CE    
195  N  N     . VAL A 28  ? 2.1249 1.5938 2.1333 -0.3158 -0.4450 0.3480  131  VAL A N     
196  C  CA    . VAL A 28  ? 2.2084 1.6983 2.1790 -0.3184 -0.4139 0.3205  131  VAL A CA    
197  C  C     . VAL A 28  ? 2.1806 1.6742 2.1782 -0.3174 -0.3891 0.3084  131  VAL A C     
198  O  O     . VAL A 28  ? 2.0228 1.5305 2.0801 -0.3049 -0.3785 0.3040  131  VAL A O     
199  C  CB    . VAL A 28  ? 2.1234 1.6524 2.1018 -0.3060 -0.3996 0.3020  131  VAL A CB    
200  C  CG1   . VAL A 28  ? 2.0270 1.5806 1.9725 -0.3085 -0.3684 0.2761  131  VAL A CG1   
201  C  CG2   . VAL A 28  ? 2.0184 1.5402 1.9670 -0.3084 -0.4227 0.3133  131  VAL A CG2   
202  N  N     . LYS A 29  ? 2.2538 1.7331 2.2065 -0.3314 -0.3784 0.3026  132  LYS A N     
203  C  CA    . LYS A 29  ? 2.2026 1.6821 2.1734 -0.3337 -0.3547 0.2906  132  LYS A CA    
204  C  C     . LYS A 29  ? 2.2173 1.7381 2.1982 -0.3274 -0.3222 0.2612  132  LYS A C     
205  O  O     . LYS A 29  ? 2.6057 2.1305 2.6106 -0.3282 -0.3011 0.2492  132  LYS A O     
206  C  CB    . LYS A 29  ? 2.2818 1.7322 2.1991 -0.3523 -0.3545 0.2946  132  LYS A CB    
207  C  CG    . LYS A 29  ? 2.5120 1.9502 2.4487 -0.3572 -0.3366 0.2893  132  LYS A CG    
208  C  CD    . LYS A 29  ? 2.4945 1.9073 2.3735 -0.3762 -0.3340 0.2909  132  LYS A CD    
209  C  CE    . LYS A 29  ? 2.4642 1.8662 2.3608 -0.3820 -0.3135 0.2832  132  LYS A CE    
210  N  NZ    . LYS A 29  ? 2.8690 2.2475 2.7093 -0.4011 -0.3090 0.2837  132  LYS A NZ    
211  N  N     . ASP A 30  ? 1.9461 1.4963 1.9090 -0.3221 -0.3180 0.2501  133  ASP A N     
212  C  CA    . ASP A 30  ? 1.8187 1.4100 1.7880 -0.3172 -0.2897 0.2244  133  ASP A CA    
213  C  C     . ASP A 30  ? 1.7788 1.3847 1.8104 -0.3049 -0.2786 0.2175  133  ASP A C     
214  O  O     . ASP A 30  ? 1.8304 1.4359 1.8984 -0.2930 -0.2928 0.2284  133  ASP A O     
215  C  CB    . ASP A 30  ? 1.8094 1.4268 1.7521 -0.3121 -0.2904 0.2182  133  ASP A CB    
216  C  CG    . ASP A 30  ? 2.0042 1.6625 1.9377 -0.3116 -0.2627 0.1942  133  ASP A CG    
217  O  OD1   . ASP A 30  ? 1.9985 1.6759 1.9654 -0.3084 -0.2449 0.1807  133  ASP A OD1   
218  O  OD2   . ASP A 30  ? 2.0929 1.7639 1.9858 -0.3151 -0.2584 0.1894  133  ASP A OD2   
219  N  N     . PRO A 31  ? 1.6157 1.2333 1.6608 -0.3085 -0.2530 0.1996  134  PRO A N     
220  C  CA    . PRO A 31  ? 1.7581 1.3867 1.8590 -0.2982 -0.2390 0.1911  134  PRO A CA    
221  C  C     . PRO A 31  ? 1.8871 1.5540 2.0006 -0.2866 -0.2317 0.1791  134  PRO A C     
222  O  O     . PRO A 31  ? 1.7906 1.4619 1.9519 -0.2751 -0.2286 0.1790  134  PRO A O     
223  C  CB    . PRO A 31  ? 1.6833 1.3122 1.7813 -0.3096 -0.2125 0.1733  134  PRO A CB    
224  C  CG    . PRO A 31  ? 1.8056 1.4454 1.8464 -0.3228 -0.2084 0.1657  134  PRO A CG    
225  C  CD    . PRO A 31  ? 1.6988 1.3172 1.7088 -0.3237 -0.2351 0.1865  134  PRO A CD    
226  N  N     . GLU A 32  ? 1.7044 1.3985 1.7780 -0.2891 -0.2278 0.1695  135  GLU A N     
227  C  CA    . GLU A 32  ? 1.4496 1.1791 1.5336 -0.2778 -0.2222 0.1602  135  GLU A CA    
228  C  C     . GLU A 32  ? 1.5903 1.3114 1.6919 -0.2655 -0.2454 0.1774  135  GLU A C     
229  O  O     . GLU A 32  ? 1.6578 1.3977 1.7916 -0.2536 -0.2418 0.1734  135  GLU A O     
230  C  CB    . GLU A 32  ? 1.5245 1.2842 1.5639 -0.2829 -0.2129 0.1486  135  GLU A CB    
231  C  CG    . GLU A 32  ? 2.0045 1.8033 2.0540 -0.2720 -0.2043 0.1381  135  GLU A CG    
232  C  CD    . GLU A 32  ? 1.7700 1.6000 1.7808 -0.2763 -0.1947 0.1289  135  GLU A CD    
233  O  OE1   . GLU A 32  ? 1.4292 1.2485 1.4039 -0.2867 -0.1963 0.1319  135  GLU A OE1   
234  O  OE2   . GLU A 32  ? 1.3314 1.1964 1.3492 -0.2692 -0.1851 0.1196  135  GLU A OE2   
235  N  N     . VAL A 33  ? 1.6954 1.3877 1.7749 -0.2697 -0.2693 0.1965  136  VAL A N     
236  C  CA    . VAL A 33  ? 1.6927 1.3750 1.7866 -0.2611 -0.2940 0.2142  136  VAL A CA    
237  C  C     . VAL A 33  ? 1.4954 1.1669 1.6528 -0.2517 -0.2995 0.2239  136  VAL A C     
238  O  O     . VAL A 33  ? 1.9554 1.6390 2.1453 -0.2398 -0.3053 0.2273  136  VAL A O     
239  C  CB    . VAL A 33  ? 1.5180 1.1684 1.5685 -0.2716 -0.3185 0.2326  136  VAL A CB    
240  C  CG1   . VAL A 33  ? 1.6092 1.2443 1.6787 -0.2657 -0.3473 0.2536  136  VAL A CG1   
241  C  CG2   . VAL A 33  ? 1.5657 1.2285 1.5574 -0.2783 -0.3110 0.2229  136  VAL A CG2   
242  N  N     . GLN A 34  ? 1.5548 1.2030 1.7330 -0.2565 -0.2963 0.2286  137  GLN A N     
243  C  CA    . GLN A 34  ? 1.7558 1.3917 1.9991 -0.2470 -0.2995 0.2393  137  GLN A CA    
244  C  C     . GLN A 34  ? 1.7046 1.3668 1.9867 -0.2375 -0.2716 0.2190  137  GLN A C     
245  O  O     . GLN A 34  ? 1.6722 1.3374 2.0063 -0.2253 -0.2738 0.2250  137  GLN A O     
246  C  CB    . GLN A 34  ? 1.7654 1.3671 2.0200 -0.2547 -0.3018 0.2505  137  GLN A CB    
247  C  CG    . GLN A 34  ? 1.9851 1.5578 2.1976 -0.2662 -0.3292 0.2713  137  GLN A CG    
248  C  CD    . GLN A 34  ? 2.2512 1.8158 2.4705 -0.2618 -0.3626 0.2948  137  GLN A CD    
249  O  OE1   . GLN A 34  ? 2.0462 1.6146 2.3217 -0.2498 -0.3704 0.3049  137  GLN A OE1   
250  N  NE2   . GLN A 34  ? 2.0198 1.5725 2.1810 -0.2727 -0.3817 0.3033  137  GLN A NE2   
251  N  N     . ASP A 35  ? 1.4979 1.1792 1.7551 -0.2441 -0.2452 0.1952  138  ASP A N     
252  C  CA    . ASP A 35  ? 1.6078 1.3139 1.8930 -0.2380 -0.2187 0.1750  138  ASP A CA    
253  C  C     . ASP A 35  ? 1.6593 1.3953 1.9448 -0.2275 -0.2222 0.1716  138  ASP A C     
254  O  O     . ASP A 35  ? 1.5922 1.3421 1.9150 -0.2185 -0.2083 0.1631  138  ASP A O     
255  C  CB    . ASP A 35  ? 1.7842 1.5041 2.0382 -0.2506 -0.1924 0.1517  138  ASP A CB    
256  C  CG    . ASP A 35  ? 1.6957 1.3861 1.9598 -0.2602 -0.1819 0.1511  138  ASP A CG    
257  O  OD1   . ASP A 35  ? 2.0273 1.6918 2.3384 -0.2536 -0.1853 0.1635  138  ASP A OD1   
258  O  OD2   . ASP A 35  ? 1.7455 1.4389 1.9729 -0.2742 -0.1697 0.1389  138  ASP A OD2   
259  N  N     . PHE A 36  ? 1.5850 1.3292 1.8287 -0.2289 -0.2389 0.1777  139  PHE A N     
260  C  CA    . PHE A 36  ? 1.3323 1.1006 1.5765 -0.2186 -0.2441 0.1770  139  PHE A CA    
261  C  C     . PHE A 36  ? 1.3040 1.0604 1.5983 -0.2069 -0.2605 0.1937  139  PHE A C     
262  O  O     . PHE A 36  ? 1.3121 1.0865 1.6399 -0.1965 -0.2508 0.1873  139  PHE A O     
263  C  CB    . PHE A 36  ? 1.4264 1.1987 1.6159 -0.2232 -0.2582 0.1818  139  PHE A CB    
264  C  CG    . PHE A 36  ? 1.4736 1.2701 1.6583 -0.2134 -0.2609 0.1799  139  PHE A CG    
265  C  CD1   . PHE A 36  ? 1.7523 1.5765 1.9648 -0.2042 -0.2436 0.1669  139  PHE A CD1   
266  C  CD2   . PHE A 36  ? 1.4301 1.2192 1.5806 -0.2143 -0.2798 0.1910  139  PHE A CD2   
267  C  CE1   . PHE A 36  ? 1.4814 1.3267 1.6897 -0.1951 -0.2458 0.1660  139  PHE A CE1   
268  C  CE2   . PHE A 36  ? 1.5363 1.3453 1.6826 -0.2054 -0.2811 0.1892  139  PHE A CE2   
269  C  CZ    . PHE A 36  ? 1.5795 1.4172 1.7557 -0.1953 -0.2644 0.1772  139  PHE A CZ    
270  N  N     . ARG A 37  ? 1.6036 1.3300 1.9044 -0.2094 -0.2860 0.2160  140  ARG A N     
271  C  CA    . ARG A 37  ? 1.3648 1.0810 1.7149 -0.1997 -0.3054 0.2352  140  ARG A CA    
272  C  C     . ARG A 37  ? 1.5572 1.2724 1.9739 -0.1909 -0.2879 0.2319  140  ARG A C     
273  O  O     . ARG A 37  ? 1.8961 1.6158 2.3612 -0.1798 -0.2938 0.2404  140  ARG A O     
274  C  CB    . ARG A 37  ? 1.6576 1.3413 1.9980 -0.2070 -0.3374 0.2612  140  ARG A CB    
275  C  CG    . ARG A 37  ? 1.5659 1.2441 1.8351 -0.2182 -0.3513 0.2632  140  ARG A CG    
276  C  CD    . ARG A 37  ? 2.0155 1.6575 2.2639 -0.2303 -0.3759 0.2845  140  ARG A CD    
277  N  NE    . ARG A 37  ? 1.9071 1.5330 2.1688 -0.2302 -0.4097 0.3098  140  ARG A NE    
278  C  CZ    . ARG A 37  ? 1.9234 1.5311 2.2355 -0.2277 -0.4281 0.3320  140  ARG A CZ    
279  N  NH1   . ARG A 37  ? 1.9840 1.5842 2.3394 -0.2240 -0.4144 0.3320  140  ARG A NH1   
280  N  NH2   . ARG A 37  ? 2.0424 1.6387 2.3624 -0.2296 -0.4610 0.3554  140  ARG A NH2   
281  N  N     . ARG A 38  ? 1.7543 1.4627 2.1748 -0.1962 -0.2649 0.2191  141  ARG A N     
282  C  CA    . ARG A 38  ? 1.7167 1.4197 2.1981 -0.1891 -0.2439 0.2142  141  ARG A CA    
283  C  C     . ARG A 38  ? 1.5695 1.3015 2.0592 -0.1836 -0.2160 0.1906  141  ARG A C     
284  O  O     . ARG A 38  ? 1.5821 1.3179 2.1241 -0.1725 -0.2086 0.1919  141  ARG A O     
285  C  CB    . ARG A 38  ? 1.9298 1.6099 2.4100 -0.1985 -0.2288 0.2093  141  ARG A CB    
286  C  CG    . ARG A 38  ? 1.9687 1.6413 2.5046 -0.1931 -0.1996 0.1991  141  ARG A CG    
287  C  CD    . ARG A 38  ? 1.9302 1.5832 2.4527 -0.2050 -0.1789 0.1877  141  ARG A CD    
288  N  NE    . ARG A 38  ? 2.2167 1.8373 2.7449 -0.2086 -0.1991 0.2106  141  ARG A NE    
289  C  CZ    . ARG A 38  ? 2.4290 2.0260 2.9496 -0.2185 -0.1860 0.2066  141  ARG A CZ    
290  N  NH1   . ARG A 38  ? 2.7075 2.3091 3.2133 -0.2270 -0.1528 0.1799  141  ARG A NH1   
291  N  NH2   . ARG A 38  ? 2.3509 1.9182 2.8774 -0.2210 -0.2072 0.2304  141  ARG A NH2   
292  N  N     . ASN A 39  ? 1.4868 1.2398 1.9260 -0.1919 -0.2004 0.1698  142  ASN A N     
293  C  CA    . ASN A 39  ? 1.5887 1.3682 2.0307 -0.1897 -0.1731 0.1472  142  ASN A CA    
294  C  C     . ASN A 39  ? 1.5678 1.3734 2.0061 -0.1801 -0.1814 0.1482  142  ASN A C     
295  O  O     . ASN A 39  ? 1.5604 1.3830 2.0186 -0.1747 -0.1623 0.1353  142  ASN A O     
296  C  CB    . ASN A 39  ? 1.4211 1.2147 1.8131 -0.2038 -0.1542 0.1262  142  ASN A CB    
297  C  CG    . ASN A 39  ? 1.3898 1.1577 1.7849 -0.2146 -0.1417 0.1220  142  ASN A CG    
298  O  OD1   . ASN A 39  ? 1.7887 1.5485 2.2122 -0.2163 -0.1167 0.1095  142  ASN A OD1   
299  N  ND2   . ASN A 39  ? 1.7120 1.4646 2.0763 -0.2228 -0.1575 0.1322  142  ASN A ND2   
300  N  N     . ILE A 40  ? 1.6313 1.4383 2.0426 -0.1788 -0.2083 0.1627  143  ILE A N     
301  C  CA    . ILE A 40  ? 1.3573 1.1866 1.7641 -0.1700 -0.2155 0.1638  143  ILE A CA    
302  C  C     . ILE A 40  ? 1.3666 1.1905 1.8334 -0.1576 -0.2216 0.1752  143  ILE A C     
303  O  O     . ILE A 40  ? 1.5967 1.4397 2.0701 -0.1495 -0.2211 0.1730  143  ILE A O     
304  C  CB    . ILE A 40  ? 1.1837 1.0116 1.5434 -0.1734 -0.2404 0.1755  143  ILE A CB    
305  C  CG1   . ILE A 40  ? 1.2318 1.0888 1.5677 -0.1678 -0.2371 0.1678  143  ILE A CG1   
306  C  CG2   . ILE A 40  ? 1.3838 1.1859 1.7654 -0.1709 -0.2707 0.2005  143  ILE A CG2   
307  C  CD1   . ILE A 40  ? 1.0465 0.9321 1.3587 -0.1713 -0.2107 0.1459  143  ILE A CD1   
308  N  N     . LEU A 41  ? 1.3683 1.1671 1.8818 -0.1557 -0.2268 0.1881  144  LEU A N     
309  C  CA    . LEU A 41  ? 1.3862 1.1815 1.9651 -0.1437 -0.2299 0.1993  144  LEU A CA    
310  C  C     . LEU A 41  ? 1.3088 1.1194 1.9173 -0.1379 -0.1965 0.1795  144  LEU A C     
311  O  O     . LEU A 41  ? 1.5310 1.3463 2.1871 -0.1273 -0.1955 0.1849  144  LEU A O     
312  C  CB    . LEU A 41  ? 1.4020 1.1674 2.0275 -0.1429 -0.2422 0.2193  144  LEU A CB    
313  C  CG    . LEU A 41  ? 1.1388 0.8852 1.7389 -0.1497 -0.2781 0.2425  144  LEU A CG    
314  C  CD1   . LEU A 41  ? 1.5212 1.2398 2.1741 -0.1480 -0.2896 0.2641  144  LEU A CD1   
315  C  CD2   . LEU A 41  ? 1.3292 1.0855 1.9158 -0.1469 -0.3053 0.2554  144  LEU A CD2   
316  N  N     . ASN A 42  ? 1.3490 1.1666 1.9293 -0.1460 -0.1692 0.1568  145  ASN A N     
317  C  CA    . ASN A 42  ? 1.4529 1.2853 2.0489 -0.1437 -0.1375 0.1364  145  ASN A CA    
318  C  C     . ASN A 42  ? 1.6637 1.5249 2.2416 -0.1378 -0.1404 0.1322  145  ASN A C     
319  O  O     . ASN A 42  ? 1.6679 1.5379 2.2776 -0.1306 -0.1243 0.1256  145  ASN A O     
320  C  CB    . ASN A 42  ? 1.5625 1.3970 2.1229 -0.1572 -0.1111 0.1136  145  ASN A CB    
321  C  CG    . ASN A 42  ? 1.9725 1.7762 2.5511 -0.1634 -0.1048 0.1162  145  ASN A CG    
322  O  OD1   . ASN A 42  ? 1.8357 1.6177 2.4452 -0.1583 -0.1247 0.1374  145  ASN A OD1   
323  N  ND2   . ASN A 42  ? 2.1842 1.9854 2.7430 -0.1755 -0.0774 0.0952  145  ASN A ND2   
324  N  N     . VAL A 43  ? 1.4959 1.3705 2.0231 -0.1408 -0.1592 0.1361  146  VAL A N     
325  C  CA    . VAL A 43  ? 1.5436 1.4429 2.0547 -0.1343 -0.1640 0.1350  146  VAL A CA    
326  C  C     . VAL A 43  ? 1.4370 1.3293 1.9929 -0.1228 -0.1826 0.1533  146  VAL A C     
327  O  O     . VAL A 43  ? 1.4606 1.3685 2.0319 -0.1150 -0.1765 0.1503  146  VAL A O     
328  C  CB    . VAL A 43  ? 1.5142 1.4259 1.9630 -0.1400 -0.1781 0.1358  146  VAL A CB    
329  C  CG1   . VAL A 43  ? 1.4474 1.3851 1.8786 -0.1333 -0.1783 0.1329  146  VAL A CG1   
330  C  CG2   . VAL A 43  ? 1.6309 1.5489 2.0412 -0.1526 -0.1622 0.1205  146  VAL A CG2   
331  N  N     . CYS A 44  ? 1.4455 1.3144 2.0231 -0.1227 -0.2063 0.1734  147  CYS A N     
332  C  CA    . CYS A 44  ? 1.3597 1.2223 1.9831 -0.1137 -0.2267 0.1930  147  CYS A CA    
333  C  C     . CYS A 44  ? 1.3137 1.1744 2.0064 -0.1049 -0.2069 0.1908  147  CYS A C     
334  O  O     . CYS A 44  ? 1.4174 1.2876 2.1432 -0.0961 -0.2093 0.1959  147  CYS A O     
335  C  CB    . CYS A 44  ? 1.3696 1.2077 1.9965 -0.1181 -0.2585 0.2165  147  CYS A CB    
336  S  SG    . CYS A 44  ? 1.5045 1.3386 2.0486 -0.1302 -0.2791 0.2189  147  CYS A SG    
337  N  N     . LYS A 45  ? 1.4364 1.2835 2.1521 -0.1075 -0.1856 0.1829  148  LYS A N     
338  C  CA    . LYS A 45  ? 1.1894 1.0313 1.9717 -0.0995 -0.1622 0.1795  148  LYS A CA    
339  C  C     . LYS A 45  ? 1.5896 1.4530 2.3648 -0.0968 -0.1345 0.1585  148  LYS A C     
340  O  O     . LYS A 45  ? 1.5427 1.4097 2.3677 -0.0875 -0.1257 0.1610  148  LYS A O     
341  C  CB    . LYS A 45  ? 1.4518 1.2711 2.2533 -0.1043 -0.1422 0.1736  148  LYS A CB    
342  N  N     . GLU A 46  ? 1.6631 1.5414 2.3775 -0.1055 -0.1207 0.1387  149  GLU A N     
343  C  CA    . GLU A 46  ? 1.6219 1.5217 2.3230 -0.1046 -0.0970 0.1204  149  GLU A CA    
344  C  C     . GLU A 46  ? 1.4438 1.3621 2.1418 -0.0961 -0.1143 0.1294  149  GLU A C     
345  O  O     . GLU A 46  ? 1.4935 1.4258 2.2000 -0.0920 -0.0964 0.1195  149  GLU A O     
346  C  CB    . GLU A 46  ? 1.8067 1.7204 2.4434 -0.1172 -0.0823 0.1002  149  GLU A CB    
347  C  CG    . GLU A 46  ? 1.7135 1.6102 2.3504 -0.1278 -0.0581 0.0860  149  GLU A CG    
348  C  CD    . GLU A 46  ? 1.8316 1.7447 2.4047 -0.1421 -0.0467 0.0676  149  GLU A CD    
349  O  OE1   . GLU A 46  ? 1.9444 1.8831 2.4762 -0.1423 -0.0575 0.0672  149  GLU A OE1   
350  O  OE2   . GLU A 46  ? 2.0460 1.9465 2.6118 -0.1535 -0.0266 0.0541  149  GLU A OE2   
351  N  N     . ALA A 47  ? 1.6046 1.5210 2.2883 -0.0946 -0.1475 0.1477  150  ALA A N     
352  C  CA    . ALA A 47  ? 1.6703 1.6005 2.3489 -0.0879 -0.1646 0.1567  150  ALA A CA    
353  C  C     . ALA A 47  ? 1.5097 1.4315 2.2553 -0.0784 -0.1758 0.1737  150  ALA A C     
354  O  O     . ALA A 47  ? 1.6610 1.5957 2.4245 -0.0715 -0.1706 0.1726  150  ALA A O     
355  C  CB    . ALA A 47  ? 1.3773 1.3073 2.0040 -0.0927 -0.1932 0.1669  150  ALA A CB    
356  N  N     . VAL A 48  ? 1.5542 1.4552 2.3391 -0.0782 -0.1916 0.1907  151  VAL A N     
357  C  CA    . VAL A 48  ? 1.5479 1.4431 2.4020 -0.0697 -0.2044 0.2097  151  VAL A CA    
358  C  C     . VAL A 48  ? 1.7453 1.6427 2.6570 -0.0622 -0.1710 0.1991  151  VAL A C     
359  O  O     . VAL A 48  ? 1.9695 1.8721 2.9326 -0.0539 -0.1730 0.2083  151  VAL A O     
360  C  CB    . VAL A 48  ? 1.4910 1.3644 2.3729 -0.0722 -0.2317 0.2331  151  VAL A CB    
361  C  CG1   . VAL A 48  ? 0.9893 0.8580 1.8098 -0.0811 -0.2641 0.2432  151  VAL A CG1   
362  C  CG2   . VAL A 48  ? 1.6693 1.5261 2.5695 -0.0745 -0.2109 0.2263  151  VAL A CG2   
363  N  N     . ASP A 49  ? 1.6019 1.4943 2.5055 -0.0661 -0.1389 0.1794  152  ASP A N     
364  C  CA    . ASP A 49  ? 1.6168 1.5091 2.5650 -0.0611 -0.1024 0.1657  152  ASP A CA    
365  C  C     . ASP A 49  ? 1.4645 1.3787 2.3838 -0.0602 -0.0858 0.1495  152  ASP A C     
366  O  O     . ASP A 49  ? 1.5555 1.4710 2.5143 -0.0551 -0.0598 0.1415  152  ASP A O     
367  C  CB    . ASP A 49  ? 1.7861 1.6623 2.7300 -0.0681 -0.0725 0.1489  152  ASP A CB    
368  C  CG    . ASP A 49  ? 1.6822 1.5334 2.6783 -0.0657 -0.0799 0.1654  152  ASP A CG    
369  O  OD1   . ASP A 49  ? 1.5737 1.4190 2.5582 -0.0676 -0.1137 0.1842  152  ASP A OD1   
370  O  OD2   . ASP A 49  ? 1.9771 1.8132 3.0256 -0.0622 -0.0509 0.1599  152  ASP A OD2   
371  N  N     . LEU A 50  ? 1.4913 1.4218 2.3436 -0.0650 -0.0993 0.1451  153  LEU A N     
372  C  CA    . LEU A 50  ? 1.7449 1.6968 2.5707 -0.0631 -0.0882 0.1340  153  LEU A CA    
373  C  C     . LEU A 50  ? 1.7720 1.7311 2.6242 -0.0543 -0.1102 0.1510  153  LEU A C     
374  O  O     . LEU A 50  ? 1.7159 1.6873 2.5780 -0.0495 -0.0961 0.1449  153  LEU A O     
375  C  CB    . LEU A 50  ? 1.5898 1.5570 2.3367 -0.0714 -0.0913 0.1231  153  LEU A CB    
376  C  CG    . LEU A 50  ? 1.7595 1.7500 2.4719 -0.0708 -0.0775 0.1107  153  LEU A CG    
377  C  CD1   . LEU A 50  ? 1.5766 1.5675 2.3031 -0.0737 -0.0398 0.0917  153  LEU A CD1   
378  C  CD2   . LEU A 50  ? 1.7352 1.7412 2.3765 -0.0779 -0.0857 0.1053  153  LEU A CD2   
379  N  N     . ARG A 51  ? 1.7308 1.6816 2.5927 -0.0534 -0.1447 0.1723  154  ARG A N     
380  C  CA    . ARG A 51  ? 1.5782 1.5330 2.4676 -0.0474 -0.1683 0.1899  154  ARG A CA    
381  C  C     . ARG A 51  ? 1.6892 1.6380 2.6643 -0.0394 -0.1624 0.2005  154  ARG A C     
382  O  O     . ARG A 51  ? 1.7931 1.7471 2.7988 -0.0349 -0.1795 0.2147  154  ARG A O     
383  C  CB    . ARG A 51  ? 1.6137 1.5591 2.4795 -0.0523 -0.2080 0.2093  154  ARG A CB    
384  C  CG    . ARG A 51  ? 1.5140 1.4638 2.2987 -0.0599 -0.2150 0.2012  154  ARG A CG    
385  C  CD    . ARG A 51  ? 1.7461 1.6780 2.5119 -0.0674 -0.2446 0.2165  154  ARG A CD    
386  N  NE    . ARG A 51  ? 1.5075 1.4306 2.3002 -0.0673 -0.2775 0.2399  154  ARG A NE    
387  C  CZ    . ARG A 51  ? 1.3688 1.2744 2.1502 -0.0748 -0.3077 0.2573  154  ARG A CZ    
388  N  NH1   . ARG A 51  ? 1.2358 1.1301 1.9808 -0.0820 -0.3089 0.2543  154  ARG A NH1   
389  N  NH2   . ARG A 51  ? 2.0081 1.9070 2.8139 -0.0765 -0.3380 0.2787  154  ARG A NH2   
390  N  N     . ASP A 52  ? 1.6665 1.6039 2.6824 -0.0381 -0.1379 0.1942  155  ASP A N     
391  C  CA    . ASP A 52  ? 1.7158 1.6462 2.8198 -0.0297 -0.1300 0.2055  155  ASP A CA    
392  C  C     . ASP A 52  ? 1.7043 1.6334 2.8342 -0.0268 -0.0835 0.1845  155  ASP A C     
393  O  O     . ASP A 52  ? 1.7470 1.6652 2.9499 -0.0205 -0.0680 0.1901  155  ASP A O     
394  C  CB    . ASP A 52  ? 1.9814 1.8931 3.1266 -0.0298 -0.1479 0.2248  155  ASP A CB    
395  C  CG    . ASP A 52  ? 1.9125 1.8226 3.0374 -0.0341 -0.1952 0.2481  155  ASP A CG    
396  O  OD1   . ASP A 52  ? 1.6557 1.5780 2.7672 -0.0339 -0.2151 0.2554  155  ASP A OD1   
397  O  OD2   . ASP A 52  ? 2.0537 1.9485 3.1739 -0.0387 -0.2117 0.2590  155  ASP A OD2   
398  N  N     . LEU A 53  ? 1.6369 1.5761 2.7090 -0.0318 -0.0604 0.1611  156  LEU A N     
399  C  CA    . LEU A 53  ? 1.6290 1.5664 2.7178 -0.0314 -0.0164 0.1405  156  LEU A CA    
400  C  C     . LEU A 53  ? 1.8375 1.7811 2.9879 -0.0217 -0.0098 0.1482  156  LEU A C     
401  O  O     . LEU A 53  ? 2.0222 1.9541 3.2456 -0.0156 0.0083  0.1524  156  LEU A O     
402  C  CB    . LEU A 53  ? 1.5876 1.5376 2.5978 -0.0403 0.0010  0.1172  156  LEU A CB    
403  C  CG    . LEU A 53  ? 1.8470 1.7916 2.7995 -0.0517 0.0042  0.1049  156  LEU A CG    
404  C  CD1   . LEU A 53  ? 1.6968 1.6577 2.5797 -0.0606 0.0215  0.0839  156  LEU A CD1   
405  C  CD2   . LEU A 53  ? 2.0064 1.9268 2.9967 -0.0544 0.0292  0.0981  156  LEU A CD2   
406  N  N     . ASN A 54  ? 1.8393 1.8011 2.9631 -0.0201 -0.0231 0.1503  157  ASN A N     
407  C  CA    . ASN A 54  ? 1.9661 1.9350 3.1473 -0.0115 -0.0251 0.1617  157  ASN A CA    
408  C  C     . ASN A 54  ? 2.0571 2.0249 3.2801 -0.0075 -0.0667 0.1907  157  ASN A C     
409  O  O     . ASN A 54  ? 2.1297 2.0986 3.3084 -0.0122 -0.0999 0.2002  157  ASN A O     
410  C  CB    . ASN A 54  ? 1.7808 1.7676 2.9152 -0.0121 -0.0229 0.1531  157  ASN A CB    
411  C  CG    . ASN A 54  ? 1.9446 1.9383 3.1370 -0.0043 -0.0197 0.1620  157  ASN A CG    
412  O  OD1   . ASN A 54  ? 2.1061 2.1087 3.3018 -0.0020 -0.0496 0.1780  157  ASN A OD1   
413  N  ND2   . ASN A 54  ? 1.9924 1.9805 3.2300 -0.0012 0.0180  0.1513  157  ASN A ND2   
414  N  N     . SER A 55  ? 1.9897 1.9551 3.2992 0.0004  -0.0647 0.2052  158  SER A N     
415  C  CA    . SER A 55  ? 2.0378 2.0007 3.3952 0.0026  -0.1039 0.2347  158  SER A CA    
416  C  C     . SER A 55  ? 1.9675 1.9425 3.2928 -0.0007 -0.1431 0.2486  158  SER A C     
417  O  O     . SER A 55  ? 2.1837 2.1538 3.4796 -0.0065 -0.1786 0.2626  158  SER A O     
418  C  CB    . SER A 55  ? 2.0312 1.9910 3.4944 0.0119  -0.0913 0.2481  158  SER A CB    
419  O  OG    . SER A 55  ? 2.0765 2.0203 3.5681 0.0144  -0.0546 0.2357  158  SER A OG    
420  N  N     . PRO A 56  ? 1.7219 1.7106 3.0484 0.0018  -0.1386 0.2455  159  PRO A N     
421  C  CA    . PRO A 56  ? 1.6740 1.6706 2.9720 -0.0024 -0.1763 0.2597  159  PRO A CA    
422  C  C     . PRO A 56  ? 1.8000 1.8011 3.0013 -0.0081 -0.1785 0.2445  159  PRO A C     
423  O  O     . PRO A 56  ? 1.4823 1.4807 2.6394 -0.0145 -0.2113 0.2545  159  PRO A O     
424  C  CB    . PRO A 56  ? 1.4014 1.4092 2.7597 0.0034  -0.1688 0.2657  159  PRO A CB    
425  C  CG    . PRO A 56  ? 1.5748 1.5836 2.9445 0.0089  -0.1196 0.2427  159  PRO A CG    
426  C  CD    . PRO A 56  ? 1.7261 1.7211 3.0905 0.0081  -0.1007 0.2325  159  PRO A CD    
427  N  N     . HIS A 57  ? 1.7234 1.7308 2.8913 -0.0064 -0.1436 0.2211  160  HIS A N     
428  C  CA    . HIS A 57  ? 1.5443 1.5600 2.6306 -0.0100 -0.1445 0.2092  160  HIS A CA    
429  C  C     . HIS A 57  ? 1.5606 1.5709 2.5810 -0.0167 -0.1538 0.2035  160  HIS A C     
430  O  O     . HIS A 57  ? 1.5765 1.5895 2.5383 -0.0206 -0.1731 0.2053  160  HIS A O     
431  C  CB    . HIS A 57  ? 1.7137 1.7389 2.7870 -0.0070 -0.1057 0.1883  160  HIS A CB    
432  C  CG    . HIS A 57  ? 1.6387 1.6749 2.6389 -0.0091 -0.1065 0.1793  160  HIS A CG    
433  N  ND1   . HIS A 57  ? 1.6160 1.6612 2.5824 -0.0091 -0.0753 0.1602  160  HIS A ND1   
434  C  CD2   . HIS A 57  ? 1.7875 1.8263 2.7428 -0.0114 -0.1339 0.1877  160  HIS A CD2   
435  C  CE1   . HIS A 57  ? 1.8185 1.8732 2.7260 -0.0101 -0.0844 0.1587  160  HIS A CE1   
436  N  NE2   . HIS A 57  ? 1.9631 2.0131 2.8630 -0.0111 -0.1184 0.1744  160  HIS A NE2   
437  N  N     . SER A 58  ? 1.7615 1.7630 2.7908 -0.0183 -0.1389 0.1963  161  SER A N     
438  C  CA    . SER A 58  ? 1.5034 1.5007 2.4707 -0.0253 -0.1444 0.1893  161  SER A CA    
439  C  C     . SER A 58  ? 1.5148 1.5037 2.4623 -0.0300 -0.1849 0.2080  161  SER A C     
440  O  O     . SER A 58  ? 1.5163 1.5059 2.3980 -0.0356 -0.1947 0.2037  161  SER A O     
441  C  CB    . SER A 58  ? 1.5892 1.5756 2.5765 -0.0270 -0.1212 0.1795  161  SER A CB    
442  O  OG    . SER A 58  ? 1.8308 1.8225 2.8198 -0.0261 -0.0819 0.1591  161  SER A OG    
443  N  N     . ARG A 59  ? 1.5327 1.5136 2.5360 -0.0286 -0.2086 0.2293  162  ARG A N     
444  C  CA    . ARG A 59  ? 1.2015 1.1728 2.1826 -0.0355 -0.2487 0.2480  162  ARG A CA    
445  C  C     . ARG A 59  ? 1.3171 1.2947 2.2588 -0.0378 -0.2657 0.2512  162  ARG A C     
446  O  O     . ARG A 59  ? 1.1690 1.1393 2.0543 -0.0453 -0.2877 0.2556  162  ARG A O     
447  C  CB    . ARG A 59  ? 1.4041 1.3656 2.4580 -0.0349 -0.2708 0.2720  162  ARG A CB    
448  C  CG    . ARG A 59  ? 1.3691 1.3223 2.4726 -0.0311 -0.2519 0.2706  162  ARG A CG    
449  C  CD    . ARG A 59  ? 1.5200 1.4614 2.6791 -0.0326 -0.2824 0.2983  162  ARG A CD    
450  N  NE    . ARG A 59  ? 2.0202 1.9687 3.2268 -0.0315 -0.3062 0.3185  162  ARG A NE    
451  C  CZ    . ARG A 59  ? 2.2410 2.1975 3.5295 -0.0230 -0.2938 0.3252  162  ARG A CZ    
452  N  NH1   . ARG A 59  ? 2.3632 2.3192 3.6952 -0.0143 -0.2558 0.3127  162  ARG A NH1   
453  N  NH2   . ARG A 59  ? 1.8113 1.7753 3.1387 -0.0240 -0.3191 0.3447  162  ARG A NH2   
454  N  N     . ALA A 60  ? 1.5435 1.5326 2.5133 -0.0319 -0.2539 0.2488  163  ALA A N     
455  C  CA    . ALA A 60  ? 1.3410 1.3345 2.2747 -0.0339 -0.2670 0.2510  163  ALA A CA    
456  C  C     . ALA A 60  ? 1.1820 1.1823 2.0391 -0.0342 -0.2513 0.2330  163  ALA A C     
457  O  O     . ALA A 60  ? 1.4053 1.4021 2.2114 -0.0386 -0.2677 0.2359  163  ALA A O     
458  C  CB    . ALA A 60  ? 1.4364 1.4402 2.4232 -0.0276 -0.2568 0.2532  163  ALA A CB    
459  N  N     . MET A 61  ? 1.3846 1.3943 2.2333 -0.0302 -0.2192 0.2148  164  MET A N     
460  C  CA    . MET A 61  ? 1.2268 1.2459 2.0065 -0.0311 -0.2054 0.1996  164  MET A CA    
461  C  C     . MET A 61  ? 1.4698 1.4797 2.1977 -0.0384 -0.2234 0.2022  164  MET A C     
462  O  O     . MET A 61  ? 1.3312 1.3456 2.0011 -0.0400 -0.2251 0.1977  164  MET A O     
463  C  CB    . MET A 61  ? 1.3525 1.3826 2.1351 -0.0283 -0.1695 0.1809  164  MET A CB    
464  C  CG    . MET A 61  ? 1.7702 1.8141 2.4867 -0.0297 -0.1552 0.1667  164  MET A CG    
465  S  SD    . MET A 61  ? 1.4528 1.5125 2.1547 -0.0233 -0.1417 0.1622  164  MET A SD    
466  C  CE    . MET A 61  ? 1.3081 1.3735 2.0545 -0.0208 -0.1058 0.1488  164  MET A CE    
467  N  N     . TYR A 62  ? 1.4611 1.4575 2.2104 -0.0428 -0.2359 0.2101  165  TYR A N     
468  C  CA    . TYR A 62  ? 1.3881 1.3736 2.0893 -0.0507 -0.2528 0.2132  165  TYR A CA    
469  C  C     . TYR A 62  ? 1.5061 1.4799 2.1783 -0.0562 -0.2835 0.2273  165  TYR A C     
470  O  O     . TYR A 62  ? 1.3873 1.3597 1.9986 -0.0600 -0.2869 0.2233  165  TYR A O     
471  C  CB    . TYR A 62  ? 1.4110 1.3831 2.1454 -0.0541 -0.2584 0.2195  165  TYR A CB    
472  C  CG    . TYR A 62  ? 1.3533 1.3092 2.0471 -0.0635 -0.2826 0.2283  165  TYR A CG    
473  C  CD1   . TYR A 62  ? 1.5536 1.5124 2.1838 -0.0679 -0.2753 0.2167  165  TYR A CD1   
474  C  CD2   . TYR A 62  ? 1.3340 1.2719 2.0537 -0.0688 -0.3128 0.2490  165  TYR A CD2   
475  C  CE1   . TYR A 62  ? 1.6063 1.5490 2.1985 -0.0770 -0.2953 0.2242  165  TYR A CE1   
476  C  CE2   . TYR A 62  ? 1.4583 1.3791 2.1370 -0.0788 -0.3344 0.2571  165  TYR A CE2   
477  C  CZ    . TYR A 62  ? 1.5845 1.5069 2.1990 -0.0828 -0.3244 0.2439  165  TYR A CZ    
478  O  OH    . TYR A 62  ? 1.3411 1.2453 1.9141 -0.0932 -0.3438 0.2514  165  TYR A OH    
479  N  N     . VAL A 63  ? 1.4343 1.3991 2.1499 -0.0577 -0.3053 0.2442  166  VAL A N     
480  C  CA    . VAL A 63  ? 1.3424 1.2926 2.0293 -0.0662 -0.3362 0.2582  166  VAL A CA    
481  C  C     . VAL A 63  ? 1.3582 1.3155 2.0087 -0.0636 -0.3290 0.2512  166  VAL A C     
482  O  O     . VAL A 63  ? 1.5476 1.4927 2.1449 -0.0707 -0.3431 0.2540  166  VAL A O     
483  C  CB    . VAL A 63  ? 1.3932 1.3342 2.1398 -0.0700 -0.3628 0.2795  166  VAL A CB    
484  C  CG1   . VAL A 63  ? 1.3522 1.2751 2.0634 -0.0825 -0.3967 0.2941  166  VAL A CG1   
485  C  CG2   . VAL A 63  ? 1.4713 1.4055 2.2582 -0.0708 -0.3676 0.2875  166  VAL A CG2   
486  N  N     . TYR A 64  ? 1.3839 1.3588 2.0610 -0.0539 -0.3055 0.2420  167  TYR A N     
487  C  CA    . TYR A 64  ? 1.4397 1.4220 2.0879 -0.0501 -0.2964 0.2360  167  TYR A CA    
488  C  C     . TYR A 64  ? 1.5353 1.5380 2.1671 -0.0414 -0.2626 0.2177  167  TYR A C     
489  O  O     . TYR A 64  ? 1.3425 1.3583 2.0079 -0.0342 -0.2432 0.2119  167  TYR A O     
490  C  CB    . TYR A 64  ? 1.4324 1.4154 2.1286 -0.0485 -0.3039 0.2453  167  TYR A CB    
491  C  CG    . TYR A 64  ? 1.4224 1.3873 2.1365 -0.0592 -0.3398 0.2651  167  TYR A CG    
492  C  CD1   . TYR A 64  ? 1.6037 1.5510 2.2661 -0.0695 -0.3615 0.2714  167  TYR A CD1   
493  C  CD2   . TYR A 64  ? 1.2986 1.2631 2.0812 -0.0600 -0.3519 0.2781  167  TYR A CD2   
494  C  CE1   . TYR A 64  ? 1.4353 1.3650 2.1092 -0.0822 -0.3960 0.2899  167  TYR A CE1   
495  C  CE2   . TYR A 64  ? 1.2814 1.2313 2.0812 -0.0711 -0.3875 0.2985  167  TYR A CE2   
496  C  CZ    . TYR A 64  ? 1.2636 1.1959 2.0065 -0.0832 -0.4103 0.3042  167  TYR A CZ    
497  O  OH    . TYR A 64  ? 1.6679 1.5846 2.4231 -0.0970 -0.4472 0.3249  167  TYR A OH    
498  N  N     . PRO A 65  ? 1.4191 1.4249 1.9992 -0.0428 -0.2550 0.2090  168  PRO A N     
499  C  CA    . PRO A 65  ? 1.1117 1.1385 1.6728 -0.0366 -0.2257 0.1934  168  PRO A CA    
500  C  C     . PRO A 65  ? 1.2041 1.2399 1.7390 -0.0310 -0.2171 0.1910  168  PRO A C     
501  O  O     . PRO A 65  ? 1.4497 1.4736 1.9556 -0.0334 -0.2322 0.1982  168  PRO A O     
502  C  CB    . PRO A 65  ? 1.2615 1.2879 1.7773 -0.0417 -0.2258 0.1883  168  PRO A CB    
503  C  CG    . PRO A 65  ? 1.1637 1.1686 1.6533 -0.0489 -0.2528 0.2002  168  PRO A CG    
504  C  CD    . PRO A 65  ? 1.1680 1.1584 1.7049 -0.0515 -0.2731 0.2137  168  PRO A CD    
505  N  N     . PRO A 66  ? 1.1224 1.1772 1.6649 -0.0242 -0.1923 0.1812  169  PRO A N     
506  C  CA    . PRO A 66  ? 1.1780 1.2413 1.6982 -0.0182 -0.1833 0.1803  169  PRO A CA    
507  C  C     . PRO A 66  ? 1.2270 1.2948 1.6881 -0.0178 -0.1824 0.1787  169  PRO A C     
508  O  O     . PRO A 66  ? 1.3666 1.4524 1.8053 -0.0164 -0.1668 0.1703  169  PRO A O     
509  C  CB    . PRO A 66  ? 1.1887 1.2709 1.7301 -0.0130 -0.1563 0.1700  169  PRO A CB    
510  C  CG    . PRO A 66  ? 1.2446 1.3310 1.7940 -0.0175 -0.1477 0.1617  169  PRO A CG    
511  C  CD    . PRO A 66  ? 1.3505 1.4175 1.9203 -0.0230 -0.1704 0.1705  169  PRO A CD    
512  N  N     . ASN A 67  ? 1.4395 1.4907 1.8757 -0.0198 -0.1987 0.1869  170  ASN A N     
513  C  CA    . ASN A 67  ? 1.3964 1.4492 1.7795 -0.0185 -0.1958 0.1864  170  ASN A CA    
514  C  C     . ASN A 67  ? 1.3997 1.4724 1.7726 -0.0087 -0.1748 0.1826  170  ASN A C     
515  O  O     . ASN A 67  ? 1.5375 1.6036 1.9109 -0.0047 -0.1744 0.1870  170  ASN A O     
516  C  CB    . ASN A 67  ? 1.2322 1.2576 1.5917 -0.0242 -0.2157 0.1953  170  ASN A CB    
517  C  CG    . ASN A 67  ? 1.4048 1.4276 1.7107 -0.0237 -0.2113 0.1945  170  ASN A CG    
518  O  OD1   . ASN A 67  ? 1.5363 1.5783 1.8252 -0.0206 -0.1981 0.1888  170  ASN A OD1   
519  N  ND2   . ASN A 67  ? 1.3798 1.3782 1.6593 -0.0277 -0.2217 0.2004  170  ASN A ND2   
520  N  N     . VAL A 68  ? 1.3841 1.4812 1.7471 -0.0059 -0.1577 0.1752  171  VAL A N     
521  C  CA    . VAL A 68  ? 1.0194 1.1383 1.3749 0.0021  -0.1382 0.1727  171  VAL A CA    
522  C  C     . VAL A 68  ? 1.2888 1.4254 1.6042 0.0043  -0.1306 0.1721  171  VAL A C     
523  O  O     . VAL A 68  ? 1.5934 1.7283 1.8911 -0.0011 -0.1371 0.1710  171  VAL A O     
524  C  CB    . VAL A 68  ? 0.9306 1.0652 1.3169 0.0019  -0.1229 0.1648  171  VAL A CB    
525  C  CG1   . VAL A 68  ? 1.1687 1.2877 1.6006 0.0012  -0.1281 0.1664  171  VAL A CG1   
526  C  CG2   . VAL A 68  ? 0.7918 0.9359 1.1758 -0.0052 -0.1194 0.1567  171  VAL A CG2   
527  N  N     . GLU A 69  ? 1.3078 1.4621 1.6111 0.0123  -0.1165 0.1741  172  GLU A N     
528  C  CA    . GLU A 69  ? 1.0701 1.2467 1.3422 0.0153  -0.1080 0.1757  172  GLU A CA    
529  C  C     . GLU A 69  ? 1.2325 1.4332 1.5060 0.0089  -0.1003 0.1677  172  GLU A C     
530  O  O     . GLU A 69  ? 1.0986 1.2973 1.3963 0.0031  -0.0981 0.1601  172  GLU A O     
531  C  CB    . GLU A 69  ? 1.1500 1.3391 1.4127 0.0259  -0.0958 0.1824  172  GLU A CB    
532  C  CG    . GLU A 69  ? 0.9744 1.1387 1.2294 0.0318  -0.1008 0.1899  172  GLU A CG    
533  C  CD    . GLU A 69  ? 1.5424 1.6966 1.7669 0.0322  -0.1056 0.1942  172  GLU A CD    
534  O  OE1   . GLU A 69  ? 1.7533 1.9267 1.9630 0.0309  -0.1023 0.1935  172  GLU A OE1   
535  O  OE2   . GLU A 69  ? 1.2903 1.4164 1.5050 0.0327  -0.1118 0.1981  172  GLU A OE2   
536  N  N     . SER A 70  ? 1.3047 1.5281 1.5527 0.0094  -0.0951 0.1697  173  SER A N     
537  C  CA    . SER A 70  ? 1.0229 1.2692 1.2672 0.0008  -0.0891 0.1622  173  SER A CA    
538  C  C     . SER A 70  ? 1.0309 1.3009 1.2785 0.0008  -0.0746 0.1600  173  SER A C     
539  O  O     . SER A 70  ? 1.3394 1.6203 1.5900 -0.0091 -0.0683 0.1508  173  SER A O     
540  C  CB    . SER A 70  ? 1.0231 1.2856 1.2407 -0.0007 -0.0908 0.1659  173  SER A CB    
541  O  OG    . SER A 70  ? 1.2951 1.5335 1.5062 -0.0032 -0.1030 0.1665  173  SER A OG    
542  N  N     . SER A 71  ? 1.1005 1.3769 1.3455 0.0107  -0.0685 0.1682  174  SER A N     
543  C  CA    . SER A 71  ? 1.1738 1.4718 1.4181 0.0102  -0.0553 0.1679  174  SER A CA    
544  C  C     . SER A 71  ? 1.2804 1.5643 1.5409 0.0185  -0.0503 0.1714  174  SER A C     
545  O  O     . SER A 71  ? 1.5783 1.8483 1.8378 0.0283  -0.0551 0.1798  174  SER A O     
546  C  CB    . SER A 71  ? 1.5801 1.9108 1.7999 0.0132  -0.0513 0.1777  174  SER A CB    
547  O  OG    . SER A 71  ? 1.1126 1.4633 1.3289 0.0111  -0.0402 0.1787  174  SER A OG    
548  N  N     . PRO A 72  ? 1.0762 1.3615 1.3504 0.0140  -0.0394 0.1645  175  PRO A N     
549  C  CA    . PRO A 72  ? 1.2862 1.5599 1.5761 0.0215  -0.0329 0.1681  175  PRO A CA    
550  C  C     . PRO A 72  ? 1.5570 1.8484 1.8281 0.0303  -0.0261 0.1801  175  PRO A C     
551  O  O     . PRO A 72  ? 1.1710 1.4503 1.4516 0.0385  -0.0227 0.1856  175  PRO A O     
552  C  CB    . PRO A 72  ? 1.1907 1.4622 1.4990 0.0124  -0.0204 0.1562  175  PRO A CB    
553  C  CG    . PRO A 72  ? 1.0641 1.3562 1.3522 0.0009  -0.0161 0.1494  175  PRO A CG    
554  C  CD    . PRO A 72  ? 1.4974 1.7920 1.7731 0.0009  -0.0307 0.1523  175  PRO A CD    
555  N  N     . GLU A 73  ? 1.7593 2.0792 2.0060 0.0285  -0.0243 0.1854  176  GLU A N     
556  C  CA    . GLU A 73  ? 1.0827 1.4219 1.3141 0.0372  -0.0185 0.1994  176  GLU A CA    
557  C  C     . GLU A 73  ? 1.0223 1.3480 1.2530 0.0514  -0.0236 0.2108  176  GLU A C     
558  O  O     . GLU A 73  ? 1.0714 1.3923 1.2962 0.0530  -0.0324 0.2121  176  GLU A O     
559  C  CB    . GLU A 73  ? 1.1390 1.5138 1.3478 0.0312  -0.0184 0.2044  176  GLU A CB    
560  C  CG    . GLU A 73  ? 1.6520 2.0513 1.8474 0.0362  -0.0112 0.2187  176  GLU A CG    
561  C  CD    . GLU A 73  ? 2.0561 2.4551 2.2515 0.0281  0.0003  0.2127  176  GLU A CD    
562  O  OE1   . GLU A 73  ? 1.7891 2.1752 1.9924 0.0164  0.0042  0.1963  176  GLU A OE1   
563  O  OE2   . GLU A 73  ? 1.8820 2.2923 2.0694 0.0335  0.0067  0.2246  176  GLU A OE2   
564  N  N     . LEU A 74  ? 1.4516 1.7691 1.6869 0.0608  -0.0168 0.2185  177  LEU A N     
565  C  CA    . LEU A 74  ? 1.2578 1.5572 1.4918 0.0734  -0.0188 0.2281  177  LEU A CA    
566  C  C     . LEU A 74  ? 1.3179 1.6410 1.5355 0.0837  -0.0134 0.2445  177  LEU A C     
567  O  O     . LEU A 74  ? 1.4474 1.7946 1.6598 0.0841  -0.0060 0.2517  177  LEU A O     
568  C  CB    . LEU A 74  ? 1.3481 1.6230 1.5979 0.0776  -0.0139 0.2275  177  LEU A CB    
569  C  CG    . LEU A 74  ? 1.3696 1.6119 1.6230 0.0838  -0.0195 0.2298  177  LEU A CG    
570  C  CD1   . LEU A 74  ? 1.1818 1.4058 1.4401 0.0755  -0.0337 0.2203  177  LEU A CD1   
571  C  CD2   . LEU A 74  ? 1.2397 1.4623 1.5100 0.0862  -0.0140 0.2295  177  LEU A CD2   
572  N  N     . PRO A 75  ? 1.4106 1.7271 1.6204 0.0914  -0.0163 0.2515  178  PRO A N     
573  C  CA    . PRO A 75  ? 1.2636 1.6015 1.4638 0.1032  -0.0095 0.2689  178  PRO A CA    
574  C  C     . PRO A 75  ? 1.3237 1.6566 1.5276 0.1139  0.0011  0.2797  178  PRO A C     
575  O  O     . PRO A 75  ? 1.3859 1.6914 1.5982 0.1139  0.0032  0.2738  178  PRO A O     
576  C  CB    . PRO A 75  ? 1.0942 1.4133 1.2879 0.1090  -0.0119 0.2708  178  PRO A CB    
577  C  CG    . PRO A 75  ? 0.9205 1.2223 1.1150 0.0963  -0.0236 0.2548  178  PRO A CG    
578  C  CD    . PRO A 75  ? 1.3866 1.6765 1.5952 0.0886  -0.0257 0.2440  178  PRO A CD    
579  N  N     . LYS A 76  ? 1.3962 1.7571 1.5950 0.1227  0.0076  0.2970  179  LYS A N     
580  C  CA    . LYS A 76  ? 1.2054 1.5654 1.4067 0.1326  0.0180  0.3095  179  LYS A CA    
581  C  C     . LYS A 76  ? 1.1782 1.5000 1.3830 0.1436  0.0245  0.3112  179  LYS A C     
582  O  O     . LYS A 76  ? 1.1719 1.4748 1.3820 0.1456  0.0304  0.3104  179  LYS A O     
583  C  CB    . LYS A 76  ? 1.3283 1.7267 1.5255 0.1404  0.0219  0.3307  179  LYS A CB    
584  C  CG    . LYS A 76  ? 1.5790 1.9803 1.7776 0.1496  0.0320  0.3456  179  LYS A CG    
585  C  CD    . LYS A 76  ? 1.6769 2.0792 1.8728 0.1374  0.0326  0.3363  179  LYS A CD    
586  C  CE    . LYS A 76  ? 1.8847 2.3228 2.0703 0.1225  0.0253  0.3340  179  LYS A CE    
587  N  NZ    . LYS A 76  ? 1.9550 2.3906 2.1353 0.1093  0.0291  0.3237  179  LYS A NZ    
588  N  N     . HIS A 77  ? 1.4791 1.7874 1.6793 0.1495  0.0244  0.3131  180  HIS A N     
589  C  CA    . HIS A 77  ? 1.3537 1.6225 1.5522 0.1577  0.0315  0.3139  180  HIS A CA    
590  C  C     . HIS A 77  ? 1.2678 1.4998 1.4681 0.1468  0.0231  0.2961  180  HIS A C     
591  O  O     . HIS A 77  ? 1.4436 1.6427 1.6439 0.1501  0.0281  0.2955  180  HIS A O     
592  C  CB    . HIS A 77  ? 1.2154 1.4791 1.4059 0.1663  0.0367  0.3212  180  HIS A CB    
593  C  CG    . HIS A 77  ? 1.0684 1.3220 1.2510 0.1557  0.0260  0.3079  180  HIS A CG    
594  N  ND1   . HIS A 77  ? 1.3052 1.5889 1.4885 0.1466  0.0160  0.3034  180  HIS A ND1   
595  C  CD2   . HIS A 77  ? 1.1562 1.3715 1.3277 0.1517  0.0237  0.2985  180  HIS A CD2   
596  C  CE1   . HIS A 77  ? 1.3548 1.6194 1.5297 0.1386  0.0083  0.2922  180  HIS A CE1   
597  N  NE2   . HIS A 77  ? 1.3252 1.5484 1.4919 0.1411  0.0123  0.2894  180  HIS A NE2   
598  N  N     . ILE A 78  ? 1.3461 1.5829 1.5493 0.1335  0.0103  0.2825  181  ILE A N     
599  C  CA    . ILE A 78  ? 1.4040 1.6097 1.6146 0.1229  0.0007  0.2680  181  ILE A CA    
600  C  C     . ILE A 78  ? 1.3736 1.5787 1.6006 0.1202  0.0038  0.2649  181  ILE A C     
601  O  O     . ILE A 78  ? 1.2645 1.4403 1.5006 0.1175  0.0020  0.2598  181  ILE A O     
602  C  CB    . ILE A 78  ? 1.0226 1.2329 1.2335 0.1106  -0.0132 0.2562  181  ILE A CB    
603  C  CG1   . ILE A 78  ? 1.0161 1.2266 1.2097 0.1129  -0.0146 0.2596  181  ILE A CG1   
604  C  CG2   . ILE A 78  ? 1.0017 1.1809 1.2238 0.1001  -0.0246 0.2441  181  ILE A CG2   
605  N  N     . TYR A 79  ? 1.5360 1.7728 1.7662 0.1197  0.0089  0.2681  182  TYR A N     
606  C  CA    . TYR A 79  ? 1.1914 1.4275 1.4348 0.1169  0.0151  0.2653  182  TYR A CA    
607  C  C     . TYR A 79  ? 1.3777 1.5982 1.6210 0.1277  0.0264  0.2759  182  TYR A C     
608  O  O     . TYR A 79  ? 1.5607 1.7650 1.8175 0.1250  0.0301  0.2714  182  TYR A O     
609  C  CB    . TYR A 79  ? 1.0905 1.3623 1.3302 0.1121  0.0192  0.2668  182  TYR A CB    
610  C  CG    . TYR A 79  ? 1.1667 1.4385 1.4156 0.1088  0.0288  0.2647  182  TYR A CG    
611  C  CD1   . TYR A 79  ? 1.4043 1.6656 1.6705 0.0976  0.0277  0.2495  182  TYR A CD1   
612  C  CD2   . TYR A 79  ? 1.3013 1.5830 1.5425 0.1170  0.0401  0.2787  182  TYR A CD2   
613  C  CE1   . TYR A 79  ? 1.2798 1.5398 1.5549 0.0941  0.0392  0.2470  182  TYR A CE1   
614  C  CE2   . TYR A 79  ? 1.4013 1.6812 1.6483 0.1130  0.0501  0.2767  182  TYR A CE2   
615  C  CZ    . TYR A 79  ? 1.3811 1.6500 1.6448 0.1013  0.0503  0.2602  182  TYR A CZ    
616  O  OH    . TYR A 79  ? 1.5675 1.8334 1.8375 0.0970  0.0628  0.2576  182  TYR A OH    
617  N  N     . ASN A 80  ? 1.2065 1.4310 1.4369 0.1400  0.0331  0.2901  183  ASN A N     
618  C  CA    . ASN A 80  ? 1.2910 1.4988 1.5208 0.1510  0.0455  0.3010  183  ASN A CA    
619  C  C     . ASN A 80  ? 1.4033 1.5677 1.6357 0.1493  0.0437  0.2936  183  ASN A C     
620  O  O     . ASN A 80  ? 1.6309 1.7760 1.8655 0.1549  0.0536  0.2988  183  ASN A O     
621  C  CB    . ASN A 80  ? 1.2125 1.4357 1.4312 0.1654  0.0544  0.3193  183  ASN A CB    
622  C  CG    . ASN A 80  ? 1.4414 1.7090 1.6578 0.1667  0.0554  0.3304  183  ASN A CG    
623  O  OD1   . ASN A 80  ? 1.2062 1.4881 1.4256 0.1584  0.0546  0.3263  183  ASN A OD1   
624  N  ND2   . ASN A 80  ? 1.3058 1.5952 1.5169 0.1760  0.0576  0.3448  183  ASN A ND2   
625  N  N     . LYS A 81  ? 1.2157 1.3638 1.4467 0.1404  0.0309  0.2822  184  LYS A N     
626  C  CA    . LYS A 81  ? 1.2352 1.3425 1.4670 0.1349  0.0259  0.2750  184  LYS A CA    
627  C  C     . LYS A 81  ? 1.3931 1.4902 1.6474 0.1259  0.0215  0.2667  184  LYS A C     
628  O  O     . LYS A 81  ? 1.5981 1.6630 1.8560 0.1210  0.0180  0.2630  184  LYS A O     
629  C  CB    . LYS A 81  ? 1.2641 1.3576 1.4857 0.1264  0.0119  0.2667  184  LYS A CB    
630  C  CG    . LYS A 81  ? 1.4130 1.5077 1.6125 0.1345  0.0180  0.2739  184  LYS A CG    
631  C  CD    . LYS A 81  ? 1.5766 1.6275 1.7579 0.1311  0.0174  0.2708  184  LYS A CD    
632  C  CE    . LYS A 81  ? 1.6395 1.6628 1.8209 0.1352  0.0284  0.2747  184  LYS A CE    
633  N  NZ    . LYS A 81  ? 1.7960 1.7733 1.9556 0.1288  0.0280  0.2703  184  LYS A NZ    
634  N  N     . LEU A 82  ? 1.4041 1.5269 1.6736 0.1226  0.0225  0.2636  185  LEU A N     
635  C  CA    . LEU A 82  ? 1.5269 1.6422 1.8222 0.1143  0.0208  0.2555  185  LEU A CA    
636  C  C     . LEU A 82  ? 1.5756 1.6881 1.8752 0.1208  0.0365  0.2628  185  LEU A C     
637  O  O     . LEU A 82  ? 1.4952 1.6257 1.7813 0.1303  0.0485  0.2737  185  LEU A O     
638  C  CB    . LEU A 82  ? 1.5448 1.6854 1.8535 0.1066  0.0175  0.2472  185  LEU A CB    
639  C  CG    . LEU A 82  ? 1.3297 1.4757 1.6345 0.0999  0.0030  0.2402  185  LEU A CG    
640  C  CD1   . LEU A 82  ? 1.3957 1.5685 1.7085 0.0935  0.0046  0.2333  185  LEU A CD1   
641  C  CD2   . LEU A 82  ? 1.3564 1.4739 1.6760 0.0912  -0.0124 0.2329  185  LEU A CD2   
642  N  N     . ASP A 83  ? 1.6529 1.7433 1.9728 0.1151  0.0358  0.2580  186  ASP A N     
643  C  CA    . ASP A 83  ? 1.4640 1.5493 1.7910 0.1194  0.0509  0.2635  186  ASP A CA    
644  C  C     . ASP A 83  ? 1.4075 1.5199 1.7443 0.1174  0.0601  0.2616  186  ASP A C     
645  O  O     . ASP A 83  ? 1.7914 1.9050 2.1533 0.1079  0.0574  0.2512  186  ASP A O     
646  C  CB    . ASP A 83  ? 1.7008 1.7562 2.0493 0.1118  0.0463  0.2581  186  ASP A CB    
647  C  CG    . ASP A 83  ? 1.8405 1.8876 2.1958 0.1159  0.0627  0.2638  186  ASP A CG    
648  O  OD1   . ASP A 83  ? 1.6085 1.6680 1.9466 0.1262  0.0772  0.2740  186  ASP A OD1   
649  O  OD2   . ASP A 83  ? 1.9697 1.9984 2.3488 0.1083  0.0606  0.2591  186  ASP A OD2   
650  N  N     . LYS A 84  ? 1.2000 1.3336 1.5171 0.1256  0.0713  0.2722  187  LYS A N     
651  C  CA    . LYS A 84  ? 1.4687 1.6272 1.7860 0.1221  0.0809  0.2717  187  LYS A CA    
652  C  C     . LYS A 84  ? 1.3187 1.4940 1.6423 0.1116  0.0724  0.2594  187  LYS A C     
653  O  O     . LYS A 84  ? 1.5066 1.6901 1.8413 0.1033  0.0796  0.2515  187  LYS A O     
654  C  CB    . LYS A 84  ? 1.9591 2.1052 2.2949 0.1186  0.0935  0.2691  187  LYS A CB    
655  C  CG    . LYS A 84  ? 1.7156 1.8394 2.0486 0.1271  0.1018  0.2792  187  LYS A CG    
656  C  CD    . LYS A 84  ? 1.5143 1.6246 1.8698 0.1218  0.1132  0.2748  187  LYS A CD    
657  C  CE    . LYS A 84  ? 1.8284 1.9126 2.1827 0.1285  0.1202  0.2833  187  LYS A CE    
658  N  NZ    . LYS A 84  ? 1.8067 1.8981 2.1328 0.1414  0.1304  0.3003  187  LYS A NZ    
659  N  N     . GLY A 85  ? 1.3155 1.4941 1.6314 0.1115  0.0587  0.2574  188  GLY A N     
660  C  CA    . GLY A 85  ? 1.2896 1.4810 1.6117 0.1016  0.0504  0.2458  188  GLY A CA    
661  C  C     . GLY A 85  ? 1.2526 1.4255 1.6065 0.0925  0.0434  0.2327  188  GLY A C     
662  O  O     . GLY A 85  ? 1.3638 1.5459 1.7293 0.0837  0.0418  0.2224  188  GLY A O     
663  N  N     . GLN A 86  ? 1.2332 1.3799 1.6026 0.0937  0.0392  0.2335  189  GLN A N     
664  C  CA    . GLN A 86  ? 1.3271 1.4571 1.7314 0.0851  0.0306  0.2241  189  GLN A CA    
665  C  C     . GLN A 86  ? 1.2382 1.3451 1.6408 0.0841  0.0129  0.2257  189  GLN A C     
666  O  O     . GLN A 86  ? 1.2009 1.2981 1.5779 0.0908  0.0126  0.2335  189  GLN A O     
667  C  CB    . GLN A 86  ? 1.1020 1.2225 1.5324 0.0836  0.0432  0.2232  189  GLN A CB    
668  C  CG    . GLN A 86  ? 1.1457 1.2849 1.5775 0.0816  0.0619  0.2199  189  GLN A CG    
669  C  CD    . GLN A 86  ? 1.5798 1.7083 2.0339 0.0807  0.0769  0.2200  189  GLN A CD    
670  O  OE1   . GLN A 86  ? 1.8487 1.9592 2.3078 0.0843  0.0756  0.2259  189  GLN A OE1   
671  N  NE2   . GLN A 86  ? 1.5251 1.6631 1.9917 0.0749  0.0924  0.2128  189  GLN A NE2   
672  N  N     . ILE A 87  ? 1.1273 1.2242 1.5572 0.0751  -0.0013 0.2187  190  ILE A N     
673  C  CA    . ILE A 87  ? 1.1285 1.2031 1.5555 0.0704  -0.0210 0.2197  190  ILE A CA    
674  C  C     . ILE A 87  ? 1.2122 1.2668 1.6738 0.0633  -0.0282 0.2192  190  ILE A C     
675  O  O     . ILE A 87  ? 1.2146 1.2760 1.7132 0.0600  -0.0223 0.2153  190  ILE A O     
676  C  CB    . ILE A 87  ? 1.1489 1.2302 1.5755 0.0646  -0.0359 0.2144  190  ILE A CB    
677  C  CG1   . ILE A 87  ? 1.2190 1.2753 1.6365 0.0582  -0.0568 0.2163  190  ILE A CG1   
678  C  CG2   . ILE A 87  ? 1.1236 1.2150 1.5899 0.0581  -0.0357 0.2068  190  ILE A CG2   
679  C  CD1   . ILE A 87  ? 1.4027 1.4455 1.7790 0.0639  -0.0544 0.2223  190  ILE A CD1   
680  N  N     . ILE A 88  ? 1.1211 1.1502 1.5706 0.0601  -0.0398 0.2233  191  ILE A N     
681  C  CA    . ILE A 88  ? 1.2657 1.2746 1.7449 0.0508  -0.0506 0.2242  191  ILE A CA    
682  C  C     . ILE A 88  ? 1.1808 1.1805 1.6711 0.0395  -0.0762 0.2227  191  ILE A C     
683  O  O     . ILE A 88  ? 1.0405 1.0219 1.4996 0.0352  -0.0894 0.2247  191  ILE A O     
684  C  CB    . ILE A 88  ? 1.4676 1.4516 1.9238 0.0517  -0.0470 0.2295  191  ILE A CB    
685  C  CG1   . ILE A 88  ? 1.2597 1.2529 1.7058 0.0635  -0.0216 0.2328  191  ILE A CG1   
686  C  CG2   . ILE A 88  ? 1.0512 1.0147 1.5375 0.0392  -0.0610 0.2305  191  ILE A CG2   
687  C  CD1   . ILE A 88  ? 1.2068 1.2071 1.6925 0.0621  -0.0107 0.2314  191  ILE A CD1   
688  N  N     . VAL A 89  ? 1.3825 1.3933 1.9173 0.0344  -0.0825 0.2198  192  VAL A N     
689  C  CA    . VAL A 89  ? 1.2160 1.2198 1.7682 0.0238  -0.1075 0.2205  192  VAL A CA    
690  C  C     . VAL A 89  ? 1.0762 1.0667 1.6701 0.0134  -0.1218 0.2253  192  VAL A C     
691  O  O     . VAL A 89  ? 1.1403 1.1343 1.7635 0.0152  -0.1092 0.2257  192  VAL A O     
692  C  CB    . VAL A 89  ? 0.8538 0.8792 1.4290 0.0252  -0.1055 0.2152  192  VAL A CB    
693  C  CG1   . VAL A 89  ? 1.1625 1.2021 1.6953 0.0333  -0.0935 0.2111  192  VAL A CG1   
694  C  CG2   . VAL A 89  ? 0.9761 1.0160 1.5998 0.0275  -0.0891 0.2120  192  VAL A CG2   
695  N  N     . VAL A 90  ? 1.2121 1.1873 1.8084 0.0014  -0.1490 0.2297  193  VAL A N     
696  C  CA    . VAL A 90  ? 1.3866 1.3493 2.0210 -0.0113 -0.1685 0.2365  193  VAL A CA    
697  C  C     . VAL A 90  ? 1.6167 1.5903 2.2991 -0.0170 -0.1860 0.2397  193  VAL A C     
698  O  O     . VAL A 90  ? 1.3411 1.3114 2.0051 -0.0208 -0.2014 0.2404  193  VAL A O     
699  C  CB    . VAL A 90  ? 1.2471 1.1792 1.8413 -0.0236 -0.1879 0.2411  193  VAL A CB    
700  C  CG1   . VAL A 90  ? 0.9317 0.8525 1.5651 -0.0384 -0.2076 0.2489  193  VAL A CG1   
701  C  CG2   . VAL A 90  ? 1.1208 1.0406 1.6635 -0.0159 -0.1676 0.2377  193  VAL A CG2   
702  N  N     . ILE A 91  ? 1.4157 1.4015 2.1610 -0.0174 -0.1824 0.2421  194  ILE A N     
703  C  CA    . ILE A 91  ? 1.2503 1.2468 2.0519 -0.0215 -0.1963 0.2467  194  ILE A CA    
704  C  C     . ILE A 91  ? 1.3478 1.3320 2.1821 -0.0369 -0.2265 0.2593  194  ILE A C     
705  O  O     . ILE A 91  ? 1.5640 1.5447 2.4206 -0.0408 -0.2244 0.2627  194  ILE A O     
706  C  CB    . ILE A 91  ? 1.3249 1.3431 2.1792 -0.0120 -0.1704 0.2414  194  ILE A CB    
707  C  CG1   . ILE A 91  ? 1.3669 1.3968 2.1833 0.0003  -0.1423 0.2294  194  ILE A CG1   
708  C  CG2   . ILE A 91  ? 0.9266 0.9541 1.8443 -0.0155 -0.1830 0.2472  194  ILE A CG2   
709  C  CD1   . ILE A 91  ? 1.2492 1.2813 2.0357 0.0009  -0.1506 0.2263  194  ILE A CD1   
710  N  N     . TRP A 92  ? 1.2191 1.1968 2.0559 -0.0467 -0.2552 0.2670  195  TRP A N     
711  C  CA    . TRP A 92  ? 1.3588 1.3259 2.2252 -0.0637 -0.2887 0.2813  195  TRP A CA    
712  C  C     . TRP A 92  ? 1.3585 1.3437 2.3035 -0.0639 -0.2989 0.2904  195  TRP A C     
713  O  O     . TRP A 92  ? 1.2692 1.2632 2.2209 -0.0576 -0.2961 0.2882  195  TRP A O     
714  C  CB    . TRP A 92  ? 1.3524 1.2953 2.1600 -0.0774 -0.3164 0.2856  195  TRP A CB    
715  C  CG    . TRP A 92  ? 1.4366 1.3564 2.1748 -0.0807 -0.3096 0.2794  195  TRP A CG    
716  C  CD1   . TRP A 92  ? 1.6948 1.6100 2.3735 -0.0697 -0.2873 0.2680  195  TRP A CD1   
717  C  CD2   . TRP A 92  ? 1.6793 1.5769 2.4022 -0.0963 -0.3245 0.2848  195  TRP A CD2   
718  N  NE1   . TRP A 92  ? 1.4845 1.3749 2.1136 -0.0761 -0.2856 0.2662  195  TRP A NE1   
719  C  CE2   . TRP A 92  ? 1.8313 1.7091 2.4839 -0.0931 -0.3078 0.2754  195  TRP A CE2   
720  C  CE3   . TRP A 92  ? 1.5869 1.4794 2.3496 -0.1136 -0.3503 0.2972  195  TRP A CE3   
721  C  CZ2   . TRP A 92  ? 1.9978 1.8479 2.6166 -0.1065 -0.3140 0.2766  195  TRP A CZ2   
722  C  CZ3   . TRP A 92  ? 1.7294 1.5959 2.4568 -0.1284 -0.3585 0.2983  195  TRP A CZ3   
723  C  CH2   . TRP A 92  ? 1.9920 1.8360 2.6468 -0.1248 -0.3394 0.2873  195  TRP A CH2   
724  N  N     . VAL A 93  ? 1.5932 1.5838 2.5994 -0.0713 -0.3098 0.3012  196  VAL A N     
725  C  CA    . VAL A 93  ? 1.1307 1.1393 2.2222 -0.0710 -0.3184 0.3124  196  VAL A CA    
726  C  C     . VAL A 93  ? 1.2602 1.2623 2.3838 -0.0904 -0.3582 0.3318  196  VAL A C     
727  O  O     . VAL A 93  ? 1.2239 1.2164 2.3372 -0.1006 -0.3652 0.3345  196  VAL A O     
728  C  CB    . VAL A 93  ? 1.0618 1.0899 2.2131 -0.0583 -0.2847 0.3064  196  VAL A CB    
729  C  CG1   . VAL A 93  ? 1.4627 1.5080 2.7081 -0.0582 -0.2927 0.3193  196  VAL A CG1   
730  C  CG2   . VAL A 93  ? 1.4311 1.4653 2.5477 -0.0419 -0.2470 0.2879  196  VAL A CG2   
731  N  N     . ILE A 94  ? 1.4594 1.4665 2.6212 -0.0962 -0.3846 0.3460  197  ILE A N     
732  C  CA    . ILE A 94  ? 1.6893 1.6942 2.8902 -0.1154 -0.4255 0.3677  197  ILE A CA    
733  C  C     . ILE A 94  ? 1.7392 1.7696 3.0465 -0.1104 -0.4203 0.3789  197  ILE A C     
734  O  O     . ILE A 94  ? 1.7573 1.8039 3.1160 -0.0967 -0.4044 0.3786  197  ILE A O     
735  C  CB    . ILE A 94  ? 1.6082 1.6033 2.7899 -0.1259 -0.4598 0.3797  197  ILE A CB    
736  C  CG1   . ILE A 94  ? 1.5371 1.5065 2.6138 -0.1299 -0.4601 0.3672  197  ILE A CG1   
737  C  CG2   . ILE A 94  ? 1.6876 1.6808 2.9073 -0.1481 -0.5049 0.4042  197  ILE A CG2   
738  C  CD1   . ILE A 94  ? 1.6483 1.5946 2.6660 -0.1450 -0.4690 0.3644  197  ILE A CD1   
739  N  N     . VAL A 95  ? 1.7030 1.7361 3.0444 -0.1219 -0.4325 0.3886  198  VAL A N     
740  C  CA    . VAL A 95  ? 1.9259 1.9838 3.3703 -0.1171 -0.4242 0.3988  198  VAL A CA    
741  C  C     . VAL A 95  ? 2.1342 2.2005 3.6418 -0.1343 -0.4694 0.4267  198  VAL A C     
742  O  O     . VAL A 95  ? 2.1640 2.2481 3.7459 -0.1278 -0.4743 0.4397  198  VAL A O     
743  C  CB    . VAL A 95  ? 2.0492 2.1083 3.4976 -0.1163 -0.4009 0.3899  198  VAL A CB    
744  C  CG1   . VAL A 95  ? 2.2012 2.2858 3.7591 -0.1122 -0.3917 0.4009  198  VAL A CG1   
745  C  CG2   . VAL A 95  ? 1.7145 1.7668 3.1028 -0.0993 -0.3572 0.3647  198  VAL A CG2   
746  N  N     . SER A 96  ? 2.2568 2.3097 3.7357 -0.1568 -0.5025 0.4368  199  SER A N     
747  C  CA    . SER A 96  ? 2.3030 2.3648 3.8400 -0.1763 -0.5485 0.4650  199  SER A CA    
748  C  C     . SER A 96  ? 2.4365 2.4904 3.9521 -0.1829 -0.5804 0.4774  199  SER A C     
749  O  O     . SER A 96  ? 2.1861 2.2175 3.6134 -0.1827 -0.5779 0.4641  199  SER A O     
750  C  CB    . SER A 96  ? 2.4326 2.4789 3.9347 -0.2017 -0.5749 0.4708  199  SER A CB    
751  O  OG    . SER A 96  ? 2.1449 2.2009 3.7016 -0.2232 -0.6224 0.4996  199  SER A OG    
752  N  N     . PRO A 97  ? 2.5771 2.6496 4.1748 -0.1888 -0.6105 0.5039  200  PRO A N     
753  C  CA    . PRO A 97  ? 2.4818 2.5456 4.0600 -0.1973 -0.6445 0.5186  200  PRO A CA    
754  C  C     . PRO A 97  ? 2.6091 2.6446 4.1025 -0.2261 -0.6857 0.5251  200  PRO A C     
755  O  O     . PRO A 97  ? 2.4764 2.4979 3.9300 -0.2338 -0.7099 0.5325  200  PRO A O     
756  C  CB    . PRO A 97  ? 2.0974 2.1866 3.7890 -0.1966 -0.6639 0.5473  200  PRO A CB    
757  C  CG    . PRO A 97  ? 1.9697 2.0706 3.7144 -0.1994 -0.6555 0.5515  200  PRO A CG    
758  C  CD    . PRO A 97  ? 2.1948 2.2978 3.9106 -0.1868 -0.6130 0.5225  200  PRO A CD    
759  N  N     . ASN A 98  ? 2.6600 2.6845 4.1227 -0.2431 -0.6933 0.5221  201  ASN A N     
760  C  CA    . ASN A 98  ? 2.5220 2.5147 3.8965 -0.2722 -0.7277 0.5251  201  ASN A CA    
761  C  C     . ASN A 98  ? 2.5300 2.4903 3.7891 -0.2674 -0.7017 0.4968  201  ASN A C     
762  O  O     . ASN A 98  ? 2.5303 2.4609 3.7120 -0.2891 -0.7162 0.4922  201  ASN A O     
763  C  CB    . ASN A 98  ? 2.3951 2.3884 3.7888 -0.2946 -0.7471 0.5346  201  ASN A CB    
764  C  CG    . ASN A 98  ? 2.4707 2.4937 3.9732 -0.2998 -0.7737 0.5644  201  ASN A CG    
765  O  OD1   . ASN A 98  ? 2.5687 2.5931 4.0962 -0.2938 -0.7874 0.5820  201  ASN A OD1   
766  N  ND2   . ASN A 98  ? 2.5783 2.6106 4.1205 -0.3040 -0.7684 0.5674  201  ASN A ND2   
767  N  N     . ASN A 99  ? 2.3304 2.2957 3.5781 -0.2404 -0.6633 0.4785  202  ASN A N     
768  C  CA    . ASN A 99  ? 2.3392 2.2789 3.4864 -0.2328 -0.6367 0.4531  202  ASN A CA    
769  C  C     . ASN A 99  ? 2.3924 2.3180 3.4957 -0.2351 -0.6144 0.4364  202  ASN A C     
770  O  O     . ASN A 99  ? 2.4004 2.2944 3.4221 -0.2526 -0.6245 0.4304  202  ASN A O     
771  C  CB    . ASN A 99  ? 2.3119 2.2221 3.3800 -0.2517 -0.6671 0.4577  202  ASN A CB    
772  C  CG    . ASN A 99  ? 2.2137 2.1355 3.3171 -0.2468 -0.6842 0.4720  202  ASN A CG    
773  O  OD1   . ASN A 99  ? 2.3398 2.2725 3.5002 -0.2603 -0.7213 0.4978  202  ASN A OD1   
774  N  ND2   . ASN A 99  ? 1.9617 1.8814 3.0326 -0.2277 -0.6575 0.4564  202  ASN A ND2   
775  N  N     . ASP A 100 ? 2.2371 2.1849 3.3959 -0.2173 -0.5823 0.4290  203  ASP A N     
776  C  CA    . ASP A 100 ? 1.9718 1.9093 3.0964 -0.2145 -0.5547 0.4124  203  ASP A CA    
777  C  C     . ASP A 100 ? 2.0051 1.9444 3.0949 -0.1877 -0.5078 0.3891  203  ASP A C     
778  O  O     . ASP A 100 ? 1.8884 1.8482 3.0165 -0.1684 -0.4898 0.3862  203  ASP A O     
779  C  CB    . ASP A 100 ? 1.8270 1.7865 3.0352 -0.2159 -0.5518 0.4212  203  ASP A CB    
780  C  CG    . ASP A 100 ? 1.8708 1.8260 3.1022 -0.2460 -0.5979 0.4431  203  ASP A CG    
781  O  OD1   . ASP A 100 ? 1.9542 1.8872 3.1321 -0.2668 -0.6321 0.4511  203  ASP A OD1   
782  O  OD2   . ASP A 100 ? 1.6877 1.6615 2.9898 -0.2502 -0.6000 0.4526  203  ASP A OD2   
783  N  N     . LYS A 101 ? 1.9632 1.8802 2.9801 -0.1874 -0.4882 0.3730  204  LYS A N     
784  C  CA    . LYS A 101 ? 1.6405 1.5559 2.6105 -0.1652 -0.4484 0.3524  204  LYS A CA    
785  C  C     . LYS A 101 ? 1.6597 1.5855 2.6509 -0.1517 -0.4127 0.3420  204  LYS A C     
786  O  O     . LYS A 101 ? 1.5897 1.5079 2.5894 -0.1635 -0.4174 0.3453  204  LYS A O     
787  C  CB    . LYS A 101 ? 1.7083 1.5899 2.5762 -0.1729 -0.4501 0.3426  204  LYS A CB    
788  C  CG    . LYS A 101 ? 1.7379 1.6087 2.5710 -0.1804 -0.4741 0.3477  204  LYS A CG    
789  C  CD    . LYS A 101 ? 2.0057 1.8654 2.8514 -0.2082 -0.5213 0.3674  204  LYS A CD    
790  C  CE    . LYS A 101 ? 2.2371 2.0675 3.0374 -0.2310 -0.5337 0.3675  204  LYS A CE    
791  N  NZ    . LYS A 101 ? 2.0329 1.8534 2.8452 -0.2609 -0.5818 0.3878  204  LYS A NZ    
792  N  N     . GLN A 102 ? 1.5944 1.5364 2.5918 -0.1283 -0.3772 0.3294  205  GLN A N     
793  C  CA    . GLN A 102 ? 1.7554 1.7061 2.7640 -0.1141 -0.3402 0.3184  205  GLN A CA    
794  C  C     . GLN A 102 ? 1.5585 1.5100 2.5152 -0.0947 -0.3080 0.3020  205  GLN A C     
795  O  O     . GLN A 102 ? 1.4605 1.4282 2.4348 -0.0830 -0.2991 0.2989  205  GLN A O     
796  C  CB    . GLN A 102 ? 1.4316 1.4108 2.5356 -0.1070 -0.3298 0.3243  205  GLN A CB    
797  C  CG    . GLN A 102 ? 1.4075 1.3901 2.5708 -0.1248 -0.3563 0.3407  205  GLN A CG    
798  C  CD    . GLN A 102 ? 1.7023 1.7129 2.9610 -0.1157 -0.3395 0.3453  205  GLN A CD    
799  O  OE1   . GLN A 102 ? 1.6720 1.6971 2.9496 -0.0969 -0.3071 0.3352  205  GLN A OE1   
800  N  NE2   . GLN A 102 ? 1.6580 1.6758 2.9773 -0.1302 -0.3607 0.3606  205  GLN A NE2   
801  N  N     . LYS A 103 ? 1.3224 1.2567 2.2170 -0.0919 -0.2907 0.2923  206  LYS A N     
802  C  CA    . LYS A 103 ? 1.5286 1.4650 2.3740 -0.0742 -0.2612 0.2788  206  LYS A CA    
803  C  C     . LYS A 103 ? 1.3625 1.3176 2.2383 -0.0585 -0.2256 0.2715  206  LYS A C     
804  O  O     . LYS A 103 ? 1.3507 1.3089 2.2673 -0.0619 -0.2203 0.2749  206  LYS A O     
805  C  CB    . LYS A 103 ? 1.3531 1.2613 2.1169 -0.0779 -0.2592 0.2735  206  LYS A CB    
806  C  CG    . LYS A 103 ? 1.5060 1.4041 2.2560 -0.0755 -0.2381 0.2695  206  LYS A CG    
807  C  CD    . LYS A 103 ? 1.4568 1.3238 2.1286 -0.0796 -0.2360 0.2651  206  LYS A CD    
808  C  CE    . LYS A 103 ? 1.7219 1.5618 2.3714 -0.1034 -0.2704 0.2721  206  LYS A CE    
809  N  NZ    . LYS A 103 ? 1.5705 1.3757 2.1431 -0.1086 -0.2648 0.2666  206  LYS A NZ    
810  N  N     . TYR A 104 ? 1.2771 1.2444 2.1315 -0.0425 -0.2012 0.2617  207  TYR A N     
811  C  CA    . TYR A 104 ? 1.2981 1.2818 2.1721 -0.0285 -0.1664 0.2541  207  TYR A CA    
812  C  C     . TYR A 104 ? 1.3513 1.3359 2.1624 -0.0157 -0.1449 0.2444  207  TYR A C     
813  O  O     . TYR A 104 ? 1.4032 1.4011 2.2090 -0.0085 -0.1386 0.2394  207  TYR A O     
814  C  CB    . TYR A 104 ? 1.3267 1.3330 2.2704 -0.0243 -0.1592 0.2544  207  TYR A CB    
815  C  CG    . TYR A 104 ? 1.6326 1.6425 2.6488 -0.0350 -0.1763 0.2656  207  TYR A CG    
816  C  CD1   . TYR A 104 ? 1.7102 1.7241 2.7653 -0.0350 -0.1603 0.2664  207  TYR A CD1   
817  C  CD2   . TYR A 104 ? 1.4391 1.4492 2.4866 -0.0454 -0.2088 0.2767  207  TYR A CD2   
818  C  CE1   . TYR A 104 ? 1.5797 1.5993 2.7055 -0.0450 -0.1760 0.2777  207  TYR A CE1   
819  C  CE2   . TYR A 104 ? 1.4322 1.4485 2.5503 -0.0554 -0.2262 0.2894  207  TYR A CE2   
820  C  CZ    . TYR A 104 ? 1.5145 1.5364 2.6729 -0.0552 -0.2096 0.2898  207  TYR A CZ    
821  O  OH    . TYR A 104 ? 1.5732 1.6036 2.8062 -0.0654 -0.2271 0.3034  207  TYR A OH    
822  N  N     . THR A 105 ? 1.2442 1.2146 2.0096 -0.0133 -0.1340 0.2426  208  THR A N     
823  C  CA    . THR A 105 ? 1.3005 1.2733 2.0106 -0.0006 -0.1133 0.2361  208  THR A CA    
824  C  C     . THR A 105 ? 1.4357 1.4294 2.1641 0.0114  -0.0826 0.2304  208  THR A C     
825  O  O     . THR A 105 ? 1.4303 1.4286 2.2009 0.0105  -0.0713 0.2309  208  THR A O     
826  C  CB    . THR A 105 ? 1.1110 1.0605 1.7706 -0.0013 -0.1100 0.2376  208  THR A CB    
827  O  OG1   . THR A 105 ? 1.4098 1.3526 2.0954 -0.0048 -0.1019 0.2402  208  THR A OG1   
828  C  CG2   . THR A 105 ? 1.1089 1.0342 1.7376 -0.0142 -0.1375 0.2413  208  THR A CG2   
829  N  N     . LEU A 106 ? 1.2810 1.2872 1.9760 0.0212  -0.0690 0.2249  209  LEU A N     
830  C  CA    . LEU A 106 ? 1.3623 1.3872 2.0649 0.0304  -0.0406 0.2192  209  LEU A CA    
831  C  C     . LEU A 106 ? 1.3401 1.3733 1.9872 0.0397  -0.0295 0.2164  209  LEU A C     
832  O  O     . LEU A 106 ? 1.0432 1.0760 1.6636 0.0393  -0.0433 0.2161  209  LEU A O     
833  C  CB    . LEU A 106 ? 1.4306 1.4711 2.1853 0.0283  -0.0377 0.2147  209  LEU A CB    
834  C  CG    . LEU A 106 ? 1.1645 1.2103 1.9203 0.0257  -0.0547 0.2131  209  LEU A CG    
835  C  CD1   . LEU A 106 ? 1.5223 1.5841 2.2482 0.0327  -0.0374 0.2050  209  LEU A CD1   
836  C  CD2   . LEU A 106 ? 1.0770 1.1261 1.9000 0.0192  -0.0648 0.2152  209  LEU A CD2   
837  N  N     . LYS A 107 ? 1.3305 1.3714 1.9610 0.0476  -0.0051 0.2154  210  LYS A N     
838  C  CA    . LYS A 107 ? 1.0615 1.1150 1.6452 0.0562  0.0065  0.2147  210  LYS A CA    
839  C  C     . LYS A 107 ? 1.1172 1.1923 1.7131 0.0562  0.0187  0.2069  210  LYS A C     
840  O  O     . LYS A 107 ? 1.4556 1.5355 2.0853 0.0540  0.0338  0.2027  210  LYS A O     
841  C  CB    . LYS A 107 ? 1.0717 1.1223 1.6285 0.0639  0.0250  0.2199  210  LYS A CB    
842  C  CG    . LYS A 107 ? 1.2404 1.3053 1.7503 0.0730  0.0342  0.2227  210  LYS A CG    
843  C  CD    . LYS A 107 ? 1.0560 1.1107 1.5353 0.0812  0.0442  0.2319  210  LYS A CD    
844  C  CE    . LYS A 107 ? 1.6854 1.7390 2.1796 0.0826  0.0641  0.2336  210  LYS A CE    
845  N  NZ    . LYS A 107 ? 1.7488 1.7921 2.2132 0.0914  0.0747  0.2437  210  LYS A NZ    
846  N  N     . ILE A 108 ? 0.9990 1.0855 1.5669 0.0578  0.0136  0.2046  211  ILE A N     
847  C  CA    . ILE A 108 ? 0.9806 1.0850 1.5553 0.0556  0.0233  0.1963  211  ILE A CA    
848  C  C     . ILE A 108 ? 1.2432 1.3624 1.7693 0.0599  0.0244  0.1971  211  ILE A C     
849  O  O     . ILE A 108 ? 0.9478 1.0623 1.4432 0.0642  0.0135  0.2036  211  ILE A O     
850  C  CB    . ILE A 108 ? 1.0770 1.1782 1.6914 0.0484  0.0087  0.1914  211  ILE A CB    
851  C  CG1   . ILE A 108 ? 1.3224 1.4359 1.9600 0.0451  0.0264  0.1815  211  ILE A CG1   
852  C  CG2   . ILE A 108 ? 1.0001 1.0994 1.5897 0.0473  -0.0128 0.1931  211  ILE A CG2   
853  N  N     . ASN A 109 ? 1.1785 1.3152 1.6976 0.0578  0.0387  0.1905  212  ASN A N     
854  C  CA    . ASN A 109 ? 0.8960 1.0504 1.3726 0.0599  0.0389  0.1916  212  ASN A CA    
855  C  C     . ASN A 109 ? 1.1625 1.3151 1.6329 0.0580  0.0183  0.1906  212  ASN A C     
856  O  O     . ASN A 109 ? 1.3933 1.5353 1.8943 0.0527  0.0068  0.1862  212  ASN A O     
857  C  CB    . ASN A 109 ? 0.8213 0.9926 1.2923 0.0541  0.0569  0.1833  212  ASN A CB    
858  C  CG    . ASN A 109 ? 1.0162 1.1908 1.4796 0.0554  0.0780  0.1857  212  ASN A CG    
859  O  OD1   . ASN A 109 ? 1.1152 1.2855 1.5655 0.0629  0.0791  0.1960  212  ASN A OD1   
860  N  ND2   . ASN A 109 ? 1.0693 1.2496 1.5390 0.0475  0.0961  0.1762  212  ASN A ND2   
861  N  N     . HIS A 110 ? 1.1408 1.3042 1.5722 0.0623  0.0138  0.1959  213  HIS A N     
862  C  CA    . HIS A 110 ? 1.0653 1.2258 1.4863 0.0606  -0.0044 0.1956  213  HIS A CA    
863  C  C     . HIS A 110 ? 1.0757 1.2469 1.5050 0.0525  -0.0057 0.1857  213  HIS A C     
864  O  O     . HIS A 110 ? 1.3498 1.5123 1.7879 0.0484  -0.0213 0.1832  213  HIS A O     
865  C  CB    . HIS A 110 ? 1.3044 1.4737 1.6847 0.0680  -0.0061 0.2044  213  HIS A CB    
866  C  CG    . HIS A 110 ? 1.1507 1.3484 1.5072 0.0684  0.0044  0.2049  213  HIS A CG    
867  N  ND1   . HIS A 110 ? 0.8988 1.1112 1.2438 0.0628  -0.0013 0.2000  213  HIS A ND1   
868  C  CD2   . HIS A 110 ? 1.2814 1.4955 1.6224 0.0722  0.0191  0.2107  213  HIS A CD2   
869  C  CE1   . HIS A 110 ? 1.1787 1.4163 1.5025 0.0624  0.0088  0.2024  213  HIS A CE1   
870  N  NE2   . HIS A 110 ? 1.1723 1.4116 1.4928 0.0680  0.0207  0.2094  213  HIS A NE2   
871  N  N     . ASP A 111 ? 1.0297 1.2180 1.4547 0.0490  0.0107  0.1799  214  ASP A N     
872  C  CA    . ASP A 111 ? 1.0744 1.2716 1.5035 0.0401  0.0129  0.1693  214  ASP A CA    
873  C  C     . ASP A 111 ? 1.2535 1.4391 1.7264 0.0341  0.0210  0.1599  214  ASP A C     
874  O  O     . ASP A 111 ? 1.6594 1.8522 2.1350 0.0268  0.0362  0.1500  214  ASP A O     
875  C  CB    . ASP A 111 ? 1.0157 1.2369 1.4109 0.0369  0.0260  0.1680  214  ASP A CB    
876  C  CG    . ASP A 111 ? 1.2440 1.4691 1.6375 0.0370  0.0457  0.1686  214  ASP A CG    
877  O  OD1   . ASP A 111 ? 1.6733 1.8855 2.0829 0.0434  0.0479  0.1740  214  ASP A OD1   
878  O  OD2   . ASP A 111 ? 0.9088 1.1489 1.2831 0.0293  0.0589  0.1636  214  ASP A OD2   
879  N  N     . CYS A 112 ? 1.2472 1.4143 1.7558 0.0361  0.0118  0.1629  215  CYS A N     
880  C  CA    . CYS A 112 ? 1.1853 1.3421 1.7438 0.0317  0.0186  0.1564  215  CYS A CA    
881  C  C     . CYS A 112 ? 1.4094 1.5584 1.9915 0.0273  0.0024  0.1540  215  CYS A C     
882  O  O     . CYS A 112 ? 1.1762 1.3185 1.7486 0.0285  -0.0197 0.1607  215  CYS A O     
883  C  CB    . CYS A 112 ? 1.2454 1.3889 1.8350 0.0355  0.0177  0.1627  215  CYS A CB    
884  S  SG    . CYS A 112 ? 1.5225 1.6716 2.0968 0.0393  0.0420  0.1641  215  CYS A SG    
885  N  N     . VAL A 113 ? 1.4765 1.6247 2.0888 0.0218  0.0147  0.1446  216  VAL A N     
886  C  CA    . VAL A 113 ? 1.1817 1.3216 1.8234 0.0179  0.0018  0.1429  216  VAL A CA    
887  C  C     . VAL A 113 ? 1.2637 1.3888 1.9538 0.0199  -0.0141 0.1521  216  VAL A C     
888  O  O     . VAL A 113 ? 1.2730 1.3951 1.9831 0.0228  -0.0073 0.1555  216  VAL A O     
889  C  CB    . VAL A 113 ? 1.1026 1.2438 1.7640 0.0116  0.0233  0.1300  216  VAL A CB    
890  C  CG1   . VAL A 113 ? 1.1397 1.2955 1.7489 0.0067  0.0362  0.1215  216  VAL A CG1   
891  C  CG2   . VAL A 113 ? 1.2728 1.4088 1.9751 0.0119  0.0460  0.1260  216  VAL A CG2   
892  N  N     . PRO A 114 ? 1.0719 1.1880 1.7815 0.0174  -0.0364 0.1572  217  PRO A N     
893  C  CA    . PRO A 114 ? 0.9373 1.0408 1.6936 0.0172  -0.0545 0.1678  217  PRO A CA    
894  C  C     . PRO A 114 ? 1.1277 1.2298 1.9467 0.0176  -0.0381 0.1661  217  PRO A C     
895  O  O     . PRO A 114 ? 1.1599 1.2555 2.0172 0.0178  -0.0494 0.1755  217  PRO A O     
896  C  CB    . PRO A 114 ? 0.9305 1.0262 1.6933 0.0128  -0.0788 0.1727  217  PRO A CB    
897  C  CG    . PRO A 114 ? 0.9123 1.0148 1.6154 0.0122  -0.0787 0.1672  217  PRO A CG    
898  C  CD    . PRO A 114 ? 1.2168 1.3336 1.9009 0.0138  -0.0489 0.1555  217  PRO A CD    
899  N  N     . GLU A 115 ? 1.3103 1.4176 2.1414 0.0168  -0.0110 0.1542  218  GLU A N     
900  C  CA    . GLU A 115 ? 1.0306 1.1351 1.9217 0.0174  0.0092  0.1517  218  GLU A CA    
901  C  C     . GLU A 115 ? 1.1131 1.2203 1.9992 0.0202  0.0243  0.1517  218  GLU A C     
902  O  O     . GLU A 115 ? 1.2278 1.3314 2.1675 0.0212  0.0317  0.1551  218  GLU A O     
903  C  CB    . GLU A 115 ? 1.2882 1.3933 2.1882 0.0142  0.0372  0.1374  218  GLU A CB    
904  C  CG    . GLU A 115 ? 1.5696 1.6690 2.5378 0.0147  0.0605  0.1343  218  GLU A CG    
905  C  CD    . GLU A 115 ? 1.5204 1.6158 2.4940 0.0103  0.0904  0.1188  218  GLU A CD    
906  O  OE1   . GLU A 115 ? 1.3430 1.4416 2.2639 0.0058  0.0926  0.1101  218  GLU A OE1   
907  O  OE2   . GLU A 115 ? 1.4988 1.5871 2.5301 0.0107  0.1127  0.1152  218  GLU A OE2   
908  N  N     . GLN A 116 ? 1.1455 1.2595 1.9704 0.0215  0.0289  0.1492  219  GLN A N     
909  C  CA    . GLN A 116 ? 1.1572 1.2728 1.9732 0.0243  0.0436  0.1501  219  GLN A CA    
910  C  C     . GLN A 116 ? 1.0960 1.2047 1.9218 0.0270  0.0215  0.1632  219  GLN A C     
911  O  O     . GLN A 116 ? 1.1470 1.2527 1.9993 0.0282  0.0309  0.1659  219  GLN A O     
912  C  CB    . GLN A 116 ? 1.1223 1.2482 1.8715 0.0249  0.0561  0.1449  219  GLN A CB    
913  C  CG    . GLN A 116 ? 1.2854 1.4170 2.0227 0.0194  0.0836  0.1310  219  GLN A CG    
914  C  CD    . GLN A 116 ? 1.2536 1.3982 1.9236 0.0182  0.0897  0.1284  219  GLN A CD    
915  O  OE1   . GLN A 116 ? 1.3471 1.4982 1.9806 0.0209  0.0702  0.1348  219  GLN A OE1   
916  N  NE2   . GLN A 116 ? 1.4435 1.5919 2.0972 0.0132  0.1171  0.1198  219  GLN A NE2   
917  N  N     . VAL A 117 ? 1.0690 1.1736 1.8719 0.0267  -0.0070 0.1709  220  VAL A N     
918  C  CA    . VAL A 117 ? 1.1242 1.2187 1.9325 0.0265  -0.0285 0.1824  220  VAL A CA    
919  C  C     . VAL A 117 ? 1.2830 1.3710 2.1606 0.0225  -0.0410 0.1895  220  VAL A C     
920  O  O     . VAL A 117 ? 1.4649 1.5463 2.3638 0.0209  -0.0499 0.1976  220  VAL A O     
921  C  CB    . VAL A 117 ? 1.0977 1.1868 1.8562 0.0257  -0.0528 0.1877  220  VAL A CB    
922  C  CG1   . VAL A 117 ? 1.2347 1.3219 2.0041 0.0214  -0.0704 0.1882  220  VAL A CG1   
923  C  CG2   . VAL A 117 ? 1.0143 1.0892 1.7688 0.0237  -0.0717 0.1980  220  VAL A CG2   
924  N  N     . ILE A 118 ? 1.2041 1.2942 2.1201 0.0206  -0.0418 0.1875  221  ILE A N     
925  C  CA    . ILE A 118 ? 1.1006 1.1876 2.0911 0.0178  -0.0511 0.1959  221  ILE A CA    
926  C  C     . ILE A 118 ? 1.0224 1.1130 2.0570 0.0201  -0.0243 0.1926  221  ILE A C     
927  O  O     . ILE A 118 ? 1.2204 1.3087 2.3015 0.0180  -0.0335 0.2023  221  ILE A O     
928  C  CB    . ILE A 118 ? 1.3663 1.4541 2.3886 0.0165  -0.0550 0.1949  221  ILE A CB    
929  C  CG1   . ILE A 118 ? 1.2247 1.3063 2.2146 0.0125  -0.0877 0.2022  221  ILE A CG1   
930  C  CG2   . ILE A 118 ? 1.0922 1.1803 2.2016 0.0158  -0.0550 0.2027  221  ILE A CG2   
931  C  CD1   . ILE A 118 ? 1.4114 1.4842 2.4174 0.0066  -0.1214 0.2182  221  ILE A CD1   
932  N  N     . ALA A 119 ? 1.1020 1.1979 2.1211 0.0230  0.0092  0.1792  222  ALA A N     
933  C  CA    . ALA A 119 ? 1.0962 1.1934 2.1520 0.0243  0.0383  0.1748  222  ALA A CA    
934  C  C     . ALA A 119 ? 1.2335 1.3285 2.2705 0.0251  0.0367  0.1801  222  ALA A C     
935  O  O     . ALA A 119 ? 1.6623 1.7564 2.7453 0.0248  0.0489  0.1825  222  ALA A O     
936  C  CB    . ALA A 119 ? 1.4208 1.5211 2.4515 0.0247  0.0740  0.1586  222  ALA A CB    
937  N  N     . GLU A 120 ? 1.3489 1.4423 2.3209 0.0262  0.0233  0.1822  223  GLU A N     
938  C  CA    . GLU A 120 ? 0.9639 1.0522 1.9175 0.0270  0.0210  0.1881  223  GLU A CA    
939  C  C     . GLU A 120 ? 1.2004 1.2807 2.1920 0.0221  -0.0077 0.2010  223  GLU A C     
940  O  O     . GLU A 120 ? 1.4814 1.5578 2.4952 0.0206  -0.0044 0.2057  223  GLU A O     
941  C  CB    . GLU A 120 ? 0.8968 0.9847 1.7727 0.0303  0.0170  0.1873  223  GLU A CB    
942  C  CG    . GLU A 120 ? 1.0971 1.1772 1.9495 0.0320  0.0169  0.1933  223  GLU A CG    
943  C  CD    . GLU A 120 ? 1.3326 1.4153 2.1960 0.0341  0.0477  0.1890  223  GLU A CD    
944  O  OE1   . GLU A 120 ? 0.8551 0.9458 1.7261 0.0345  0.0717  0.1797  223  GLU A OE1   
945  O  OE2   . GLU A 120 ? 1.5559 1.6307 2.4180 0.0344  0.0487  0.1946  223  GLU A OE2   
946  N  N     . ALA A 121 ? 0.8970 0.9745 1.8953 0.0182  -0.0364 0.2073  224  ALA A N     
947  C  CA    . ALA A 121 ? 0.9958 1.0664 2.0334 0.0108  -0.0659 0.2208  224  ALA A CA    
948  C  C     . ALA A 121 ? 1.0448 1.1220 2.1679 0.0093  -0.0583 0.2251  224  ALA A C     
949  O  O     . ALA A 121 ? 1.0792 1.1535 2.2407 0.0031  -0.0749 0.2361  224  ALA A O     
950  C  CB    . ALA A 121 ? 0.9437 1.0093 1.9675 0.0059  -0.0977 0.2271  224  ALA A CB    
951  N  N     . ILE A 122 ? 1.3986 1.4842 2.5534 0.0141  -0.0326 0.2166  225  ILE A N     
952  C  CA    . ILE A 122 ? 1.2339 1.3254 2.4718 0.0141  -0.0181 0.2195  225  ILE A CA    
953  C  C     . ILE A 122 ? 1.1493 1.2402 2.3946 0.0145  0.0023  0.2178  225  ILE A C     
954  O  O     . ILE A 122 ? 1.2964 1.3897 2.6044 0.0110  -0.0017 0.2269  225  ILE A O     
955  C  CB    . ILE A 122 ? 1.2005 1.2968 2.4627 0.0188  0.0099  0.2085  225  ILE A CB    
956  C  CG1   . ILE A 122 ? 1.1790 1.2752 2.4474 0.0178  -0.0123 0.2127  225  ILE A CG1   
957  C  CG2   . ILE A 122 ? 1.3620 1.4628 2.7075 0.0200  0.0335  0.2094  225  ILE A CG2   
958  C  CD1   . ILE A 122 ? 1.3297 1.4275 2.6182 0.0215  0.0153  0.2013  225  ILE A CD1   
959  N  N     . ARG A 123 ? 1.0197 1.1079 2.2023 0.0182  0.0238  0.2072  226  ARG A N     
960  C  CA    . ARG A 123 ? 1.2787 1.3643 2.4608 0.0184  0.0425  0.2063  226  ARG A CA    
961  C  C     . ARG A 123 ? 1.4225 1.5004 2.5988 0.0128  0.0146  0.2184  226  ARG A C     
962  O  O     . ARG A 123 ? 1.3390 1.4152 2.5466 0.0102  0.0222  0.2222  226  ARG A O     
963  C  CB    . ARG A 123 ? 1.0941 1.1785 2.2065 0.0232  0.0688  0.1946  226  ARG A CB    
964  C  CG    . ARG A 123 ? 1.5235 1.6049 2.6376 0.0239  0.0954  0.1922  226  ARG A CG    
965  C  CD    . ARG A 123 ? 1.4658 1.5390 2.5276 0.0242  0.0836  0.1981  226  ARG A CD    
966  N  NE    . ARG A 123 ? 1.2656 1.3391 2.2500 0.0290  0.0861  0.1934  226  ARG A NE    
967  C  CZ    . ARG A 123 ? 1.6045 1.6799 2.5492 0.0325  0.1132  0.1868  226  ARG A CZ    
968  N  NH1   . ARG A 123 ? 1.2437 1.3184 2.2133 0.0316  0.1420  0.1826  226  ARG A NH1   
969  N  NH2   . ARG A 123 ? 1.6491 1.7275 2.5281 0.0366  0.1112  0.1852  226  ARG A NH2   
970  N  N     . LYS A 124 ? 1.4085 1.4801 2.5442 0.0098  -0.0166 0.2239  227  LYS A N     
971  C  CA    . LYS A 124 ? 1.6025 1.6632 2.7297 0.0019  -0.0444 0.2348  227  LYS A CA    
972  C  C     . LYS A 124 ? 1.3566 1.4205 2.5582 -0.0073 -0.0688 0.2478  227  LYS A C     
973  O  O     . LYS A 124 ? 1.6296 1.6844 2.8314 -0.0169 -0.0919 0.2573  227  LYS A O     
974  C  CB    . LYS A 124 ? 1.2525 1.3028 2.3098 0.0004  -0.0675 0.2357  227  LYS A CB    
975  C  CG    . LYS A 124 ? 1.1878 1.2310 2.1713 0.0068  -0.0515 0.2290  227  LYS A CG    
976  C  CD    . LYS A 124 ? 1.2649 1.2958 2.2427 0.0029  -0.0501 0.2335  227  LYS A CD    
977  C  CE    . LYS A 124 ? 1.5972 1.6197 2.5033 0.0100  -0.0353 0.2291  227  LYS A CE    
978  N  NZ    . LYS A 124 ? 1.5276 1.5346 2.4254 0.0058  -0.0342 0.2337  227  LYS A NZ    
979  N  N     . LYS A 125 ? 1.1763 1.2524 2.4412 -0.0053 -0.0643 0.2492  228  LYS A N     
980  C  CA    . LYS A 125 ? 1.3502 1.4329 2.6950 -0.0129 -0.0865 0.2640  228  LYS A CA    
981  C  C     . LYS A 125 ? 1.1986 1.2927 2.6226 -0.0102 -0.0598 0.2641  228  LYS A C     
982  O  O     . LYS A 125 ? 0.9236 1.0259 2.4227 -0.0162 -0.0764 0.2781  228  LYS A O     
983  C  CB    . LYS A 125 ? 1.3964 1.4837 2.7619 -0.0132 -0.1071 0.2697  228  LYS A CB    
984  C  CG    . LYS A 125 ? 1.6406 1.7161 2.9375 -0.0184 -0.1381 0.2723  228  LYS A CG    
985  C  CD    . LYS A 125 ? 1.9211 1.9870 3.2153 -0.0327 -0.1744 0.2864  228  LYS A CD    
986  C  CE    . LYS A 125 ? 1.8826 1.9588 3.2635 -0.0410 -0.1993 0.3044  228  LYS A CE    
987  N  NZ    . LYS A 125 ? 1.5066 1.5728 2.8806 -0.0582 -0.2375 0.3188  228  LYS A NZ    
988  N  N     . THR A 126 ? 1.4905 1.5854 2.9006 -0.0020 -0.0190 0.2499  229  THR A N     
989  C  CA    . THR A 126 ? 1.3310 1.4342 2.8124 0.0008  0.0121  0.2478  229  THR A CA    
990  C  C     . THR A 126 ? 1.5358 1.6338 2.9979 0.0007  0.0370  0.2419  229  THR A C     
991  O  O     . THR A 126 ? 1.7701 1.8728 3.2943 -0.0031 0.0433  0.2484  229  THR A O     
992  C  CB    . THR A 126 ? 1.4739 1.5809 2.9659 0.0091  0.0437  0.2352  229  THR A CB    
993  O  OG1   . THR A 126 ? 1.6221 1.7219 3.0284 0.0136  0.0626  0.2201  229  THR A OG1   
994  C  CG2   . THR A 126 ? 0.9239 1.0356 2.4457 0.0094  0.0208  0.2422  229  THR A CG2   
995  N  N     . ARG A 127 ? 1.9194 2.0084 3.2988 0.0048  0.0513  0.2309  230  ARG A N     
996  C  CA    . ARG A 127 ? 1.9273 2.0098 3.2797 0.0057  0.0770  0.2253  230  ARG A CA    
997  C  C     . ARG A 127 ? 1.8021 1.8902 3.2084 0.0085  0.1170  0.2179  230  ARG A C     
998  O  O     . ARG A 127 ? 2.1952 2.2849 3.5895 0.0136  0.1410  0.2064  230  ARG A O     
999  C  CB    . ARG A 127 ? 1.7096 1.7854 3.0658 -0.0026 0.0532  0.2367  230  ARG A CB    
1000 C  CG    . ARG A 127 ? 1.8158 1.8827 3.1202 -0.0072 0.0148  0.2433  230  ARG A CG    
1001 C  CD    . ARG A 127 ? 1.8814 1.9357 3.1689 -0.0157 0.0006  0.2504  230  ARG A CD    
1002 N  NE    . ARG A 127 ? 1.6673 1.7121 2.9031 -0.0102 0.0285  0.2424  230  ARG A NE    
1003 C  CZ    . ARG A 127 ? 1.8516 1.8829 3.0669 -0.0155 0.0260  0.2461  230  ARG A CZ    
1004 N  NH1   . ARG A 127 ? 2.0373 2.0625 3.2769 -0.0282 -0.0029 0.2565  230  ARG A NH1   
1005 N  NH2   . ARG A 127 ? 1.5683 1.5914 2.7368 -0.0091 0.0530  0.2397  230  ARG A NH2   
1006 N  N     . SER A 128 ? 1.3101 1.4000 2.7736 0.0046  0.1269  0.2232  231  SER A N     
1007 C  CA    . SER A 128 ? 1.5316 1.6260 3.0562 0.0065  0.1655  0.2171  231  SER A CA    
1008 C  C     . SER A 128 ? 1.6192 1.7256 3.2456 0.0021  0.1492  0.2313  231  SER A C     
1009 O  O     . SER A 128 ? 1.2711 1.3795 2.9357 -0.0040 0.1441  0.2401  231  SER A O     
1010 C  CB    . SER A 128 ? 1.3070 1.3931 2.8068 0.0059  0.1972  0.2105  231  SER A CB    
1011 O  OG    . SER A 128 ? 1.4561 1.5399 2.9698 -0.0005 0.1788  0.2216  231  SER A OG    
1012 N  N     . MET A 129 ? 1.4771 1.5920 3.1489 0.0047  0.1409  0.2344  232  MET A N     
1013 C  CA    . MET A 129 ? 1.3415 1.4698 3.1068 0.0009  0.1167  0.2516  232  MET A CA    
1014 C  C     . MET A 129 ? 1.6980 1.8339 3.5510 0.0058  0.1533  0.2488  232  MET A C     
1015 O  O     . MET A 129 ? 1.4610 1.5903 3.3080 0.0084  0.1969  0.2353  232  MET A O     
1016 C  CB    . MET A 129 ? 1.2589 1.3896 3.0079 0.0000  0.0759  0.2601  232  MET A CB    
1017 C  CG    . MET A 129 ? 1.6613 1.8038 3.4806 -0.0081 0.0342  0.2826  232  MET A CG    
1018 S  SD    . MET A 129 ? 1.5737 1.7157 3.3646 -0.0106 -0.0130 0.2925  232  MET A SD    
1019 C  CE    . MET A 129 ? 1.0379 1.1643 2.7258 -0.0196 -0.0427 0.2919  232  MET A CE    
1020 N  N     . LEU A 130 ? 1.9978 2.1461 3.9308 0.0067  0.1370  0.2618  233  LEU A N     
1021 C  CA    . LEU A 130 ? 1.7328 1.8894 3.7647 0.0113  0.1683  0.2632  233  LEU A CA    
1022 C  C     . LEU A 130 ? 1.8152 1.9645 3.8377 0.0196  0.1959  0.2492  233  LEU A C     
1023 O  O     . LEU A 130 ? 1.7913 1.9393 3.7826 0.0212  0.1714  0.2510  233  LEU A O     
1024 C  CB    . LEU A 130 ? 1.6778 1.8535 3.8112 0.0076  0.1342  0.2883  233  LEU A CB    
1025 C  CG    . LEU A 130 ? 1.8474 2.0349 4.0967 0.0139  0.1585  0.2951  233  LEU A CG    
1026 C  CD1   . LEU A 130 ? 1.7502 1.9335 4.0329 0.0167  0.2135  0.2822  233  LEU A CD1   
1027 C  CD2   . LEU A 130 ? 1.3997 1.6048 3.7347 0.0084  0.1163  0.3233  233  LEU A CD2   
1028 N  N     . LEU A 131 ? 2.0602 2.2030 4.1087 0.0236  0.2478  0.2350  234  LEU A N     
1029 C  CA    . LEU A 131 ? 2.0991 2.2321 4.1456 0.0296  0.2803  0.2204  234  LEU A CA    
1030 C  C     . LEU A 131 ? 2.1806 2.3109 4.3044 0.0324  0.3320  0.2138  234  LEU A C     
1031 O  O     . LEU A 131 ? 2.1547 2.2755 4.2516 0.0296  0.3667  0.2010  234  LEU A O     
1032 C  CB    . LEU A 131 ? 1.9505 2.0673 3.8791 0.0288  0.2940  0.1996  234  LEU A CB    
1033 C  CG    . LEU A 131 ? 2.1785 2.2946 4.0383 0.0290  0.2564  0.2010  234  LEU A CG    
1034 C  CD1   . LEU A 131 ? 2.2503 2.3530 4.0009 0.0277  0.2747  0.1811  234  LEU A CD1   
1035 C  CD2   . LEU A 131 ? 1.9703 2.0891 3.8840 0.0335  0.2508  0.2059  234  LEU A CD2   
1036 N  N     . SER A 132 ? 1.8596 1.9971 4.0798 0.0377  0.3379  0.2231  235  SER A N     
1037 C  CA    . SER A 132 ? 1.5136 1.6392 3.7955 0.0412  0.3906  0.2141  235  SER A CA    
1038 C  C     . SER A 132 ? 1.6234 1.7332 3.8729 0.0441  0.4305  0.1922  235  SER A C     
1039 O  O     . SER A 132 ? 1.7822 1.8872 3.9679 0.0444  0.4095  0.1879  235  SER A O     
1040 C  CB    . SER A 132 ? 1.5963 1.7155 3.9634 0.0443  0.3729  0.2348  235  SER A CB    
1041 O  OG    . SER A 132 ? 1.1694 1.3018 3.5665 0.0398  0.3388  0.2542  235  SER A OG    
1042 N  N     . SER A 133 ? 1.6306 1.7150 3.8926 0.0442  0.4836  0.1767  236  SER A N     
1043 C  CA    . SER A 133 ? 1.5473 1.6122 3.7740 0.0441  0.5267  0.1536  236  SER A CA    
1044 C  C     . SER A 133 ? 1.5512 1.6087 3.8163 0.0500  0.5167  0.1594  236  SER A C     
1045 O  O     . SER A 133 ? 1.8432 1.8817 4.0852 0.0494  0.5531  0.1404  236  SER A O     
1046 C  CB    . SER A 133 ? 1.4404 1.4756 3.6681 0.0407  0.5863  0.1354  236  SER A CB    
1047 O  OG    . SER A 133 ? 1.8268 1.8399 4.0150 0.0379  0.6290  0.1119  236  SER A OG    
1048 N  N     . GLU A 134 ? 1.4074 1.4774 3.7279 0.0539  0.4694  0.1852  237  GLU A N     
1049 C  CA    . GLU A 134 ? 1.4615 1.5283 3.8114 0.0584  0.4512  0.1943  237  GLU A CA    
1050 C  C     . GLU A 134 ? 1.3514 1.4444 3.6765 0.0591  0.3927  0.2092  237  GLU A C     
1051 O  O     . GLU A 134 ? 1.3331 1.4259 3.6830 0.0622  0.3681  0.2213  237  GLU A O     
1052 C  CB    . GLU A 134 ? 1.2732 1.3280 3.7131 0.0604  0.4478  0.2139  237  GLU A CB    
1053 C  CG    . GLU A 134 ? 1.3843 1.4080 3.8559 0.0603  0.5077  0.1996  237  GLU A CG    
1054 C  CD    . GLU A 134 ? 1.8753 1.8965 4.3584 0.0576  0.5249  0.1984  237  GLU A CD    
1055 O  OE1   . GLU A 134 ? 1.8126 1.8566 4.2750 0.0555  0.4925  0.2071  237  GLU A OE1   
1056 O  OE2   . GLU A 134 ? 1.5146 1.5094 4.0276 0.0572  0.5715  0.1887  237  GLU A OE2   
1057 N  N     . GLN A 135 ? 1.5488 1.6618 3.8228 0.0555  0.3704  0.2090  238  GLN A N     
1058 C  CA    . GLN A 135 ? 1.5605 1.6835 3.7813 0.0527  0.3113  0.2219  238  GLN A CA    
1059 C  C     . GLN A 135 ? 1.7817 1.8903 3.8743 0.0485  0.3102  0.2020  238  GLN A C     
1060 O  O     . GLN A 135 ? 1.6368 1.7513 3.6663 0.0448  0.2676  0.2086  238  GLN A O     
1061 C  CB    . GLN A 135 ? 1.3609 1.5014 3.5949 0.0479  0.2746  0.2398  238  GLN A CB    
1062 C  CG    . GLN A 135 ? 0.8539 1.0005 3.1902 0.0485  0.2637  0.2621  238  GLN A CG    
1063 C  CD    . GLN A 135 ? 1.2211 1.3829 3.5634 0.0414  0.2275  0.2785  238  GLN A CD    
1064 O  OE1   . GLN A 135 ? 1.2763 1.4413 3.5959 0.0381  0.2462  0.2691  238  GLN A OE1   
1065 N  NE2   . GLN A 135 ? 1.0193 1.1892 3.3900 0.0375  0.1757  0.3032  238  GLN A NE2   
1066 N  N     . LEU A 136 ? 1.9743 2.0638 4.0274 0.0480  0.3565  0.1780  239  LEU A N     
1067 C  CA    . LEU A 136 ? 1.8259 1.9038 3.7613 0.0430  0.3563  0.1600  239  LEU A CA    
1068 C  C     . LEU A 136 ? 2.0959 2.1766 4.0075 0.0446  0.3177  0.1675  239  LEU A C     
1069 O  O     . LEU A 136 ? 2.1588 2.2473 4.0119 0.0421  0.2758  0.1750  239  LEU A O     
1070 C  CB    . LEU A 136 ? 1.8470 1.9031 3.7503 0.0396  0.4140  0.1336  239  LEU A CB    
1071 C  CG    . LEU A 136 ? 1.8343 1.8824 3.7347 0.0355  0.4568  0.1216  239  LEU A CG    
1072 C  CD1   . LEU A 136 ? 2.0471 2.0943 4.0633 0.0403  0.4896  0.1267  239  LEU A CD1   
1073 C  CD2   . LEU A 136 ? 1.7623 1.7893 3.5720 0.0271  0.4959  0.0949  239  LEU A CD2   
1074 N  N     . LYS A 137 ? 2.1365 2.2094 4.0946 0.0485  0.3328  0.1657  240  LYS A N     
1075 C  CA    . LYS A 137 ? 2.1597 2.2335 4.0988 0.0498  0.2991  0.1727  240  LYS A CA    
1076 C  C     . LYS A 137 ? 1.9491 2.0416 3.9250 0.0515  0.2418  0.2007  240  LYS A C     
1077 O  O     . LYS A 137 ? 2.1192 2.2131 4.0589 0.0505  0.2061  0.2075  240  LYS A O     
1078 C  CB    . LYS A 137 ? 2.1627 2.2235 4.1593 0.0544  0.3286  0.1678  240  LYS A CB    
1079 C  CG    . LYS A 137 ? 2.2120 2.2508 4.1342 0.0490  0.3667  0.1397  240  LYS A CG    
1080 C  CD    . LYS A 137 ? 2.3299 2.3571 4.2185 0.0432  0.4147  0.1185  240  LYS A CD    
1081 C  CE    . LYS A 137 ? 2.3135 2.3190 4.1213 0.0347  0.4489  0.0913  240  LYS A CE    
1082 N  NZ    . LYS A 137 ? 2.0188 2.0117 3.7867 0.0268  0.4940  0.0714  240  LYS A NZ    
1083 N  N     . LEU A 138 ? 1.4178 1.5242 3.4637 0.0526  0.2324  0.2172  241  LEU A N     
1084 C  CA    . LEU A 138 ? 1.2731 1.3964 3.3422 0.0506  0.1763  0.2431  241  LEU A CA    
1085 C  C     . LEU A 138 ? 1.5224 1.6455 3.4859 0.0438  0.1448  0.2396  241  LEU A C     
1086 O  O     . LEU A 138 ? 1.4612 1.5900 3.4072 0.0405  0.0976  0.2549  241  LEU A O     
1087 C  CB    . LEU A 138 ? 1.6709 1.8091 3.8337 0.0511  0.1762  0.2597  241  LEU A CB    
1088 C  CG    . LEU A 138 ? 1.4676 1.6247 3.6800 0.0472  0.1210  0.2896  241  LEU A CG    
1089 C  CD1   . LEU A 138 ? 1.4702 1.6304 3.6115 0.0382  0.0918  0.2909  241  LEU A CD1   
1090 C  CD2   . LEU A 138 ? 0.9080 1.0664 3.1276 0.0480  0.0837  0.3044  241  LEU A CD2   
1091 N  N     . CYS A 139 ? 1.7425 1.8581 3.6350 0.0413  0.1709  0.2204  242  CYS A N     
1092 C  CA    . CYS A 139 ? 1.5236 1.6380 3.3167 0.0362  0.1467  0.2164  242  CYS A CA    
1093 C  C     . CYS A 139 ? 1.5542 1.6571 3.2536 0.0355  0.1619  0.1960  242  CYS A C     
1094 O  O     . CYS A 139 ? 1.8474 1.9502 3.4687 0.0325  0.1358  0.1956  242  CYS A O     
1095 C  CB    . CYS A 139 ? 1.5650 1.6816 3.3448 0.0334  0.1581  0.2140  242  CYS A CB    
1096 S  SG    . CYS A 139 ? 1.2571 1.3892 3.1310 0.0308  0.1308  0.2394  242  CYS A SG    
1097 N  N     . VAL A 140 ? 1.4098 1.5024 3.1148 0.0373  0.2040  0.1792  243  VAL A N     
1098 C  CA    . VAL A 140 ? 1.5577 1.6404 3.1772 0.0346  0.2157  0.1610  243  VAL A CA    
1099 C  C     . VAL A 140 ? 1.6023 1.6857 3.2124 0.0354  0.1826  0.1689  243  VAL A C     
1100 O  O     . VAL A 140 ? 1.7664 1.8471 3.2956 0.0323  0.1721  0.1607  243  VAL A O     
1101 C  CB    . VAL A 140 ? 1.4874 1.5560 3.1144 0.0336  0.2707  0.1403  243  VAL A CB    
1102 C  CG1   . VAL A 140 ? 1.7690 1.8281 3.3081 0.0284  0.2813  0.1219  243  VAL A CG1   
1103 C  CG2   . VAL A 140 ? 1.1277 1.1941 2.7555 0.0315  0.3028  0.1325  243  VAL A CG2   
1104 N  N     . LEU A 141 ? 1.4419 1.5297 3.1351 0.0391  0.1649  0.1861  244  LEU A N     
1105 C  CA    . LEU A 141 ? 1.6633 1.7512 3.3508 0.0392  0.1304  0.1964  244  LEU A CA    
1106 C  C     . LEU A 141 ? 1.5213 1.6151 3.1423 0.0349  0.0849  0.2056  244  LEU A C     
1107 O  O     . LEU A 141 ? 1.5882 1.6792 3.1718 0.0332  0.0607  0.2081  244  LEU A O     
1108 C  CB    . LEU A 141 ? 1.3745 1.4677 3.1695 0.0438  0.1172  0.2173  244  LEU A CB    
1109 C  CG    . LEU A 141 ? 1.2146 1.3042 3.0206 0.0449  0.0927  0.2270  244  LEU A CG    
1110 C  CD1   . LEU A 141 ? 1.5284 1.6025 3.3008 0.0455  0.1281  0.2054  244  LEU A CD1   
1111 C  CD2   . LEU A 141 ? 1.0767 1.1742 2.9958 0.0496  0.0784  0.2513  244  LEU A CD2   
1112 N  N     . GLU A 142 ? 1.4038 1.5038 3.0090 0.0326  0.0747  0.2102  245  GLU A N     
1113 C  CA    . GLU A 142 ? 1.5605 1.6623 3.0950 0.0281  0.0379  0.2159  245  GLU A CA    
1114 C  C     . GLU A 142 ? 1.4342 1.5303 2.8706 0.0271  0.0493  0.1979  245  GLU A C     
1115 O  O     . GLU A 142 ? 1.2338 1.3287 2.6139 0.0245  0.0206  0.2011  245  GLU A O     
1116 C  CB    . GLU A 142 ? 1.5727 1.6797 3.1128 0.0257  0.0304  0.2231  245  GLU A CB    
1117 C  CG    . GLU A 142 ? 1.3694 1.4847 3.0095 0.0255  0.0215  0.2409  245  GLU A CG    
1118 C  CD    . GLU A 142 ? 1.4983 1.6179 3.1685 0.0210  -0.0270 0.2633  245  GLU A CD    
1119 O  OE1   . GLU A 142 ? 1.5310 1.6456 3.1338 0.0163  -0.0572 0.2655  245  GLU A OE1   
1120 O  OE2   . GLU A 142 ? 1.7134 1.8411 3.4750 0.0218  -0.0346 0.2794  245  GLU A OE2   
1121 N  N     . TYR A 143 ? 1.6794 1.7719 3.0944 0.0281  0.0910  0.1794  246  TYR A N     
1122 C  CA    . TYR A 143 ? 1.6540 1.7435 2.9794 0.0260  0.1030  0.1632  246  TYR A CA    
1123 C  C     . TYR A 143 ? 1.7213 1.8055 3.0313 0.0248  0.1066  0.1552  246  TYR A C     
1124 O  O     . TYR A 143 ? 2.0092 2.0928 3.2454 0.0219  0.1114  0.1435  246  TYR A O     
1125 C  CB    . TYR A 143 ? 1.7360 1.8229 3.0410 0.0250  0.1450  0.1473  246  TYR A CB    
1126 C  CG    . TYR A 143 ? 1.6575 1.7483 2.9711 0.0258  0.1452  0.1537  246  TYR A CG    
1127 C  CD1   . TYR A 143 ? 1.5850 1.6789 2.8319 0.0250  0.1289  0.1560  246  TYR A CD1   
1128 C  CD2   . TYR A 143 ? 1.6321 1.7228 3.0223 0.0273  0.1631  0.1576  246  TYR A CD2   
1129 C  CE1   . TYR A 143 ? 1.6956 1.7909 2.9494 0.0254  0.1301  0.1616  246  TYR A CE1   
1130 C  CE2   . TYR A 143 ? 1.5800 1.6737 2.9781 0.0271  0.1637  0.1632  246  TYR A CE2   
1131 C  CZ    . TYR A 143 ? 1.6439 1.7391 2.9724 0.0259  0.1471  0.1649  246  TYR A CZ    
1132 O  OH    . TYR A 143 ? 1.6179 1.7140 2.9534 0.0254  0.1487  0.1703  246  TYR A OH    
1133 N  N     . GLN A 144 ? 1.5018 1.5826 2.8808 0.0269  0.1044  0.1621  247  GLN A N     
1134 C  CA    . GLN A 144 ? 1.5380 1.6116 2.9069 0.0257  0.1076  0.1555  247  GLN A CA    
1135 C  C     . GLN A 144 ? 1.4739 1.5502 2.8100 0.0243  0.0630  0.1679  247  GLN A C     
1136 O  O     . GLN A 144 ? 1.7792 1.8612 3.0869 0.0232  0.0338  0.1781  247  GLN A O     
1137 C  CB    . GLN A 144 ? 1.6181 1.6850 3.0771 0.0294  0.1270  0.1582  247  GLN A CB    
1138 C  CG    . GLN A 144 ? 1.6424 1.7052 3.1436 0.0308  0.1714  0.1479  247  GLN A CG    
1139 C  CD    . GLN A 144 ? 1.9437 1.9969 3.3811 0.0251  0.2115  0.1227  247  GLN A CD    
1140 O  OE1   . GLN A 144 ? 1.8660 1.9171 3.2986 0.0233  0.2417  0.1128  247  GLN A OE1   
1141 N  NE2   . GLN A 144 ? 1.9806 2.0275 3.3680 0.0207  0.2118  0.1124  247  GLN A NE2   
1142 N  N     . GLY A 145 ? 1.1622 1.2321 2.5003 0.0234  0.0587  0.1667  248  GLY A N     
1143 C  CA    . GLY A 145 ? 1.2870 1.3572 2.5975 0.0212  0.0182  0.1787  248  GLY A CA    
1144 C  C     . GLY A 145 ? 1.5044 1.5768 2.8803 0.0226  -0.0157 0.2028  248  GLY A C     
1145 O  O     . GLY A 145 ? 2.0797 2.1480 3.5170 0.0246  -0.0196 0.2122  248  GLY A O     
1146 N  N     . LYS A 146 ? 1.1050 1.1833 2.4684 0.0207  -0.0409 0.2137  249  LYS A N     
1147 C  CA    . LYS A 146 ? 1.4342 1.5157 2.8600 0.0194  -0.0734 0.2371  249  LYS A CA    
1148 C  C     . LYS A 146 ? 1.4650 1.5450 2.8384 0.0125  -0.1155 0.2485  249  LYS A C     
1149 O  O     . LYS A 146 ? 1.2195 1.2980 2.6222 0.0080  -0.1508 0.2679  249  LYS A O     
1150 C  CB    . LYS A 146 ? 1.2304 1.3192 2.7183 0.0222  -0.0569 0.2407  249  LYS A CB    
1151 C  CG    . LYS A 146 ? 1.2456 1.3406 2.8080 0.0199  -0.0892 0.2660  249  LYS A CG    
1152 C  CD    . LYS A 146 ? 1.1120 1.2154 2.7374 0.0225  -0.0696 0.2684  249  LYS A CD    
1153 C  CE    . LYS A 146 ? 1.1570 1.2693 2.8582 0.0186  -0.1041 0.2951  249  LYS A CE    
1154 N  NZ    . LYS A 146 ? 0.8101 0.9320 2.5763 0.0207  -0.0849 0.2980  249  LYS A NZ    
1155 N  N     . TYR A 147 ? 1.3738 1.4534 2.6698 0.0110  -0.1118 0.2374  250  TYR A N     
1156 C  CA    . TYR A 147 ? 1.1805 1.2558 2.4236 0.0044  -0.1459 0.2460  250  TYR A CA    
1157 C  C     . TYR A 147 ? 1.0754 1.1459 2.2319 0.0035  -0.1461 0.2344  250  TYR A C     
1158 O  O     . TYR A 147 ? 1.3312 1.4050 2.4588 0.0076  -0.1167 0.2177  250  TYR A O     
1159 C  CB    . TYR A 147 ? 1.2426 1.3207 2.4775 0.0036  -0.1434 0.2467  250  TYR A CB    
1160 C  CG    . TYR A 147 ? 1.3370 1.4213 2.6568 0.0033  -0.1445 0.2589  250  TYR A CG    
1161 C  CD1   . TYR A 147 ? 1.1398 1.2231 2.4997 -0.0043 -0.1821 0.2801  250  TYR A CD1   
1162 C  CD2   . TYR A 147 ? 1.4726 1.5636 2.8321 0.0095  -0.1081 0.2498  250  TYR A CD2   
1163 C  CE1   . TYR A 147 ? 1.1771 1.2689 2.6187 -0.0051 -0.1843 0.2928  250  TYR A CE1   
1164 C  CE2   . TYR A 147 ? 1.5298 1.6275 2.9704 0.0095  -0.1077 0.2613  250  TYR A CE2   
1165 C  CZ    . TYR A 147 ? 1.3948 1.4942 2.8784 0.0025  -0.1463 0.2832  250  TYR A CZ    
1166 O  OH    . TYR A 147 ? 1.5773 1.6862 3.1457 0.0018  -0.1470 0.2962  250  TYR A OH    
1167 N  N     . ILE A 148 ? 0.9734 1.0359 2.0885 -0.0033 -0.1795 0.2438  251  ILE A N     
1168 C  CA    . ILE A 148 ? 1.2116 1.2697 2.2453 -0.0046 -0.1822 0.2349  251  ILE A CA    
1169 C  C     . ILE A 148 ? 1.3334 1.3863 2.3148 -0.0080 -0.1946 0.2370  251  ILE A C     
1170 O  O     . ILE A 148 ? 1.6362 1.6900 2.6409 -0.0085 -0.1951 0.2419  251  ILE A O     
1171 C  CB    . ILE A 148 ? 1.0326 1.0819 2.0578 -0.0101 -0.2070 0.2426  251  ILE A CB    
1172 C  CG1   . ILE A 148 ? 1.0514 1.0911 2.0968 -0.0193 -0.2466 0.2631  251  ILE A CG1   
1173 C  CG2   . ILE A 148 ? 1.2025 1.2548 2.2775 -0.0061 -0.1914 0.2396  251  ILE A CG2   
1174 C  CD1   . ILE A 148 ? 0.9048 0.9334 1.9337 -0.0263 -0.2736 0.2722  251  ILE A CD1   
1175 N  N     . LEU A 149 ? 1.4652 1.5117 2.3769 -0.0103 -0.2033 0.2333  252  LEU A N     
1176 C  CA    . LEU A 149 ? 1.2984 1.3369 2.1566 -0.0132 -0.2126 0.2346  252  LEU A CA    
1177 C  C     . LEU A 149 ? 1.1445 1.1686 1.9528 -0.0209 -0.2383 0.2396  252  LEU A C     
1178 O  O     . LEU A 149 ? 1.5092 1.5341 2.3030 -0.0210 -0.2388 0.2361  252  LEU A O     
1179 C  CB    . LEU A 149 ? 0.9818 1.0297 1.7975 -0.0048 -0.1829 0.2209  252  LEU A CB    
1180 C  CG    . LEU A 149 ? 1.0220 1.0650 1.8166 -0.0043 -0.1810 0.2228  252  LEU A CG    
1181 C  CD1   . LEU A 149 ? 1.2602 1.3019 2.1162 -0.0074 -0.1870 0.2315  252  LEU A CD1   
1182 C  CD2   . LEU A 149 ? 1.1192 1.1742 1.8823 0.0049  -0.1500 0.2111  252  LEU A CD2   
1183 N  N     . LYS A 150 ? 1.0983 1.1074 1.8785 -0.0286 -0.2583 0.2472  253  LYS A N     
1184 C  CA    . LYS A 150 ? 1.0747 1.0655 1.8086 -0.0387 -0.2841 0.2531  253  LYS A CA    
1185 C  C     . LYS A 150 ? 1.1797 1.1558 1.8555 -0.0421 -0.2858 0.2516  253  LYS A C     
1186 O  O     . LYS A 150 ? 1.4171 1.3915 2.1046 -0.0422 -0.2822 0.2533  253  LYS A O     
1187 C  CB    . LYS A 150 ? 1.2083 1.1888 1.9825 -0.0509 -0.3175 0.2697  253  LYS A CB    
1188 C  CG    . LYS A 150 ? 0.9799 0.9375 1.7034 -0.0646 -0.3464 0.2772  253  LYS A CG    
1189 C  CD    . LYS A 150 ? 0.9177 0.8660 1.6826 -0.0784 -0.3817 0.2962  253  LYS A CD    
1190 C  CE    . LYS A 150 ? 1.4107 1.3327 2.1183 -0.0949 -0.4108 0.3037  253  LYS A CE    
1191 N  NZ    . LYS A 150 ? 1.4199 1.3241 2.0659 -0.1007 -0.4083 0.2979  253  LYS A NZ    
1192 N  N     . VAL A 151 ? 1.0883 1.0528 1.7026 -0.0449 -0.2897 0.2483  254  VAL A N     
1193 C  CA    . VAL A 151 ? 1.3313 1.2774 1.8885 -0.0488 -0.2907 0.2472  254  VAL A CA    
1194 C  C     . VAL A 151 ? 1.1915 1.1131 1.7487 -0.0659 -0.3214 0.2592  254  VAL A C     
1195 O  O     . VAL A 151 ? 1.2969 1.2104 1.8685 -0.0770 -0.3473 0.2688  254  VAL A O     
1196 C  CB    . VAL A 151 ? 1.2670 1.2078 1.7627 -0.0471 -0.2844 0.2406  254  VAL A CB    
1197 C  CG1   . VAL A 151 ? 1.4493 1.3696 1.8882 -0.0498 -0.2809 0.2390  254  VAL A CG1   
1198 C  CG2   . VAL A 151 ? 0.9594 0.9266 1.4571 -0.0326 -0.2571 0.2300  254  VAL A CG2   
1199 N  N     . CYS A 152 ? 1.2843 1.1932 1.8242 -0.0692 -0.3192 0.2595  255  CYS A N     
1200 C  CA    . CYS A 152 ? 1.4434 1.3271 1.9771 -0.0880 -0.3476 0.2701  255  CYS A CA    
1201 C  C     . CYS A 152 ? 1.4073 1.2622 1.8712 -0.1001 -0.3605 0.2699  255  CYS A C     
1202 O  O     . CYS A 152 ? 1.6135 1.4571 2.0235 -0.0956 -0.3424 0.2612  255  CYS A O     
1203 C  CB    . CYS A 152 ? 1.4280 1.3061 1.9647 -0.0881 -0.3381 0.2691  255  CYS A CB    
1204 S  SG    . CYS A 152 ? 1.1546 1.0630 1.7733 -0.0763 -0.3226 0.2698  255  CYS A SG    
1205 N  N     . GLY A 153 ? 1.4316 1.2738 1.8972 -0.1157 -0.3910 0.2802  256  GLY A N     
1206 C  CA    . GLY A 153 ? 1.5510 1.3627 1.9495 -0.1300 -0.4045 0.2806  256  GLY A CA    
1207 C  C     . GLY A 153 ? 1.7965 1.6134 2.1840 -0.1275 -0.4074 0.2799  256  GLY A C     
1208 O  O     . GLY A 153 ? 1.7646 1.5590 2.1224 -0.1441 -0.4315 0.2869  256  GLY A O     
1209 N  N     . CYS A 154 ? 1.5645 1.4095 1.9736 -0.1085 -0.3832 0.2714  257  CYS A N     
1210 C  CA    . CYS A 154 ? 1.5087 1.3608 1.9095 -0.1052 -0.3824 0.2692  257  CYS A CA    
1211 C  C     . CYS A 154 ? 1.6679 1.5418 2.1388 -0.1010 -0.3904 0.2758  257  CYS A C     
1212 O  O     . CYS A 154 ? 1.2798 1.1636 1.8067 -0.1006 -0.3967 0.2827  257  CYS A O     
1213 C  CB    . CYS A 154 ? 1.4482 1.3151 1.8185 -0.0889 -0.3496 0.2549  257  CYS A CB    
1214 S  SG    . CYS A 154 ? 2.1078 1.9467 2.3916 -0.0945 -0.3419 0.2487  257  CYS A SG    
1215 N  N     . ASP A 155 ? 1.7791 1.6599 2.2479 -0.0979 -0.3885 0.2737  258  ASP A N     
1216 C  CA    . ASP A 155 ? 1.6874 1.5860 2.2187 -0.0931 -0.3921 0.2787  258  ASP A CA    
1217 C  C     . ASP A 155 ? 1.6762 1.6014 2.2233 -0.0757 -0.3593 0.2647  258  ASP A C     
1218 O  O     . ASP A 155 ? 1.5043 1.4402 2.0853 -0.0721 -0.3572 0.2650  258  ASP A O     
1219 C  CB    . ASP A 155 ? 1.8137 1.6970 2.3349 -0.1052 -0.4174 0.2887  258  ASP A CB    
1220 C  CG    . ASP A 155 ? 1.8887 1.7464 2.3996 -0.1252 -0.4534 0.3049  258  ASP A CG    
1221 O  OD1   . ASP A 155 ? 1.8161 1.6752 2.3613 -0.1289 -0.4636 0.3126  258  ASP A OD1   
1222 O  OD2   . ASP A 155 ? 1.9153 1.7508 2.3826 -0.1385 -0.4718 0.3102  258  ASP A OD2   
1223 N  N     . GLU A 156 ? 1.6074 1.5425 2.1295 -0.0657 -0.3338 0.2529  259  GLU A N     
1224 C  CA    . GLU A 156 ? 1.5466 1.5069 2.0783 -0.0514 -0.3035 0.2402  259  GLU A CA    
1225 C  C     . GLU A 156 ? 1.2166 1.1942 1.8100 -0.0435 -0.2908 0.2395  259  GLU A C     
1226 O  O     . GLU A 156 ? 1.2831 1.2567 1.8956 -0.0451 -0.2959 0.2449  259  GLU A O     
1227 C  CB    . GLU A 156 ? 1.2522 1.2165 1.7291 -0.0446 -0.2828 0.2301  259  GLU A CB    
1228 C  CG    . GLU A 156 ? 1.2968 1.2473 1.7149 -0.0503 -0.2884 0.2287  259  GLU A CG    
1229 C  CD    . GLU A 156 ? 1.4622 1.4208 1.8349 -0.0415 -0.2655 0.2200  259  GLU A CD    
1230 O  OE1   . GLU A 156 ? 1.9227 1.8916 2.3029 -0.0329 -0.2497 0.2172  259  GLU A OE1   
1231 O  OE2   . GLU A 156 ? 1.6859 1.6410 2.0175 -0.0432 -0.2630 0.2169  259  GLU A OE2   
1232 N  N     . TYR A 157 ? 1.3488 1.3442 1.9723 -0.0361 -0.2729 0.2323  260  TYR A N     
1233 C  CA    . TYR A 157 ? 1.1044 1.1146 1.7877 -0.0291 -0.2573 0.2303  260  TYR A CA    
1234 C  C     . TYR A 157 ? 1.0598 1.0896 1.7308 -0.0192 -0.2239 0.2149  260  TYR A C     
1235 O  O     . TYR A 157 ? 1.1828 1.2179 1.8196 -0.0184 -0.2155 0.2071  260  TYR A O     
1236 C  CB    . TYR A 157 ? 1.2385 1.2479 1.9822 -0.0318 -0.2679 0.2381  260  TYR A CB    
1237 C  CG    . TYR A 157 ? 1.2190 1.2130 1.9886 -0.0421 -0.3020 0.2563  260  TYR A CG    
1238 C  CD1   . TYR A 157 ? 1.1436 1.1193 1.8752 -0.0532 -0.3291 0.2648  260  TYR A CD1   
1239 C  CD2   . TYR A 157 ? 1.2831 1.2810 2.1152 -0.0420 -0.3074 0.2657  260  TYR A CD2   
1240 C  CE1   . TYR A 157 ? 1.1955 1.1566 1.9472 -0.0650 -0.3623 0.2826  260  TYR A CE1   
1241 C  CE2   . TYR A 157 ? 1.2482 1.2343 2.1053 -0.0531 -0.3409 0.2841  260  TYR A CE2   
1242 C  CZ    . TYR A 157 ? 1.0849 1.0524 1.9001 -0.0652 -0.3691 0.2927  260  TYR A CZ    
1243 O  OH    . TYR A 157 ? 1.3036 1.2588 2.1401 -0.0786 -0.4045 0.3120  260  TYR A OH    
1244 N  N     . PHE A 158 ? 1.0731 1.1133 1.7713 -0.0129 -0.2054 0.2112  261  PHE A N     
1245 C  CA    . PHE A 158 ? 1.1787 1.2368 1.8668 -0.0052 -0.1738 0.1977  261  PHE A CA    
1246 C  C     . PHE A 158 ? 1.2182 1.2832 1.9570 -0.0040 -0.1587 0.1922  261  PHE A C     
1247 O  O     . PHE A 158 ? 1.1122 1.1839 1.8886 -0.0001 -0.1398 0.1884  261  PHE A O     
1248 C  CB    . PHE A 158 ? 1.0998 1.1631 1.7848 0.0001  -0.1603 0.1965  261  PHE A CB    
1249 C  CG    . PHE A 158 ? 1.0154 1.0695 1.6515 -0.0005 -0.1713 0.2012  261  PHE A CG    
1250 C  CD1   . PHE A 158 ? 1.2820 1.3178 1.9234 -0.0072 -0.1957 0.2123  261  PHE A CD1   
1251 C  CD2   . PHE A 158 ? 1.0873 1.1504 1.6728 0.0049  -0.1564 0.1951  261  PHE A CD2   
1252 C  CE1   . PHE A 158 ? 1.2516 1.2749 1.8458 -0.0088 -0.2028 0.2152  261  PHE A CE1   
1253 C  CE2   . PHE A 158 ? 1.1817 1.2344 1.7250 0.0053  -0.1634 0.1996  261  PHE A CE2   
1254 C  CZ    . PHE A 158 ? 0.9606 0.9918 1.5070 -0.0017 -0.1853 0.2086  261  PHE A CZ    
1255 N  N     . LEU A 159 ? 0.9696 1.0308 1.7082 -0.0079 -0.1659 0.1916  262  LEU A N     
1256 C  CA    . LEU A 159 ? 1.1180 1.1807 1.9066 -0.0076 -0.1529 0.1875  262  LEU A CA    
1257 C  C     . LEU A 159 ? 1.3631 1.4387 2.1356 -0.0053 -0.1199 0.1704  262  LEU A C     
1258 O  O     . LEU A 159 ? 1.1488 1.2261 1.9645 -0.0036 -0.0989 0.1644  262  LEU A O     
1259 C  CB    . LEU A 159 ? 1.2552 1.3066 2.0503 -0.0131 -0.1728 0.1942  262  LEU A CB    
1260 C  CG    . LEU A 159 ? 1.2175 1.2550 2.0418 -0.0177 -0.2062 0.2129  262  LEU A CG    
1261 C  CD1   . LEU A 159 ? 1.2970 1.3229 2.1182 -0.0238 -0.2253 0.2196  262  LEU A CD1   
1262 C  CD2   . LEU A 159 ? 0.9388 0.9779 1.8386 -0.0146 -0.2035 0.2205  262  LEU A CD2   
1263 N  N     . GLU A 160 ? 1.1711 1.2554 1.8829 -0.0060 -0.1144 0.1630  263  GLU A N     
1264 C  CA    . GLU A 160 ? 1.1561 1.2534 1.8465 -0.0067 -0.0864 0.1479  263  GLU A CA    
1265 C  C     . GLU A 160 ? 1.1649 1.2736 1.8438 -0.0023 -0.0677 0.1436  263  GLU A C     
1266 O  O     . GLU A 160 ? 1.1414 1.2495 1.8123 0.0018  -0.0774 0.1517  263  GLU A O     
1267 C  CB    . GLU A 160 ? 1.3813 1.4852 2.0156 -0.0107 -0.0908 0.1435  263  GLU A CB    
1268 C  CG    . GLU A 160 ? 1.5030 1.6197 2.1153 -0.0151 -0.0656 0.1284  263  GLU A CG    
1269 C  CD    . GLU A 160 ? 1.5290 1.6370 2.1839 -0.0191 -0.0496 0.1202  263  GLU A CD    
1270 O  OE1   . GLU A 160 ? 1.2421 1.3479 1.9335 -0.0168 -0.0315 0.1165  263  GLU A OE1   
1271 O  OE2   . GLU A 160 ? 1.6647 1.7666 2.3170 -0.0245 -0.0536 0.1173  263  GLU A OE2   
1272 N  N     . LYS A 161 ? 1.1047 1.2220 1.7810 -0.0043 -0.0399 0.1307  264  LYS A N     
1273 C  CA    . LYS A 161 ? 0.9325 1.0597 1.5977 -0.0017 -0.0193 0.1261  264  LYS A CA    
1274 C  C     . LYS A 161 ? 1.0108 1.1539 1.6138 -0.0012 -0.0189 0.1256  264  LYS A C     
1275 O  O     . LYS A 161 ? 1.2295 1.3842 1.8109 -0.0030 0.0019  0.1182  264  LYS A O     
1276 C  CB    . LYS A 161 ? 1.5174 1.6440 2.2047 -0.0063 0.0110  0.1125  264  LYS A CB    
1277 C  CG    . LYS A 161 ? 1.1487 1.2779 1.8106 -0.0149 0.0208  0.1008  264  LYS A CG    
1278 C  CD    . LYS A 161 ? 1.5299 1.6540 2.2110 -0.0211 0.0536  0.0861  264  LYS A CD    
1279 C  CE    . LYS A 161 ? 1.6853 1.8100 2.3381 -0.0319 0.0637  0.0735  264  LYS A CE    
1280 N  NZ    . LYS A 161 ? 1.4246 1.5401 2.0916 -0.0400 0.0981  0.0576  264  LYS A NZ    
1281 N  N     . TYR A 162 ? 1.2483 1.3918 1.8222 0.0009  -0.0410 0.1340  265  TYR A N     
1282 C  CA    . TYR A 162 ? 1.1763 1.3352 1.6977 0.0031  -0.0407 0.1360  265  TYR A CA    
1283 C  C     . TYR A 162 ? 1.1491 1.3089 1.6676 0.0107  -0.0380 0.1432  265  TYR A C     
1284 O  O     . TYR A 162 ? 1.3371 1.4831 1.8892 0.0136  -0.0448 0.1487  265  TYR A O     
1285 C  CB    . TYR A 162 ? 1.1796 1.3360 1.6726 0.0028  -0.0622 0.1422  265  TYR A CB    
1286 C  CG    . TYR A 162 ? 1.6525 1.8110 2.1375 -0.0049 -0.0637 0.1353  265  TYR A CG    
1287 C  CD1   . TYR A 162 ? 1.7174 1.8860 2.2007 -0.0115 -0.0439 0.1233  265  TYR A CD1   
1288 C  CD2   . TYR A 162 ? 1.5809 1.7290 2.0573 -0.0071 -0.0841 0.1404  265  TYR A CD2   
1289 C  CE1   . TYR A 162 ? 1.8095 1.9784 2.2846 -0.0196 -0.0443 0.1164  265  TYR A CE1   
1290 C  CE2   . TYR A 162 ? 1.3592 1.5081 1.8281 -0.0145 -0.0849 0.1343  265  TYR A CE2   
1291 C  CZ    . TYR A 162 ? 1.6387 1.7982 2.1080 -0.0205 -0.0649 0.1222  265  TYR A CZ    
1292 O  OH    . TYR A 162 ? 1.7724 1.9313 2.2335 -0.0288 -0.0649 0.1156  265  TYR A OH    
1293 N  N     . PRO A 163 ? 1.2919 1.4681 1.7723 0.0134  -0.0284 0.1440  266  PRO A N     
1294 C  CA    . PRO A 163 ? 1.3605 1.5362 1.8351 0.0212  -0.0263 0.1521  266  PRO A CA    
1295 C  C     . PRO A 163 ? 1.1462 1.3062 1.6197 0.0257  -0.0475 0.1623  266  PRO A C     
1296 O  O     . PRO A 163 ? 1.1662 1.3218 1.6235 0.0238  -0.0631 0.1646  266  PRO A O     
1297 C  CB    . PRO A 163 ? 1.0720 1.2698 1.5020 0.0229  -0.0163 0.1535  266  PRO A CB    
1298 C  CG    . PRO A 163 ? 1.0832 1.2935 1.5053 0.0134  -0.0058 0.1427  266  PRO A CG    
1299 C  CD    . PRO A 163 ? 1.3908 1.5875 1.8350 0.0085  -0.0177 0.1381  266  PRO A CD    
1300 N  N     . LEU A 164 ? 1.0168 1.1665 1.5060 0.0302  -0.0473 0.1681  267  LEU A N     
1301 C  CA    . LEU A 164 ? 1.0694 1.2002 1.5585 0.0317  -0.0668 0.1769  267  LEU A CA    
1302 C  C     . LEU A 164 ? 1.0812 1.2136 1.5230 0.0355  -0.0732 0.1823  267  LEU A C     
1303 O  O     . LEU A 164 ? 1.3783 1.4940 1.8102 0.0333  -0.0908 0.1868  267  LEU A O     
1304 C  CB    . LEU A 164 ? 1.2061 1.3268 1.7174 0.0350  -0.0627 0.1814  267  LEU A CB    
1305 C  CG    . LEU A 164 ? 1.1095 1.2073 1.6274 0.0330  -0.0832 0.1895  267  LEU A CG    
1306 C  CD1   . LEU A 164 ? 0.8057 0.8923 1.3598 0.0250  -0.1017 0.1901  267  LEU A CD1   
1307 C  CD2   . LEU A 164 ? 0.8832 0.9735 1.4163 0.0361  -0.0760 0.1936  267  LEU A CD2   
1308 N  N     . SER A 165 ? 1.3423 1.4945 1.7550 0.0406  -0.0588 0.1825  268  SER A N     
1309 C  CA    . SER A 165 ? 1.2065 1.3624 1.5794 0.0455  -0.0622 0.1889  268  SER A CA    
1310 C  C     . SER A 165 ? 1.2727 1.4312 1.6300 0.0403  -0.0732 0.1862  268  SER A C     
1311 O  O     . SER A 165 ? 1.0286 1.1806 1.3594 0.0425  -0.0805 0.1913  268  SER A O     
1312 C  CB    . SER A 165 ? 1.0335 1.2131 1.3847 0.0522  -0.0450 0.1923  268  SER A CB    
1313 O  OG    . SER A 165 ? 1.2348 1.4096 1.5963 0.0575  -0.0347 0.1961  268  SER A OG    
1314 N  N     . GLN A 166 ? 1.0906 1.2568 1.4636 0.0331  -0.0728 0.1778  269  GLN A N     
1315 C  CA    . GLN A 166 ? 1.0733 1.2422 1.4315 0.0274  -0.0821 0.1749  269  GLN A CA    
1316 C  C     . GLN A 166 ? 1.1078 1.2506 1.4676 0.0239  -0.1023 0.1786  269  GLN A C     
1317 O  O     . GLN A 166 ? 1.4063 1.5469 1.7405 0.0217  -0.1103 0.1800  269  GLN A O     
1318 C  CB    . GLN A 166 ? 1.1140 1.2925 1.4904 0.0196  -0.0759 0.1647  269  GLN A CB    
1319 C  CG    . GLN A 166 ? 1.2535 1.4580 1.6170 0.0188  -0.0572 0.1599  269  GLN A CG    
1320 C  CD    . GLN A 166 ? 1.3909 1.6060 1.7510 0.0089  -0.0537 0.1502  269  GLN A CD    
1321 O  OE1   . GLN A 166 ? 1.2988 1.5215 1.6681 0.0033  -0.0391 0.1416  269  GLN A OE1   
1322 N  NE2   . GLN A 166 ? 1.1273 1.3408 1.4720 0.0058  -0.0659 0.1509  269  GLN A NE2   
1323 N  N     . TYR A 167 ? 1.0414 1.1642 1.4303 0.0221  -0.1111 0.1808  270  TYR A N     
1324 C  CA    . TYR A 167 ? 1.2541 1.3514 1.6438 0.0162  -0.1327 0.1855  270  TYR A CA    
1325 C  C     . TYR A 167 ? 1.0969 1.1817 1.4471 0.0188  -0.1370 0.1916  270  TYR A C     
1326 O  O     . TYR A 167 ? 1.1451 1.2304 1.4857 0.0259  -0.1271 0.1950  270  TYR A O     
1327 C  CB    . TYR A 167 ? 0.9304 1.0121 1.3621 0.0131  -0.1415 0.1884  270  TYR A CB    
1328 C  CG    . TYR A 167 ? 1.0545 1.1418 1.5295 0.0093  -0.1401 0.1835  270  TYR A CG    
1329 C  CD1   . TYR A 167 ? 0.9782 1.0818 1.4762 0.0129  -0.1194 0.1769  270  TYR A CD1   
1330 C  CD2   . TYR A 167 ? 1.1092 1.1838 1.6014 0.0017  -0.1582 0.1858  270  TYR A CD2   
1331 C  CE1   . TYR A 167 ? 0.8690 0.9748 1.4071 0.0093  -0.1146 0.1716  270  TYR A CE1   
1332 C  CE2   . TYR A 167 ? 0.9345 1.0128 1.4697 -0.0008 -0.1550 0.1820  270  TYR A CE2   
1333 C  CZ    . TYR A 167 ? 1.0605 1.1538 1.6189 0.0032  -0.1320 0.1744  270  TYR A CZ    
1334 O  OH    . TYR A 167 ? 0.9740 1.0680 1.5756 0.0007  -0.1254 0.1699  270  TYR A OH    
1335 N  N     . LYS A 168 ? 1.4576 1.5291 1.7843 0.0128  -0.1502 0.1930  271  LYS A N     
1336 C  CA    . LYS A 168 ? 1.4895 1.5475 1.7755 0.0146  -0.1508 0.1974  271  LYS A CA    
1337 C  C     . LYS A 168 ? 1.5968 1.6287 1.8813 0.0134  -0.1570 0.2027  271  LYS A C     
1338 O  O     . LYS A 168 ? 1.4660 1.4912 1.7236 0.0191  -0.1475 0.2057  271  LYS A O     
1339 C  CB    . LYS A 168 ? 1.6250 1.6701 1.8868 0.0062  -0.1637 0.1972  271  LYS A CB    
1340 C  CG    . LYS A 168 ? 1.6107 1.6809 1.8611 0.0079  -0.1546 0.1926  271  LYS A CG    
1341 C  CD    . LYS A 168 ? 1.8828 1.9377 2.1064 -0.0006 -0.1660 0.1929  271  LYS A CD    
1342 C  CE    . LYS A 168 ? 1.8550 1.9357 2.0633 0.0015  -0.1551 0.1892  271  LYS A CE    
1343 N  NZ    . LYS A 168 ? 1.8437 1.9486 2.0796 0.0004  -0.1503 0.1829  271  LYS A NZ    
1344 N  N     . TYR A 169 ? 1.5731 1.5900 1.8877 0.0057  -0.1724 0.2045  272  TYR A N     
1345 C  CA    . TYR A 169 ? 1.4178 1.4105 1.7323 0.0022  -0.1796 0.2095  272  TYR A CA    
1346 C  C     . TYR A 169 ? 1.5054 1.5095 1.8282 0.0131  -0.1602 0.2096  272  TYR A C     
1347 O  O     . TYR A 169 ? 1.6850 1.6737 1.9836 0.0156  -0.1545 0.2126  272  TYR A O     
1348 C  CB    . TYR A 169 ? 1.6126 1.5924 1.9648 -0.0086 -0.2011 0.2131  272  TYR A CB    
1349 C  CG    . TYR A 169 ? 1.5569 1.5167 1.9172 -0.0131 -0.2081 0.2182  272  TYR A CG    
1350 C  CD1   . TYR A 169 ? 1.6637 1.5921 1.9873 -0.0229 -0.2204 0.2220  272  TYR A CD1   
1351 C  CD2   . TYR A 169 ? 1.3438 1.3146 1.7468 -0.0089 -0.2014 0.2187  272  TYR A CD2   
1352 C  CE1   . TYR A 169 ? 1.5451 1.4540 1.8738 -0.0291 -0.2269 0.2261  272  TYR A CE1   
1353 C  CE2   . TYR A 169 ? 1.4353 1.3885 1.8466 -0.0140 -0.2078 0.2234  272  TYR A CE2   
1354 C  CZ    . TYR A 169 ? 1.6073 1.5297 1.9812 -0.0244 -0.2211 0.2271  272  TYR A CZ    
1355 O  OH    . TYR A 169 ? 1.5837 1.4874 1.9638 -0.0315 -0.2277 0.2313  272  TYR A OH    
1356 N  N     . ILE A 170 ? 1.3272 1.3563 1.6826 0.0190  -0.1485 0.2063  273  ILE A N     
1357 C  CA    . ILE A 170 ? 1.1728 1.2136 1.5344 0.0287  -0.1293 0.2068  273  ILE A CA    
1358 C  C     . ILE A 170 ? 1.3034 1.3561 1.6272 0.0387  -0.1130 0.2082  273  ILE A C     
1359 O  O     . ILE A 170 ? 1.2316 1.2797 1.5434 0.0458  -0.1017 0.2124  273  ILE A O     
1360 C  CB    . ILE A 170 ? 1.1956 1.2586 1.5969 0.0309  -0.1192 0.2021  273  ILE A CB    
1361 C  CG1   . ILE A 170 ? 1.3215 1.3741 1.7662 0.0219  -0.1350 0.2020  273  ILE A CG1   
1362 C  CG2   . ILE A 170 ? 1.2029 1.2742 1.6106 0.0391  -0.1005 0.2034  273  ILE A CG2   
1363 C  CD1   . ILE A 170 ? 1.1293 1.1608 1.5909 0.0175  -0.1454 0.2080  273  ILE A CD1   
1364 N  N     . ARG A 171 ? 1.4731 1.5418 1.7800 0.0394  -0.1115 0.2057  274  ARG A N     
1365 C  CA    . ARG A 171 ? 1.1917 1.2749 1.4672 0.0486  -0.0974 0.2090  274  ARG A CA    
1366 C  C     . ARG A 171 ? 1.2283 1.2851 1.4724 0.0498  -0.0986 0.2140  274  ARG A C     
1367 O  O     . ARG A 171 ? 1.2091 1.2694 1.4374 0.0600  -0.0836 0.2195  274  ARG A O     
1368 C  CB    . ARG A 171 ? 1.2141 1.3186 1.4798 0.0466  -0.0979 0.2053  274  ARG A CB    
1369 C  CG    . ARG A 171 ? 1.1166 1.2417 1.3558 0.0556  -0.0845 0.2102  274  ARG A CG    
1370 C  CD    . ARG A 171 ? 0.9934 1.1479 1.2418 0.0633  -0.0688 0.2126  274  ARG A CD    
1371 N  NE    . ARG A 171 ? 1.0002 1.1764 1.2647 0.0570  -0.0685 0.2051  274  ARG A NE    
1372 C  CZ    . ARG A 171 ? 1.1896 1.3914 1.4429 0.0549  -0.0657 0.2036  274  ARG A CZ    
1373 N  NH1   . ARG A 171 ? 1.4535 1.6656 1.6831 0.0596  -0.0635 0.2100  274  ARG A NH1   
1374 N  NH2   . ARG A 171 ? 1.0279 1.2444 1.2948 0.0474  -0.0641 0.1954  274  ARG A NH2   
1375 N  N     . SER A 172 ? 1.2858 1.3146 1.5200 0.0390  -0.1155 0.2128  275  SER A N     
1376 C  CA    . SER A 172 ? 1.2004 1.1987 1.4005 0.0373  -0.1155 0.2160  275  SER A CA    
1377 C  C     . SER A 172 ? 1.5029 1.4812 1.7064 0.0390  -0.1109 0.2191  275  SER A C     
1378 O  O     . SER A 172 ? 1.4757 1.4359 1.6517 0.0432  -0.1000 0.2223  275  SER A O     
1379 C  CB    . SER A 172 ? 1.3323 1.3037 1.5175 0.0224  -0.1361 0.2139  275  SER A CB    
1380 O  OG    . SER A 172 ? 1.9775 1.9378 2.1914 0.0119  -0.1547 0.2135  275  SER A OG    
1381 N  N     . CYS A 173 ? 1.7176 1.6978 1.9558 0.0355  -0.1177 0.2183  276  CYS A N     
1382 C  CA    . CYS A 173 ? 1.5539 1.5174 1.7981 0.0366  -0.1124 0.2212  276  CYS A CA    
1383 C  C     . CYS A 173 ? 1.4282 1.4101 1.6696 0.0524  -0.0882 0.2248  276  CYS A C     
1384 O  O     . CYS A 173 ? 1.5883 1.5518 1.8185 0.0560  -0.0787 0.2284  276  CYS A O     
1385 C  CB    . CYS A 173 ? 1.5197 1.4837 1.8066 0.0290  -0.1249 0.2201  276  CYS A CB    
1386 S  SG    . CYS A 173 ? 1.4350 1.3724 1.7286 0.0092  -0.1565 0.2203  276  CYS A SG    
1387 N  N     . ILE A 174 ? 1.1425 1.1595 1.3929 0.0610  -0.0784 0.2246  277  ILE A N     
1388 C  CA    . ILE A 174 ? 1.1021 1.1388 1.3474 0.0752  -0.0574 0.2304  277  ILE A CA    
1389 C  C     . ILE A 174 ? 1.2780 1.3068 1.4891 0.0829  -0.0471 0.2361  277  ILE A C     
1390 O  O     . ILE A 174 ? 1.6614 1.6845 1.8637 0.0927  -0.0318 0.2430  277  ILE A O     
1391 C  CB    . ILE A 174 ? 1.3283 1.4042 1.5892 0.0790  -0.0516 0.2288  277  ILE A CB    
1392 C  CG1   . ILE A 174 ? 1.2788 1.3590 1.5755 0.0717  -0.0575 0.2225  277  ILE A CG1   
1393 C  CG2   . ILE A 174 ? 1.0635 1.1610 1.3171 0.0922  -0.0322 0.2371  277  ILE A CG2   
1394 C  CD1   . ILE A 174 ? 0.9558 1.0691 1.2648 0.0724  -0.0507 0.2187  277  ILE A CD1   
1395 N  N     . MET A 175 ? 1.2890 1.3163 1.4816 0.0788  -0.0540 0.2339  278  MET A N     
1396 C  CA    . MET A 175 ? 1.2429 1.2610 1.4050 0.0856  -0.0427 0.2389  278  MET A CA    
1397 C  C     . MET A 175 ? 1.3817 1.3560 1.5239 0.0823  -0.0398 0.2394  278  MET A C     
1398 O  O     . MET A 175 ? 1.6315 1.5981 1.7626 0.0931  -0.0216 0.2460  278  MET A O     
1399 C  CB    . MET A 175 ? 1.6139 1.6358 1.7610 0.0793  -0.0515 0.2350  278  MET A CB    
1400 C  CG    . MET A 175 ? 1.3665 1.4269 1.5314 0.0785  -0.0567 0.2324  278  MET A CG    
1401 S  SD    . MET A 175 ? 1.6049 1.7112 1.7742 0.0939  -0.0382 0.2416  278  MET A SD    
1402 C  CE    . MET A 175 ? 1.4836 1.6225 1.6634 0.0855  -0.0488 0.2346  278  MET A CE    
1403 N  N     . LEU A 176 ? 1.4488 1.3928 1.5858 0.0664  -0.0578 0.2330  279  LEU A N     
1404 C  CA    . LEU A 176 ? 1.8055 1.7044 1.9181 0.0589  -0.0572 0.2323  279  LEU A CA    
1405 C  C     . LEU A 176 ? 1.7031 1.5926 1.8313 0.0615  -0.0509 0.2348  279  LEU A C     
1406 O  O     . LEU A 176 ? 1.5307 1.3843 1.6370 0.0580  -0.0442 0.2351  279  LEU A O     
1407 C  CB    . LEU A 176 ? 1.6233 1.4943 1.7252 0.0385  -0.0816 0.2263  279  LEU A CB    
1408 C  CG    . LEU A 176 ? 1.5723 1.4299 1.6415 0.0312  -0.0864 0.2235  279  LEU A CG    
1409 C  CD1   . LEU A 176 ? 1.5911 1.4880 1.6742 0.0375  -0.0878 0.2232  279  LEU A CD1   
1410 C  CD2   . LEU A 176 ? 1.7513 1.5739 1.8063 0.0092  -0.1111 0.2196  279  LEU A CD2   
1411 N  N     . GLY A 177 ? 1.4386 1.3573 1.6021 0.0667  -0.0513 0.2360  280  GLY A N     
1412 C  CA    . GLY A 177 ? 1.3264 1.2366 1.5070 0.0679  -0.0458 0.2380  280  GLY A CA    
1413 C  C     . GLY A 177 ? 1.3469 1.2264 1.5334 0.0500  -0.0652 0.2336  280  GLY A C     
1414 O  O     . GLY A 177 ? 1.3257 1.1707 1.4938 0.0443  -0.0621 0.2339  280  GLY A O     
1415 N  N     . ARG A 178 ? 1.5991 1.4907 1.8120 0.0402  -0.0852 0.2301  281  ARG A N     
1416 C  CA    . ARG A 178 ? 1.5413 1.4088 1.7654 0.0222  -0.1077 0.2282  281  ARG A CA    
1417 C  C     . ARG A 178 ? 1.5853 1.4771 1.8609 0.0210  -0.1160 0.2279  281  ARG A C     
1418 O  O     . ARG A 178 ? 1.4586 1.3836 1.7553 0.0315  -0.1063 0.2271  281  ARG A O     
1419 C  CB    . ARG A 178 ? 1.4293 1.2793 1.6301 0.0083  -0.1277 0.2259  281  ARG A CB    
1420 C  CG    . ARG A 178 ? 1.9486 1.7594 2.1363 -0.0122 -0.1477 0.2261  281  ARG A CG    
1421 C  CD    . ARG A 178 ? 2.2292 2.0167 2.3778 -0.0249 -0.1613 0.2243  281  ARG A CD    
1422 N  NE    . ARG A 178 ? 1.9963 1.7785 2.1046 -0.0144 -0.1396 0.2224  281  ARG A NE    
1423 C  CZ    . ARG A 178 ? 2.2872 2.0373 2.3576 -0.0149 -0.1240 0.2216  281  ARG A CZ    
1424 N  NH1   . ARG A 178 ? 2.5135 2.2319 2.5758 -0.0266 -0.1279 0.2215  281  ARG A NH1   
1425 N  NH2   . ARG A 178 ? 2.2011 1.9506 2.2424 -0.0036 -0.1030 0.2211  281  ARG A NH2   
1426 N  N     . MET A 179 ? 1.4391 1.3134 1.7351 0.0069  -0.1333 0.2288  282  MET A N     
1427 C  CA    . MET A 179 ? 1.4410 1.3353 1.7911 0.0051  -0.1402 0.2292  282  MET A CA    
1428 C  C     . MET A 179 ? 1.6812 1.5892 2.0528 -0.0012 -0.1590 0.2282  282  MET A C     
1429 O  O     . MET A 179 ? 1.3332 1.2212 1.6944 -0.0155 -0.1818 0.2301  282  MET A O     
1430 C  CB    . MET A 179 ? 1.7677 1.6401 2.1362 -0.0077 -0.1516 0.2323  282  MET A CB    
1431 C  CG    . MET A 179 ? 1.6533 1.5169 2.0155 -0.0008 -0.1308 0.2332  282  MET A CG    
1432 S  SD    . MET A 179 ? 1.6597 1.5588 2.0665 0.0146  -0.1086 0.2329  282  MET A SD    
1433 C  CE    . MET A 179 ? 2.0738 1.9903 2.4432 0.0341  -0.0831 0.2325  282  MET A CE    
1434 N  N     . PRO A 180 ? 1.5917 1.5314 1.9912 0.0081  -0.1500 0.2255  283  PRO A N     
1435 C  CA    . PRO A 180 ? 1.3870 1.3379 1.8122 0.0021  -0.1664 0.2246  283  PRO A CA    
1436 C  C     . PRO A 180 ? 1.3285 1.2756 1.8043 -0.0084 -0.1840 0.2287  283  PRO A C     
1437 O  O     . PRO A 180 ? 1.4092 1.3742 1.9294 -0.0035 -0.1739 0.2278  283  PRO A O     
1438 C  CB    . PRO A 180 ? 1.2472 1.2307 1.6851 0.0148  -0.1467 0.2195  283  PRO A CB    
1439 C  CG    . PRO A 180 ? 1.2859 1.2748 1.6925 0.0269  -0.1236 0.2192  283  PRO A CG    
1440 C  CD    . PRO A 180 ? 1.3980 1.3629 1.7999 0.0236  -0.1238 0.2232  283  PRO A CD    
1441 N  N     . ASN A 181 ? 1.2775 1.2013 1.7476 -0.0237 -0.2101 0.2341  284  ASN A N     
1442 C  CA    . ASN A 181 ? 1.2880 1.2090 1.8081 -0.0352 -0.2310 0.2409  284  ASN A CA    
1443 C  C     . ASN A 181 ? 1.2922 1.2286 1.8474 -0.0367 -0.2435 0.2426  284  ASN A C     
1444 O  O     . ASN A 181 ? 1.2944 1.2226 1.8227 -0.0423 -0.2575 0.2435  284  ASN A O     
1445 C  CB    . ASN A 181 ? 1.4092 1.2975 1.9048 -0.0534 -0.2553 0.2473  284  ASN A CB    
1446 C  CG    . ASN A 181 ? 1.6528 1.5220 2.1151 -0.0530 -0.2416 0.2452  284  ASN A CG    
1447 O  OD1   . ASN A 181 ? 1.6733 1.5415 2.1645 -0.0554 -0.2394 0.2477  284  ASN A OD1   
1448 N  ND2   . ASN A 181 ? 1.8058 1.6588 2.2085 -0.0499 -0.2309 0.2407  284  ASN A ND2   
1449 N  N     . LEU A 182 ? 1.2781 1.2353 1.8933 -0.0317 -0.2367 0.2431  285  LEU A N     
1450 C  CA    . LEU A 182 ? 1.2673 1.2395 1.9224 -0.0312 -0.2432 0.2441  285  LEU A CA    
1451 C  C     . LEU A 182 ? 1.4180 1.3923 2.1406 -0.0389 -0.2598 0.2541  285  LEU A C     
1452 O  O     . LEU A 182 ? 1.4390 1.4212 2.1985 -0.0355 -0.2475 0.2542  285  LEU A O     
1453 C  CB    . LEU A 182 ? 0.8531 0.8498 1.5178 -0.0167 -0.2135 0.2338  285  LEU A CB    
1454 C  CG    . LEU A 182 ? 0.8508 0.8514 1.4556 -0.0080 -0.1950 0.2254  285  LEU A CG    
1455 C  CD1   . LEU A 182 ? 0.8300 0.8555 1.4470 0.0030  -0.1686 0.2163  285  LEU A CD1   
1456 C  CD2   . LEU A 182 ? 0.8967 0.8853 1.4579 -0.0137 -0.2112 0.2264  285  LEU A CD2   
1457 N  N     . MET A 183 ? 1.3334 1.3013 2.0738 -0.0494 -0.2877 0.2636  286  MET A N     
1458 C  CA    . MET A 183 ? 1.3300 1.3025 2.1403 -0.0568 -0.3065 0.2761  286  MET A CA    
1459 C  C     . MET A 183 ? 1.2325 1.2274 2.1026 -0.0462 -0.2907 0.2737  286  MET A C     
1460 O  O     . MET A 183 ? 1.3828 1.3833 2.2376 -0.0403 -0.2820 0.2671  286  MET A O     
1461 C  CB    . MET A 183 ? 1.4626 1.4175 2.2651 -0.0740 -0.3455 0.2898  286  MET A CB    
1462 C  CG    . MET A 183 ? 1.3635 1.3252 2.2417 -0.0825 -0.3691 0.3063  286  MET A CG    
1463 S  SD    . MET A 183 ? 1.9643 1.9032 2.8252 -0.1063 -0.4185 0.3248  286  MET A SD    
1464 C  CE    . MET A 183 ? 1.7916 1.7241 2.6024 -0.1026 -0.4180 0.3187  286  MET A CE    
1465 N  N     . LEU A 184 ? 1.1705 1.1771 2.1088 -0.0446 -0.2855 0.2787  287  LEU A N     
1466 C  CA    . LEU A 184 ? 1.1423 1.1675 2.1422 -0.0347 -0.2657 0.2757  287  LEU A CA    
1467 C  C     . LEU A 184 ? 1.1044 1.1313 2.1645 -0.0415 -0.2920 0.2916  287  LEU A C     
1468 O  O     . LEU A 184 ? 1.3502 1.3723 2.4397 -0.0528 -0.3199 0.3072  287  LEU A O     
1469 C  CB    . LEU A 184 ? 1.0795 1.1161 2.1214 -0.0282 -0.2403 0.2716  287  LEU A CB    
1470 C  CG    . LEU A 184 ? 0.8252 0.8780 1.9052 -0.0160 -0.2049 0.2607  287  LEU A CG    
1471 C  CD1   . LEU A 184 ? 1.3192 1.3777 2.4046 -0.0103 -0.1764 0.2528  287  LEU A CD1   
1472 C  CD2   . LEU A 184 ? 1.3269 1.3878 2.4907 -0.0163 -0.2109 0.2707  287  LEU A CD2   
1473 N  N     . MET A 185 ? 1.4020 1.4355 2.4804 -0.0352 -0.2834 0.2884  288  MET A N     
1474 C  CA    . MET A 185 ? 1.2385 1.2744 2.3784 -0.0390 -0.3041 0.3036  288  MET A CA    
1475 C  C     . MET A 185 ? 1.4828 1.5333 2.6855 -0.0269 -0.2732 0.2973  288  MET A C     
1476 O  O     . MET A 185 ? 1.5215 1.5788 2.7118 -0.0175 -0.2375 0.2803  288  MET A O     
1477 C  CB    . MET A 185 ? 1.3853 1.4088 2.4815 -0.0454 -0.3270 0.3076  288  MET A CB    
1478 C  CG    . MET A 185 ? 1.6962 1.7016 2.7452 -0.0611 -0.3636 0.3189  288  MET A CG    
1479 S  SD    . MET A 185 ? 1.5073 1.4975 2.5126 -0.0691 -0.3887 0.3246  288  MET A SD    
1480 C  CE    . MET A 185 ? 1.9535 1.9206 2.9148 -0.0908 -0.4312 0.3395  288  MET A CE    
1481 N  N     . ALA A 186 ? 1.4302 1.4842 2.7002 -0.0278 -0.2868 0.3116  289  ALA A N     
1482 C  CA    . ALA A 186 ? 1.0423 1.1056 2.3727 -0.0172 -0.2582 0.3064  289  ALA A CA    
1483 C  C     . ALA A 186 ? 1.3644 1.4209 2.6728 -0.0159 -0.2598 0.3033  289  ALA A C     
1484 O  O     . ALA A 186 ? 1.5009 1.5468 2.7637 -0.0241 -0.2889 0.3102  289  ALA A O     
1485 C  CB    . ALA A 186 ? 0.8565 0.9294 2.2890 -0.0172 -0.2678 0.3256  289  ALA A CB    
1486 N  N     . LYS A 187 ? 1.4645 1.5253 2.8041 -0.0066 -0.2266 0.2919  290  LYS A N     
1487 C  CA    . LYS A 187 ? 1.0921 1.1457 2.4151 -0.0055 -0.2246 0.2878  290  LYS A CA    
1488 C  C     . LYS A 187 ? 1.2725 1.3214 2.6434 -0.0105 -0.2593 0.3116  290  LYS A C     
1489 O  O     . LYS A 187 ? 1.5940 1.6328 2.9272 -0.0152 -0.2771 0.3146  290  LYS A O     
1490 C  CB    . LYS A 187 ? 1.1921 1.2488 2.5427 0.0038  -0.1801 0.2707  290  LYS A CB    
1491 C  CG    . LYS A 187 ? 1.2269 1.2863 2.5126 0.0064  -0.1477 0.2463  290  LYS A CG    
1492 C  CD    . LYS A 187 ? 1.2736 1.3326 2.5818 0.0122  -0.1051 0.2292  290  LYS A CD    
1493 C  CE    . LYS A 187 ? 1.5192 1.5813 2.7565 0.0123  -0.0764 0.2065  290  LYS A CE    
1494 N  NZ    . LYS A 187 ? 1.7669 1.8267 2.9225 0.0076  -0.0919 0.2014  290  LYS A NZ    
1495 N  N     . GLU A 188 ? 1.4041 1.4606 2.8590 -0.0100 -0.2702 0.3300  291  GLU A N     
1496 C  CA    . GLU A 188 ? 1.3358 1.3899 2.8430 -0.0149 -0.3051 0.3560  291  GLU A CA    
1497 C  C     . GLU A 188 ? 1.3224 1.3678 2.7779 -0.0297 -0.3520 0.3709  291  GLU A C     
1498 O  O     . GLU A 188 ? 1.2918 1.3294 2.7528 -0.0363 -0.3822 0.3880  291  GLU A O     
1499 C  CB    . GLU A 188 ? 1.4489 1.5163 3.0644 -0.0106 -0.3040 0.3734  291  GLU A CB    
1500 C  CG    . GLU A 188 ? 1.5311 1.6036 3.2047 0.0032  -0.2558 0.3598  291  GLU A CG    
1501 C  CD    . GLU A 188 ? 1.6387 1.7018 3.3274 0.0087  -0.2436 0.3578  291  GLU A CD    
1502 O  OE1   . GLU A 188 ? 1.7391 1.7955 3.4256 0.0030  -0.2775 0.3753  291  GLU A OE1   
1503 O  OE2   . GLU A 188 ? 2.0506 2.1111 3.7511 0.0176  -0.1994 0.3384  291  GLU A OE2   
1504 N  N     . SER A 189 ? 1.3551 1.3997 2.7588 -0.0358 -0.3577 0.3648  292  SER A N     
1505 C  CA    . SER A 189 ? 1.4749 1.5074 2.8247 -0.0516 -0.3993 0.3770  292  SER A CA    
1506 C  C     . SER A 189 ? 1.4825 1.4991 2.7523 -0.0558 -0.4067 0.3694  292  SER A C     
1507 O  O     . SER A 189 ? 1.4774 1.4807 2.7168 -0.0694 -0.4437 0.3840  292  SER A O     
1508 C  CB    . SER A 189 ? 1.8245 1.8568 3.1340 -0.0563 -0.3974 0.3692  292  SER A CB    
1509 O  OG    . SER A 189 ? 1.9368 1.9836 3.3205 -0.0539 -0.3923 0.3773  292  SER A OG    
1510 N  N     . LEU A 190 ? 1.3101 1.3272 2.5442 -0.0457 -0.3724 0.3471  293  LEU A N     
1511 C  CA    . LEU A 190 ? 1.2251 1.2294 2.3868 -0.0488 -0.3753 0.3385  293  LEU A CA    
1512 C  C     . LEU A 190 ? 1.3064 1.3085 2.5019 -0.0448 -0.3719 0.3424  293  LEU A C     
1513 O  O     . LEU A 190 ? 1.3995 1.3883 2.5607 -0.0526 -0.3944 0.3498  293  LEU A O     
1514 C  CB    . LEU A 190 ? 1.3366 1.3440 2.4328 -0.0420 -0.3420 0.3124  293  LEU A CB    
1515 C  CG    . LEU A 190 ? 1.4473 1.4446 2.4677 -0.0446 -0.3409 0.3017  293  LEU A CG    
1516 C  CD1   . LEU A 190 ? 1.4567 1.4371 2.4196 -0.0584 -0.3756 0.3120  293  LEU A CD1   
1517 C  CD2   . LEU A 190 ? 1.2543 1.2602 2.2269 -0.0364 -0.3053 0.2779  293  LEU A CD2   
1518 N  N     . TYR A 191 ? 1.2826 1.2951 2.5440 -0.0332 -0.3426 0.3375  294  TYR A N     
1519 C  CA    . TYR A 191 ? 1.0652 1.0731 2.3580 -0.0286 -0.3338 0.3389  294  TYR A CA    
1520 C  C     . TYR A 191 ? 1.2864 1.2889 2.6326 -0.0347 -0.3712 0.3681  294  TYR A C     
1521 O  O     . TYR A 191 ? 1.4427 1.4353 2.7906 -0.0352 -0.3765 0.3731  294  TYR A O     
1522 C  CB    . TYR A 191 ? 1.4279 1.4452 2.7792 -0.0157 -0.2906 0.3259  294  TYR A CB    
1523 C  CG    . TYR A 191 ? 1.0616 1.0836 2.3591 -0.0108 -0.2524 0.2973  294  TYR A CG    
1524 C  CD1   . TYR A 191 ? 1.0167 1.0344 2.2222 -0.0157 -0.2548 0.2841  294  TYR A CD1   
1525 C  CD2   . TYR A 191 ? 1.2410 1.2714 2.5803 -0.0020 -0.2138 0.2844  294  TYR A CD2   
1526 C  CE1   . TYR A 191 ? 1.1160 1.1402 2.2750 -0.0117 -0.2222 0.2607  294  TYR A CE1   
1527 C  CE2   . TYR A 191 ? 1.3944 1.4287 2.6822 0.0007  -0.1808 0.2599  294  TYR A CE2   
1528 C  CZ    . TYR A 191 ? 1.4346 1.4670 2.6333 -0.0041 -0.1864 0.2490  294  TYR A CZ    
1529 O  OH    . TYR A 191 ? 1.7568 1.7953 2.9067 -0.0019 -0.1558 0.2271  294  TYR A OH    
1530 N  N     . SER A 192 ? 1.4707 1.4794 2.8605 -0.0401 -0.3981 0.3886  295  SER A N     
1531 C  CA    . SER A 192 ? 1.5972 1.6034 3.0432 -0.0470 -0.4364 0.4196  295  SER A CA    
1532 C  C     . SER A 192 ? 1.7969 1.7856 3.1749 -0.0628 -0.4763 0.4310  295  SER A C     
1533 O  O     . SER A 192 ? 1.7117 1.6967 3.1269 -0.0711 -0.5124 0.4584  295  SER A O     
1534 C  CB    . SER A 192 ? 1.4889 1.5092 3.0026 -0.0499 -0.4540 0.4385  295  SER A CB    
1535 O  OG    . SER A 192 ? 1.8033 1.8389 3.3887 -0.0355 -0.4167 0.4303  295  SER A OG    
1536 N  N     . GLN A 193 ? 1.7169 1.6946 2.9983 -0.0675 -0.4706 0.4118  296  GLN A N     
1537 C  CA    . GLN A 193 ? 1.6461 1.6042 2.8563 -0.0828 -0.5033 0.4196  296  GLN A CA    
1538 C  C     . GLN A 193 ? 1.8423 1.7895 3.0090 -0.0796 -0.4882 0.4069  296  GLN A C     
1539 O  O     . GLN A 193 ? 2.0072 1.9373 3.1031 -0.0912 -0.5074 0.4078  296  GLN A O     
1540 C  CB    . GLN A 193 ? 1.7143 1.6653 2.8458 -0.0928 -0.5110 0.4098  296  GLN A CB    
1541 C  CG    . GLN A 193 ? 1.7193 1.6780 2.8851 -0.0992 -0.5286 0.4224  296  GLN A CG    
1542 C  CD    . GLN A 193 ? 2.0090 1.9630 3.2153 -0.1141 -0.5755 0.4547  296  GLN A CD    
1543 O  OE1   . GLN A 193 ? 2.2681 2.2058 3.4447 -0.1249 -0.6017 0.4669  296  GLN A OE1   
1544 N  NE2   . GLN A 193 ? 1.8329 1.8013 3.1076 -0.1156 -0.5870 0.4696  296  GLN A NE2   
1545 N  N     . LEU A 194 ? 1.6765 1.6318 2.8822 -0.0653 -0.4534 0.3947  297  LEU A N     
1546 C  CA    . LEU A 194 ? 1.7302 1.6760 2.8985 -0.0626 -0.4361 0.3812  297  LEU A CA    
1547 C  C     . LEU A 194 ? 1.7191 1.6645 2.9658 -0.0550 -0.4292 0.3925  297  LEU A C     
1548 O  O     . LEU A 194 ? 1.5125 1.4696 2.8226 -0.0426 -0.3989 0.3857  297  LEU A O     
1549 C  CB    . LEU A 194 ? 1.6421 1.5956 2.7647 -0.0543 -0.3944 0.3498  297  LEU A CB    
1550 C  CG    . LEU A 194 ? 1.4620 1.4136 2.4953 -0.0603 -0.3954 0.3357  297  LEU A CG    
1551 C  CD1   . LEU A 194 ? 1.5852 1.5454 2.6264 -0.0609 -0.4009 0.3382  297  LEU A CD1   
1552 C  CD2   . LEU A 194 ? 1.5006 1.4584 2.4893 -0.0532 -0.3577 0.3084  297  LEU A CD2   
1553 N  N     . PRO A 195 ? 2.0313 1.9621 3.2771 -0.0619 -0.4541 0.4096  298  PRO A N     
1554 C  CA    . PRO A 195 ? 2.2526 2.1807 3.5735 -0.0540 -0.4468 0.4215  298  PRO A CA    
1555 C  C     . PRO A 195 ? 2.2140 2.1372 3.5134 -0.0460 -0.4055 0.3959  298  PRO A C     
1556 O  O     . PRO A 195 ? 2.1065 2.0305 3.3341 -0.0472 -0.3855 0.3707  298  PRO A O     
1557 C  CB    . PRO A 195 ? 2.3289 2.2412 3.6409 -0.0668 -0.4918 0.4493  298  PRO A CB    
1558 C  CG    . PRO A 195 ? 2.2528 2.1534 3.4583 -0.0801 -0.5060 0.4385  298  PRO A CG    
1559 C  CD    . PRO A 195 ? 2.1247 2.0385 3.3009 -0.0782 -0.4914 0.4206  298  PRO A CD    
1560 N  N     . MET A 196 ? 1.9943 1.9121 3.3590 -0.0385 -0.3930 0.4035  299  MET A N     
1561 C  CA    . MET A 196 ? 2.1578 2.0677 3.5098 -0.0326 -0.3543 0.3811  299  MET A CA    
1562 C  C     . MET A 196 ? 2.2669 2.1572 3.5858 -0.0407 -0.3741 0.3909  299  MET A C     
1563 O  O     . MET A 196 ? 2.1222 2.0029 3.5000 -0.0385 -0.3853 0.4122  299  MET A O     
1564 C  CB    . MET A 196 ? 2.1497 2.0630 3.5943 -0.0191 -0.3211 0.3802  299  MET A CB    
1565 C  CG    . MET A 196 ? 2.1265 2.0576 3.6033 -0.0114 -0.2970 0.3688  299  MET A CG    
1566 S  SD    . MET A 196 ? 2.7621 2.6932 4.3472 0.0038  -0.2535 0.3666  299  MET A SD    
1567 C  CE    . MET A 196 ? 2.2298 2.1422 3.7680 0.0033  -0.2131 0.3378  299  MET A CE    
1568 N  N     . ASP A 197 ? 2.2551 2.1393 3.4806 -0.0500 -0.3778 0.3760  300  ASP A N     
1569 C  CA    . ASP A 197 ? 2.0560 1.9209 3.2395 -0.0591 -0.3952 0.3830  300  ASP A CA    
1570 C  C     . ASP A 197 ? 2.1174 1.9737 3.3100 -0.0536 -0.3588 0.3660  300  ASP A C     
1571 O  O     . ASP A 197 ? 2.0650 1.9256 3.2081 -0.0534 -0.3283 0.3377  300  ASP A O     
1572 C  CB    . ASP A 197 ? 2.0265 1.8881 3.1092 -0.0711 -0.4099 0.3730  300  ASP A CB    
1573 C  CG    . ASP A 197 ? 2.1908 2.0531 3.2581 -0.0802 -0.4494 0.3920  300  ASP A CG    
1574 O  OD1   . ASP A 197 ? 2.5895 2.4603 3.7235 -0.0766 -0.4631 0.4101  300  ASP A OD1   
1575 O  OD2   . ASP A 197 ? 2.0221 1.8758 3.0108 -0.0917 -0.4660 0.3890  300  ASP A OD2   
1576 N  N     . CYS A 198 ? 2.3428 2.1865 3.5989 -0.0498 -0.3622 0.3841  301  CYS A N     
1577 C  CA    . CYS A 198 ? 2.3778 2.2082 3.6408 -0.0464 -0.3294 0.3696  301  CYS A CA    
1578 C  C     . CYS A 198 ? 2.4465 2.2623 3.6270 -0.0584 -0.3391 0.3628  301  CYS A C     
1579 O  O     . CYS A 198 ? 2.4788 2.2863 3.6269 -0.0682 -0.3776 0.3819  301  CYS A O     
1580 C  CB    . CYS A 198 ? 2.2137 2.0329 3.5716 -0.0383 -0.3305 0.3931  301  CYS A CB    
1581 S  SG    . CYS A 198 ? 2.5742 2.3722 3.9480 -0.0342 -0.2873 0.3760  301  CYS A SG    
1582 N  N     . PHE A 199 ? 2.2263 2.0385 3.3714 -0.0591 -0.3036 0.3354  302  PHE A N     
1583 C  CA    . PHE A 199 ? 2.0685 1.8691 3.1361 -0.0705 -0.3080 0.3262  302  PHE A CA    
1584 C  C     . PHE A 199 ? 2.3316 2.1085 3.4197 -0.0746 -0.3298 0.3498  302  PHE A C     
1585 O  O     . PHE A 199 ? 2.1695 1.9335 3.3115 -0.0688 -0.3106 0.3521  302  PHE A O     
1586 C  CB    . PHE A 199 ? 1.8310 1.6339 2.8658 -0.0712 -0.2646 0.2931  302  PHE A CB    
1587 C  CG    . PHE A 199 ? 1.8894 1.6877 2.8384 -0.0834 -0.2676 0.2804  302  PHE A CG    
1588 C  CD1   . PHE A 199 ? 1.7676 1.5651 2.6622 -0.0918 -0.3020 0.2921  302  PHE A CD1   
1589 C  CD2   . PHE A 199 ? 1.8419 1.6357 2.7648 -0.0875 -0.2351 0.2568  302  PHE A CD2   
1590 C  CE1   . PHE A 199 ? 1.5466 1.3400 2.3658 -0.1027 -0.3026 0.2808  302  PHE A CE1   
1591 C  CE2   . PHE A 199 ? 1.7709 1.5626 2.6190 -0.0990 -0.2378 0.2461  302  PHE A CE2   
1592 C  CZ    . PHE A 199 ? 1.6613 1.4533 2.4593 -0.1058 -0.2710 0.2583  302  PHE A CZ    
1593 N  N     . THR A 200 ? 2.4409 2.2098 3.4851 -0.0853 -0.3688 0.3675  303  THR A N     
1594 C  CA    . THR A 200 ? 2.4797 2.2252 3.5345 -0.0913 -0.3944 0.3925  303  THR A CA    
1595 C  C     . THR A 200 ? 2.3445 2.0764 3.3202 -0.1026 -0.3876 0.3771  303  THR A C     
1596 O  O     . THR A 200 ? 2.2015 1.9327 3.1043 -0.1137 -0.4070 0.3756  303  THR A O     
1597 C  CB    . THR A 200 ? 2.4411 2.1842 3.4990 -0.0982 -0.4436 0.4242  303  THR A CB    
1598 O  OG1   . THR A 200 ? 2.4088 2.1680 3.5412 -0.0883 -0.4489 0.4372  303  THR A OG1   
1599 C  CG2   . THR A 200 ? 2.0654 1.7840 3.1387 -0.1048 -0.4711 0.4527  303  THR A CG2   
1600 N  N     . MET A 201 ? 2.2094 1.9295 3.2000 -0.1003 -0.3583 0.3653  304  MET A N     
1601 C  CA    . MET A 201 ? 2.2496 1.9568 3.1713 -0.1116 -0.3506 0.3513  304  MET A CA    
1602 C  C     . MET A 201 ? 2.3701 2.0530 3.2779 -0.1212 -0.3867 0.3791  304  MET A C     
1603 O  O     . MET A 201 ? 2.2715 1.9424 3.2431 -0.1168 -0.4043 0.4065  304  MET A O     
1604 C  CB    . MET A 201 ? 2.2816 1.9815 3.2231 -0.1080 -0.3079 0.3300  304  MET A CB    
1605 C  CG    . MET A 201 ? 2.3605 2.0818 3.3025 -0.1021 -0.2703 0.3000  304  MET A CG    
1606 S  SD    . MET A 201 ? 2.1929 1.9018 3.1443 -0.1030 -0.2203 0.2728  304  MET A SD    
1607 C  CE    . MET A 201 ? 1.7801 1.5167 2.7232 -0.0986 -0.1857 0.2422  304  MET A CE    
1608 N  N     . PRO A 202 ? 2.4664 2.1416 3.2928 -0.1349 -0.3982 0.3737  305  PRO A N     
1609 C  CA    . PRO A 202 ? 2.5269 2.1769 3.3323 -0.1462 -0.4330 0.3999  305  PRO A CA    
1610 C  C     . PRO A 202 ? 2.4939 2.1201 3.3286 -0.1462 -0.4222 0.4068  305  PRO A C     
1611 O  O     . PRO A 202 ? 2.4344 2.0621 3.3115 -0.1370 -0.3873 0.3918  305  PRO A O     
1612 C  CB    . PRO A 202 ? 2.3917 2.0415 3.0993 -0.1601 -0.4388 0.3860  305  PRO A CB    
1613 C  CG    . PRO A 202 ? 2.3542 2.0241 3.0383 -0.1559 -0.3984 0.3506  305  PRO A CG    
1614 C  CD    . PRO A 202 ? 2.1931 1.8828 2.9437 -0.1408 -0.3804 0.3447  305  PRO A CD    
1615 N  N     . SER A 203 ? 2.4845 2.0862 3.2945 -0.1575 -0.4513 0.4293  306  SER A N     
1616 C  CA    . SER A 203 ? 2.4863 2.0626 3.3240 -0.1579 -0.4440 0.4393  306  SER A CA    
1617 C  C     . SER A 203 ? 2.5987 2.1687 3.3845 -0.1644 -0.4104 0.4096  306  SER A C     
1618 O  O     . SER A 203 ? 2.6353 2.1907 3.4555 -0.1607 -0.3865 0.4055  306  SER A O     
1619 C  CB    . SER A 203 ? 2.4701 2.0216 3.2955 -0.1692 -0.4877 0.4747  306  SER A CB    
1620 O  OG    . SER A 203 ? 2.4973 2.0426 3.2293 -0.1859 -0.5043 0.4694  306  SER A OG    
1621 N  N     . TYR A 204 ? 2.6351 2.2156 3.3405 -0.1744 -0.4073 0.3891  307  TYR A N     
1622 C  CA    . TYR A 204 ? 2.6786 2.2569 3.3326 -0.1822 -0.3779 0.3619  307  TYR A CA    
1623 C  C     . TYR A 204 ? 2.7705 2.3720 3.4379 -0.1744 -0.3364 0.3296  307  TYR A C     
1624 O  O     . TYR A 204 ? 2.8184 2.4284 3.4329 -0.1821 -0.3148 0.3042  307  TYR A O     
1625 C  CB    . TYR A 204 ? 2.5730 2.1523 3.1374 -0.1967 -0.3925 0.3561  307  TYR A CB    
1626 C  CG    . TYR A 204 ? 2.5559 2.1598 3.0939 -0.1947 -0.4026 0.3503  307  TYR A CG    
1627 C  CD1   . TYR A 204 ? 2.4214 2.0536 2.9391 -0.1906 -0.3747 0.3211  307  TYR A CD1   
1628 C  CD2   . TYR A 204 ? 2.4550 2.0527 2.9867 -0.1981 -0.4402 0.3746  307  TYR A CD2   
1629 C  CE1   . TYR A 204 ? 2.3397 1.9929 2.8344 -0.1881 -0.3828 0.3166  307  TYR A CE1   
1630 C  CE2   . TYR A 204 ? 2.6346 2.2520 3.1411 -0.1969 -0.4479 0.3687  307  TYR A CE2   
1631 C  CZ    . TYR A 204 ? 2.4731 2.1178 2.9622 -0.1911 -0.4185 0.3398  307  TYR A CZ    
1632 O  OH    . TYR A 204 ? 2.3174 1.9804 2.7828 -0.1893 -0.4250 0.3347  307  TYR A OH    
1633 N  N     . SER A 205 ? 2.5031 2.1151 3.2396 -0.1603 -0.3250 0.3306  308  SER A N     
1634 C  CA    . SER A 205 ? 2.3650 1.9957 3.1171 -0.1537 -0.2849 0.3012  308  SER A CA    
1635 C  C     . SER A 205 ? 2.5622 2.1737 3.3645 -0.1501 -0.2543 0.2952  308  SER A C     
1636 O  O     . SER A 205 ? 2.7206 2.3393 3.5713 -0.1404 -0.2266 0.2832  308  SER A O     
1637 C  CB    . SER A 205 ? 2.2780 1.9319 3.0696 -0.1414 -0.2874 0.3029  308  SER A CB    
1638 O  OG    . SER A 205 ? 2.2523 1.8957 3.1207 -0.1314 -0.3037 0.3305  308  SER A OG    
1639 N  N     . ARG A 206 ? 2.5648 2.1493 3.3549 -0.1582 -0.2569 0.3029  309  ARG A N     
1640 C  CA    . ARG A 206 ? 2.6310 2.1919 3.4683 -0.1555 -0.2287 0.2996  309  ARG A CA    
1641 C  C     . ARG A 206 ? 2.7495 2.3137 3.5462 -0.1649 -0.1886 0.2633  309  ARG A C     
1642 O  O     . ARG A 206 ? 2.7385 2.3199 3.4653 -0.1756 -0.1881 0.2455  309  ARG A O     
1643 C  CB    . ARG A 206 ? 2.5960 2.1246 3.4400 -0.1604 -0.2505 0.3264  309  ARG A CB    
1644 C  CG    . ARG A 206 ? 2.4376 1.9639 3.2976 -0.1575 -0.2980 0.3631  309  ARG A CG    
1645 C  CD    . ARG A 206 ? 2.3944 1.8882 3.2524 -0.1647 -0.3205 0.3898  309  ARG A CD    
1646 N  NE    . ARG A 206 ? 2.6557 2.1481 3.5039 -0.1680 -0.3690 0.4220  309  ARG A NE    
1647 C  CZ    . ARG A 206 ? 2.7543 2.2454 3.6702 -0.1583 -0.3942 0.4535  309  ARG A CZ    
1648 N  NH1   . ARG A 206 ? 2.6780 2.1693 3.6816 -0.1427 -0.3747 0.4582  309  ARG A NH1   
1649 N  NH2   . ARG A 206 ? 2.4398 1.9291 3.3350 -0.1654 -0.4397 0.4812  309  ARG A NH2   
1650 N  N     . ARG A 207 ? 2.6474 2.1942 3.4899 -0.1614 -0.1544 0.2530  310  ARG A N     
1651 C  CA    . ARG A 207 ? 2.6791 2.2252 3.4875 -0.1723 -0.1147 0.2188  310  ARG A CA    
1652 C  C     . ARG A 207 ? 2.6920 2.2167 3.4533 -0.1877 -0.1156 0.2169  310  ARG A C     
1653 O  O     . ARG A 207 ? 2.4978 2.0372 3.1888 -0.2009 -0.1178 0.2016  310  ARG A O     
1654 C  CB    . ARG A 207 ? 2.5794 2.1103 3.4519 -0.1646 -0.0752 0.2074  310  ARG A CB    
1655 C  CG    . ARG A 207 ? 2.4702 1.9947 3.3084 -0.1786 -0.0327 0.1722  310  ARG A CG    
1656 C  CD    . ARG A 207 ? 2.5023 1.9863 3.3620 -0.1836 -0.0141 0.1744  310  ARG A CD    
1657 N  NE    . ARG A 207 ? 2.6574 2.1334 3.4818 -0.1995 0.0265  0.1400  310  ARG A NE    
1658 C  CZ    . ARG A 207 ? 2.7021 2.1426 3.5356 -0.2073 0.0511  0.1338  310  ARG A CZ    
1659 N  NH1   . ARG A 207 ? 2.3122 1.7216 3.1912 -0.1996 0.0402  0.1604  310  ARG A NH1   
1660 N  NH2   . ARG A 207 ? 2.6481 2.0837 3.4436 -0.2243 0.0871  0.1008  310  ARG A NH2   
1661 N  N     . SER A 220 ? 2.5504 2.1604 2.5321 -0.5659 0.1405  -0.1155 323  SER A N     
1662 C  CA    . SER A 220 ? 2.6482 2.2998 2.6011 -0.5880 0.1511  -0.1376 323  SER A CA    
1663 C  C     . SER A 220 ? 2.6408 2.3401 2.5974 -0.5722 0.1353  -0.1330 323  SER A C     
1664 O  O     . SER A 220 ? 2.8704 2.5798 2.8312 -0.5751 0.1483  -0.1473 323  SER A O     
1665 C  CB    . SER A 220 ? 2.5722 2.2479 2.4867 -0.6125 0.1476  -0.1422 323  SER A CB    
1666 O  OG    . SER A 220 ? 2.4736 2.1900 2.3619 -0.6362 0.1566  -0.1623 323  SER A OG    
1667 N  N     . THR A 221 ? 2.3355 2.0615 2.2888 -0.5562 0.1087  -0.1132 324  THR A N     
1668 C  CA    . THR A 221 ? 2.4089 2.1790 2.3659 -0.5391 0.0916  -0.1055 324  THR A CA    
1669 C  C     . THR A 221 ? 2.5341 2.3516 2.4675 -0.5581 0.0995  -0.1237 324  THR A C     
1670 O  O     . THR A 221 ? 2.6277 2.4535 2.5694 -0.5564 0.1087  -0.1339 324  THR A O     
1671 C  CB    . THR A 221 ? 2.4579 2.2065 2.4533 -0.5131 0.0896  -0.0972 324  THR A CB    
1672 O  OG1   . THR A 221 ? 2.8774 2.6095 2.8836 -0.5224 0.1155  -0.1170 324  THR A OG1   
1673 C  CG2   . THR A 221 ? 2.5482 2.2496 2.5688 -0.4967 0.0808  -0.0779 324  THR A CG2   
1674 N  N     . LYS A 222 ? 2.2174 2.0664 2.1214 -0.5771 0.0952  -0.1264 325  LYS A N     
1675 C  CA    . LYS A 222 ? 2.0457 1.9447 1.9268 -0.5971 0.0985  -0.1399 325  LYS A CA    
1676 C  C     . LYS A 222 ? 1.8847 1.8342 1.7687 -0.5786 0.0779  -0.1263 325  LYS A C     
1677 O  O     . LYS A 222 ? 2.0988 2.0424 1.9999 -0.5517 0.0623  -0.1082 325  LYS A O     
1678 C  CB    . LYS A 222 ? 2.1082 2.0215 1.9612 -0.6263 0.1028  -0.1475 325  LYS A CB    
1679 C  CG    . LYS A 222 ? 2.5580 2.4216 2.4052 -0.6473 0.1251  -0.1626 325  LYS A CG    
1680 C  CD    . LYS A 222 ? 2.7421 2.5861 2.5904 -0.6595 0.1478  -0.1836 325  LYS A CD    
1681 C  CE    . LYS A 222 ? 2.6018 2.4956 2.4235 -0.6840 0.1502  -0.1984 325  LYS A CE    
1682 N  NZ    . LYS A 222 ? 2.5031 2.3749 2.3207 -0.6973 0.1734  -0.2197 325  LYS A NZ    
1683 N  N     . SER A 223 ? 1.7999 1.7988 1.6664 -0.5941 0.0776  -0.1345 326  SER A N     
1684 C  CA    . SER A 223 ? 1.6723 1.7208 1.5421 -0.5781 0.0603  -0.1224 326  SER A CA    
1685 C  C     . SER A 223 ? 1.7453 1.8315 1.6043 -0.5797 0.0458  -0.1095 326  SER A C     
1686 O  O     . SER A 223 ? 2.0786 2.1559 1.9255 -0.5956 0.0494  -0.1112 326  SER A O     
1687 C  CB    . SER A 223 ? 1.9248 2.0077 1.7839 -0.5927 0.0667  -0.1356 326  SER A CB    
1688 O  OG    . SER A 223 ? 2.1880 2.2947 2.0212 -0.6262 0.0735  -0.1483 326  SER A OG    
1689 N  N     . LEU A 224 ? 1.8109 1.9390 1.6756 -0.5627 0.0308  -0.0962 327  LEU A N     
1690 C  CA    . LEU A 224 ? 1.6372 1.8031 1.4958 -0.5615 0.0190  -0.0829 327  LEU A CA    
1691 C  C     . LEU A 224 ? 1.5678 1.7859 1.4116 -0.5881 0.0210  -0.0900 327  LEU A C     
1692 O  O     . LEU A 224 ? 1.8026 2.0415 1.6394 -0.5987 0.0184  -0.0848 327  LEU A O     
1693 C  CB    . LEU A 224 ? 1.5132 1.6999 1.3852 -0.5319 0.0038  -0.0652 327  LEU A CB    
1694 C  CG    . LEU A 224 ? 1.6665 1.8901 1.5355 -0.5263 -0.0064 -0.0501 327  LEU A CG    
1695 C  CD1   . LEU A 224 ? 1.5957 1.7824 1.4589 -0.5230 -0.0074 -0.0427 327  LEU A CD1   
1696 C  CD2   . LEU A 224 ? 1.4418 1.6922 1.3233 -0.5006 -0.0181 -0.0362 327  LEU A CD2   
1697 N  N     . TRP A 225 ? 1.5868 1.8264 1.4257 -0.6004 0.0254  -0.1011 328  TRP A N     
1698 C  CA    . TRP A 225 ? 1.7919 2.0850 1.6170 -0.6266 0.0241  -0.1059 328  TRP A CA    
1699 C  C     . TRP A 225 ? 2.1313 2.4097 1.9361 -0.6624 0.0379  -0.1241 328  TRP A C     
1700 O  O     . TRP A 225 ? 1.8267 2.1396 1.6162 -0.6892 0.0394  -0.1332 328  TRP A O     
1701 C  CB    . TRP A 225 ? 1.7363 2.0586 1.5607 -0.6259 0.0215  -0.1087 328  TRP A CB    
1702 C  CG    . TRP A 225 ? 1.6677 2.0172 1.5104 -0.5948 0.0070  -0.0898 328  TRP A CG    
1703 C  CD1   . TRP A 225 ? 1.8914 2.2457 1.7480 -0.5712 -0.0031 -0.0719 328  TRP A CD1   
1704 C  CD2   . TRP A 225 ? 1.7849 2.1577 1.6318 -0.5848 0.0023  -0.0873 328  TRP A CD2   
1705 N  NE1   . TRP A 225 ? 1.9625 2.3414 1.8325 -0.5472 -0.0133 -0.0588 328  TRP A NE1   
1706 C  CE2   . TRP A 225 ? 1.7556 2.1470 1.6210 -0.5545 -0.0107 -0.0674 328  TRP A CE2   
1707 C  CE3   . TRP A 225 ? 1.6984 2.0761 1.5330 -0.5996 0.0089  -0.1003 328  TRP A CE3   
1708 C  CZ2   . TRP A 225 ? 1.6570 2.0724 1.5310 -0.5378 -0.0177 -0.0596 328  TRP A CZ2   
1709 C  CZ3   . TRP A 225 ? 1.7502 2.1523 1.5925 -0.5832 0.0015  -0.0921 328  TRP A CZ3   
1710 C  CH2   . TRP A 225 ? 1.6043 2.0254 1.4671 -0.5522 -0.0119 -0.0717 328  TRP A CH2   
1711 N  N     . VAL A 226 ? 2.1344 2.3622 1.9376 -0.6646 0.0475  -0.1289 329  VAL A N     
1712 C  CA    . VAL A 226 ? 2.0470 2.2572 1.8311 -0.6982 0.0617  -0.1457 329  VAL A CA    
1713 C  C     . VAL A 226 ? 2.2486 2.4464 2.0330 -0.6988 0.0602  -0.1374 329  VAL A C     
1714 O  O     . VAL A 226 ? 2.3229 2.4969 2.0936 -0.7231 0.0723  -0.1492 329  VAL A O     
1715 C  CB    . VAL A 226 ? 2.0225 2.1726 1.8022 -0.7048 0.0811  -0.1642 329  VAL A CB    
1716 C  CG1   . VAL A 226 ? 2.1295 2.2918 1.9043 -0.7089 0.0855  -0.1746 329  VAL A CG1   
1717 C  CG2   . VAL A 226 ? 2.1010 2.1974 1.9014 -0.6749 0.0817  -0.1551 329  VAL A CG2   
1718 N  N     . ILE A 227 ? 2.0702 2.2822 1.8684 -0.6730 0.0466  -0.1175 330  ILE A N     
1719 C  CA    . ILE A 227 ? 1.6206 1.8195 1.4169 -0.6724 0.0457  -0.1086 330  ILE A CA    
1720 C  C     . ILE A 227 ? 2.2374 2.4888 2.0265 -0.6962 0.0439  -0.1075 330  ILE A C     
1721 O  O     . ILE A 227 ? 2.6868 2.9247 2.4642 -0.7190 0.0528  -0.1147 330  ILE A O     
1722 C  CB    . ILE A 227 ? 1.4375 1.6275 1.2475 -0.6378 0.0335  -0.0886 330  ILE A CB    
1723 C  CG1   . ILE A 227 ? 1.8986 2.0320 1.7176 -0.6171 0.0348  -0.0886 330  ILE A CG1   
1724 C  CG2   . ILE A 227 ? 1.6353 1.8187 1.4394 -0.6394 0.0326  -0.0786 330  ILE A CG2   
1725 C  CD1   . ILE A 227 ? 1.5862 1.6606 1.3988 -0.6287 0.0473  -0.0977 330  ILE A CD1   
1726 N  N     . ASN A 228 ? 2.0651 2.3773 1.8636 -0.6911 0.0324  -0.0974 331  ASN A N     
1727 C  CA    . ASN A 228 ? 2.2036 2.5744 2.0025 -0.7120 0.0287  -0.0932 331  ASN A CA    
1728 C  C     . ASN A 228 ? 2.1901 2.5538 1.9906 -0.7109 0.0310  -0.0838 331  ASN A C     
1729 O  O     . ASN A 228 ? 2.3279 2.6926 2.1187 -0.7376 0.0387  -0.0911 331  ASN A O     
1730 C  CB    . ASN A 228 ? 2.2179 2.6010 1.9995 -0.7509 0.0361  -0.1117 331  ASN A CB    
1731 C  CG    . ASN A 228 ? 2.4853 2.8736 2.2607 -0.7546 0.0356  -0.1219 331  ASN A CG    
1732 O  OD1   . ASN A 228 ? 2.4739 2.8886 2.2618 -0.7333 0.0250  -0.1112 331  ASN A OD1   
1733 N  ND2   . ASN A 228 ? 2.5087 2.8692 2.2632 -0.7824 0.0485  -0.1430 331  ASN A ND2   
1734 N  N     . SER A 229 ? 2.0380 2.3931 1.8493 -0.6805 0.0251  -0.0677 332  SER A N     
1735 C  CA    . SER A 229 ? 1.9497 2.2953 1.7604 -0.6766 0.0279  -0.0575 332  SER A CA    
1736 C  C     . SER A 229 ? 2.0266 2.4004 1.8531 -0.6483 0.0192  -0.0382 332  SER A C     
1737 O  O     . SER A 229 ? 1.9232 2.3215 1.7615 -0.6318 0.0108  -0.0328 332  SER A O     
1738 C  CB    . SER A 229 ? 1.8876 2.1593 1.6839 -0.6720 0.0347  -0.0617 332  SER A CB    
1739 O  OG    . SER A 229 ? 2.0237 2.2834 1.8155 -0.6679 0.0371  -0.0509 332  SER A OG    
1740 N  N     . ALA A 230 ? 1.9688 2.3369 1.7943 -0.6436 0.0230  -0.0280 333  ALA A N     
1741 C  CA    . ALA A 230 ? 1.3648 1.7528 1.2025 -0.6183 0.0187  -0.0105 333  ALA A CA    
1742 C  C     . ALA A 230 ? 1.4420 1.7689 1.2669 -0.5951 0.0171  -0.0050 333  ALA A C     
1743 O  O     . ALA A 230 ? 1.5060 1.7800 1.3130 -0.6021 0.0217  -0.0104 333  ALA A O     
1744 C  CB    . ALA A 230 ? 2.0321 2.4558 1.8776 -0.6285 0.0259  -0.0021 333  ALA A CB    
1745 N  N     . LEU A 231 ? 1.4483 1.7824 1.2821 -0.5683 0.0100  0.0064  334  LEU A N     
1746 C  CA    . LEU A 231 ? 1.3886 1.6679 1.2098 -0.5468 0.0060  0.0130  334  LEU A CA    
1747 C  C     . LEU A 231 ? 1.5451 1.8013 1.3507 -0.5486 0.0136  0.0205  334  LEU A C     
1748 O  O     . LEU A 231 ? 1.7458 2.0378 1.5593 -0.5469 0.0195  0.0289  334  LEU A O     
1749 C  CB    . LEU A 231 ? 1.3045 1.6002 1.1383 -0.5199 -0.0027 0.0229  334  LEU A CB    
1750 C  CG    . LEU A 231 ? 1.3871 1.6292 1.2080 -0.4984 -0.0088 0.0305  334  LEU A CG    
1751 C  CD1   . LEU A 231 ? 1.7126 1.9019 1.5250 -0.5012 -0.0135 0.0223  334  LEU A CD1   
1752 C  CD2   . LEU A 231 ? 1.4309 1.6932 1.2647 -0.4736 -0.0162 0.0397  334  LEU A CD2   
1753 N  N     . ARG A 232 ? 1.4290 1.6246 1.2132 -0.5521 0.0141  0.0183  335  ARG A N     
1754 C  CA    . ARG A 232 ? 1.7031 1.8685 1.4665 -0.5564 0.0214  0.0247  335  ARG A CA    
1755 C  C     . ARG A 232 ? 1.8194 1.9197 1.5623 -0.5423 0.0130  0.0310  335  ARG A C     
1756 O  O     . ARG A 232 ? 2.2079 2.2688 1.9463 -0.5459 0.0079  0.0257  335  ARG A O     
1757 C  CB    . ARG A 232 ? 1.8188 1.9793 1.5740 -0.5846 0.0321  0.0155  335  ARG A CB    
1758 C  CG    . ARG A 232 ? 1.9902 2.1306 1.7461 -0.5983 0.0305  0.0017  335  ARG A CG    
1759 C  CD    . ARG A 232 ? 1.9261 2.0690 1.6751 -0.6281 0.0424  -0.0081 335  ARG A CD    
1760 N  NE    . ARG A 232 ? 2.1512 2.2484 1.8769 -0.6339 0.0489  -0.0032 335  ARG A NE    
1761 C  CZ    . ARG A 232 ? 2.1364 2.1728 1.8451 -0.6380 0.0484  -0.0054 335  ARG A CZ    
1762 N  NH1   . ARG A 232 ? 2.3324 2.3448 2.0475 -0.6358 0.0434  -0.0128 335  ARG A NH1   
1763 N  NH2   . ARG A 232 ? 1.9231 1.9212 1.6088 -0.6445 0.0541  0.0006  335  ARG A NH2   
1764 N  N     . ILE A 233 ? 1.5605 1.6492 1.2917 -0.5271 0.0118  0.0428  336  ILE A N     
1765 C  CA    . ILE A 233 ? 1.6724 1.7013 1.3809 -0.5152 0.0021  0.0511  336  ILE A CA    
1766 C  C     . ILE A 233 ? 1.7848 1.7843 1.4632 -0.5231 0.0110  0.0579  336  ILE A C     
1767 O  O     . ILE A 233 ? 1.9953 2.0252 1.6741 -0.5240 0.0233  0.0608  336  ILE A O     
1768 C  CB    . ILE A 233 ? 1.8059 1.8406 1.5220 -0.4903 -0.0086 0.0588  336  ILE A CB    
1769 C  CG1   . ILE A 233 ? 2.0401 2.1141 1.7872 -0.4835 -0.0141 0.0520  336  ILE A CG1   
1770 C  CG2   . ILE A 233 ? 1.9127 1.8856 1.6078 -0.4807 -0.0222 0.0670  336  ILE A CG2   
1771 C  CD1   . ILE A 233 ? 2.1578 2.2076 1.9117 -0.4911 -0.0196 0.0428  336  ILE A CD1   
1772 N  N     . LYS A 234 ? 1.8656 1.8054 1.5185 -0.5290 0.0055  0.0611  337  LYS A N     
1773 C  CA    . LYS A 234 ? 2.0442 1.9479 1.6627 -0.5390 0.0134  0.0676  337  LYS A CA    
1774 C  C     . LYS A 234 ? 2.1110 1.9669 1.7018 -0.5256 0.0014  0.0800  337  LYS A C     
1775 O  O     . LYS A 234 ? 2.2099 2.0369 1.8029 -0.5159 -0.0160 0.0841  337  LYS A O     
1776 C  CB    . LYS A 234 ? 2.2661 2.1355 1.8717 -0.5597 0.0168  0.0632  337  LYS A CB    
1777 C  CG    . LYS A 234 ? 2.1898 2.0121 1.7551 -0.5704 0.0227  0.0711  337  LYS A CG    
1778 C  CD    . LYS A 234 ? 2.3949 2.1852 1.9495 -0.5911 0.0270  0.0671  337  LYS A CD    
1779 C  CE    . LYS A 234 ? 2.5704 2.3292 2.1364 -0.5870 0.0116  0.0668  337  LYS A CE    
1780 N  NZ    . LYS A 234 ? 2.4478 2.1737 2.0053 -0.6067 0.0175  0.0630  337  LYS A NZ    
1781 N  N     . ILE A 235 ? 2.1157 1.9631 1.6807 -0.5260 0.0114  0.0862  338  ILE A N     
1782 C  CA    . ILE A 235 ? 2.1002 1.8961 1.6287 -0.5193 0.0023  0.0977  338  ILE A CA    
1783 C  C     . ILE A 235 ? 2.1278 1.8704 1.6173 -0.5380 0.0051  0.1019  338  ILE A C     
1784 O  O     . ILE A 235 ? 2.1084 1.8584 1.5865 -0.5524 0.0243  0.0986  338  ILE A O     
1785 C  CB    . ILE A 235 ? 2.0487 1.8630 1.5690 -0.5086 0.0137  0.1013  338  ILE A CB    
1786 C  CG1   . ILE A 235 ? 2.0072 1.8539 1.5564 -0.4868 0.0038  0.1017  338  ILE A CG1   
1787 C  CG2   . ILE A 235 ? 2.1136 1.8684 1.5824 -0.5122 0.0125  0.1110  338  ILE A CG2   
1788 C  CD1   . ILE A 235 ? 1.7924 1.7063 1.3885 -0.4830 0.0096  0.0930  338  ILE A CD1   
1789 N  N     . LEU A 236 ? 2.4554 2.1448 1.9262 -0.5382 -0.0142 0.1104  339  LEU A N     
1790 C  CA    . LEU A 236 ? 2.5539 2.1895 1.9878 -0.5562 -0.0144 0.1164  339  LEU A CA    
1791 C  C     . LEU A 236 ? 2.4568 2.0547 1.8401 -0.5607 -0.0100 0.1256  339  LEU A C     
1792 O  O     . LEU A 236 ? 2.4755 2.0738 1.8377 -0.5739 0.0110  0.1227  339  LEU A O     
1793 C  CB    . LEU A 236 ? 2.4120 2.0067 1.8500 -0.5547 -0.0373 0.1240  339  LEU A CB    
1794 C  CG    . LEU A 236 ? 2.5792 2.1953 2.0582 -0.5569 -0.0367 0.1142  339  LEU A CG    
1795 C  CD1   . LEU A 236 ? 2.5681 2.1420 2.0549 -0.5521 -0.0584 0.1238  339  LEU A CD1   
1796 C  CD2   . LEU A 236 ? 2.7200 2.3406 2.1930 -0.5781 -0.0172 0.1056  339  LEU A CD2   
1797 N  N     . CYS A 237 ? 2.4690 2.0330 1.8315 -0.5512 -0.0288 0.1366  340  CYS A N     
1798 C  CA    . CYS A 237 ? 2.4955 2.0167 1.8036 -0.5575 -0.0263 0.1453  340  CYS A CA    
1799 C  C     . CYS A 237 ? 2.5077 2.0268 1.8133 -0.5405 -0.0405 0.1508  340  CYS A C     
1800 O  O     . CYS A 237 ? 2.6493 2.2088 1.9975 -0.5232 -0.0467 0.1464  340  CYS A O     
1801 C  CB    . CYS A 237 ? 2.7083 2.1643 1.9737 -0.5749 -0.0385 0.1570  340  CYS A CB    
1802 S  SG    . CYS A 237 ? 2.8802 2.3031 2.1608 -0.5676 -0.0754 0.1705  340  CYS A SG    
1803 N  N     . ALA A 238 ? 2.4722 1.9422 1.7248 -0.5468 -0.0452 0.1604  341  ALA A N     
1804 C  CA    . ALA A 238 ? 2.4484 1.9089 1.6905 -0.5340 -0.0584 0.1660  341  ALA A CA    
1805 C  C     . ALA A 238 ? 2.5351 1.9258 1.7132 -0.5484 -0.0729 0.1798  341  ALA A C     
1806 O  O     . ALA A 238 ? 2.9870 2.3400 2.1272 -0.5676 -0.0684 0.1841  341  ALA A O     
1807 C  CB    . ALA A 238 ? 2.2004 1.6993 1.4502 -0.5235 -0.0341 0.1569  341  ALA A CB    
1808 N  N     . THR A 239 ? 2.1653 1.5387 1.3304 -0.5401 -0.0910 0.1871  342  THR A N     
1809 C  CA    . THR A 239 ? 2.4427 1.7513 1.5449 -0.5543 -0.1076 0.2008  342  THR A CA    
1810 C  C     . THR A 239 ? 2.6839 1.9862 1.7554 -0.5504 -0.0965 0.1976  342  THR A C     
1811 O  O     . THR A 239 ? 2.3585 1.7075 1.4654 -0.5330 -0.0817 0.1873  342  THR A O     
1812 C  CB    . THR A 239 ? 2.4448 1.7291 1.5580 -0.5516 -0.1467 0.2165  342  THR A CB    
1813 O  OG1   . THR A 239 ? 2.6736 1.9935 1.8312 -0.5300 -0.1575 0.2140  342  THR A OG1   
1814 C  CG2   . THR A 239 ? 2.2146 1.5019 1.3599 -0.5549 -0.1551 0.2198  342  THR A CG2   
1815 N  N     . TYR A 240 ? 2.8503 2.0923 1.8536 -0.5677 -0.1035 0.2069  343  TYR A N     
1816 C  CA    . TYR A 240 ? 2.8721 2.0950 1.8343 -0.5684 -0.0922 0.2041  343  TYR A CA    
1817 C  C     . TYR A 240 ? 2.7661 2.0223 1.7364 -0.5628 -0.0495 0.1883  343  TYR A C     
1818 O  O     . TYR A 240 ? 2.4063 1.6910 1.3966 -0.5468 -0.0377 0.1813  343  TYR A O     
1819 C  CB    . TYR A 240 ? 2.7425 1.9805 1.7317 -0.5509 -0.1146 0.2075  343  TYR A CB    
1820 C  CG    . TYR A 240 ? 2.8527 2.0513 1.8265 -0.5581 -0.1566 0.2254  343  TYR A CG    
1821 C  CD1   . TYR A 240 ? 2.8131 2.0281 1.8355 -0.5514 -0.1807 0.2332  343  TYR A CD1   
1822 C  CD2   . TYR A 240 ? 2.9572 2.1022 1.8692 -0.5724 -0.1718 0.2351  343  TYR A CD2   
1823 C  CE1   . TYR A 240 ? 2.9655 2.1468 1.9803 -0.5570 -0.2190 0.2517  343  TYR A CE1   
1824 C  CE2   . TYR A 240 ? 3.0461 2.1581 1.9472 -0.5799 -0.2124 0.2537  343  TYR A CE2   
1825 C  CZ    . TYR A 240 ? 3.0276 2.1591 1.9829 -0.5713 -0.2360 0.2627  343  TYR A CZ    
1826 O  OH    . TYR A 240 ? 2.8833 1.9842 1.8340 -0.5777 -0.2764 0.2833  343  TYR A OH    
1827 N  N     . LYS A 250 ? 2.2133 1.7418 1.3433 -0.5459 0.3203  0.1155  353  LYS A N     
1828 C  CA    . LYS A 250 ? 2.6108 2.2147 1.8144 -0.5362 0.3061  0.1160  353  LYS A CA    
1829 C  C     . LYS A 250 ? 2.7178 2.3578 1.9606 -0.5141 0.2768  0.1186  353  LYS A C     
1830 O  O     . LYS A 250 ? 2.4356 2.0904 1.6952 -0.4961 0.2872  0.1195  353  LYS A O     
1831 C  CB    . LYS A 250 ? 2.4428 2.1065 1.7024 -0.5308 0.3425  0.1146  353  LYS A CB    
1832 N  N     . ILE A 251 ? 2.8417 2.4940 2.0991 -0.5156 0.2417  0.1196  354  ILE A N     
1833 C  CA    . ILE A 251 ? 2.6055 2.2904 1.8996 -0.4967 0.2127  0.1216  354  ILE A CA    
1834 C  C     . ILE A 251 ? 2.5983 2.3401 1.9465 -0.4963 0.1969  0.1199  354  ILE A C     
1835 O  O     . ILE A 251 ? 2.3676 2.1147 1.7175 -0.5124 0.2039  0.1174  354  ILE A O     
1836 C  CB    . ILE A 251 ? 2.3436 1.9693 1.5893 -0.4992 0.1810  0.1251  354  ILE A CB    
1837 C  CG1   . ILE A 251 ? 2.3124 1.8948 1.5210 -0.5208 0.1624  0.1268  354  ILE A CG1   
1838 C  CG2   . ILE A 251 ? 2.5079 2.0802 1.7005 -0.4995 0.1950  0.1262  354  ILE A CG2   
1839 C  CD1   . ILE A 251 ? 2.0720 1.5995 1.2386 -0.5242 0.1288  0.1331  354  ILE A CD1   
1840 N  N     . TYR A 252 ? 2.3232 2.1063 1.7138 -0.4787 0.1764  0.1207  355  TYR A N     
1841 C  CA    . TYR A 252 ? 2.1850 2.0190 1.6236 -0.4784 0.1596  0.1182  355  TYR A CA    
1842 C  C     . TYR A 252 ? 2.0891 1.9364 1.5484 -0.4615 0.1314  0.1196  355  TYR A C     
1843 O  O     . TYR A 252 ? 2.1976 2.0163 1.6356 -0.4506 0.1250  0.1229  355  TYR A O     
1844 C  CB    . TYR A 252 ? 2.2075 2.1129 1.7011 -0.4757 0.1818  0.1168  355  TYR A CB    
1845 C  CG    . TYR A 252 ? 2.3797 2.3313 1.9131 -0.4533 0.1927  0.1207  355  TYR A CG    
1846 C  CD1   . TYR A 252 ? 2.4764 2.4099 1.9940 -0.4463 0.2194  0.1237  355  TYR A CD1   
1847 C  CD2   . TYR A 252 ? 2.4164 2.4281 2.0024 -0.4398 0.1775  0.1216  355  TYR A CD2   
1848 C  CE1   . TYR A 252 ? 2.4773 2.4519 2.0336 -0.4250 0.2305  0.1283  355  TYR A CE1   
1849 C  CE2   . TYR A 252 ? 2.3289 2.3827 1.9517 -0.4193 0.1867  0.1269  355  TYR A CE2   
1850 C  CZ    . TYR A 252 ? 2.4353 2.4708 2.0448 -0.4113 0.2132  0.1306  355  TYR A CZ    
1851 O  OH    . TYR A 252 ? 2.2071 2.2834 1.8557 -0.3900 0.2235  0.1369  355  TYR A OH    
1852 N  N     . VAL A 253 ? 2.0256 1.9151 1.5255 -0.4605 0.1154  0.1166  356  VAL A N     
1853 C  CA    . VAL A 253 ? 2.1717 2.0734 1.6927 -0.4467 0.0890  0.1169  356  VAL A CA    
1854 C  C     . VAL A 253 ? 2.0614 2.0392 1.6417 -0.4342 0.0928  0.1155  356  VAL A C     
1855 O  O     . VAL A 253 ? 1.7688 1.7885 1.3778 -0.4437 0.0995  0.1120  356  VAL A O     
1856 C  CB    . VAL A 253 ? 1.7133 1.5881 1.2247 -0.4580 0.0648  0.1147  356  VAL A CB    
1857 C  CG1   . VAL A 253 ? 2.2616 2.1519 1.7998 -0.4433 0.0407  0.1146  356  VAL A CG1   
1858 C  CG2   . VAL A 253 ? 1.7832 1.5830 1.2361 -0.4707 0.0585  0.1189  356  VAL A CG2   
1859 N  N     . ARG A 254 ? 2.0308 2.0258 1.6282 -0.4142 0.0877  0.1189  357  ARG A N     
1860 C  CA    . ARG A 254 ? 2.0045 2.0688 1.6558 -0.4013 0.0871  0.1194  357  ARG A CA    
1861 C  C     . ARG A 254 ? 2.1006 2.1727 1.7675 -0.3988 0.0604  0.1156  357  ARG A C     
1862 O  O     . ARG A 254 ? 2.0430 2.0821 1.6945 -0.3897 0.0437  0.1171  357  ARG A O     
1863 C  CB    . ARG A 254 ? 2.0025 2.0815 1.6654 -0.3806 0.0979  0.1257  357  ARG A CB    
1864 C  CG    . ARG A 254 ? 2.3811 2.4754 2.0498 -0.3801 0.1293  0.1297  357  ARG A CG    
1865 C  CD    . ARG A 254 ? 2.3492 2.5125 2.0668 -0.3852 0.1391  0.1306  357  ARG A CD    
1866 N  NE    . ARG A 254 ? 2.0545 2.2801 1.8221 -0.3680 0.1358  0.1363  357  ARG A NE    
1867 C  CZ    . ARG A 254 ? 2.0644 2.3295 1.8646 -0.3558 0.1564  0.1449  357  ARG A CZ    
1868 N  NH1   . ARG A 254 ? 2.1874 2.4370 1.9775 -0.3582 0.1844  0.1476  357  ARG A NH1   
1869 N  NH2   . ARG A 254 ? 2.1701 2.4908 2.0148 -0.3408 0.1498  0.1514  357  ARG A NH2   
1870 N  N     . THR A 255 ? 2.0181 2.1327 1.7152 -0.4080 0.0572  0.1107  358  THR A N     
1871 C  CA    . THR A 255 ? 1.5602 1.6839 1.2734 -0.4080 0.0361  0.1054  358  THR A CA    
1872 C  C     . THR A 255 ? 1.6984 1.8908 1.4572 -0.3989 0.0358  0.1058  358  THR A C     
1873 O  O     . THR A 255 ? 1.6959 1.9365 1.4789 -0.4039 0.0494  0.1075  358  THR A O     
1874 C  CB    . THR A 255 ? 1.6268 1.7355 1.3315 -0.4295 0.0322  0.0979  358  THR A CB    
1875 O  OG1   . THR A 255 ? 1.9271 2.0870 1.6570 -0.4416 0.0455  0.0949  358  THR A OG1   
1876 C  CG2   . THR A 255 ? 2.0266 2.0714 1.6861 -0.4405 0.0352  0.0996  358  THR A CG2   
1877 N  N     . GLY A 256 ? 1.7597 1.9568 1.5306 -0.3863 0.0198  0.1052  359  GLY A N     
1878 C  CA    . GLY A 256 ? 1.6826 1.9411 1.4927 -0.3780 0.0176  0.1063  359  GLY A CA    
1879 C  C     . GLY A 256 ? 1.6197 1.8748 1.4377 -0.3753 -0.0011 0.1003  359  GLY A C     
1880 O  O     . GLY A 256 ? 1.5704 1.7780 1.3696 -0.3695 -0.0127 0.0994  359  GLY A O     
1881 N  N     . ILE A 257 ? 1.3387 1.6445 1.1850 -0.3806 -0.0037 0.0966  360  ILE A N     
1882 C  CA    . ILE A 257 ? 1.6371 1.9460 1.4937 -0.3788 -0.0180 0.0901  360  ILE A CA    
1883 C  C     . ILE A 257 ? 1.6001 1.9486 1.4803 -0.3604 -0.0207 0.0971  360  ILE A C     
1884 O  O     . ILE A 257 ? 1.3953 1.7986 1.2987 -0.3606 -0.0142 0.1025  360  ILE A O     
1885 C  CB    . ILE A 257 ? 1.5396 1.8718 1.4051 -0.4007 -0.0187 0.0795  360  ILE A CB    
1886 C  CG1   . ILE A 257 ? 1.4919 1.7722 1.3334 -0.4161 -0.0195 0.0714  360  ILE A CG1   
1887 C  CG2   . ILE A 257 ? 1.6755 2.0301 1.5580 -0.3980 -0.0286 0.0742  360  ILE A CG2   
1888 C  CD1   . ILE A 257 ? 1.4769 1.7437 1.3016 -0.4275 -0.0076 0.0740  360  ILE A CD1   
1889 N  N     . TYR A 258 ? 1.5966 1.9183 1.4727 -0.3447 -0.0306 0.0981  361  TYR A N     
1890 C  CA    . TYR A 258 ? 1.6357 1.9865 1.5306 -0.3257 -0.0329 0.1054  361  TYR A CA    
1891 C  C     . TYR A 258 ? 1.6313 1.9788 1.5345 -0.3221 -0.0458 0.0991  361  TYR A C     
1892 O  O     . TYR A 258 ? 1.6255 1.9354 1.5177 -0.3293 -0.0530 0.0908  361  TYR A O     
1893 C  CB    . TYR A 258 ? 1.5986 1.9190 1.4800 -0.3077 -0.0294 0.1143  361  TYR A CB    
1894 C  CG    . TYR A 258 ? 1.6177 1.9499 1.4969 -0.3071 -0.0123 0.1219  361  TYR A CG    
1895 C  CD1   . TYR A 258 ? 1.5359 1.8409 1.3932 -0.3215 -0.0042 0.1192  361  TYR A CD1   
1896 C  CD2   . TYR A 258 ? 1.6685 2.0376 1.5686 -0.2919 -0.0029 0.1323  361  TYR A CD2   
1897 C  CE1   . TYR A 258 ? 1.5584 1.8728 1.4145 -0.3212 0.0140  0.1257  361  TYR A CE1   
1898 C  CE2   . TYR A 258 ? 1.6279 2.0069 1.5298 -0.2905 0.0156  0.1396  361  TYR A CE2   
1899 C  CZ    . TYR A 258 ? 1.6083 1.9597 1.4879 -0.3054 0.0245  0.1357  361  TYR A CZ    
1900 O  OH    . TYR A 258 ? 1.9406 2.3005 1.8227 -0.3043 0.0454  0.1425  361  TYR A OH    
1901 N  N     . HIS A 259 ? 1.5043 1.8918 1.4287 -0.3107 -0.0476 0.1040  362  HIS A N     
1902 C  CA    . HIS A 259 ? 1.4031 1.7906 1.3365 -0.3048 -0.0576 0.0994  362  HIS A CA    
1903 C  C     . HIS A 259 ? 1.6828 2.0689 1.6220 -0.2813 -0.0594 0.1093  362  HIS A C     
1904 O  O     . HIS A 259 ? 1.3842 1.8132 1.3423 -0.2727 -0.0581 0.1161  362  HIS A O     
1905 C  CB    . HIS A 259 ? 1.2965 1.7350 1.2467 -0.3172 -0.0582 0.0950  362  HIS A CB    
1906 C  CG    . HIS A 259 ? 1.3949 1.8298 1.3509 -0.3146 -0.0658 0.0881  362  HIS A CG    
1907 N  ND1   . HIS A 259 ? 1.1236 1.5952 1.0953 -0.3046 -0.0685 0.0938  362  HIS A ND1   
1908 C  CD2   . HIS A 259 ? 1.6459 2.0441 1.5953 -0.3206 -0.0700 0.0765  362  HIS A CD2   
1909 C  CE1   . HIS A 259 ? 1.4036 1.8605 1.3758 -0.3054 -0.0733 0.0849  362  HIS A CE1   
1910 N  NE2   . HIS A 259 ? 1.3678 1.7806 1.3284 -0.3146 -0.0737 0.0743  362  HIS A NE2   
1911 N  N     . GLY A 260 ? 1.6440 1.9796 1.5662 -0.2719 -0.0629 0.1109  363  GLY A N     
1912 C  CA    . GLY A 260 ? 1.6227 1.9499 1.5457 -0.2515 -0.0635 0.1198  363  GLY A CA    
1913 C  C     . GLY A 260 ? 1.7810 2.1099 1.6961 -0.2455 -0.0508 0.1290  363  GLY A C     
1914 O  O     . GLY A 260 ? 2.0544 2.3387 1.9444 -0.2466 -0.0490 0.1296  363  GLY A O     
1915 N  N     . GLY A 261 ? 1.3767 1.7561 1.3131 -0.2397 -0.0415 0.1368  364  GLY A N     
1916 C  CA    . GLY A 261 ? 1.5058 1.8915 1.4410 -0.2335 -0.0258 0.1459  364  GLY A CA    
1917 C  C     . GLY A 261 ? 1.7272 2.1661 1.6838 -0.2432 -0.0161 0.1498  364  GLY A C     
1918 O  O     . GLY A 261 ? 1.6493 2.0939 1.6069 -0.2422 -0.0009 0.1562  364  GLY A O     
1919 N  N     . GLU A 262 ? 1.8154 2.2934 1.7893 -0.2537 -0.0245 0.1461  365  GLU A N     
1920 C  CA    . GLU A 262 ? 1.6441 2.1770 1.6395 -0.2663 -0.0192 0.1499  365  GLU A CA    
1921 C  C     . GLU A 262 ? 1.8163 2.3320 1.7953 -0.2889 -0.0179 0.1395  365  GLU A C     
1922 O  O     . GLU A 262 ? 1.8100 2.2917 1.7709 -0.2988 -0.0272 0.1274  365  GLU A O     
1923 C  CB    . GLU A 262 ? 1.6006 2.1820 1.6176 -0.2698 -0.0298 0.1508  365  GLU A CB    
1924 C  CG    . GLU A 262 ? 1.9119 2.5520 1.9501 -0.2865 -0.0282 0.1550  365  GLU A CG    
1925 C  CD    . GLU A 262 ? 2.0507 2.7326 2.1020 -0.2941 -0.0405 0.1544  365  GLU A CD    
1926 O  OE1   . GLU A 262 ? 1.9624 2.6282 2.0081 -0.2845 -0.0482 0.1511  365  GLU A OE1   
1927 O  OE2   . GLU A 262 ? 1.7092 2.4396 1.7753 -0.3110 -0.0423 0.1574  365  GLU A OE2   
1928 N  N     . PRO A 263 ? 1.5826 2.1201 1.5694 -0.2973 -0.0056 0.1442  366  PRO A N     
1929 C  CA    . PRO A 263 ? 1.6008 2.1238 1.5725 -0.3199 -0.0036 0.1344  366  PRO A CA    
1930 C  C     . PRO A 263 ? 1.6460 2.2151 1.6336 -0.3399 -0.0105 0.1297  366  PRO A C     
1931 O  O     . PRO A 263 ? 1.5003 2.1272 1.5161 -0.3389 -0.0123 0.1384  366  PRO A O     
1932 C  CB    . PRO A 263 ? 1.6853 2.2126 1.6601 -0.3189 0.0149  0.1427  366  PRO A CB    
1933 C  CG    . PRO A 263 ? 1.5062 2.0747 1.5114 -0.2990 0.0223  0.1582  366  PRO A CG    
1934 C  CD    . PRO A 263 ? 1.4556 2.0347 1.4691 -0.2865 0.0080  0.1594  366  PRO A CD    
1935 N  N     . LEU A 264 ? 1.5539 2.0951 1.5217 -0.3592 -0.0145 0.1159  367  LEU A N     
1936 C  CA    . LEU A 264 ? 1.6285 2.2040 1.6042 -0.3821 -0.0198 0.1084  367  LEU A CA    
1937 C  C     . LEU A 264 ? 1.7277 2.3375 1.7145 -0.3996 -0.0104 0.1116  367  LEU A C     
1938 O  O     . LEU A 264 ? 1.6648 2.3267 1.6699 -0.4149 -0.0143 0.1127  367  LEU A O     
1939 C  CB    . LEU A 264 ? 1.6864 2.2149 1.6378 -0.3954 -0.0263 0.0916  367  LEU A CB    
1940 C  CG    . LEU A 264 ? 1.5816 2.0916 1.5297 -0.3867 -0.0370 0.0855  367  LEU A CG    
1941 C  CD1   . LEU A 264 ? 1.6607 2.1303 1.6012 -0.3621 -0.0391 0.0911  367  LEU A CD1   
1942 C  CD2   . LEU A 264 ? 1.6519 2.1287 1.5840 -0.4052 -0.0399 0.0690  367  LEU A CD2   
1943 N  N     . CYS A 265 ? 1.9073 2.4888 1.8827 -0.3991 0.0017  0.1134  368  CYS A N     
1944 C  CA    . CYS A 265 ? 1.5048 2.1144 1.4908 -0.4158 0.0127  0.1161  368  CYS A CA    
1945 C  C     . CYS A 265 ? 1.5826 2.1764 1.5681 -0.4019 0.0293  0.1261  368  CYS A C     
1946 O  O     . CYS A 265 ? 1.5281 2.0857 1.5005 -0.3817 0.0313  0.1293  368  CYS A O     
1947 C  CB    . CYS A 265 ? 1.5319 2.1120 1.4948 -0.4413 0.0121  0.1011  368  CYS A CB    
1948 S  SG    . CYS A 265 ? 1.8847 2.3744 1.8051 -0.4366 0.0115  0.0911  368  CYS A SG    
1949 N  N     . ASP A 266 ? 1.7146 2.3349 1.7138 -0.4140 0.0423  0.1305  369  ASP A N     
1950 C  CA    . ASP A 266 ? 1.5469 2.1518 1.5455 -0.4033 0.0620  0.1390  369  ASP A CA    
1951 C  C     . ASP A 266 ? 1.5386 2.0655 1.4909 -0.4049 0.0663  0.1295  369  ASP A C     
1952 O  O     . ASP A 266 ? 1.6162 2.1116 1.5443 -0.4219 0.0587  0.1174  369  ASP A O     
1953 C  CB    . ASP A 266 ? 1.5357 2.1874 1.5619 -0.4180 0.0757  0.1454  369  ASP A CB    
1954 C  CG    . ASP A 266 ? 1.6683 2.4005 1.7434 -0.4166 0.0704  0.1586  369  ASP A CG    
1955 O  OD1   . ASP A 266 ? 1.7196 2.4692 1.8036 -0.4051 0.0562  0.1617  369  ASP A OD1   
1956 O  OD2   . ASP A 266 ? 1.8411 2.6195 1.9464 -0.4274 0.0800  0.1667  369  ASP A OD2   
1957 N  N     . ASN A 267 ? 1.9231 2.4179 1.8627 -0.3878 0.0786  0.1356  370  ASN A N     
1958 C  CA    . ASN A 267 ? 1.9769 2.3963 1.8696 -0.3886 0.0809  0.1289  370  ASN A CA    
1959 C  C     . ASN A 267 ? 2.1285 2.5300 2.0043 -0.4104 0.0928  0.1238  370  ASN A C     
1960 O  O     . ASN A 267 ? 2.2110 2.6304 2.0989 -0.4124 0.1133  0.1300  370  ASN A O     
1961 C  CB    . ASN A 267 ? 2.1825 2.5755 2.0647 -0.3678 0.0934  0.1369  370  ASN A CB    
1962 C  CG    . ASN A 267 ? 2.3373 2.6523 2.1688 -0.3671 0.0886  0.1311  370  ASN A CG    
1963 O  OD1   . ASN A 267 ? 2.4955 2.7708 2.2966 -0.3837 0.0890  0.1246  370  ASN A OD1   
1964 N  ND2   . ASN A 267 ? 2.0858 2.3783 1.9081 -0.3486 0.0831  0.1344  370  ASN A ND2   
1965 N  N     . VAL A 268 ? 1.8277 2.1934 1.6774 -0.4264 0.0812  0.1129  371  VAL A N     
1966 C  CA    . VAL A 268 ? 1.6972 2.0405 1.5275 -0.4483 0.0907  0.1073  371  VAL A CA    
1967 C  C     . VAL A 268 ? 2.0632 2.3305 1.8451 -0.4470 0.0939  0.1060  371  VAL A C     
1968 O  O     . VAL A 268 ? 2.0165 2.2404 1.7748 -0.4415 0.0775  0.1030  371  VAL A O     
1969 C  CB    . VAL A 268 ? 1.5190 1.8695 1.3509 -0.4685 0.0774  0.0965  371  VAL A CB    
1970 C  CG1   . VAL A 268 ? 1.5785 1.9031 1.3895 -0.4913 0.0880  0.0910  371  VAL A CG1   
1971 C  CG2   . VAL A 268 ? 1.6836 2.1086 1.5586 -0.4725 0.0728  0.0979  371  VAL A CG2   
1972 N  N     . ASN A 269 ? 2.2592 2.5102 2.0263 -0.4531 0.1148  0.1090  372  ASN A N     
1973 C  CA    . ASN A 269 ? 2.1395 2.3182 1.8562 -0.4550 0.1197  0.1088  372  ASN A CA    
1974 C  C     . ASN A 269 ? 2.1059 2.2596 1.8000 -0.4788 0.1292  0.1039  372  ASN A C     
1975 O  O     . ASN A 269 ? 1.9569 2.1526 1.6770 -0.4927 0.1367  0.1014  372  ASN A O     
1976 C  CB    . ASN A 269 ? 2.0184 2.1884 1.7286 -0.4401 0.1395  0.1166  372  ASN A CB    
1977 C  CG    . ASN A 269 ? 2.1769 2.4078 1.9300 -0.4381 0.1624  0.1225  372  ASN A CG    
1978 O  OD1   . ASN A 269 ? 2.2521 2.5251 2.0322 -0.4522 0.1653  0.1208  372  ASN A OD1   
1979 N  ND2   . ASN A 269 ? 2.0776 2.3135 1.8387 -0.4207 0.1792  0.1301  372  ASN A ND2   
1980 N  N     . THR A 270 ? 2.1024 2.1863 1.7463 -0.4847 0.1281  0.1032  373  THR A N     
1981 C  CA    . THR A 270 ? 2.0555 2.1055 1.6708 -0.5071 0.1360  0.0995  373  THR A CA    
1982 C  C     . THR A 270 ? 2.2948 2.3345 1.8947 -0.5117 0.1653  0.1032  373  THR A C     
1983 O  O     . THR A 270 ? 2.1937 2.2499 1.8051 -0.4968 0.1799  0.1086  373  THR A O     
1984 C  CB    . THR A 270 ? 1.8296 1.8088 1.3992 -0.5126 0.1172  0.0985  373  THR A CB    
1985 O  OG1   . THR A 270 ? 2.8319 2.7761 2.3721 -0.5346 0.1256  0.0961  373  THR A OG1   
1986 C  CG2   . THR A 270 ? 1.7605 1.6927 1.2945 -0.4996 0.1148  0.1048  373  THR A CG2   
1987 N  N     . GLN A 271 ? 2.3957 2.4061 1.9696 -0.5326 0.1757  0.1003  374  GLN A N     
1988 C  CA    . GLN A 271 ? 2.2464 2.2439 1.8038 -0.5397 0.2059  0.1028  374  GLN A CA    
1989 C  C     . GLN A 271 ? 2.4651 2.3999 1.9719 -0.5323 0.2112  0.1068  374  GLN A C     
1990 O  O     . GLN A 271 ? 2.5355 2.4211 2.0067 -0.5300 0.1894  0.1075  374  GLN A O     
1991 C  CB    . GLN A 271 ? 2.2068 2.1834 1.7447 -0.5654 0.2144  0.0984  374  GLN A CB    
1992 N  N     . ARG A 272 ? 2.6235 2.5600 2.1279 -0.5294 0.2413  0.1096  375  ARG A N     
1993 C  CA    . ARG A 272 ? 2.5626 2.4399 2.0170 -0.5243 0.2517  0.1123  375  ARG A CA    
1994 C  C     . ARG A 272 ? 2.4289 2.2349 1.8191 -0.5469 0.2559  0.1106  375  ARG A C     
1995 O  O     . ARG A 272 ? 2.6009 2.3953 1.9765 -0.5596 0.2850  0.1097  375  ARG A O     
1996 C  CB    . ARG A 272 ? 2.4594 2.3642 1.9373 -0.5127 0.2856  0.1156  375  ARG A CB    
1997 C  CG    . ARG A 272 ? 2.4492 2.4282 1.9942 -0.4908 0.2826  0.1196  375  ARG A CG    
1998 C  CD    . ARG A 272 ? 2.1406 2.1394 1.7075 -0.4778 0.3174  0.1247  375  ARG A CD    
1999 N  NE    . ARG A 272 ? 2.4476 2.4529 2.0201 -0.4922 0.3498  0.1244  375  ARG A NE    
2000 C  CZ    . ARG A 272 ? 2.2701 2.3446 1.9030 -0.4943 0.3607  0.1276  375  ARG A CZ    
2001 N  NH1   . ARG A 272 ? 2.0444 2.1879 1.7349 -0.4841 0.3416  0.1314  375  ARG A NH1   
2002 N  NH2   . ARG A 272 ? 2.3452 2.4195 1.9799 -0.5082 0.3914  0.1274  375  ARG A NH2   
2003 N  N     . VAL A 273 ? 2.4284 2.1861 1.7808 -0.5522 0.2268  0.1112  376  VAL A N     
2004 C  CA    . VAL A 273 ? 2.5944 2.2804 1.8826 -0.5734 0.2257  0.1121  376  VAL A CA    
2005 C  C     . VAL A 273 ? 2.7526 2.3792 1.9834 -0.5728 0.2362  0.1153  376  VAL A C     
2006 O  O     . VAL A 273 ? 2.7785 2.4104 2.0156 -0.5549 0.2310  0.1171  376  VAL A O     
2007 C  CB    . VAL A 273 ? 2.5512 2.2111 1.8271 -0.5793 0.1897  0.1137  376  VAL A CB    
2008 C  CG1   . VAL A 273 ? 2.8446 2.5609 2.1750 -0.5813 0.1822  0.1087  376  VAL A CG1   
2009 C  CG2   . VAL A 273 ? 2.5144 2.1580 1.7839 -0.5627 0.1624  0.1180  376  VAL A CG2   
2010 N  N     . PRO A 274 ? 2.7515 2.3199 1.9239 -0.5928 0.2518  0.1158  377  PRO A N     
2011 C  CA    . PRO A 274 ? 2.8166 2.3235 1.9271 -0.5955 0.2624  0.1180  377  PRO A CA    
2012 C  C     . PRO A 274 ? 2.8526 2.3117 1.9241 -0.5942 0.2252  0.1239  377  PRO A C     
2013 O  O     . PRO A 274 ? 2.8114 2.2753 1.8973 -0.5937 0.1928  0.1271  377  PRO A O     
2014 C  CB    . PRO A 274 ? 3.0639 2.5227 2.1225 -0.6209 0.2867  0.1169  377  PRO A CB    
2015 C  CG    . PRO A 274 ? 2.6836 2.1568 1.7603 -0.6332 0.2719  0.1168  377  PRO A CG    
2016 C  CD    . PRO A 274 ? 2.6473 2.2028 1.8057 -0.6154 0.2628  0.1139  377  PRO A CD    
2017 N  N     . CYS A 275 ? 3.0177 2.4294 2.0397 -0.5941 0.2313  0.1256  378  CYS A N     
2018 C  CA    . CYS A 275 ? 2.9655 2.3283 1.9457 -0.5953 0.1969  0.1324  378  CYS A CA    
2019 C  C     . CYS A 275 ? 3.3193 2.6214 2.2432 -0.6198 0.1782  0.1390  378  CYS A C     
2020 O  O     . CYS A 275 ? 3.3679 2.6553 2.2725 -0.6375 0.1969  0.1373  378  CYS A O     
2021 C  CB    . CYS A 275 ? 2.8519 2.1763 1.7883 -0.5925 0.2105  0.1319  378  CYS A CB    
2022 S  SG    . CYS A 275 ? 2.6110 2.0005 1.6119 -0.5620 0.2300  0.1266  378  CYS A SG    
2023 N  N     . SER A 276 ? 3.1715 2.4394 2.0715 -0.6207 0.1402  0.1478  379  SER A N     
2024 C  CA    . SER A 276 ? 3.3219 2.5333 2.1737 -0.6413 0.1147  0.1579  379  SER A CA    
2025 C  C     . SER A 276 ? 3.1666 2.4044 2.0560 -0.6457 0.1079  0.1580  379  SER A C     
2026 O  O     . SER A 276 ? 2.8944 2.0872 1.7475 -0.6636 0.0917  0.1665  379  SER A O     
2027 C  CB    . SER A 276 ? 2.9397 2.0799 1.7066 -0.6669 0.1331  0.1600  379  SER A CB    
2028 O  OG    . SER A 276 ? 2.7778 1.8640 1.4984 -0.6872 0.1064  0.1719  379  SER A OG    
2029 N  N     . ASN A 277 ? 3.1837 2.4923 2.1439 -0.6308 0.1197  0.1493  380  ASN A N     
2030 C  CA    . ASN A 277 ? 3.2042 2.5425 2.2043 -0.6346 0.1139  0.1475  380  ASN A CA    
2031 C  C     . ASN A 277 ? 3.4373 2.8378 2.5088 -0.6121 0.0970  0.1441  380  ASN A C     
2032 O  O     . ASN A 277 ? 3.1928 2.6559 2.3174 -0.6027 0.1146  0.1352  380  ASN A O     
2033 C  CB    . ASN A 277 ? 3.0631 2.4249 2.0729 -0.6454 0.1506  0.1390  380  ASN A CB    
2034 N  N     . PRO A 278 ? 3.6577 3.0431 2.7325 -0.6039 0.0627  0.1516  381  PRO A N     
2035 C  CA    . PRO A 278 ? 3.2629 2.7032 2.4022 -0.5827 0.0471  0.1482  381  PRO A CA    
2036 C  C     . PRO A 278 ? 3.2983 2.7664 2.4792 -0.5860 0.0405  0.1447  381  PRO A C     
2037 O  O     . PRO A 278 ? 3.3870 2.8490 2.5861 -0.5814 0.0140  0.1493  381  PRO A O     
2038 C  CB    . PRO A 278 ? 3.2484 2.6519 2.3679 -0.5758 0.0148  0.1588  381  PRO A CB    
2039 C  CG    . PRO A 278 ? 3.2829 2.6162 2.3410 -0.5974 0.0032  0.1698  381  PRO A CG    
2040 C  CD    . PRO A 278 ? 3.4985 2.8150 2.5176 -0.6145 0.0363  0.1648  381  PRO A CD    
2041 N  N     . ARG A 279 ? 2.8560 2.3543 2.0530 -0.5949 0.0661  0.1362  382  ARG A N     
2042 C  CA    . ARG A 279 ? 2.7931 2.3182 2.0264 -0.6013 0.0643  0.1308  382  ARG A CA    
2043 C  C     . ARG A 279 ? 2.6807 2.2796 1.9665 -0.5947 0.0855  0.1195  382  ARG A C     
2044 O  O     . ARG A 279 ? 2.7469 2.3644 2.0298 -0.5951 0.1110  0.1166  382  ARG A O     
2045 C  CB    . ARG A 279 ? 2.8928 2.3736 2.0876 -0.6255 0.0720  0.1335  382  ARG A CB    
2046 C  CG    . ARG A 279 ? 2.9678 2.3729 2.1042 -0.6351 0.0522  0.1472  382  ARG A CG    
2047 C  CD    . ARG A 279 ? 2.8157 2.2069 1.9703 -0.6265 0.0179  0.1551  382  ARG A CD    
2048 N  NE    . ARG A 279 ? 2.8053 2.1982 1.9831 -0.6353 0.0139  0.1533  382  ARG A NE    
2049 C  CZ    . ARG A 279 ? 2.8767 2.3191 2.1108 -0.6271 0.0145  0.1434  382  ARG A CZ    
2050 N  NH1   . ARG A 279 ? 3.0916 2.5887 2.3662 -0.6095 0.0172  0.1354  382  ARG A NH1   
2051 N  NH2   . ARG A 279 ? 2.9738 2.4087 2.2218 -0.6377 0.0128  0.1417  382  ARG A NH2   
2052 N  N     . TRP A 280 ? 2.4998 2.1399 1.8338 -0.5893 0.0753  0.1137  383  TRP A N     
2053 C  CA    . TRP A 280 ? 2.2813 1.9937 1.6660 -0.5852 0.0910  0.1042  383  TRP A CA    
2054 C  C     . TRP A 280 ? 2.4402 2.1726 1.8515 -0.5981 0.0891  0.0968  383  TRP A C     
2055 O  O     . TRP A 280 ? 2.6909 2.4460 2.1103 -0.6128 0.1087  0.0913  383  TRP A O     
2056 C  CB    . TRP A 280 ? 2.5757 2.3306 1.9969 -0.5619 0.0812  0.1035  383  TRP A CB    
2057 C  CG    . TRP A 280 ? 2.6087 2.3547 2.0110 -0.5492 0.0889  0.1088  383  TRP A CG    
2058 C  CD1   . TRP A 280 ? 2.4517 2.2333 1.8673 -0.5440 0.1135  0.1074  383  TRP A CD1   
2059 C  CD2   . TRP A 280 ? 2.3210 2.0186 1.6887 -0.5406 0.0725  0.1166  383  TRP A CD2   
2060 N  NE1   . TRP A 280 ? 2.0946 1.8502 1.4843 -0.5325 0.1155  0.1127  383  TRP A NE1   
2061 C  CE2   . TRP A 280 ? 2.1685 1.8725 1.5267 -0.5313 0.0898  0.1180  383  TRP A CE2   
2062 C  CE3   . TRP A 280 ? 2.2753 1.9252 1.6209 -0.5405 0.0450  0.1233  383  TRP A CE3   
2063 C  CZ2   . TRP A 280 ? 2.1973 1.8598 1.5204 -0.5235 0.0806  0.1244  383  TRP A CZ2   
2064 C  CZ3   . TRP A 280 ? 2.6111 2.2231 1.9244 -0.5327 0.0337  0.1310  383  TRP A CZ3   
2065 C  CH2   . TRP A 280 ? 2.4045 2.0221 1.7046 -0.5252 0.0515  0.1308  383  TRP A CH2   
2066 N  N     . ASN A 281 ? 2.5222 2.2456 1.9479 -0.5932 0.0667  0.0964  384  ASN A N     
2067 C  CA    . ASN A 281 ? 2.3005 2.0384 1.7511 -0.6048 0.0646  0.0883  384  ASN A CA    
2068 C  C     . ASN A 281 ? 2.3009 2.1117 1.7946 -0.6072 0.0795  0.0777  384  ASN A C     
2069 O  O     . ASN A 281 ? 2.5863 2.4131 2.0851 -0.6256 0.0945  0.0716  384  ASN A O     
2070 C  CB    . ASN A 281 ? 2.3809 2.0702 1.7981 -0.6268 0.0705  0.0901  384  ASN A CB    
2071 C  CG    . ASN A 281 ? 2.8470 2.4646 2.2195 -0.6263 0.0544  0.1031  384  ASN A CG    
2072 O  OD1   . ASN A 281 ? 2.9267 2.5161 2.3031 -0.6224 0.0341  0.1075  384  ASN A OD1   
2073 N  ND2   . ASN A 281 ? 2.9232 2.5105 2.2531 -0.6311 0.0638  0.1099  384  ASN A ND2   
2074 N  N     . GLU A 282 ? 2.3145 2.1700 1.8392 -0.5891 0.0741  0.0767  385  GLU A N     
2075 C  CA    . GLU A 282 ? 2.4083 2.3365 1.9748 -0.5892 0.0850  0.0698  385  GLU A CA    
2076 C  C     . GLU A 282 ? 2.1310 2.0910 1.7310 -0.5767 0.0689  0.0654  385  GLU A C     
2077 O  O     . GLU A 282 ? 2.1609 2.1128 1.7614 -0.5571 0.0563  0.0706  385  GLU A O     
2078 C  CB    . GLU A 282 ? 2.3045 2.2614 1.8751 -0.5794 0.1009  0.0754  385  GLU A CB    
2079 C  CG    . GLU A 282 ? 2.3866 2.4207 2.0060 -0.5713 0.1053  0.0730  385  GLU A CG    
2080 C  CD    . GLU A 282 ? 2.6875 2.7671 2.3331 -0.5915 0.1153  0.0657  385  GLU A CD    
2081 O  OE1   . GLU A 282 ? 2.8531 2.9084 2.4792 -0.6111 0.1264  0.0632  385  GLU A OE1   
2082 O  OE2   . GLU A 282 ? 2.6986 2.8378 2.3831 -0.5891 0.1116  0.0627  385  GLU A OE2   
2083 N  N     . TRP A 283 ? 1.8589 1.8533 1.4847 -0.5893 0.0700  0.0555  386  TRP A N     
2084 C  CA    . TRP A 283 ? 2.0150 2.0452 1.6725 -0.5807 0.0582  0.0497  386  TRP A CA    
2085 C  C     . TRP A 283 ? 1.9462 2.0424 1.6334 -0.5702 0.0637  0.0524  386  TRP A C     
2086 O  O     . TRP A 283 ? 2.3667 2.5118 2.0743 -0.5829 0.0749  0.0492  386  TRP A O     
2087 C  CB    . TRP A 283 ? 2.2412 2.2806 1.9104 -0.6010 0.0591  0.0374  386  TRP A CB    
2088 C  CG    . TRP A 283 ? 2.1558 2.1331 1.8053 -0.6066 0.0513  0.0350  386  TRP A CG    
2089 C  CD1   . TRP A 283 ? 2.2083 2.1370 1.8300 -0.6212 0.0570  0.0366  386  TRP A CD1   
2090 C  CD2   . TRP A 283 ? 2.1980 2.1552 1.8571 -0.5977 0.0374  0.0317  386  TRP A CD2   
2091 N  NE1   . TRP A 283 ? 2.1023 1.9826 1.7173 -0.6211 0.0466  0.0357  386  TRP A NE1   
2092 C  CE2   . TRP A 283 ? 2.2476 2.1445 1.8867 -0.6065 0.0351  0.0325  386  TRP A CE2   
2093 C  CE3   . TRP A 283 ? 2.0075 1.9913 1.6912 -0.5830 0.0275  0.0287  386  TRP A CE3   
2094 C  CZ2   . TRP A 283 ? 2.3358 2.1997 1.9826 -0.6003 0.0241  0.0309  386  TRP A CZ2   
2095 C  CZ3   . TRP A 283 ? 2.0461 1.9962 1.7350 -0.5776 0.0173  0.0258  386  TRP A CZ3   
2096 C  CH2   . TRP A 283 ? 2.1788 2.0701 1.8512 -0.5858 0.0160  0.0271  386  TRP A CH2   
2097 N  N     . LEU A 284 ? 1.8254 1.9235 1.5165 -0.5471 0.0555  0.0593  387  LEU A N     
2098 C  CA    . LEU A 284 ? 1.9716 2.1294 1.6923 -0.5344 0.0600  0.0638  387  LEU A CA    
2099 C  C     . LEU A 284 ? 1.8752 2.0863 1.6295 -0.5392 0.0532  0.0565  387  LEU A C     
2100 O  O     . LEU A 284 ? 1.9192 2.1214 1.6778 -0.5321 0.0393  0.0523  387  LEU A O     
2101 C  CB    . LEU A 284 ? 2.1275 2.2682 1.8416 -0.5092 0.0526  0.0722  387  LEU A CB    
2102 C  CG    . LEU A 284 ? 1.7727 1.8777 1.4576 -0.5028 0.0633  0.0809  387  LEU A CG    
2103 C  CD1   . LEU A 284 ? 1.9294 2.0703 1.6257 -0.5108 0.0860  0.0834  387  LEU A CD1   
2104 C  CD2   . LEU A 284 ? 1.8377 1.8699 1.4794 -0.5119 0.0582  0.0812  387  LEU A CD2   
2105 N  N     . ASN A 285 ? 1.7304 1.9967 1.5082 -0.5525 0.0632  0.0553  388  ASN A N     
2106 C  CA    . ASN A 285 ? 1.6437 1.9635 1.4500 -0.5614 0.0568  0.0491  388  ASN A CA    
2107 C  C     . ASN A 285 ? 1.6521 2.0218 1.4866 -0.5414 0.0521  0.0579  388  ASN A C     
2108 O  O     . ASN A 285 ? 1.6375 2.0399 1.4883 -0.5338 0.0622  0.0683  388  ASN A O     
2109 C  CB    . ASN A 285 ? 1.8987 2.2560 1.7172 -0.5875 0.0676  0.0450  388  ASN A CB    
2110 C  CG    . ASN A 285 ? 2.0598 2.3672 1.8501 -0.6079 0.0742  0.0368  388  ASN A CG    
2111 O  OD1   . ASN A 285 ? 2.1723 2.4549 1.9463 -0.6107 0.0863  0.0415  388  ASN A OD1   
2112 N  ND2   . ASN A 285 ? 2.0868 2.3772 1.8704 -0.6225 0.0676  0.0245  388  ASN A ND2   
2113 N  N     . TYR A 286 ? 1.8314 2.2059 1.6728 -0.5327 0.0382  0.0542  389  TYR A N     
2114 C  CA    . TYR A 286 ? 1.4717 1.8899 1.3382 -0.5137 0.0322  0.0625  389  TYR A CA    
2115 C  C     . TYR A 286 ? 1.5181 2.0006 1.4115 -0.5280 0.0276  0.0597  389  TYR A C     
2116 O  O     . TYR A 286 ? 1.7759 2.2593 1.6640 -0.5512 0.0259  0.0480  389  TYR A O     
2117 C  CB    . TYR A 286 ? 1.4406 1.8225 1.2969 -0.4939 0.0197  0.0615  389  TYR A CB    
2118 C  CG    . TYR A 286 ? 1.6315 1.9477 1.4586 -0.4826 0.0204  0.0646  389  TYR A CG    
2119 C  CD1   . TYR A 286 ? 1.5243 1.8345 1.3468 -0.4664 0.0277  0.0757  389  TYR A CD1   
2120 C  CD2   . TYR A 286 ? 1.6914 1.9507 1.4952 -0.4889 0.0140  0.0571  389  TYR A CD2   
2121 C  CE1   . TYR A 286 ? 1.5435 1.7924 1.3346 -0.4590 0.0273  0.0786  389  TYR A CE1   
2122 C  CE2   . TYR A 286 ? 1.8009 2.0015 1.5774 -0.4802 0.0120  0.0620  389  TYR A CE2   
2123 C  CZ    . TYR A 286 ? 1.7148 1.9102 1.4828 -0.4663 0.0180  0.0724  389  TYR A CZ    
2124 O  OH    . TYR A 286 ? 1.8314 1.9668 1.5674 -0.4606 0.0149  0.0773  389  TYR A OH    
2125 N  N     . ASP A 287 ? 1.4329 1.9683 1.3544 -0.5146 0.0256  0.0711  390  ASP A N     
2126 C  CA    . ASP A 287 ? 1.5273 2.1292 1.4755 -0.5276 0.0194  0.0724  390  ASP A CA    
2127 C  C     . ASP A 287 ? 1.6525 2.2550 1.5973 -0.5271 0.0053  0.0643  390  ASP A C     
2128 O  O     . ASP A 287 ? 1.9449 2.6001 1.9073 -0.5383 -0.0017 0.0654  390  ASP A O     
2129 C  CB    . ASP A 287 ? 1.6123 2.2721 1.5953 -0.5130 0.0232  0.0907  390  ASP A CB    
2130 C  CG    . ASP A 287 ? 2.0391 2.7722 2.0522 -0.5325 0.0191  0.0957  390  ASP A CG    
2131 O  OD1   . ASP A 287 ? 2.1704 2.9070 2.1737 -0.5603 0.0159  0.0837  390  ASP A OD1   
2132 O  OD2   . ASP A 287 ? 2.2805 3.0674 2.3274 -0.5208 0.0189  0.1122  390  ASP A OD2   
2133 N  N     . ILE A 288 ? 1.6043 2.1501 1.5274 -0.5154 0.0011  0.0570  391  ILE A N     
2134 C  CA    . ILE A 288 ? 1.6579 2.1995 1.5786 -0.5132 -0.0097 0.0491  391  ILE A CA    
2135 C  C     . ILE A 288 ? 1.6265 2.1446 1.5302 -0.5392 -0.0092 0.0314  391  ILE A C     
2136 O  O     . ILE A 288 ? 1.7080 2.1824 1.5937 -0.5489 -0.0026 0.0245  391  ILE A O     
2137 C  CB    . ILE A 288 ? 1.6913 2.1862 1.6026 -0.4863 -0.0142 0.0515  391  ILE A CB    
2138 C  CG1   . ILE A 288 ? 1.7262 2.1582 1.6142 -0.4834 -0.0089 0.0497  391  ILE A CG1   
2139 C  CG2   . ILE A 288 ? 1.8722 2.3984 1.8025 -0.4619 -0.0160 0.0672  391  ILE A CG2   
2140 N  N     . TYR A 289 ? 1.5991 2.1446 1.5068 -0.5515 -0.0152 0.0240  392  TYR A N     
2141 C  CA    . TYR A 289 ? 1.5929 2.1131 1.4832 -0.5758 -0.0129 0.0055  392  TYR A CA    
2142 C  C     . TYR A 289 ? 1.7583 2.2191 1.6363 -0.5617 -0.0142 -0.0026 392  TYR A C     
2143 O  O     . TYR A 289 ? 2.0768 2.5371 1.9625 -0.5392 -0.0207 0.0033  392  TYR A O     
2144 C  CB    . TYR A 289 ? 1.5873 2.1595 1.4834 -0.5970 -0.0180 0.0006  392  TYR A CB    
2145 C  CG    . TYR A 289 ? 1.7398 2.3040 1.6192 -0.6321 -0.0122 -0.0166 392  TYR A CG    
2146 C  CD1   . TYR A 289 ? 1.9284 2.4855 1.8028 -0.6493 -0.0041 -0.0189 392  TYR A CD1   
2147 C  CD2   . TYR A 289 ? 1.8977 2.4607 1.7651 -0.6493 -0.0133 -0.0311 392  TYR A CD2   
2148 C  CE1   . TYR A 289 ? 2.3214 2.8697 2.1799 -0.6825 0.0020  -0.0351 392  TYR A CE1   
2149 C  CE2   . TYR A 289 ? 1.9189 2.4716 1.7685 -0.6830 -0.0063 -0.0480 392  TYR A CE2   
2150 C  CZ    . TYR A 289 ? 2.3247 2.8704 2.1704 -0.6994 0.0010  -0.0499 392  TYR A CZ    
2151 O  OH    . TYR A 289 ? 2.5728 3.1067 2.4001 -0.7338 0.0088  -0.0671 392  TYR A OH    
2152 N  N     . ILE A 290 ? 1.5362 1.9466 1.3973 -0.5749 -0.0075 -0.0154 393  ILE A N     
2153 C  CA    . ILE A 290 ? 1.6289 1.9802 1.4830 -0.5608 -0.0081 -0.0208 393  ILE A CA    
2154 C  C     . ILE A 290 ? 1.7153 2.0737 1.5747 -0.5578 -0.0114 -0.0283 393  ILE A C     
2155 O  O     . ILE A 290 ? 1.6046 1.9410 1.4704 -0.5340 -0.0166 -0.0235 393  ILE A O     
2156 C  CB    . ILE A 290 ? 1.5201 1.8186 1.3583 -0.5768 0.0006  -0.0316 393  ILE A CB    
2157 C  CG1   . ILE A 290 ? 1.7266 2.0085 1.5573 -0.5740 0.0030  -0.0217 393  ILE A CG1   
2158 C  CG2   . ILE A 290 ? 1.6894 1.9313 1.5263 -0.5647 0.0003  -0.0371 393  ILE A CG2   
2159 C  CD1   . ILE A 290 ? 2.0524 2.2832 1.8670 -0.5899 0.0113  -0.0301 393  ILE A CD1   
2160 N  N     . PRO A 291 ? 1.5301 1.9169 1.3857 -0.5816 -0.0084 -0.0400 394  PRO A N     
2161 C  CA    . PRO A 291 ? 1.5590 1.9537 1.4171 -0.5786 -0.0106 -0.0464 394  PRO A CA    
2162 C  C     . PRO A 291 ? 1.5459 1.9846 1.4194 -0.5576 -0.0214 -0.0315 394  PRO A C     
2163 O  O     . PRO A 291 ? 1.6762 2.1203 1.5517 -0.5527 -0.0237 -0.0351 394  PRO A O     
2164 C  CB    . PRO A 291 ? 1.4721 1.8907 1.3172 -0.6139 -0.0049 -0.0613 394  PRO A CB    
2165 C  CG    . PRO A 291 ? 1.3855 1.7825 1.2201 -0.6335 0.0034  -0.0677 394  PRO A CG    
2166 C  CD    . PRO A 291 ? 1.6914 2.0937 1.5360 -0.6151 -0.0013 -0.0505 394  PRO A CD    
2167 N  N     . ASP A 292 ? 1.5267 1.9952 1.4113 -0.5452 -0.0266 -0.0149 395  ASP A N     
2168 C  CA    . ASP A 292 ? 1.7357 2.2455 1.6367 -0.5247 -0.0353 0.0004  395  ASP A CA    
2169 C  C     . ASP A 292 ? 1.6272 2.1054 1.5346 -0.4923 -0.0384 0.0111  395  ASP A C     
2170 O  O     . ASP A 292 ? 1.3815 1.8885 1.3024 -0.4732 -0.0441 0.0243  395  ASP A O     
2171 C  CB    . ASP A 292 ? 1.4975 2.0672 1.4111 -0.5324 -0.0376 0.0131  395  ASP A CB    
2172 C  CG    . ASP A 292 ? 1.6127 2.2268 1.5232 -0.5634 -0.0393 0.0063  395  ASP A CG    
2173 O  OD1   . ASP A 292 ? 2.1043 2.7013 1.9996 -0.5894 -0.0328 -0.0078 395  ASP A OD1   
2174 O  OD2   . ASP A 292 ? 1.9012 2.5668 1.8236 -0.5628 -0.0475 0.0156  395  ASP A OD2   
2175 N  N     . LEU A 293 ? 1.4660 1.8861 1.3637 -0.4866 -0.0352 0.0065  396  LEU A N     
2176 C  CA    . LEU A 293 ? 1.5759 1.9632 1.4766 -0.4587 -0.0398 0.0164  396  LEU A CA    
2177 C  C     . LEU A 293 ? 1.5896 1.9680 1.4981 -0.4440 -0.0447 0.0143  396  LEU A C     
2178 O  O     . LEU A 293 ? 1.5069 1.8586 1.4121 -0.4526 -0.0414 0.0013  396  LEU A O     
2179 C  CB    . LEU A 293 ? 1.4937 1.8217 1.3812 -0.4594 -0.0371 0.0136  396  LEU A CB    
2180 C  CG    . LEU A 293 ? 1.4156 1.7431 1.2930 -0.4701 -0.0317 0.0176  396  LEU A CG    
2181 C  CD1   . LEU A 293 ? 1.4038 1.6685 1.2660 -0.4720 -0.0302 0.0149  396  LEU A CD1   
2182 C  CD2   . LEU A 293 ? 1.4868 1.8403 1.3700 -0.4538 -0.0329 0.0334  396  LEU A CD2   
2183 N  N     . PRO A 294 ? 1.4767 1.8750 1.3962 -0.4222 -0.0508 0.0263  397  PRO A N     
2184 C  CA    . PRO A 294 ? 1.5931 1.9823 1.5205 -0.4081 -0.0550 0.0246  397  PRO A CA    
2185 C  C     . PRO A 294 ? 1.6170 1.9456 1.5429 -0.3963 -0.0568 0.0222  397  PRO A C     
2186 O  O     . PRO A 294 ? 1.4753 1.7687 1.3925 -0.3968 -0.0567 0.0241  397  PRO A O     
2187 C  CB    . PRO A 294 ? 1.5386 1.9626 1.4776 -0.3876 -0.0604 0.0402  397  PRO A CB    
2188 C  CG    . PRO A 294 ? 1.3232 1.7488 1.2589 -0.3838 -0.0585 0.0505  397  PRO A CG    
2189 C  CD    . PRO A 294 ? 1.4484 1.8770 1.3746 -0.4094 -0.0524 0.0421  397  PRO A CD    
2190 N  N     . ARG A 295 ? 1.6837 2.0006 1.6191 -0.3859 -0.0589 0.0189  398  ARG A N     
2191 C  CA    . ARG A 295 ? 1.5800 1.8427 1.5201 -0.3749 -0.0615 0.0177  398  ARG A CA    
2192 C  C     . ARG A 295 ? 1.3048 1.5463 1.2437 -0.3549 -0.0706 0.0324  398  ARG A C     
2193 O  O     . ARG A 295 ? 1.2177 1.4130 1.1542 -0.3514 -0.0745 0.0344  398  ARG A O     
2194 C  CB    . ARG A 295 ? 1.5002 1.7593 1.4540 -0.3679 -0.0603 0.0116  398  ARG A CB    
2195 C  CG    . ARG A 295 ? 1.2824 1.4884 1.2477 -0.3581 -0.0619 0.0103  398  ARG A CG    
2196 C  CD    . ARG A 295 ? 1.4080 1.5775 1.3673 -0.3735 -0.0562 0.0028  398  ARG A CD    
2197 N  NE    . ARG A 295 ? 1.5957 1.7150 1.5689 -0.3618 -0.0608 0.0069  398  ARG A NE    
2198 C  CZ    . ARG A 295 ? 1.5462 1.6411 1.5179 -0.3489 -0.0730 0.0209  398  ARG A CZ    
2199 N  NH1   . ARG A 295 ? 1.4642 1.5767 1.4197 -0.3451 -0.0794 0.0307  398  ARG A NH1   
2200 N  NH2   . ARG A 295 ? 1.6996 1.7509 1.6865 -0.3402 -0.0787 0.0256  398  ARG A NH2   
2201 N  N     . ALA A 296 ? 1.5113 1.7847 1.4510 -0.3427 -0.0739 0.0433  399  ALA A N     
2202 C  CA    . ALA A 296 ? 1.4958 1.7494 1.4303 -0.3255 -0.0805 0.0563  399  ALA A CA    
2203 C  C     . ALA A 296 ? 1.4826 1.7433 1.4021 -0.3320 -0.0765 0.0621  399  ALA A C     
2204 O  O     . ALA A 296 ? 1.5444 1.8091 1.4594 -0.3192 -0.0775 0.0729  399  ALA A O     
2205 C  CB    . ALA A 296 ? 1.3316 1.6089 1.2770 -0.3061 -0.0843 0.0647  399  ALA A CB    
2206 N  N     . ALA A 297 ? 1.5933 1.8540 1.5048 -0.3521 -0.0703 0.0545  400  ALA A N     
2207 C  CA    . ALA A 297 ? 1.5117 1.7784 1.4099 -0.3599 -0.0648 0.0593  400  ALA A CA    
2208 C  C     . ALA A 297 ? 1.4688 1.6839 1.3494 -0.3529 -0.0691 0.0662  400  ALA A C     
2209 O  O     . ALA A 297 ? 1.4249 1.5955 1.3013 -0.3539 -0.0753 0.0636  400  ALA A O     
2210 C  CB    . ALA A 297 ? 1.5408 1.8177 1.4347 -0.3848 -0.0574 0.0489  400  ALA A CB    
2211 N  N     . ARG A 298 ? 1.3852 1.6055 1.2554 -0.3466 -0.0655 0.0758  401  ARG A N     
2212 C  CA    . ARG A 298 ? 1.4404 1.6124 1.2881 -0.3412 -0.0692 0.0831  401  ARG A CA    
2213 C  C     . ARG A 298 ? 1.6892 1.8609 1.5190 -0.3530 -0.0583 0.0852  401  ARG A C     
2214 O  O     . ARG A 298 ? 1.6516 1.8683 1.4912 -0.3574 -0.0477 0.0856  401  ARG A O     
2215 C  CB    . ARG A 298 ? 1.7007 1.8687 1.5480 -0.3204 -0.0737 0.0927  401  ARG A CB    
2216 C  CG    . ARG A 298 ? 1.8357 2.0017 1.7006 -0.3076 -0.0842 0.0917  401  ARG A CG    
2217 C  CD    . ARG A 298 ? 1.9069 2.0786 1.7731 -0.2884 -0.0858 0.1008  401  ARG A CD    
2218 N  NE    . ARG A 298 ? 2.1360 2.2704 1.9750 -0.2857 -0.0859 0.1084  401  ARG A NE    
2219 C  CZ    . ARG A 298 ? 2.1513 2.2807 1.9834 -0.2716 -0.0850 0.1161  401  ARG A CZ    
2220 N  NH1   . ARG A 298 ? 2.4680 2.6284 2.3206 -0.2572 -0.0843 0.1183  401  ARG A NH1   
2221 N  NH2   . ARG A 298 ? 1.9319 2.0225 1.7338 -0.2731 -0.0839 0.1215  401  ARG A NH2   
2222 N  N     . LEU A 299 ? 1.6579 1.7789 1.4624 -0.3585 -0.0613 0.0876  402  LEU A N     
2223 C  CA    . LEU A 299 ? 1.3622 1.4727 1.1443 -0.3693 -0.0505 0.0904  402  LEU A CA    
2224 C  C     . LEU A 299 ? 1.4453 1.5281 1.2048 -0.3576 -0.0501 0.1002  402  LEU A C     
2225 O  O     . LEU A 299 ? 1.6294 1.6710 1.3759 -0.3502 -0.0632 0.1046  402  LEU A O     
2226 C  CB    . LEU A 299 ? 1.4518 1.5218 1.2165 -0.3867 -0.0527 0.0862  402  LEU A CB    
2227 C  CG    . LEU A 299 ? 1.4479 1.4994 1.1854 -0.3995 -0.0417 0.0889  402  LEU A CG    
2228 C  CD1   . LEU A 299 ? 1.5442 1.6486 1.2960 -0.4084 -0.0251 0.0853  402  LEU A CD1   
2229 C  CD2   . LEU A 299 ? 1.4284 1.4325 1.1474 -0.4147 -0.0467 0.0866  402  LEU A CD2   
2230 N  N     . CYS A 300 ? 1.3856 1.4904 1.1411 -0.3568 -0.0346 0.1040  403  CYS A N     
2231 C  CA    . CYS A 300 ? 1.9230 2.0034 1.6560 -0.3468 -0.0293 0.1120  403  CYS A CA    
2232 C  C     . CYS A 300 ? 1.8789 1.9322 1.5812 -0.3610 -0.0163 0.1132  403  CYS A C     
2233 O  O     . CYS A 300 ? 1.6670 1.7530 1.3799 -0.3698 -0.0009 0.1111  403  CYS A O     
2234 C  CB    . CYS A 300 ? 1.9729 2.1002 1.7296 -0.3311 -0.0188 0.1164  403  CYS A CB    
2235 S  SG    . CYS A 300 ? 1.5529 1.7145 1.3443 -0.3151 -0.0324 0.1156  403  CYS A SG    
2236 N  N     . LEU A 301 ? 1.7882 1.7821 1.4523 -0.3641 -0.0228 0.1171  404  LEU A N     
2237 C  CA    . LEU A 301 ? 1.9487 1.9074 1.5763 -0.3789 -0.0115 0.1185  404  LEU A CA    
2238 C  C     . LEU A 301 ? 2.1197 2.0469 1.7152 -0.3723 -0.0033 0.1246  404  LEU A C     
2239 O  O     . LEU A 301 ? 2.3665 2.2763 1.9563 -0.3602 -0.0147 0.1284  404  LEU A O     
2240 C  CB    . LEU A 301 ? 2.2695 2.1787 1.8729 -0.3934 -0.0266 0.1183  404  LEU A CB    
2241 C  CG    . LEU A 301 ? 2.1218 2.0495 1.7526 -0.4007 -0.0350 0.1115  404  LEU A CG    
2242 C  CD1   . LEU A 301 ? 1.8933 1.7662 1.4992 -0.4136 -0.0482 0.1138  404  LEU A CD1   
2243 C  CD2   . LEU A 301 ? 1.7968 1.7725 1.4481 -0.4107 -0.0172 0.1047  404  LEU A CD2   
2244 N  N     . SER A 302 ? 2.3873 2.3057 1.9611 -0.3815 0.0180  0.1250  405  SER A N     
2245 C  CA    . SER A 302 ? 2.3157 2.1977 1.8527 -0.3789 0.0305  0.1294  405  SER A CA    
2246 C  C     . SER A 302 ? 2.3186 2.1778 1.8247 -0.3961 0.0511  0.1284  405  SER A C     
2247 O  O     . SER A 302 ? 2.3847 2.2756 1.9113 -0.4051 0.0617  0.1248  405  SER A O     
2248 C  CB    . SER A 302 ? 2.3884 2.3092 1.9520 -0.3598 0.0455  0.1314  405  SER A CB    
2249 O  OG    . SER A 302 ? 2.4145 2.3914 2.0143 -0.3590 0.0659  0.1302  405  SER A OG    
2250 N  N     . ILE A 303 ? 2.2851 2.0881 1.7400 -0.4021 0.0571  0.1314  406  ILE A N     
2251 C  CA    . ILE A 303 ? 2.3098 2.0815 1.7269 -0.4193 0.0783  0.1306  406  ILE A CA    
2252 C  C     . ILE A 303 ? 2.3034 2.0784 1.7138 -0.4115 0.1086  0.1310  406  ILE A C     
2253 O  O     . ILE A 303 ? 2.2533 2.0046 1.6453 -0.4018 0.1074  0.1333  406  ILE A O     
2254 C  CB    . ILE A 303 ? 2.2579 1.9556 1.6144 -0.4363 0.0623  0.1341  406  ILE A CB    
2255 C  CG1   . ILE A 303 ? 2.2238 1.9185 1.5924 -0.4432 0.0347  0.1349  406  ILE A CG1   
2256 C  CG2   . ILE A 303 ? 2.2595 1.9216 1.5718 -0.4547 0.0867  0.1331  406  ILE A CG2   
2257 C  CD1   . ILE A 303 ? 1.6869 1.3122 1.0012 -0.4604 0.0173  0.1410  406  ILE A CD1   
2258 N  N     . CYS A 304 ? 2.3432 2.1470 1.7702 -0.4159 0.1368  0.1290  407  CYS A N     
2259 C  CA    . CYS A 304 ? 2.5403 2.3515 1.9691 -0.4082 0.1702  0.1299  407  CYS A CA    
2260 C  C     . CYS A 304 ? 2.6491 2.4176 2.0331 -0.4274 0.1954  0.1278  407  CYS A C     
2261 O  O     . CYS A 304 ? 2.5383 2.3011 1.9137 -0.4446 0.1928  0.1259  407  CYS A O     
2262 C  CB    . CYS A 304 ? 2.3804 2.2722 1.8790 -0.3938 0.1845  0.1314  407  CYS A CB    
2263 S  SG    . CYS A 304 ? 2.6482 2.5946 2.2001 -0.3739 0.1556  0.1335  407  CYS A SG    
2264 N  N     . SER A 305 ? 2.5315 2.2681 1.8858 -0.4252 0.2214  0.1280  408  SER A N     
2265 C  CA    . SER A 305 ? 2.6027 2.2931 1.9094 -0.4433 0.2496  0.1255  408  SER A CA    
2266 C  C     . SER A 305 ? 2.8384 2.5732 2.1865 -0.4361 0.2899  0.1255  408  SER A C     
2267 O  O     . SER A 305 ? 2.7939 2.5715 2.1873 -0.4152 0.3011  0.1285  408  SER A O     
2268 C  CB    . SER A 305 ? 2.7569 2.3709 1.9927 -0.4498 0.2532  0.1248  408  SER A CB    
2269 O  OG    . SER A 305 ? 2.9569 2.5820 2.2089 -0.4303 0.2673  0.1256  408  SER A OG    
2270 N  N     . VAL A 306 ? 2.8991 2.6238 2.2335 -0.4535 0.3117  0.1231  409  VAL A N     
2271 C  CA    . VAL A 306 ? 2.8535 2.6179 2.2275 -0.4495 0.3516  0.1240  409  VAL A CA    
2272 C  C     . VAL A 306 ? 3.0944 2.7926 2.4075 -0.4642 0.3862  0.1202  409  VAL A C     
2273 O  O     . VAL A 306 ? 3.2886 2.9357 2.5469 -0.4873 0.3830  0.1170  409  VAL A O     
2274 C  CB    . VAL A 306 ? 2.7778 2.5980 2.1985 -0.4578 0.3496  0.1244  409  VAL A CB    
2275 C  CG1   . VAL A 306 ? 2.7647 2.6284 2.2308 -0.4538 0.3906  0.1271  409  VAL A CG1   
2276 C  CG2   . VAL A 306 ? 2.5553 2.4354 2.0290 -0.4461 0.3156  0.1268  409  VAL A CG2   
2277 N  N     . LYS A 307 ? 3.0159 2.7131 2.3377 -0.4514 0.4203  0.1210  410  LYS A N     
2278 C  CA    . LYS A 307 ? 3.0932 2.7261 2.3573 -0.4647 0.4584  0.1163  410  LYS A CA    
2279 C  C     . LYS A 307 ? 2.9333 2.6064 2.2465 -0.4596 0.5051  0.1180  410  LYS A C     
2280 O  O     . LYS A 307 ? 2.7022 2.4181 2.0530 -0.4667 0.5086  0.1195  410  LYS A O     
2281 C  CB    . LYS A 307 ? 2.9082 2.4889 2.1282 -0.4572 0.4635  0.1144  410  LYS A CB    
2282 C  CG    . LYS A 307 ? 2.7404 2.2791 1.9118 -0.4630 0.4181  0.1140  410  LYS A CG    
2283 C  CD    . LYS A 307 ? 2.8607 2.3366 1.9600 -0.4924 0.4034  0.1114  410  LYS A CD    
2284 C  CE    . LYS A 307 ? 2.7908 2.1934 1.8178 -0.5113 0.4407  0.1058  410  LYS A CE    
2285 N  NZ    . LYS A 307 ? 2.8088 2.1495 1.7632 -0.5410 0.4256  0.1048  410  LYS A NZ    
2286 N  N     . LYS A 313 ? 2.1957 2.3936 2.1166 -0.3176 0.6527  0.1976  416  LYS A N     
2287 C  CA    . LYS A 313 ? 2.5185 2.6566 2.3741 -0.3141 0.6292  0.1884  416  LYS A CA    
2288 C  C     . LYS A 313 ? 2.5733 2.7120 2.3980 -0.3282 0.5760  0.1816  416  LYS A C     
2289 O  O     . LYS A 313 ? 2.4532 2.6316 2.3002 -0.3423 0.5601  0.1823  416  LYS A O     
2290 C  CB    . LYS A 313 ? 2.4977 2.5362 2.2684 -0.3256 0.6600  0.1750  416  LYS A CB    
2291 C  CG    . LYS A 313 ? 2.3871 2.3810 2.1028 -0.3556 0.6664  0.1641  416  LYS A CG    
2292 C  CD    . LYS A 313 ? 2.4352 2.3292 2.0637 -0.3681 0.6973  0.1517  416  LYS A CD    
2293 C  CE    . LYS A 313 ? 2.7814 2.6284 2.3506 -0.3990 0.7013  0.1417  416  LYS A CE    
2294 N  NZ    . LYS A 313 ? 2.8836 2.6296 2.3596 -0.4143 0.7283  0.1298  416  LYS A NZ    
2295 N  N     . GLU A 314 ? 2.6333 2.7270 2.4077 -0.3247 0.5497  0.1751  417  GLU A N     
2296 C  CA    . GLU A 314 ? 2.7523 2.8426 2.4990 -0.3356 0.5007  0.1692  417  GLU A CA    
2297 C  C     . GLU A 314 ? 2.7991 2.8077 2.4661 -0.3393 0.4863  0.1593  417  GLU A C     
2298 O  O     . GLU A 314 ? 2.9544 2.9378 2.6113 -0.3241 0.4999  0.1605  417  GLU A O     
2299 C  CB    . GLU A 314 ? 2.7930 2.9632 2.6067 -0.3195 0.4694  0.1792  417  GLU A CB    
2300 C  CG    . GLU A 314 ? 2.7881 2.9666 2.5862 -0.3328 0.4234  0.1734  417  GLU A CG    
2301 C  CD    . GLU A 314 ? 2.8394 3.0416 2.6479 -0.3547 0.4221  0.1709  417  GLU A CD    
2302 O  OE1   . GLU A 314 ? 2.8936 3.1317 2.7438 -0.3558 0.4518  0.1773  417  GLU A OE1   
2303 O  OE2   . GLU A 314 ? 2.8243 3.0088 2.6011 -0.3709 0.3923  0.1629  417  GLU A OE2   
2304 N  N     . GLU A 315 ? 2.7832 2.7508 2.3952 -0.3601 0.4585  0.1505  418  GLU A N     
2305 C  CA    . GLU A 315 ? 2.7898 2.6813 2.3259 -0.3671 0.4392  0.1427  418  GLU A CA    
2306 C  C     . GLU A 315 ? 2.7466 2.6520 2.2812 -0.3715 0.3895  0.1414  418  GLU A C     
2307 O  O     . GLU A 315 ? 2.8571 2.7520 2.3713 -0.3910 0.3745  0.1373  418  GLU A O     
2308 C  CB    . GLU A 315 ? 2.8553 2.6671 2.3144 -0.3909 0.4591  0.1342  418  GLU A CB    
2309 C  CG    . GLU A 315 ? 3.0282 2.8216 2.4856 -0.3895 0.5128  0.1339  418  GLU A CG    
2310 C  CD    . GLU A 315 ? 2.9687 2.8104 2.4747 -0.3953 0.5376  0.1373  418  GLU A CD    
2311 O  OE1   . GLU A 315 ? 2.8775 2.7601 2.4091 -0.4039 0.5123  0.1386  418  GLU A OE1   
2312 O  OE2   . GLU A 315 ? 2.7938 2.6320 2.3134 -0.3919 0.5835  0.1387  418  GLU A OE2   
2313 N  N     . HIS A 316 ? 2.5391 2.4666 2.0959 -0.3536 0.3659  0.1448  419  HIS A N     
2314 C  CA    . HIS A 316 ? 2.4829 2.4226 2.0412 -0.3555 0.3211  0.1435  419  HIS A CA    
2315 C  C     . HIS A 316 ? 2.5910 2.4933 2.1197 -0.3449 0.3027  0.1427  419  HIS A C     
2316 O  O     . HIS A 316 ? 2.5297 2.4590 2.0914 -0.3238 0.3091  0.1478  419  HIS A O     
2317 C  CB    . HIS A 316 ? 2.5040 2.5313 2.1384 -0.3448 0.3081  0.1497  419  HIS A CB    
2318 C  CG    . HIS A 316 ? 2.3423 2.4039 1.9996 -0.3608 0.3123  0.1490  419  HIS A CG    
2319 N  ND1   . HIS A 316 ? 2.6396 2.6560 2.2528 -0.3826 0.3253  0.1430  419  HIS A ND1   
2320 C  CD2   . HIS A 316 ? 2.2452 2.3809 1.9628 -0.3599 0.3048  0.1535  419  HIS A CD2   
2321 C  CE1   . HIS A 316 ? 2.5680 2.6295 2.2154 -0.3936 0.3265  0.1436  419  HIS A CE1   
2322 N  NE2   . HIS A 316 ? 2.3348 2.4692 2.0453 -0.3808 0.3137  0.1497  419  HIS A NE2   
2323 N  N     . CYS A 317 ? 2.8093 2.6503 2.2774 -0.3597 0.2795  0.1375  420  CYS A N     
2324 C  CA    . CYS A 317 ? 2.7175 2.5195 2.1541 -0.3530 0.2589  0.1370  420  CYS A CA    
2325 C  C     . CYS A 317 ? 2.5310 2.3127 1.9450 -0.3648 0.2177  0.1353  420  CYS A C     
2326 O  O     . CYS A 317 ? 2.6416 2.3870 2.0169 -0.3858 0.2130  0.1325  420  CYS A O     
2327 C  CB    . CYS A 317 ? 3.1039 2.8324 2.4756 -0.3606 0.2813  0.1337  420  CYS A CB    
2328 S  SG    . CYS A 317 ? 3.5156 3.2579 2.9115 -0.3458 0.3346  0.1354  420  CYS A SG    
2329 N  N     . PRO A 318 ? 2.3340 2.1369 1.7720 -0.3521 0.1888  0.1374  421  PRO A N     
2330 C  CA    . PRO A 318 ? 2.1323 1.9158 1.5541 -0.3616 0.1511  0.1365  421  PRO A CA    
2331 C  C     . PRO A 318 ? 2.3925 2.0982 1.7458 -0.3736 0.1382  0.1364  421  PRO A C     
2332 O  O     . PRO A 318 ? 2.7534 2.4209 2.0711 -0.3733 0.1561  0.1359  421  PRO A O     
2333 C  CB    . PRO A 318 ? 2.0555 1.8895 1.5292 -0.3421 0.1305  0.1389  421  PRO A CB    
2334 C  CG    . PRO A 318 ? 2.1377 1.9850 1.6266 -0.3236 0.1518  0.1416  421  PRO A CG    
2335 C  CD    . PRO A 318 ? 2.4813 2.3289 1.9661 -0.3278 0.1906  0.1413  421  PRO A CD    
2336 N  N     . LEU A 319 ? 2.2211 1.9029 1.5565 -0.3850 0.1065  0.1375  422  LEU A N     
2337 C  CA    . LEU A 319 ? 2.3402 1.9512 1.6134 -0.3984 0.0879  0.1401  422  LEU A CA    
2338 C  C     . LEU A 319 ? 2.3693 1.9808 1.6568 -0.3952 0.0477  0.1442  422  LEU A C     
2339 O  O     . LEU A 319 ? 2.4561 2.0416 1.7268 -0.3908 0.0309  0.1474  422  LEU A O     
2340 C  CB    . LEU A 319 ? 2.4444 2.0058 1.6637 -0.4235 0.0951  0.1397  422  LEU A CB    
2341 C  CG    . LEU A 319 ? 2.7061 2.1917 1.8554 -0.4413 0.0745  0.1442  422  LEU A CG    
2342 C  CD1   . LEU A 319 ? 2.7370 2.1880 1.8504 -0.4380 0.0864  0.1433  422  LEU A CD1   
2343 C  CD2   . LEU A 319 ? 2.4335 1.8743 1.5319 -0.4664 0.0823  0.1445  422  LEU A CD2   
2344 N  N     . ALA A 320 ? 2.5835 2.2235 1.9028 -0.3978 0.0333  0.1440  423  ALA A N     
2345 C  CA    . ALA A 320 ? 2.6373 2.2800 1.9765 -0.3945 -0.0015 0.1476  423  ALA A CA    
2346 C  C     . ALA A 320 ? 2.4460 2.1559 1.8503 -0.3825 -0.0027 0.1436  423  ALA A C     
2347 O  O     . ALA A 320 ? 2.5330 2.2770 1.9576 -0.3857 0.0163  0.1393  423  ALA A O     
2348 C  CB    . ALA A 320 ? 2.4169 2.0094 1.7180 -0.4149 -0.0219 0.1525  423  ALA A CB    
2349 N  N     . TRP A 321 ? 2.1487 1.8768 1.5847 -0.3702 -0.0252 0.1451  424  TRP A N     
2350 C  CA    . TRP A 321 ? 2.1426 1.9318 1.6368 -0.3592 -0.0273 0.1409  424  TRP A CA    
2351 C  C     . TRP A 321 ? 2.1505 1.9318 1.6610 -0.3590 -0.0566 0.1427  424  TRP A C     
2352 O  O     . TRP A 321 ? 2.0605 1.7985 1.5475 -0.3611 -0.0769 0.1489  424  TRP A O     
2353 C  CB    . TRP A 321 ? 2.0790 1.9131 1.6069 -0.3388 -0.0162 0.1401  424  TRP A CB    
2354 C  CG    . TRP A 321 ? 2.1174 1.9271 1.6344 -0.3281 -0.0299 0.1443  424  TRP A CG    
2355 C  CD1   . TRP A 321 ? 2.3123 2.0811 1.7887 -0.3287 -0.0226 0.1471  424  TRP A CD1   
2356 C  CD2   . TRP A 321 ? 2.2228 2.0462 1.7690 -0.3164 -0.0521 0.1456  424  TRP A CD2   
2357 N  NE1   . TRP A 321 ? 2.4568 2.2141 1.9357 -0.3185 -0.0403 0.1504  424  TRP A NE1   
2358 C  CE2   . TRP A 321 ? 2.3581 2.1493 1.8811 -0.3103 -0.0585 0.1498  424  TRP A CE2   
2359 C  CE3   . TRP A 321 ? 2.1222 1.9803 1.7108 -0.3114 -0.0657 0.1430  424  TRP A CE3   
2360 C  CZ2   . TRP A 321 ? 2.2605 2.0556 1.8044 -0.2988 -0.0787 0.1524  424  TRP A CZ2   
2361 C  CZ3   . TRP A 321 ? 2.1958 2.0561 1.8042 -0.2997 -0.0842 0.1451  424  TRP A CZ3   
2362 C  CH2   . TRP A 321 ? 2.1554 1.9856 1.7429 -0.2932 -0.0909 0.1501  424  TRP A CH2   
2363 N  N     . GLY A 322 ? 2.1602 1.9838 1.7121 -0.3573 -0.0581 0.1376  425  GLY A N     
2364 C  CA    . GLY A 322 ? 1.9748 1.7949 1.5487 -0.3563 -0.0812 0.1379  425  GLY A CA    
2365 C  C     . GLY A 322 ? 1.9881 1.8668 1.6121 -0.3482 -0.0773 0.1306  425  GLY A C     
2366 O  O     . GLY A 322 ? 1.8083 1.7282 1.4476 -0.3499 -0.0590 0.1256  425  GLY A O     
2367 N  N     . ASN A 323 ? 1.9328 1.8149 1.5825 -0.3405 -0.0948 0.1305  426  ASN A N     
2368 C  CA    . ASN A 323 ? 1.6906 1.6233 1.3841 -0.3338 -0.0925 0.1232  426  ASN A CA    
2369 C  C     . ASN A 323 ? 1.5713 1.4888 1.2814 -0.3386 -0.1074 0.1208  426  ASN A C     
2370 O  O     . ASN A 323 ? 1.7912 1.6710 1.4958 -0.3357 -0.1251 0.1274  426  ASN A O     
2371 C  CB    . ASN A 323 ? 1.8552 1.8162 1.5697 -0.3149 -0.0934 0.1246  426  ASN A CB    
2372 C  CG    . ASN A 323 ? 1.8208 1.8145 1.5348 -0.3087 -0.0737 0.1253  426  ASN A CG    
2373 O  OD1   . ASN A 323 ? 1.8444 1.8900 1.5874 -0.3049 -0.0638 0.1217  426  ASN A OD1   
2374 N  ND2   . ASN A 323 ? 2.0142 1.9768 1.6952 -0.3084 -0.0676 0.1307  426  ASN A ND2   
2375 N  N     . ILE A 324 ? 1.6055 1.5521 1.3369 -0.3466 -0.0998 0.1119  427  ILE A N     
2376 C  CA    . ILE A 324 ? 1.4654 1.4010 1.2164 -0.3514 -0.1088 0.1075  427  ILE A CA    
2377 C  C     . ILE A 324 ? 1.5131 1.5000 1.2973 -0.3499 -0.1002 0.0968  427  ILE A C     
2378 O  O     . ILE A 324 ? 1.4732 1.4981 1.2597 -0.3565 -0.0861 0.0916  427  ILE A O     
2379 C  CB    . ILE A 324 ? 1.6951 1.5986 1.4280 -0.3696 -0.1074 0.1068  427  ILE A CB    
2380 C  CG1   . ILE A 324 ? 1.9226 1.7730 1.6182 -0.3732 -0.1172 0.1187  427  ILE A CG1   
2381 C  CG2   . ILE A 324 ? 2.0699 1.9624 1.8269 -0.3737 -0.1135 0.1019  427  ILE A CG2   
2382 C  CD1   . ILE A 324 ? 2.0042 1.8209 1.6791 -0.3912 -0.1160 0.1197  427  ILE A CD1   
2383 N  N     . ASN A 325 ? 1.7013 1.6892 1.5110 -0.3422 -0.1085 0.0940  428  ASN A N     
2384 C  CA    . ASN A 325 ? 1.8824 1.9132 1.7192 -0.3433 -0.1006 0.0832  428  ASN A CA    
2385 C  C     . ASN A 325 ? 1.7443 1.7701 1.5836 -0.3618 -0.0936 0.0733  428  ASN A C     
2386 O  O     . ASN A 325 ? 1.6766 1.6597 1.5115 -0.3675 -0.0992 0.0748  428  ASN A O     
2387 C  CB    . ASN A 325 ? 1.7784 1.8094 1.6401 -0.3291 -0.1094 0.0830  428  ASN A CB    
2388 C  CG    . ASN A 325 ? 1.8981 1.8781 1.7611 -0.3247 -0.1242 0.0904  428  ASN A CG    
2389 O  OD1   . ASN A 325 ? 2.0777 2.0215 1.9255 -0.3346 -0.1279 0.0940  428  ASN A OD1   
2390 N  ND2   . ASN A 325 ? 1.6500 1.6273 1.5324 -0.3100 -0.1334 0.0938  428  ASN A ND2   
2391 N  N     . LEU A 326 ? 1.4751 1.5447 1.3217 -0.3719 -0.0814 0.0639  429  LEU A N     
2392 C  CA    . LEU A 326 ? 1.4293 1.4967 1.2749 -0.3922 -0.0727 0.0533  429  LEU A CA    
2393 C  C     . LEU A 326 ? 1.4949 1.5411 1.3583 -0.3944 -0.0742 0.0451  429  LEU A C     
2394 O  O     . LEU A 326 ? 1.6846 1.7104 1.5450 -0.4099 -0.0681 0.0379  429  LEU A O     
2395 C  CB    . LEU A 326 ? 1.5728 1.6955 1.4227 -0.4038 -0.0611 0.0461  429  LEU A CB    
2396 C  CG    . LEU A 326 ? 1.6253 1.7720 1.4631 -0.4036 -0.0557 0.0539  429  LEU A CG    
2397 C  CD1   . LEU A 326 ? 1.5488 1.7520 1.3965 -0.4170 -0.0456 0.0481  429  LEU A CD1   
2398 C  CD2   . LEU A 326 ? 1.2367 1.3415 1.0493 -0.4117 -0.0541 0.0584  429  LEU A CD2   
2399 N  N     . PHE A 327 ? 1.6138 1.6631 1.4963 -0.3793 -0.0803 0.0459  430  PHE A N     
2400 C  CA    . PHE A 327 ? 1.4200 1.4460 1.3228 -0.3787 -0.0802 0.0394  430  PHE A CA    
2401 C  C     . PHE A 327 ? 1.5160 1.5064 1.4288 -0.3607 -0.0948 0.0515  430  PHE A C     
2402 O  O     . PHE A 327 ? 1.6547 1.6545 1.5649 -0.3461 -0.1035 0.0608  430  PHE A O     
2403 C  CB    . PHE A 327 ? 1.4989 1.5628 1.4183 -0.3796 -0.0721 0.0278  430  PHE A CB    
2404 C  CG    . PHE A 327 ? 1.4936 1.5949 1.4039 -0.3997 -0.0598 0.0164  430  PHE A CG    
2405 C  CD1   . PHE A 327 ? 1.4130 1.5014 1.3225 -0.4191 -0.0487 0.0028  430  PHE A CD1   
2406 C  CD2   . PHE A 327 ? 1.4712 1.6206 1.3750 -0.3996 -0.0593 0.0198  430  PHE A CD2   
2407 C  CE1   . PHE A 327 ? 1.4396 1.5628 1.3393 -0.4400 -0.0387 -0.0076 430  PHE A CE1   
2408 C  CE2   . PHE A 327 ? 1.4850 1.6719 1.3832 -0.4192 -0.0501 0.0111  430  PHE A CE2   
2409 C  CZ    . PHE A 327 ? 1.2491 1.4231 1.1437 -0.4404 -0.0406 -0.0029 430  PHE A CZ    
2410 N  N     . ASP A 328 ? 1.4089 1.3583 1.3345 -0.3620 -0.0974 0.0521  431  ASP A N     
2411 C  CA    . ASP A 328 ? 1.7424 1.6587 1.6829 -0.3464 -0.1127 0.0649  431  ASP A CA    
2412 C  C     . ASP A 328 ? 1.6231 1.5527 1.5953 -0.3349 -0.1104 0.0596  431  ASP A C     
2413 O  O     . ASP A 328 ? 1.6803 1.6460 1.6568 -0.3382 -0.0984 0.0473  431  ASP A O     
2414 C  CB    . ASP A 328 ? 1.4267 1.2934 1.3696 -0.3525 -0.1178 0.0715  431  ASP A CB    
2415 C  CG    . ASP A 328 ? 1.4803 1.3386 1.4394 -0.3648 -0.1017 0.0579  431  ASP A CG    
2416 O  OD1   . ASP A 328 ? 1.9160 1.8068 1.8798 -0.3710 -0.0869 0.0423  431  ASP A OD1   
2417 O  OD2   . ASP A 328 ? 1.3010 1.1186 1.2670 -0.3690 -0.1038 0.0632  431  ASP A OD2   
2418 N  N     . TYR A 329 ? 1.8293 1.7298 1.8241 -0.3220 -0.1223 0.0698  432  TYR A N     
2419 C  CA    . TYR A 329 ? 1.8036 1.7152 1.8293 -0.3095 -0.1206 0.0665  432  TYR A CA    
2420 C  C     . TYR A 329 ? 1.8160 1.7239 1.8651 -0.3171 -0.1027 0.0516  432  TYR A C     
2421 O  O     . TYR A 329 ? 1.8117 1.7324 1.8837 -0.3094 -0.0965 0.0456  432  TYR A O     
2422 C  CB    . TYR A 329 ? 1.8775 1.7603 1.9228 -0.2941 -0.1395 0.0832  432  TYR A CB    
2423 C  CG    . TYR A 329 ? 1.5849 1.4233 1.6505 -0.2961 -0.1449 0.0913  432  TYR A CG    
2424 C  CD1   . TYR A 329 ? 1.5228 1.3326 1.5661 -0.3053 -0.1535 0.1007  432  TYR A CD1   
2425 C  CD2   . TYR A 329 ? 1.7129 1.5374 1.8215 -0.2887 -0.1408 0.0905  432  TYR A CD2   
2426 C  CE1   . TYR A 329 ? 1.6581 1.4275 1.7216 -0.3068 -0.1594 0.1103  432  TYR A CE1   
2427 C  CE2   . TYR A 329 ? 1.5763 1.3609 1.7087 -0.2893 -0.1453 0.0999  432  TYR A CE2   
2428 C  CZ    . TYR A 329 ? 1.5883 1.3459 1.6981 -0.2982 -0.1555 0.1105  432  TYR A CZ    
2429 O  OH    . TYR A 329 ? 1.6604 1.3784 1.7954 -0.2986 -0.1610 0.1220  432  TYR A OH    
2430 N  N     . THR A 330 ? 1.5336 1.4226 1.5762 -0.3326 -0.0929 0.0451  433  THR A N     
2431 C  CA    . THR A 330 ? 1.5893 1.4707 1.6499 -0.3423 -0.0729 0.0293  433  THR A CA    
2432 C  C     . THR A 330 ? 1.7257 1.6396 1.7620 -0.3615 -0.0562 0.0112  433  THR A C     
2433 O  O     . THR A 330 ? 2.0025 1.9043 2.0417 -0.3763 -0.0388 -0.0028 433  THR A O     
2434 C  CB    . THR A 330 ? 1.7287 1.5622 1.8032 -0.3469 -0.0717 0.0342  433  THR A CB    
2435 O  OG1   . THR A 330 ? 2.3245 2.1485 2.4140 -0.3579 -0.0485 0.0170  433  THR A OG1   
2436 C  CG2   . THR A 330 ? 1.8305 1.6532 1.8728 -0.3592 -0.0773 0.0396  433  THR A CG2   
2437 N  N     . ASP A 331 ? 1.6947 1.6490 1.7080 -0.3621 -0.0610 0.0120  434  ASP A N     
2438 C  CA    . ASP A 331 ? 1.7666 1.7600 1.7596 -0.3795 -0.0486 -0.0020 434  ASP A CA    
2439 C  C     . ASP A 331 ? 1.8300 1.8115 1.8044 -0.4011 -0.0398 -0.0091 434  ASP A C     
2440 O  O     . ASP A 331 ? 1.9122 1.9174 1.8744 -0.4200 -0.0268 -0.0236 434  ASP A O     
2441 C  CB    . ASP A 331 ? 1.6823 1.6920 1.6874 -0.3840 -0.0342 -0.0173 434  ASP A CB    
2442 C  CG    . ASP A 331 ? 1.6947 1.7268 1.7130 -0.3653 -0.0415 -0.0115 434  ASP A CG    
2443 O  OD1   . ASP A 331 ? 1.9590 1.9901 1.9794 -0.3483 -0.0576 0.0042  434  ASP A OD1   
2444 O  OD2   . ASP A 331 ? 1.7488 1.7977 1.7731 -0.3688 -0.0305 -0.0228 434  ASP A OD2   
2445 N  N     . THR A 332 ? 1.5798 1.5250 1.5503 -0.4001 -0.0471 0.0012  435  THR A N     
2446 C  CA    . THR A 332 ? 1.7480 1.6786 1.7004 -0.4201 -0.0389 -0.0042 435  THR A CA    
2447 C  C     . THR A 332 ? 1.7772 1.7255 1.7027 -0.4233 -0.0473 0.0048  435  THR A C     
2448 O  O     . THR A 332 ? 1.7531 1.7015 1.6747 -0.4079 -0.0618 0.0193  435  THR A O     
2449 C  CB    . THR A 332 ? 1.7819 1.6565 1.7479 -0.4191 -0.0391 0.0013  435  THR A CB    
2450 O  OG1   . THR A 332 ? 1.9441 1.7968 1.9126 -0.4022 -0.0591 0.0217  435  THR A OG1   
2451 C  CG2   . THR A 332 ? 1.8804 1.7359 1.8775 -0.4155 -0.0274 -0.0077 435  THR A CG2   
2452 N  N     . LEU A 333 ? 1.8102 1.7729 1.7170 -0.4443 -0.0368 -0.0045 436  LEU A N     
2453 C  CA    . LEU A 333 ? 1.8062 1.7865 1.6897 -0.4492 -0.0410 0.0029  436  LEU A CA    
2454 C  C     . LEU A 333 ? 1.9026 1.8360 1.7748 -0.4468 -0.0491 0.0157  436  LEU A C     
2455 O  O     . LEU A 333 ? 2.2561 2.1464 2.1353 -0.4504 -0.0473 0.0156  436  LEU A O     
2456 C  CB    . LEU A 333 ? 1.8206 1.8304 1.6904 -0.4740 -0.0274 -0.0103 436  LEU A CB    
2457 C  CG    . LEU A 333 ? 1.5567 1.5963 1.4077 -0.4803 -0.0285 -0.0042 436  LEU A CG    
2458 C  CD1   . LEU A 333 ? 1.3802 1.4630 1.2362 -0.4643 -0.0359 0.0040  436  LEU A CD1   
2459 C  CD2   . LEU A 333 ? 1.7456 1.8103 1.5872 -0.5072 -0.0154 -0.0172 436  LEU A CD2   
2460 N  N     . VAL A 334 ? 1.8082 1.7490 1.6621 -0.4410 -0.0575 0.0276  437  VAL A N     
2461 C  CA    . VAL A 334 ? 1.9938 1.8906 1.8305 -0.4400 -0.0662 0.0408  437  VAL A CA    
2462 C  C     . VAL A 334 ? 1.8418 1.7241 1.6614 -0.4621 -0.0551 0.0350  437  VAL A C     
2463 O  O     . VAL A 334 ? 1.8918 1.8091 1.7046 -0.4771 -0.0428 0.0244  437  VAL A O     
2464 C  CB    . VAL A 334 ? 1.9008 1.8080 1.7193 -0.4288 -0.0756 0.0535  437  VAL A CB    
2465 C  CG1   . VAL A 334 ? 1.6201 1.5746 1.4268 -0.4378 -0.0643 0.0479  437  VAL A CG1   
2466 C  CG2   . VAL A 334 ? 1.9333 1.7911 1.7291 -0.4293 -0.0858 0.0676  437  VAL A CG2   
2467 N  N     . SER A 335 ? 1.7536 1.5844 1.5674 -0.4648 -0.0599 0.0428  438  SER A N     
2468 C  CA    . SER A 335 ? 1.9199 1.7298 1.7168 -0.4852 -0.0496 0.0387  438  SER A CA    
2469 C  C     . SER A 335 ? 2.0146 1.7705 1.7958 -0.4829 -0.0616 0.0556  438  SER A C     
2470 O  O     . SER A 335 ? 1.8520 1.5808 1.6448 -0.4676 -0.0769 0.0681  438  SER A O     
2471 C  CB    . SER A 335 ? 2.2816 2.0846 2.0962 -0.4980 -0.0353 0.0233  438  SER A CB    
2472 O  OG    . SER A 335 ? 2.2812 2.1335 2.1044 -0.5041 -0.0248 0.0076  438  SER A OG    
2473 N  N     . GLY A 336 ? 2.3191 2.0601 2.0739 -0.4993 -0.0551 0.0566  439  GLY A N     
2474 C  CA    . GLY A 336 ? 2.0618 1.7506 1.7960 -0.5008 -0.0658 0.0728  439  GLY A CA    
2475 C  C     . GLY A 336 ? 1.8494 1.5376 1.5527 -0.4958 -0.0753 0.0852  439  GLY A C     
2476 O  O     . GLY A 336 ? 1.9416 1.6708 1.6390 -0.4925 -0.0704 0.0808  439  GLY A O     
2477 N  N     . LYS A 337 ? 2.0625 1.7012 1.7452 -0.4961 -0.0887 0.1019  440  LYS A N     
2478 C  CA    . LYS A 337 ? 2.1069 1.7345 1.7545 -0.4934 -0.0980 0.1143  440  LYS A CA    
2479 C  C     . LYS A 337 ? 2.1831 1.8119 1.8414 -0.4734 -0.1164 0.1241  440  LYS A C     
2480 O  O     . LYS A 337 ? 2.1295 1.7537 1.8210 -0.4620 -0.1260 0.1262  440  LYS A O     
2481 C  CB    . LYS A 337 ? 2.2220 1.7942 1.8365 -0.5055 -0.1051 0.1285  440  LYS A CB    
2482 C  CG    . LYS A 337 ? 2.5793 2.1458 2.1798 -0.5264 -0.0867 0.1199  440  LYS A CG    
2483 C  CD    . LYS A 337 ? 2.4806 1.9923 2.0420 -0.5384 -0.0938 0.1354  440  LYS A CD    
2484 C  CE    . LYS A 337 ? 2.6299 2.0944 2.2025 -0.5313 -0.1158 0.1530  440  LYS A CE    
2485 N  NZ    . LYS A 337 ? 2.7483 2.2105 2.3627 -0.5306 -0.1100 0.1461  440  LYS A NZ    
2486 N  N     . MET A 338 ? 2.0654 1.6993 1.6955 -0.4696 -0.1198 0.1298  441  MET A N     
2487 C  CA    . MET A 338 ? 1.9036 1.5397 1.5393 -0.4522 -0.1358 0.1382  441  MET A CA    
2488 C  C     . MET A 338 ? 1.8626 1.4776 1.4521 -0.4552 -0.1406 0.1484  441  MET A C     
2489 O  O     . MET A 338 ? 1.9729 1.5966 1.5354 -0.4657 -0.1244 0.1432  441  MET A O     
2490 C  CB    . MET A 338 ? 1.9715 1.6631 1.6378 -0.4395 -0.1271 0.1254  441  MET A CB    
2491 C  CG    . MET A 338 ? 2.0920 1.7866 1.7721 -0.4208 -0.1431 0.1328  441  MET A CG    
2492 S  SD    . MET A 338 ? 2.3341 2.0920 2.0511 -0.4068 -0.1324 0.1184  441  MET A SD    
2493 C  CE    . MET A 338 ? 2.4074 2.1536 2.1364 -0.3868 -0.1539 0.1303  441  MET A CE    
2494 N  N     . ALA A 339 ? 1.6249 1.2115 1.2056 -0.4469 -0.1621 0.1628  442  ALA A N     
2495 C  CA    . ALA A 339 ? 1.8759 1.4363 1.4091 -0.4506 -0.1684 0.1728  442  ALA A CA    
2496 C  C     . ALA A 339 ? 2.2164 1.8019 1.7587 -0.4341 -0.1723 0.1717  442  ALA A C     
2497 O  O     . ALA A 339 ? 2.1069 1.6874 1.6724 -0.4224 -0.1910 0.1789  442  ALA A O     
2498 C  CB    . ALA A 339 ? 2.0736 1.5751 1.5816 -0.4586 -0.1921 0.1922  442  ALA A CB    
2499 N  N     . LEU A 340 ? 2.1533 1.7657 1.6795 -0.4331 -0.1540 0.1633  443  LEU A N     
2500 C  CA    . LEU A 340 ? 2.1203 1.7577 1.6537 -0.4177 -0.1538 0.1616  443  LEU A CA    
2501 C  C     . LEU A 340 ? 2.2819 1.8834 1.7640 -0.4226 -0.1571 0.1704  443  LEU A C     
2502 O  O     . LEU A 340 ? 2.4030 1.9885 1.8470 -0.4359 -0.1427 0.1693  443  LEU A O     
2503 C  CB    . LEU A 340 ? 1.7811 1.4768 1.3378 -0.4115 -0.1300 0.1471  443  LEU A CB    
2504 C  CG    . LEU A 340 ? 1.7689 1.4911 1.3309 -0.3958 -0.1261 0.1458  443  LEU A CG    
2505 C  CD1   . LEU A 340 ? 1.8394 1.5672 1.4332 -0.3805 -0.1446 0.1490  443  LEU A CD1   
2506 C  CD2   . LEU A 340 ? 1.8116 1.5900 1.3942 -0.3919 -0.1023 0.1346  443  LEU A CD2   
2507 N  N     . ASN A 341 ? 2.2444 1.8320 1.7245 -0.4132 -0.1750 0.1785  444  ASN A N     
2508 C  CA    . ASN A 341 ? 2.1775 1.7306 1.6080 -0.4181 -0.1785 0.1857  444  ASN A CA    
2509 C  C     . ASN A 341 ? 2.1182 1.7071 1.5563 -0.4043 -0.1614 0.1770  444  ASN A C     
2510 O  O     . ASN A 341 ? 2.3758 1.9974 1.8540 -0.3878 -0.1661 0.1741  444  ASN A O     
2511 C  CB    . ASN A 341 ? 2.3740 1.8869 1.7952 -0.4187 -0.2104 0.2013  444  ASN A CB    
2512 C  CG    . ASN A 341 ? 2.5353 1.9904 1.8912 -0.4373 -0.2194 0.2127  444  ASN A CG    
2513 O  OD1   . ASN A 341 ? 2.6520 2.0899 1.9717 -0.4520 -0.2039 0.2102  444  ASN A OD1   
2514 N  ND2   . ASN A 341 ? 2.6160 2.0401 1.9551 -0.4383 -0.2446 0.2255  444  ASN A ND2   
2515 N  N     . LEU A 342 ? 1.8219 1.4038 1.2227 -0.4111 -0.1403 0.1734  445  LEU A N     
2516 C  CA    . LEU A 342 ? 2.0776 1.6958 1.4889 -0.3981 -0.1191 0.1654  445  LEU A CA    
2517 C  C     . LEU A 342 ? 2.3612 1.9555 1.7499 -0.3918 -0.1283 0.1709  445  LEU A C     
2518 O  O     . LEU A 342 ? 2.2188 1.7637 1.5723 -0.4017 -0.1490 0.1808  445  LEU A O     
2519 C  CB    . LEU A 342 ? 2.1646 1.7874 1.5516 -0.4073 -0.0890 0.1592  445  LEU A CB    
2520 C  CG    . LEU A 342 ? 2.1708 1.8158 1.5758 -0.4165 -0.0781 0.1536  445  LEU A CG    
2521 C  CD1   . LEU A 342 ? 2.2308 1.8871 1.6189 -0.4233 -0.0467 0.1478  445  LEU A CD1   
2522 C  CD2   . LEU A 342 ? 1.8814 1.5817 1.3469 -0.4041 -0.0810 0.1472  445  LEU A CD2   
2523 N  N     . TRP A 343 ? 2.4583 2.0887 1.8678 -0.3760 -0.1129 0.1650  446  TRP A N     
2524 C  CA    . TRP A 343 ? 2.4955 2.1108 1.8903 -0.3677 -0.1175 0.1681  446  TRP A CA    
2525 C  C     . TRP A 343 ? 2.6344 2.2373 1.9921 -0.3705 -0.0896 0.1643  446  TRP A C     
2526 O  O     . TRP A 343 ? 2.7311 2.3607 2.0972 -0.3705 -0.0633 0.1580  446  TRP A O     
2527 C  CB    . TRP A 343 ? 2.2475 1.9115 1.6964 -0.3460 -0.1205 0.1649  446  TRP A CB    
2528 C  CG    . TRP A 343 ? 2.2098 1.8902 1.7005 -0.3415 -0.1426 0.1667  446  TRP A CG    
2529 C  CD1   . TRP A 343 ? 2.3782 2.0960 1.9073 -0.3398 -0.1380 0.1608  446  TRP A CD1   
2530 C  CD2   . TRP A 343 ? 2.1517 1.8108 1.6511 -0.3387 -0.1711 0.1749  446  TRP A CD2   
2531 N  NE1   . TRP A 343 ? 2.3905 2.1091 1.9506 -0.3358 -0.1598 0.1639  446  TRP A NE1   
2532 C  CE2   . TRP A 343 ? 2.1968 1.8811 1.7421 -0.3342 -0.1805 0.1733  446  TRP A CE2   
2533 C  CE3   . TRP A 343 ? 2.0668 1.6877 1.5402 -0.3406 -0.1894 0.1836  446  TRP A CE3   
2534 C  CZ2   . TRP A 343 ? 2.1858 1.8592 1.7555 -0.3299 -0.2058 0.1805  446  TRP A CZ2   
2535 C  CZ3   . TRP A 343 ? 2.0625 1.6752 1.5607 -0.3370 -0.2171 0.1917  446  TRP A CZ3   
2536 C  CH2   . TRP A 343 ? 2.1507 1.7898 1.6985 -0.3309 -0.2243 0.1904  446  TRP A CH2   
2537 N  N     . PRO A 344 ? 2.6074 2.1694 1.9244 -0.3738 -0.0934 0.1680  447  PRO A N     
2538 C  CA    . PRO A 344 ? 2.4497 1.9987 1.7338 -0.3748 -0.0633 0.1634  447  PRO A CA    
2539 C  C     . PRO A 344 ? 2.2810 1.8842 1.6115 -0.3521 -0.0430 0.1578  447  PRO A C     
2540 O  O     . PRO A 344 ? 2.3045 1.9379 1.6753 -0.3365 -0.0570 0.1589  447  PRO A O     
2541 C  CB    . PRO A 344 ? 2.5165 2.0051 1.7455 -0.3856 -0.0777 0.1690  447  PRO A CB    
2542 C  CG    . PRO A 344 ? 2.3955 1.8602 1.6212 -0.3955 -0.1159 0.1787  447  PRO A CG    
2543 C  CD    . PRO A 344 ? 2.2809 1.8010 1.5755 -0.3800 -0.1252 0.1774  447  PRO A CD    
2544 N  N     . VAL A 345 ? 2.3810 1.9963 1.7066 -0.3505 -0.0090 0.1529  448  VAL A N     
2545 C  CA    . VAL A 345 ? 2.5160 2.1832 1.8861 -0.3294 0.0128  0.1498  448  VAL A CA    
2546 C  C     . VAL A 345 ? 2.6029 2.2483 1.9577 -0.3201 0.0132  0.1511  448  VAL A C     
2547 O  O     . VAL A 345 ? 2.6602 2.2457 1.9580 -0.3337 0.0103  0.1522  448  VAL A O     
2548 C  CB    . VAL A 345 ? 2.5011 2.1857 1.8728 -0.3307 0.0497  0.1461  448  VAL A CB    
2549 C  CG1   . VAL A 345 ? 2.1682 1.8858 1.5658 -0.3379 0.0489  0.1445  448  VAL A CG1   
2550 C  CG2   . VAL A 345 ? 2.6948 2.3156 1.9996 -0.3473 0.0677  0.1447  448  VAL A CG2   
2551 N  N     . PRO A 346 ? 2.7982 2.4887 2.1998 -0.2987 0.0163  0.1513  449  PRO A N     
2552 C  CA    . PRO A 346 ? 3.0748 2.7444 2.4629 -0.2896 0.0183  0.1524  449  PRO A CA    
2553 C  C     . PRO A 346 ? 3.2206 2.8629 2.5751 -0.2912 0.0536  0.1495  449  PRO A C     
2554 O  O     . PRO A 346 ? 3.1052 2.7414 2.4440 -0.3003 0.0765  0.1470  449  PRO A O     
2555 C  CB    . PRO A 346 ? 2.8505 2.5823 2.3028 -0.2661 0.0155  0.1537  449  PRO A CB    
2556 C  CG    . PRO A 346 ? 2.7056 2.4797 2.1968 -0.2669 0.0009  0.1534  449  PRO A CG    
2557 C  CD    . PRO A 346 ? 2.6391 2.3989 2.1058 -0.2835 0.0139  0.1511  449  PRO A CD    
2558 N  N     . HIS A 347 ? 3.1342 2.7584 2.4778 -0.2825 0.0601  0.1496  450  HIS A N     
2559 C  CA    . HIS A 347 ? 3.0755 2.6698 2.3873 -0.2832 0.0966  0.1462  450  HIS A CA    
2560 C  C     . HIS A 347 ? 3.0899 2.7392 2.4517 -0.2657 0.1301  0.1466  450  HIS A C     
2561 O  O     . HIS A 347 ? 2.8710 2.5046 2.2137 -0.2711 0.1629  0.1439  450  HIS A O     
2562 C  CB    . HIS A 347 ? 3.0140 2.5765 2.3048 -0.2780 0.0950  0.1460  450  HIS A CB    
2563 C  CG    . HIS A 347 ? 3.0416 2.5770 2.3075 -0.2753 0.1359  0.1421  450  HIS A CG    
2564 N  ND1   . HIS A 347 ? 2.9035 2.4779 2.2151 -0.2514 0.1612  0.1437  450  HIS A ND1   
2565 C  CD2   . HIS A 347 ? 3.1037 2.5750 2.3034 -0.2938 0.1572  0.1368  450  HIS A CD2   
2566 C  CE1   . HIS A 347 ? 3.0509 2.5865 2.3288 -0.2541 0.1977  0.1395  450  HIS A CE1   
2567 N  NE2   . HIS A 347 ? 3.0650 2.5368 2.2732 -0.2803 0.1967  0.1345  450  HIS A NE2   
2568 N  N     . GLY A 348 ? 3.0250 2.7389 2.4513 -0.2454 0.1226  0.1506  451  GLY A N     
2569 C  CA    . GLY A 348 ? 2.7374 2.5090 2.2162 -0.2288 0.1502  0.1538  451  GLY A CA    
2570 C  C     . GLY A 348 ? 2.5856 2.4213 2.1167 -0.2251 0.1355  0.1564  451  GLY A C     
2571 O  O     . GLY A 348 ? 2.7099 2.5875 2.2823 -0.2123 0.1166  0.1596  451  GLY A O     
2572 N  N     . LEU A 349 ? 2.7242 2.5663 2.2519 -0.2377 0.1450  0.1546  452  LEU A N     
2573 C  CA    . LEU A 349 ? 2.6664 2.5664 2.2393 -0.2378 0.1342  0.1560  452  LEU A CA    
2574 C  C     . LEU A 349 ? 2.7951 2.7351 2.3996 -0.2335 0.1665  0.1592  452  LEU A C     
2575 O  O     . LEU A 349 ? 2.7278 2.6348 2.3015 -0.2432 0.1919  0.1568  452  LEU A O     
2576 C  CB    . LEU A 349 ? 2.6824 2.5548 2.2252 -0.2592 0.1115  0.1515  452  LEU A CB    
2577 C  CG    . LEU A 349 ? 2.6888 2.6139 2.2726 -0.2623 0.0992  0.1513  452  LEU A CG    
2578 C  CD1   . LEU A 349 ? 2.6148 2.5882 2.2458 -0.2470 0.0796  0.1537  452  LEU A CD1   
2579 C  CD2   . LEU A 349 ? 2.5758 2.4643 2.1255 -0.2836 0.0799  0.1472  452  LEU A CD2   
2580 N  N     . GLU A 350 ? 2.9210 2.9318 2.5867 -0.2200 0.1655  0.1650  453  GLU A N     
2581 C  CA    . GLU A 350 ? 2.8808 2.9392 2.5870 -0.2142 0.1940  0.1710  453  GLU A CA    
2582 C  C     . GLU A 350 ? 2.8118 2.8964 2.5289 -0.2305 0.1888  0.1685  453  GLU A C     
2583 O  O     . GLU A 350 ? 2.8893 2.9528 2.5856 -0.2432 0.2090  0.1659  453  GLU A O     
2584 C  CB    . GLU A 350 ? 2.8250 2.9471 2.5918 -0.1915 0.1958  0.1811  453  GLU A CB    
2585 C  CG    . GLU A 350 ? 3.0049 3.1863 2.8236 -0.1850 0.2202  0.1904  453  GLU A CG    
2586 C  CD    . GLU A 350 ? 3.0500 3.2023 2.8555 -0.1830 0.2600  0.1919  453  GLU A CD    
2587 O  OE1   . GLU A 350 ? 3.0129 3.1108 2.7813 -0.1785 0.2718  0.1887  453  GLU A OE1   
2588 O  OE2   . GLU A 350 ? 3.0131 3.1961 2.8453 -0.1869 0.2805  0.1961  453  GLU A OE2   
2589 N  N     . ASP A 351 ? 2.6206 2.7494 2.3690 -0.2313 0.1632  0.1688  454  ASP A N     
2590 C  CA    . ASP A 351 ? 2.5555 2.7128 2.3174 -0.2472 0.1582  0.1662  454  ASP A CA    
2591 C  C     . ASP A 351 ? 2.4159 2.5133 2.1234 -0.2686 0.1489  0.1572  454  ASP A C     
2592 O  O     . ASP A 351 ? 2.4176 2.4608 2.0835 -0.2714 0.1342  0.1534  454  ASP A O     
2593 C  CB    . ASP A 351 ? 2.6322 2.8449 2.4348 -0.2444 0.1332  0.1674  454  ASP A CB    
2594 C  CG    . ASP A 351 ? 2.6168 2.8673 2.4396 -0.2606 0.1311  0.1653  454  ASP A CG    
2595 O  OD1   . ASP A 351 ? 2.6115 2.9038 2.4663 -0.2598 0.1514  0.1718  454  ASP A OD1   
2596 O  OD2   . ASP A 351 ? 2.5096 2.7480 2.3180 -0.2742 0.1098  0.1577  454  ASP A OD2   
2597 N  N     . LEU A 352 ? 2.2854 2.3936 1.9944 -0.2844 0.1571  0.1548  455  LEU A N     
2598 C  CA    . LEU A 352 ? 2.3331 2.3871 1.9927 -0.3056 0.1491  0.1476  455  LEU A CA    
2599 C  C     . LEU A 352 ? 2.3143 2.3566 1.9662 -0.3108 0.1141  0.1434  455  LEU A C     
2600 O  O     . LEU A 352 ? 2.1769 2.1606 1.7835 -0.3190 0.1000  0.1407  455  LEU A O     
2601 C  CB    . LEU A 352 ? 2.0345 2.1100 1.7044 -0.3209 0.1649  0.1463  455  LEU A CB    
2602 C  CG    . LEU A 352 ? 2.2047 2.2970 1.8902 -0.3168 0.2020  0.1511  455  LEU A CG    
2603 C  CD1   . LEU A 352 ? 2.1528 2.2679 1.8505 -0.3340 0.2140  0.1495  455  LEU A CD1   
2604 C  CD2   . LEU A 352 ? 2.2788 2.3039 1.9123 -0.3172 0.2216  0.1495  455  LEU A CD2   
2605 N  N     . LEU A 353 ? 2.3311 2.4285 2.0274 -0.3067 0.1001  0.1436  456  LEU A N     
2606 C  CA    . LEU A 353 ? 2.2820 2.3726 1.9777 -0.3105 0.0704  0.1392  456  LEU A CA    
2607 C  C     . LEU A 353 ? 2.2072 2.3044 1.9168 -0.2920 0.0566  0.1420  456  LEU A C     
2608 O  O     . LEU A 353 ? 2.1722 2.3095 1.9133 -0.2762 0.0668  0.1474  456  LEU A O     
2609 C  CB    . LEU A 353 ? 2.0827 2.2246 1.8138 -0.3195 0.0643  0.1360  456  LEU A CB    
2610 C  CG    . LEU A 353 ? 1.9061 2.0432 1.6404 -0.3249 0.0378  0.1302  456  LEU A CG    
2611 C  CD1   . LEU A 353 ? 1.8212 1.8902 1.5104 -0.3362 0.0256  0.1272  456  LEU A CD1   
2612 C  CD2   . LEU A 353 ? 1.8581 2.0420 1.6214 -0.3375 0.0371  0.1257  456  LEU A CD2   
2613 N  N     . ASN A 354 ? 2.1243 2.1819 1.8121 -0.2940 0.0336  0.1394  457  ASN A N     
2614 C  CA    . ASN A 354 ? 2.1680 2.2259 1.8663 -0.2781 0.0193  0.1416  457  ASN A CA    
2615 C  C     . ASN A 354 ? 2.1753 2.2673 1.9066 -0.2772 0.0000  0.1382  457  ASN A C     
2616 O  O     . ASN A 354 ? 2.2464 2.3104 1.9656 -0.2867 -0.0180 0.1342  457  ASN A O     
2617 C  CB    . ASN A 354 ? 2.2921 2.2828 1.9456 -0.2810 0.0067  0.1422  457  ASN A CB    
2618 C  CG    . ASN A 354 ? 2.2323 2.2217 1.8976 -0.2664 -0.0100 0.1442  457  ASN A CG    
2619 O  OD1   . ASN A 354 ? 2.4538 2.4502 2.1244 -0.2521 -0.0002 0.1478  457  ASN A OD1   
2620 N  ND2   . ASN A 354 ? 2.1106 2.0902 1.7817 -0.2697 -0.0340 0.1422  457  ASN A ND2   
2621 N  N     . PRO A 355 ? 2.0661 2.2166 1.8387 -0.2667 0.0035  0.1401  458  PRO A N     
2622 C  CA    . PRO A 355 ? 1.7527 1.9323 1.5521 -0.2679 -0.0132 0.1356  458  PRO A CA    
2623 C  C     . PRO A 355 ? 1.8659 2.0219 1.6636 -0.2579 -0.0316 0.1353  458  PRO A C     
2624 O  O     . PRO A 355 ? 1.8471 1.9984 1.6517 -0.2636 -0.0469 0.1298  458  PRO A O     
2625 C  CB    . PRO A 355 ? 1.9379 2.1856 1.7775 -0.2603 -0.0032 0.1399  458  PRO A CB    
2626 C  CG    . PRO A 355 ? 2.2677 2.5157 2.1064 -0.2457 0.0139  0.1485  458  PRO A CG    
2627 C  CD    . PRO A 355 ? 2.2948 2.4870 2.0919 -0.2540 0.0232  0.1471  458  PRO A CD    
2628 N  N     . ILE A 356 ? 2.4147 2.5549 2.2047 -0.2434 -0.0293 0.1407  459  ILE A N     
2629 C  CA    . ILE A 356 ? 2.5717 2.6894 2.3609 -0.2341 -0.0463 0.1412  459  ILE A CA    
2630 C  C     . ILE A 356 ? 2.5359 2.5909 2.2891 -0.2442 -0.0598 0.1402  459  ILE A C     
2631 O  O     . ILE A 356 ? 2.4654 2.4815 2.1919 -0.2406 -0.0611 0.1442  459  ILE A O     
2632 C  CB    . ILE A 356 ? 2.4183 2.5428 2.2127 -0.2158 -0.0382 0.1476  459  ILE A CB    
2633 C  CG1   . ILE A 356 ? 2.3916 2.5016 2.1644 -0.2155 -0.0165 0.1516  459  ILE A CG1   
2634 C  CG2   . ILE A 356 ? 2.1644 2.3493 2.0005 -0.2040 -0.0352 0.1500  459  ILE A CG2   
2635 C  CD1   . ILE A 356 ? 2.6290 2.7421 2.4063 -0.1978 -0.0050 0.1578  459  ILE A CD1   
2636 N  N     . GLY A 357 ? 2.3557 2.4000 2.1076 -0.2577 -0.0702 0.1356  460  GLY A N     
2637 C  CA    . GLY A 357 ? 2.2039 2.1917 1.9253 -0.2686 -0.0846 0.1368  460  GLY A CA    
2638 C  C     . GLY A 357 ? 1.8943 1.8654 1.6288 -0.2635 -0.1065 0.1378  460  GLY A C     
2639 O  O     . GLY A 357 ? 1.9325 1.9289 1.6938 -0.2501 -0.1096 0.1375  460  GLY A O     
2640 N  N     . VAL A 358 ? 2.0725 2.0001 1.7892 -0.2746 -0.1216 0.1399  461  VAL A N     
2641 C  CA    . VAL A 358 ? 2.1320 2.0393 1.8632 -0.2709 -0.1431 0.1429  461  VAL A CA    
2642 C  C     . VAL A 358 ? 2.3065 2.2177 2.0605 -0.2785 -0.1496 0.1383  461  VAL A C     
2643 O  O     . VAL A 358 ? 2.4029 2.3016 2.1772 -0.2745 -0.1650 0.1405  461  VAL A O     
2644 C  CB    . VAL A 358 ? 1.9957 1.8465 1.6920 -0.2762 -0.1593 0.1523  461  VAL A CB    
2645 C  CG1   . VAL A 358 ? 1.9250 1.7679 1.5972 -0.2693 -0.1516 0.1553  461  VAL A CG1   
2646 C  CG2   . VAL A 358 ? 2.2587 2.0742 1.9222 -0.2943 -0.1608 0.1546  461  VAL A CG2   
2647 N  N     . THR A 359 ? 2.2598 2.1871 2.0125 -0.2895 -0.1372 0.1322  462  THR A N     
2648 C  CA    . THR A 359 ? 2.2076 2.1370 1.9794 -0.2986 -0.1399 0.1264  462  THR A CA    
2649 C  C     . THR A 359 ? 2.2539 2.1324 2.0178 -0.3045 -0.1586 0.1337  462  THR A C     
2650 O  O     . THR A 359 ? 2.2369 2.1113 2.0286 -0.3026 -0.1673 0.1326  462  THR A O     
2651 C  CB    . THR A 359 ? 2.1409 2.1105 1.9527 -0.2902 -0.1374 0.1187  462  THR A CB    
2652 O  OG1   . THR A 359 ? 2.3521 2.3082 2.1800 -0.2778 -0.1516 0.1235  462  THR A OG1   
2653 C  CG2   . THR A 359 ? 2.2798 2.3003 2.0998 -0.2840 -0.1219 0.1148  462  THR A CG2   
2654 N  N     . GLY A 360 ? 1.9757 1.8146 1.7014 -0.3122 -0.1643 0.1421  463  GLY A N     
2655 C  CA    . GLY A 360 ? 2.0566 1.8465 1.7714 -0.3192 -0.1842 0.1521  463  GLY A CA    
2656 C  C     . GLY A 360 ? 1.7636 1.5146 1.4291 -0.3334 -0.1847 0.1588  463  GLY A C     
2657 O  O     . GLY A 360 ? 1.9245 1.6827 1.5631 -0.3355 -0.1697 0.1561  463  GLY A O     
2658 N  N     . SER A 361 ? 2.0359 1.7445 1.6905 -0.3433 -0.2015 0.1683  464  SER A N     
2659 C  CA    . SER A 361 ? 2.2711 1.9364 1.8755 -0.3590 -0.2048 0.1763  464  SER A CA    
2660 C  C     . SER A 361 ? 2.2910 1.9198 1.8657 -0.3589 -0.2235 0.1888  464  SER A C     
2661 O  O     . SER A 361 ? 2.3640 1.9924 1.9628 -0.3487 -0.2407 0.1947  464  SER A O     
2662 C  CB    . SER A 361 ? 2.1873 1.8241 1.7925 -0.3717 -0.2135 0.1817  464  SER A CB    
2663 O  OG    . SER A 361 ? 2.4595 2.0804 2.0949 -0.3659 -0.2361 0.1916  464  SER A OG    
2664 N  N     . ASN A 362 ? 2.2781 1.8754 1.7991 -0.3717 -0.2193 0.1924  465  ASN A N     
2665 C  CA    . ASN A 362 ? 2.3453 1.9040 1.8283 -0.3757 -0.2352 0.2032  465  ASN A CA    
2666 C  C     . ASN A 362 ? 2.5162 2.0321 1.9933 -0.3853 -0.2660 0.2199  465  ASN A C     
2667 O  O     . ASN A 362 ? 2.7132 2.2044 2.1735 -0.3991 -0.2689 0.2249  465  ASN A O     
2668 C  CB    . ASN A 362 ? 2.3344 1.8698 1.7585 -0.3883 -0.2178 0.2007  465  ASN A CB    
2669 C  CG    . ASN A 362 ? 2.3796 1.8854 1.7654 -0.3899 -0.2255 0.2063  465  ASN A CG    
2670 O  OD1   . ASN A 362 ? 2.4108 1.8920 1.7951 -0.3913 -0.2527 0.2180  465  ASN A OD1   
2671 N  ND2   . ASN A 362 ? 2.2712 1.7791 1.6269 -0.3904 -0.2007 0.1983  465  ASN A ND2   
2672 N  N     . PRO A 363 ? 2.5875 2.0939 2.0798 -0.3789 -0.2898 0.2300  466  PRO A N     
2673 C  CA    . PRO A 363 ? 2.5921 2.0599 2.0833 -0.3881 -0.3213 0.2490  466  PRO A CA    
2674 C  C     . PRO A 363 ? 2.5538 1.9695 1.9792 -0.4068 -0.3369 0.2617  466  PRO A C     
2675 O  O     . PRO A 363 ? 2.4828 1.8701 1.9054 -0.4124 -0.3675 0.2791  466  PRO A O     
2676 C  CB    . PRO A 363 ? 2.5911 2.0796 2.1365 -0.3716 -0.3377 0.2533  466  PRO A CB    
2677 C  CG    . PRO A 363 ? 2.3347 1.8579 1.8856 -0.3578 -0.3190 0.2392  466  PRO A CG    
2678 C  CD    . PRO A 363 ? 2.4031 1.9346 1.9169 -0.3630 -0.2896 0.2259  466  PRO A CD    
2679 N  N     . ASN A 364 ? 2.6320 2.0345 2.0040 -0.4176 -0.3158 0.2535  467  ASN A N     
2680 C  CA    . ASN A 364 ? 2.9696 2.3189 2.2705 -0.4383 -0.3260 0.2633  467  ASN A CA    
2681 C  C     . ASN A 364 ? 3.2633 2.5729 2.5310 -0.4585 -0.3358 0.2745  467  ASN A C     
2682 O  O     . ASN A 364 ? 3.3643 2.6245 2.5759 -0.4779 -0.3534 0.2877  467  ASN A O     
2683 C  CB    . ASN A 364 ? 2.8598 2.2103 2.1179 -0.4403 -0.2953 0.2488  467  ASN A CB    
2684 C  CG    . ASN A 364 ? 3.0015 2.2944 2.1820 -0.4624 -0.3028 0.2565  467  ASN A CG    
2685 O  OD1   . ASN A 364 ? 3.2726 2.5346 2.4029 -0.4800 -0.2913 0.2562  467  ASN A OD1   
2686 N  ND2   . ASN A 364 ? 2.9367 2.2135 2.1051 -0.4629 -0.3216 0.2633  467  ASN A ND2   
2687 N  N     . LYS A 365 ? 3.2383 2.5673 2.5372 -0.4555 -0.3245 0.2697  468  LYS A N     
2688 C  CA    . LYS A 365 ? 3.4594 2.7548 2.7348 -0.4727 -0.3312 0.2797  468  LYS A CA    
2689 C  C     . LYS A 365 ? 3.5436 2.7921 2.7375 -0.4960 -0.3244 0.2822  468  LYS A C     
2690 O  O     . LYS A 365 ? 3.8084 3.0166 2.9696 -0.5141 -0.3373 0.2954  468  LYS A O     
2691 C  CB    . LYS A 365 ? 3.6210 2.8950 2.9230 -0.4746 -0.3679 0.3018  468  LYS A CB    
2692 C  CG    . LYS A 365 ? 3.5347 2.7657 2.7974 -0.4877 -0.4008 0.3218  468  LYS A CG    
2693 C  CD    . LYS A 365 ? 3.6600 2.8794 2.9638 -0.4863 -0.4365 0.3448  468  LYS A CD    
2694 C  CE    . LYS A 365 ? 3.5688 2.7490 2.8359 -0.5006 -0.4722 0.3664  468  LYS A CE    
2695 N  NZ    . LYS A 365 ? 3.6117 2.7840 2.9259 -0.4983 -0.5082 0.3914  468  LYS A NZ    
2696 N  N     . GLU A 366 ? 3.1767 2.4283 2.3366 -0.4961 -0.3025 0.2697  469  GLU A N     
2697 C  CA    . GLU A 366 ? 3.1312 2.3400 2.2143 -0.5176 -0.2883 0.2684  469  GLU A CA    
2698 C  C     . GLU A 366 ? 3.0519 2.2883 2.1287 -0.5116 -0.2460 0.2477  469  GLU A C     
2699 O  O     . GLU A 366 ? 3.2106 2.4145 2.2276 -0.5283 -0.2276 0.2443  469  GLU A O     
2700 C  CB    . GLU A 366 ? 3.1539 2.3168 2.1817 -0.5313 -0.3094 0.2796  469  GLU A CB    
2701 C  CG    . GLU A 366 ? 3.1936 2.3228 2.2180 -0.5424 -0.3535 0.3039  469  GLU A CG    
2702 C  CD    . GLU A 366 ? 3.3321 2.4144 2.2953 -0.5601 -0.3749 0.3150  469  GLU A CD    
2703 O  OE1   . GLU A 366 ? 3.1704 2.2389 2.0855 -0.5662 -0.3522 0.3027  469  GLU A OE1   
2704 O  OE2   . GLU A 366 ? 3.4619 2.5207 2.4259 -0.5687 -0.4140 0.3365  469  GLU A OE2   
2705 N  N     . THR A 367 ? 2.9168 2.2113 2.0533 -0.4889 -0.2300 0.2347  470  THR A N     
2706 C  CA    . THR A 367 ? 2.6231 1.9513 1.7647 -0.4814 -0.1915 0.2173  470  THR A CA    
2707 C  C     . THR A 367 ? 2.4209 1.7674 1.5784 -0.4859 -0.1740 0.2112  470  THR A C     
2708 O  O     . THR A 367 ? 2.3789 1.7181 1.5528 -0.4909 -0.1911 0.2188  470  THR A O     
2709 C  CB    . THR A 367 ? 2.7241 2.1065 1.9222 -0.4563 -0.1854 0.2085  470  THR A CB    
2710 O  OG1   . THR A 367 ? 2.7951 2.2095 2.0544 -0.4442 -0.2026 0.2110  470  THR A OG1   
2711 C  CG2   . THR A 367 ? 2.7456 2.1075 1.9223 -0.4534 -0.1980 0.2131  470  THR A CG2   
2712 N  N     . PRO A 368 ? 2.4172 1.7866 1.5709 -0.4850 -0.1391 0.1982  471  PRO A N     
2713 C  CA    . PRO A 368 ? 2.5311 1.9221 1.7031 -0.4899 -0.1220 0.1917  471  PRO A CA    
2714 C  C     . PRO A 368 ? 2.5270 1.9655 1.7678 -0.4757 -0.1314 0.1887  471  PRO A C     
2715 O  O     . PRO A 368 ? 2.2935 1.7767 1.5795 -0.4568 -0.1296 0.1826  471  PRO A O     
2716 C  CB    . PRO A 368 ? 2.4589 1.8768 1.6271 -0.4866 -0.0837 0.1789  471  PRO A CB    
2717 C  CG    . PRO A 368 ? 2.3323 1.7557 1.4984 -0.4734 -0.0813 0.1773  471  PRO A CG    
2718 C  CD    . PRO A 368 ? 2.5511 1.9221 1.6796 -0.4819 -0.1127 0.1899  471  PRO A CD    
2719 N  N     . CYS A 369 ? 2.5053 1.9311 1.7517 -0.4859 -0.1403 0.1930  472  CYS A N     
2720 C  CA    . CYS A 369 ? 2.2372 1.6977 1.5426 -0.4762 -0.1485 0.1902  472  CYS A CA    
2721 C  C     . CYS A 369 ? 2.2119 1.7037 1.5341 -0.4817 -0.1230 0.1782  472  CYS A C     
2722 O  O     . CYS A 369 ? 2.3427 1.8057 1.6332 -0.4993 -0.1161 0.1803  472  CYS A O     
2723 C  CB    . CYS A 369 ? 2.2327 1.6539 1.5373 -0.4831 -0.1786 0.2051  472  CYS A CB    
2724 S  SG    . CYS A 369 ? 2.3231 1.7754 1.6942 -0.4752 -0.1834 0.2012  472  CYS A SG    
2725 N  N     . LEU A 370 ? 2.2357 1.7860 1.6066 -0.4679 -0.1098 0.1663  473  LEU A N     
2726 C  CA    . LEU A 370 ? 1.9213 1.5089 1.3138 -0.4732 -0.0871 0.1548  473  LEU A CA    
2727 C  C     . LEU A 370 ? 2.0474 1.6465 1.4789 -0.4735 -0.0974 0.1525  473  LEU A C     
2728 O  O     . LEU A 370 ? 2.1647 1.7835 1.6340 -0.4595 -0.1104 0.1519  473  LEU A O     
2729 C  CB    . LEU A 370 ? 1.7171 1.3631 1.1388 -0.4600 -0.0667 0.1444  473  LEU A CB    
2730 C  CG    . LEU A 370 ? 2.0793 1.7703 1.5245 -0.4661 -0.0430 0.1335  473  LEU A CG    
2731 C  CD1   . LEU A 370 ? 1.8317 1.4964 1.2357 -0.4841 -0.0245 0.1340  473  LEU A CD1   
2732 C  CD2   . LEU A 370 ? 2.0048 1.7563 1.4859 -0.4508 -0.0290 0.1268  473  LEU A CD2   
2733 N  N     . GLU A 371 ? 2.1249 1.7099 1.5466 -0.4898 -0.0898 0.1508  474  GLU A N     
2734 C  CA    . GLU A 371 ? 2.2415 1.8312 1.6958 -0.4927 -0.0958 0.1478  474  GLU A CA    
2735 C  C     . GLU A 371 ? 2.2540 1.8987 1.7411 -0.4946 -0.0742 0.1320  474  GLU A C     
2736 O  O     . GLU A 371 ? 2.1048 1.7681 1.5786 -0.5028 -0.0535 0.1263  474  GLU A O     
2737 C  CB    . GLU A 371 ? 2.1574 1.6937 1.5808 -0.5105 -0.1022 0.1569  474  GLU A CB    
2738 C  CG    . GLU A 371 ? 2.0982 1.5784 1.4869 -0.5119 -0.1264 0.1750  474  GLU A CG    
2739 C  CD    . GLU A 371 ? 2.4202 1.8488 1.7816 -0.5293 -0.1345 0.1860  474  GLU A CD    
2740 O  OE1   . GLU A 371 ? 2.4521 1.8880 1.8290 -0.5380 -0.1226 0.1789  474  GLU A OE1   
2741 O  OE2   . GLU A 371 ? 2.7758 2.1557 2.0989 -0.5354 -0.1531 0.2021  474  GLU A OE2   
2742 N  N     . LEU A 372 ? 2.1128 1.7834 1.6429 -0.4881 -0.0788 0.1253  475  LEU A N     
2743 C  CA    . LEU A 372 ? 1.9800 1.7034 1.5415 -0.4913 -0.0616 0.1104  475  LEU A CA    
2744 C  C     . LEU A 372 ? 2.0519 1.7657 1.6343 -0.5001 -0.0636 0.1050  475  LEU A C     
2745 O  O     . LEU A 372 ? 2.1980 1.8671 1.7766 -0.5006 -0.0782 0.1137  475  LEU A O     
2746 C  CB    . LEU A 372 ? 2.1969 1.9716 1.7914 -0.4738 -0.0612 0.1048  475  LEU A CB    
2747 C  CG    . LEU A 372 ? 2.1919 1.9885 1.7757 -0.4636 -0.0541 0.1075  475  LEU A CG    
2748 C  CD1   . LEU A 372 ? 1.9229 1.6821 1.4862 -0.4519 -0.0711 0.1193  475  LEU A CD1   
2749 C  CD2   . LEU A 372 ? 1.9429 1.8035 1.5648 -0.4531 -0.0463 0.0990  475  LEU A CD2   
2750 N  N     . GLU A 373 ? 2.0106 1.7669 1.6160 -0.5077 -0.0483 0.0911  476  GLU A N     
2751 C  CA    . GLU A 373 ? 2.0564 1.8089 1.6834 -0.5169 -0.0461 0.0825  476  GLU A CA    
2752 C  C     . GLU A 373 ? 2.1446 1.9571 1.8027 -0.5174 -0.0350 0.0675  476  GLU A C     
2753 O  O     . GLU A 373 ? 2.0841 1.9359 1.7403 -0.5250 -0.0214 0.0620  476  GLU A O     
2754 C  CB    . GLU A 373 ? 2.2966 2.0186 1.9009 -0.5382 -0.0366 0.0819  476  GLU A CB    
2755 C  CG    . GLU A 373 ? 2.4663 2.1826 2.0915 -0.5495 -0.0309 0.0717  476  GLU A CG    
2756 C  CD    . GLU A 373 ? 2.5153 2.1956 2.1169 -0.5701 -0.0222 0.0725  476  GLU A CD    
2757 O  OE1   . GLU A 373 ? 2.4902 2.1367 2.0580 -0.5735 -0.0258 0.0846  476  GLU A OE1   
2758 O  OE2   . GLU A 373 ? 2.6848 2.3692 2.2995 -0.5841 -0.0110 0.0609  476  GLU A OE2   
2759 N  N     . PHE A 374 ? 2.0518 1.8714 1.7389 -0.5099 -0.0406 0.0618  477  PHE A N     
2760 C  CA    . PHE A 374 ? 1.8676 1.7409 1.5815 -0.5106 -0.0325 0.0483  477  PHE A CA    
2761 C  C     . PHE A 374 ? 2.0340 1.9083 1.7553 -0.5312 -0.0202 0.0345  477  PHE A C     
2762 O  O     . PHE A 374 ? 2.4126 2.2428 2.1234 -0.5417 -0.0187 0.0356  477  PHE A O     
2763 C  CB    . PHE A 374 ? 1.9089 1.7896 1.6476 -0.4911 -0.0438 0.0491  477  PHE A CB    
2764 C  CG    . PHE A 374 ? 1.9717 1.8501 1.7034 -0.4716 -0.0559 0.0619  477  PHE A CG    
2765 C  CD1   . PHE A 374 ? 2.0960 1.9244 1.8151 -0.4631 -0.0709 0.0754  477  PHE A CD1   
2766 C  CD2   . PHE A 374 ? 1.7477 1.6734 1.4854 -0.4626 -0.0526 0.0613  477  PHE A CD2   
2767 C  CE1   . PHE A 374 ? 2.0414 1.8659 1.7510 -0.4476 -0.0819 0.0863  477  PHE A CE1   
2768 C  CE2   . PHE A 374 ? 1.6723 1.5932 1.4023 -0.4454 -0.0618 0.0722  477  PHE A CE2   
2769 C  CZ    . PHE A 374 ? 2.0526 1.9222 1.7670 -0.4387 -0.0763 0.0839  477  PHE A CZ    
2770 N  N     . ASP A 375 ? 2.0275 1.9520 1.7659 -0.5380 -0.0116 0.0219  478  ASP A N     
2771 C  CA    . ASP A 375 ? 2.1073 2.0366 1.8505 -0.5602 0.0010  0.0069  478  ASP A CA    
2772 C  C     . ASP A 375 ? 2.2705 2.1604 2.0270 -0.5580 -0.0007 0.0019  478  ASP A C     
2773 O  O     . ASP A 375 ? 2.1317 2.0121 1.9035 -0.5389 -0.0109 0.0066  478  ASP A O     
2774 C  CB    . ASP A 375 ? 2.0845 2.0781 1.8415 -0.5686 0.0079  -0.0041 478  ASP A CB    
2775 C  CG    . ASP A 375 ? 2.2770 2.2833 2.0292 -0.5974 0.0220  -0.0175 478  ASP A CG    
2776 O  OD1   . ASP A 375 ? 2.3460 2.3078 2.0896 -0.6096 0.0279  -0.0223 478  ASP A OD1   
2777 O  OD2   . ASP A 375 ? 2.2314 2.2923 1.9896 -0.6084 0.0269  -0.0224 478  ASP A OD2   
2778 N  N     . TRP A 376 ? 2.4236 2.2898 2.1758 -0.5779 0.0108  -0.0078 479  TRP A N     
2779 C  CA    . TRP A 376 ? 2.5494 2.3702 2.3147 -0.5768 0.0125  -0.0114 479  TRP A CA    
2780 C  C     . TRP A 376 ? 2.6033 2.4465 2.3869 -0.5843 0.0230  -0.0295 479  TRP A C     
2781 O  O     . TRP A 376 ? 2.5981 2.4324 2.4021 -0.5693 0.0191  -0.0298 479  TRP A O     
2782 C  CB    . TRP A 376 ? 2.4069 2.1817 2.1568 -0.5938 0.0207  -0.0110 479  TRP A CB    
2783 C  CG    . TRP A 376 ? 2.5258 2.2476 2.2914 -0.5895 0.0218  -0.0101 479  TRP A CG    
2784 C  CD1   . TRP A 376 ? 2.7657 2.4649 2.5526 -0.5673 0.0098  0.0000  479  TRP A CD1   
2785 C  CD2   . TRP A 376 ? 2.5862 2.2714 2.3510 -0.6077 0.0369  -0.0189 479  TRP A CD2   
2786 N  NE1   . TRP A 376 ? 2.8198 2.4715 2.6220 -0.5696 0.0166  -0.0009 479  TRP A NE1   
2787 C  CE2   . TRP A 376 ? 2.7007 2.3415 2.4888 -0.5940 0.0338  -0.0127 479  TRP A CE2   
2788 C  CE3   . TRP A 376 ? 2.6206 2.3059 2.3685 -0.6345 0.0532  -0.0310 479  TRP A CE3   
2789 C  CZ2   . TRP A 376 ? 3.0350 2.6306 2.8308 -0.6051 0.0478  -0.0181 479  TRP A CZ2   
2790 C  CZ3   . TRP A 376 ? 2.4750 2.1142 2.2271 -0.6467 0.0667  -0.0374 479  TRP A CZ3   
2791 C  CH2   . TRP A 376 ? 2.9566 2.5508 2.7328 -0.6315 0.0645  -0.0308 479  TRP A CH2   
2792 N  N     . PHE A 377 ? 2.2388 2.1097 2.0142 -0.6089 0.0368  -0.0446 480  PHE A N     
2793 C  CA    . PHE A 377 ? 2.0240 1.9134 1.8078 -0.6240 0.0492  -0.0640 480  PHE A CA    
2794 C  C     . PHE A 377 ? 2.1977 2.0330 1.9894 -0.6300 0.0612  -0.0730 480  PHE A C     
2795 O  O     . PHE A 377 ? 2.0797 1.9214 1.8752 -0.6445 0.0746  -0.0908 480  PHE A O     
2796 C  CB    . PHE A 377 ? 1.9194 1.8483 1.7187 -0.6095 0.0424  -0.0657 480  PHE A CB    
2797 C  CG    . PHE A 377 ? 2.0358 2.0160 1.8324 -0.5996 0.0309  -0.0552 480  PHE A CG    
2798 C  CD1   . PHE A 377 ? 1.7930 1.8251 1.5821 -0.6180 0.0352  -0.0609 480  PHE A CD1   
2799 C  CD2   . PHE A 377 ? 2.3757 2.3523 2.1792 -0.5724 0.0164  -0.0391 480  PHE A CD2   
2800 C  CE1   . PHE A 377 ? 1.8881 1.9673 1.6796 -0.6077 0.0264  -0.0499 480  PHE A CE1   
2801 C  CE2   . PHE A 377 ? 2.2979 2.3187 2.0997 -0.5630 0.0085  -0.0298 480  PHE A CE2   
2802 C  CZ    . PHE A 377 ? 1.8388 1.9109 1.6362 -0.5798 0.0142  -0.0348 480  PHE A CZ    
2803 N  N     . SER A 378 ? 2.3122 2.0936 2.1063 -0.6199 0.0574  -0.0607 481  SER A N     
2804 C  CA    . SER A 378 ? 2.3470 2.0735 2.1531 -0.6235 0.0693  -0.0660 481  SER A CA    
2805 C  C     . SER A 378 ? 2.3487 2.0724 2.1807 -0.6125 0.0743  -0.0744 481  SER A C     
2806 O  O     . SER A 378 ? 2.5430 2.2341 2.3849 -0.6220 0.0918  -0.0867 481  SER A O     
2807 C  CB    . SER A 378 ? 2.2978 2.0125 2.0877 -0.6546 0.0893  -0.0824 481  SER A CB    
2808 O  OG    . SER A 378 ? 1.9940 1.7483 1.7795 -0.6735 0.1012  -0.1030 481  SER A OG    
2809 N  N     . SER A 379 ? 2.3733 2.1289 2.2163 -0.5927 0.0608  -0.0679 482  SER A N     
2810 C  CA    . SER A 379 ? 2.1446 1.9000 2.0120 -0.5813 0.0653  -0.0749 482  SER A CA    
2811 C  C     . SER A 379 ? 2.1172 1.8965 1.9965 -0.5544 0.0450  -0.0597 482  SER A C     
2812 O  O     . SER A 379 ? 2.3180 2.1229 2.1831 -0.5485 0.0305  -0.0480 482  SER A O     
2813 C  CB    . SER A 379 ? 2.1886 1.9768 2.0473 -0.6030 0.0819  -0.0984 482  SER A CB    
2814 O  OG    . SER A 379 ? 2.4896 2.2724 2.3695 -0.5932 0.0889  -0.1061 482  SER A OG    
2815 N  N     . VAL A 380 ? 2.1727 1.9420 2.0788 -0.5387 0.0460  -0.0605 483  VAL A N     
2816 C  CA    . VAL A 380 ? 1.9679 1.7564 1.8882 -0.5133 0.0282  -0.0472 483  VAL A CA    
2817 C  C     . VAL A 380 ? 1.8263 1.6710 1.7389 -0.5179 0.0305  -0.0588 483  VAL A C     
2818 O  O     . VAL A 380 ? 2.2414 2.0919 2.1656 -0.5202 0.0422  -0.0720 483  VAL A O     
2819 C  CB    . VAL A 380 ? 1.4572 1.2091 1.4133 -0.4941 0.0276  -0.0410 483  VAL A CB    
2820 C  CG1   . VAL A 380 ? 1.6728 1.4450 1.6425 -0.4692 0.0083  -0.0269 483  VAL A CG1   
2821 C  CG2   . VAL A 380 ? 1.8755 1.5725 1.8414 -0.4913 0.0250  -0.0279 483  VAL A CG2   
2822 N  N     . VAL A 381 ? 2.0729 1.9583 1.9658 -0.5196 0.0201  -0.0530 484  VAL A N     
2823 C  CA    . VAL A 381 ? 2.0365 1.9785 1.9234 -0.5237 0.0202  -0.0604 484  VAL A CA    
2824 C  C     . VAL A 381 ? 1.9593 1.9127 1.8652 -0.4982 0.0090  -0.0517 484  VAL A C     
2825 O  O     . VAL A 381 ? 2.0538 2.0031 1.9633 -0.4785 -0.0069 -0.0346 484  VAL A O     
2826 C  CB    . VAL A 381 ? 2.2407 2.2224 2.1064 -0.5321 0.0138  -0.0549 484  VAL A CB    
2827 C  CG1   . VAL A 381 ? 1.9224 1.9643 1.7853 -0.5377 0.0137  -0.0610 484  VAL A CG1   
2828 C  CG2   . VAL A 381 ? 2.2779 2.2443 2.1260 -0.5569 0.0245  -0.0621 484  VAL A CG2   
2829 N  N     . LYS A 382 ? 1.6361 1.6023 1.5523 -0.4998 0.0180  -0.0639 485  LYS A N     
2830 C  CA    . LYS A 382 ? 1.6429 1.6188 1.5785 -0.4774 0.0102  -0.0578 485  LYS A CA    
2831 C  C     . LYS A 382 ? 1.4478 1.4797 1.3740 -0.4827 0.0102  -0.0639 485  LYS A C     
2832 O  O     . LYS A 382 ? 1.5959 1.6482 1.5073 -0.5062 0.0219  -0.0789 485  LYS A O     
2833 C  CB    . LYS A 382 ? 1.4445 1.3809 1.4048 -0.4721 0.0220  -0.0651 485  LYS A CB    
2834 C  CG    . LYS A 382 ? 1.5426 1.4848 1.5265 -0.4486 0.0146  -0.0582 485  LYS A CG    
2835 C  CD    . LYS A 382 ? 1.9189 1.8211 1.9312 -0.4442 0.0290  -0.0654 485  LYS A CD    
2836 C  CE    . LYS A 382 ? 2.2003 2.1093 2.2381 -0.4213 0.0222  -0.0583 485  LYS A CE    
2837 N  NZ    . LYS A 382 ? 2.3200 2.1908 2.3901 -0.4162 0.0381  -0.0648 485  LYS A NZ    
2838 N  N     . PHE A 383 ? 1.4660 1.5219 1.4001 -0.4618 -0.0035 -0.0515 486  PHE A N     
2839 C  CA    . PHE A 383 ? 1.4518 1.5607 1.3799 -0.4640 -0.0051 -0.0540 486  PHE A CA    
2840 C  C     . PHE A 383 ? 1.5571 1.6651 1.4899 -0.4730 0.0087  -0.0703 486  PHE A C     
2841 O  O     . PHE A 383 ? 1.8920 1.9636 1.8439 -0.4623 0.0144  -0.0728 486  PHE A O     
2842 C  CB    . PHE A 383 ? 1.6964 1.8238 1.6343 -0.4378 -0.0210 -0.0372 486  PHE A CB    
2843 C  CG    . PHE A 383 ? 1.5672 1.7522 1.4985 -0.4388 -0.0248 -0.0351 486  PHE A CG    
2844 C  CD1   . PHE A 383 ? 1.4732 1.6936 1.3923 -0.4444 -0.0300 -0.0276 486  PHE A CD1   
2845 C  CD2   . PHE A 383 ? 1.8137 2.0173 1.7528 -0.4340 -0.0226 -0.0394 486  PHE A CD2   
2846 C  CE1   . PHE A 383 ? 1.5771 1.8518 1.4950 -0.4445 -0.0339 -0.0232 486  PHE A CE1   
2847 C  CE2   . PHE A 383 ? 1.5046 1.7611 1.4384 -0.4350 -0.0273 -0.0353 486  PHE A CE2   
2848 C  CZ    . PHE A 383 ? 1.2686 1.5614 1.1933 -0.4398 -0.0334 -0.0265 486  PHE A CZ    
2849 N  N     . PRO A 384 ? 1.4950 1.6413 1.4109 -0.4935 0.0148  -0.0810 487  PRO A N     
2850 C  CA    . PRO A 384 ? 1.8421 1.9834 1.7556 -0.5065 0.0301  -0.0983 487  PRO A CA    
2851 C  C     . PRO A 384 ? 1.6822 1.8302 1.6122 -0.4853 0.0265  -0.0935 487  PRO A C     
2852 O  O     . PRO A 384 ? 1.5972 1.7733 1.5338 -0.4662 0.0111  -0.0781 487  PRO A O     
2853 C  CB    . PRO A 384 ? 1.7548 1.9423 1.6423 -0.5345 0.0321  -0.1068 487  PRO A CB    
2854 C  CG    . PRO A 384 ? 1.5918 1.8223 1.4787 -0.5251 0.0143  -0.0889 487  PRO A CG    
2855 C  CD    . PRO A 384 ? 1.3909 1.5872 1.2893 -0.5071 0.0080  -0.0771 487  PRO A CD    
2856 N  N     . ASP A 385 ? 1.7174 1.8375 1.6542 -0.4893 0.0428  -0.1073 488  ASP A N     
2857 C  CA    . ASP A 385 ? 1.9912 2.1146 1.9438 -0.4719 0.0429  -0.1052 488  ASP A CA    
2858 C  C     . ASP A 385 ? 1.7468 1.9211 1.6790 -0.4833 0.0406  -0.1082 488  ASP A C     
2859 O  O     . ASP A 385 ? 1.7200 1.9271 1.6280 -0.5052 0.0384  -0.1117 488  ASP A O     
2860 C  CB    . ASP A 385 ? 2.0414 2.1166 2.0100 -0.4731 0.0640  -0.1191 488  ASP A CB    
2861 C  CG    . ASP A 385 ? 1.9746 2.0396 1.9189 -0.5058 0.0861  -0.1421 488  ASP A CG    
2862 O  OD1   . ASP A 385 ? 1.9783 2.0577 1.8988 -0.5271 0.0847  -0.1462 488  ASP A OD1   
2863 O  OD2   . ASP A 385 ? 1.9214 1.9631 1.8698 -0.5111 0.1060  -0.1564 488  ASP A OD2   
2864 N  N     . MET A 386 ? 1.6335 1.8148 1.5766 -0.4686 0.0404  -0.1057 489  MET A N     
2865 C  CA    . MET A 386 ? 1.7395 1.9678 1.6643 -0.4777 0.0370  -0.1062 489  MET A CA    
2866 C  C     . MET A 386 ? 1.8357 2.0655 1.7313 -0.5122 0.0539  -0.1271 489  MET A C     
2867 O  O     . MET A 386 ? 1.7906 2.0649 1.6628 -0.5292 0.0480  -0.1269 489  MET A O     
2868 C  CB    . MET A 386 ? 2.0214 2.2505 1.9641 -0.4549 0.0352  -0.0998 489  MET A CB    
2869 C  CG    . MET A 386 ? 2.2259 2.5010 2.1505 -0.4624 0.0314  -0.0985 489  MET A CG    
2870 S  SD    . MET A 386 ? 1.4866 1.8253 1.3988 -0.4641 0.0090  -0.0803 489  MET A SD    
2871 C  CE    . MET A 386 ? 1.4484 1.7821 1.3909 -0.4251 -0.0072 -0.0582 489  MET A CE    
2872 N  N     . SER A 387 ? 2.0194 2.2008 1.9158 -0.5237 0.0751  -0.1446 490  SER A N     
2873 C  CA    . SER A 387 ? 1.8131 1.9892 1.6781 -0.5588 0.0940  -0.1666 490  SER A CA    
2874 C  C     . SER A 387 ? 1.8572 2.0647 1.6946 -0.5856 0.0863  -0.1681 490  SER A C     
2875 O  O     . SER A 387 ? 1.8744 2.1127 1.6811 -0.6126 0.0872  -0.1760 490  SER A O     
2876 C  CB    . SER A 387 ? 1.8598 1.9731 1.7348 -0.5641 0.1202  -0.1841 490  SER A CB    
2877 O  OG    . SER A 387 ? 2.1795 2.2827 2.0207 -0.6000 0.1409  -0.2071 490  SER A OG    
2878 N  N     . VAL A 388 ? 1.7685 1.9693 1.6161 -0.5799 0.0782  -0.1599 491  VAL A N     
2879 C  CA    . VAL A 388 ? 1.5340 1.7659 1.3596 -0.6042 0.0708  -0.1599 491  VAL A CA    
2880 C  C     . VAL A 388 ? 1.8316 2.1276 1.6563 -0.5970 0.0476  -0.1407 491  VAL A C     
2881 O  O     . VAL A 388 ? 1.7401 2.0770 1.5438 -0.6218 0.0415  -0.1414 491  VAL A O     
2882 C  CB    . VAL A 388 ? 1.4658 1.6662 1.3018 -0.6010 0.0719  -0.1578 491  VAL A CB    
2883 C  CG1   . VAL A 388 ? 1.9118 2.1414 1.7253 -0.6289 0.0674  -0.1600 491  VAL A CG1   
2884 C  CG2   . VAL A 388 ? 1.7047 1.8402 1.5477 -0.6044 0.0951  -0.1740 491  VAL A CG2   
2885 N  N     . ILE A 389 ? 1.8269 2.1329 1.6756 -0.5639 0.0346  -0.1229 492  ILE A N     
2886 C  CA    . ILE A 389 ? 1.7060 2.0699 1.5575 -0.5544 0.0148  -0.1037 492  ILE A CA    
2887 C  C     . ILE A 389 ? 1.6612 2.0646 1.4934 -0.5714 0.0133  -0.1067 492  ILE A C     
2888 O  O     . ILE A 389 ? 1.7451 2.2005 1.5672 -0.5850 0.0011  -0.0980 492  ILE A O     
2889 C  CB    . ILE A 389 ? 1.6635 2.0221 1.5429 -0.5158 0.0039  -0.0856 492  ILE A CB    
2890 C  CG1   . ILE A 389 ? 1.4154 1.7432 1.3083 -0.5028 0.0011  -0.0793 492  ILE A CG1   
2891 C  CG2   . ILE A 389 ? 1.6373 2.0531 1.5206 -0.5049 -0.0129 -0.0668 492  ILE A CG2   
2892 C  CD1   . ILE A 389 ? 1.5759 1.8959 1.4917 -0.4682 -0.0104 -0.0617 492  ILE A CD1   
2893 N  N     . GLU A 390 ? 1.8454 2.2249 1.6727 -0.5718 0.0256  -0.1182 493  GLU A N     
2894 C  CA    . GLU A 390 ? 1.8754 2.2865 1.6784 -0.5916 0.0258  -0.1227 493  GLU A CA    
2895 C  C     . GLU A 390 ? 1.9478 2.3600 1.7157 -0.6344 0.0358  -0.1413 493  GLU A C     
2896 O  O     . GLU A 390 ? 1.9957 2.4473 1.7390 -0.6570 0.0295  -0.1410 493  GLU A O     
2897 C  CB    . GLU A 390 ? 2.0818 2.4643 1.8890 -0.5792 0.0380  -0.1298 493  GLU A CB    
2898 C  CG    . GLU A 390 ? 2.3859 2.7065 2.1894 -0.5893 0.0640  -0.1530 493  GLU A CG    
2899 C  CD    . GLU A 390 ? 2.4194 2.7124 2.2351 -0.5728 0.0765  -0.1576 493  GLU A CD    
2900 O  OE1   . GLU A 390 ? 1.9910 2.3098 1.8200 -0.5504 0.0634  -0.1418 493  GLU A OE1   
2901 O  OE2   . GLU A 390 ? 2.6215 2.8662 2.4347 -0.5821 0.1006  -0.1770 493  GLU A OE2   
2902 N  N     . GLU A 391 ? 2.0496 2.4188 1.8137 -0.6469 0.0508  -0.1568 494  GLU A N     
2903 C  CA    . GLU A 391 ? 2.1905 2.5598 1.9204 -0.6890 0.0601  -0.1745 494  GLU A CA    
2904 C  C     . GLU A 391 ? 2.1631 2.5864 1.8885 -0.7028 0.0408  -0.1615 494  GLU A C     
2905 O  O     . GLU A 391 ? 2.3842 2.8440 2.0819 -0.7348 0.0354  -0.1647 494  GLU A O     
2906 C  CB    . GLU A 391 ? 2.0671 2.3724 1.7972 -0.6966 0.0831  -0.1939 494  GLU A CB    
2907 C  CG    . GLU A 391 ? 2.1062 2.4071 1.8023 -0.7396 0.0934  -0.2121 494  GLU A CG    
2908 C  CD    . GLU A 391 ? 2.4743 2.7811 2.1302 -0.7738 0.1038  -0.2291 494  GLU A CD    
2909 O  OE1   . GLU A 391 ? 2.4008 2.6916 2.0558 -0.7642 0.1131  -0.2337 494  GLU A OE1   
2910 O  OE2   . GLU A 391 ? 2.7737 3.1004 2.3974 -0.8117 0.1026  -0.2379 494  GLU A OE2   
2911 N  N     . HIS A 392 ? 2.0442 2.4731 1.7967 -0.6800 0.0302  -0.1461 495  HIS A N     
2912 C  CA    . HIS A 392 ? 2.1347 2.6166 1.8896 -0.6887 0.0128  -0.1313 495  HIS A CA    
2913 C  C     . HIS A 392 ? 2.0887 2.6338 1.8501 -0.6802 -0.0070 -0.1108 495  HIS A C     
2914 O  O     . HIS A 392 ? 2.3066 2.9042 2.0656 -0.6963 -0.0206 -0.1000 495  HIS A O     
2915 C  CB    . HIS A 392 ? 2.2726 2.7394 2.0534 -0.6652 0.0091  -0.1203 495  HIS A CB    
2916 C  CG    . HIS A 392 ? 2.2161 2.7343 2.0036 -0.6714 -0.0058 -0.1048 495  HIS A CG    
2917 N  ND1   . HIS A 392 ? 2.0002 2.5660 1.8090 -0.6492 -0.0228 -0.0812 495  HIS A ND1   
2918 C  CD2   . HIS A 392 ? 2.1352 2.6644 1.9131 -0.6973 -0.0049 -0.1092 495  HIS A CD2   
2919 C  CE1   . HIS A 392 ? 2.0128 2.6173 1.8269 -0.6605 -0.0310 -0.0714 495  HIS A CE1   
2920 N  NE2   . HIS A 392 ? 2.2240 2.8081 2.0195 -0.6900 -0.0210 -0.0880 495  HIS A NE2   
2921 N  N     . ALA A 393 ? 1.8788 2.4203 1.6507 -0.6554 -0.0086 -0.1042 496  ALA A N     
2922 C  CA    . ALA A 393 ? 2.0008 2.5994 1.7776 -0.6481 -0.0260 -0.0849 496  ALA A CA    
2923 C  C     . ALA A 393 ? 2.2071 2.8406 1.9512 -0.6867 -0.0296 -0.0910 496  ALA A C     
2924 O  O     . ALA A 393 ? 2.3591 3.0525 2.1067 -0.6907 -0.0478 -0.0724 496  ALA A O     
2925 C  CB    . ALA A 393 ? 1.9351 2.5162 1.7259 -0.6168 -0.0243 -0.0796 496  ALA A CB    
2926 N  N     . ASN A 394 ? 2.2798 2.8759 1.9920 -0.7162 -0.0124 -0.1162 497  ASN A N     
2927 C  CA    . ASN A 394 ? 2.2845 2.9093 1.9590 -0.7585 -0.0154 -0.1240 497  ASN A CA    
2928 C  C     . ASN A 394 ? 2.2427 2.9069 1.9138 -0.7844 -0.0271 -0.1188 497  ASN A C     
2929 O  O     . ASN A 394 ? 2.2684 2.9872 1.9256 -0.8087 -0.0432 -0.1089 497  ASN A O     
2930 C  CB    . ASN A 394 ? 2.3412 2.9089 1.9803 -0.7841 0.0098  -0.1544 497  ASN A CB    
2931 C  CG    . ASN A 394 ? 2.3165 2.8483 1.9591 -0.7619 0.0226  -0.1598 497  ASN A CG    
2932 O  OD1   . ASN A 394 ? 2.3194 2.8566 1.9947 -0.7233 0.0149  -0.1432 497  ASN A OD1   
2933 N  ND2   . ASN A 394 ? 2.2968 2.7904 1.9051 -0.7871 0.0436  -0.1837 497  ASN A ND2   
2934 N  N     . TRP A 395 ? 2.4040 3.0421 2.0887 -0.7800 -0.0197 -0.1241 498  TRP A N     
2935 C  CA    . TRP A 395 ? 2.5503 3.2215 2.2327 -0.8055 -0.0281 -0.1208 498  TRP A CA    
2936 C  C     . TRP A 395 ? 2.4342 3.1779 2.1449 -0.7930 -0.0527 -0.0907 498  TRP A C     
2937 O  O     . TRP A 395 ? 2.3702 3.1600 2.0770 -0.8200 -0.0643 -0.0842 498  TRP A O     
2938 C  CB    . TRP A 395 ? 2.6770 3.3020 2.3702 -0.7991 -0.0144 -0.1309 498  TRP A CB    
2939 C  CG    . TRP A 395 ? 2.7974 3.3609 2.4605 -0.8244 0.0095  -0.1607 498  TRP A CG    
2940 C  CD1   . TRP A 395 ? 2.8495 3.3931 2.4765 -0.8516 0.0216  -0.1802 498  TRP A CD1   
2941 C  CD2   . TRP A 395 ? 2.9888 3.5006 2.6548 -0.8254 0.0259  -0.1741 498  TRP A CD2   
2942 N  NE1   . TRP A 395 ? 3.0883 3.5702 2.6974 -0.8687 0.0461  -0.2056 498  TRP A NE1   
2943 C  CE2   . TRP A 395 ? 3.2052 3.6673 2.8389 -0.8527 0.0484  -0.2016 498  TRP A CE2   
2944 C  CE3   . TRP A 395 ? 2.8477 3.3487 2.5394 -0.8065 0.0245  -0.1653 498  TRP A CE3   
2945 C  CZ2   . TRP A 395 ? 3.2998 3.7031 2.9295 -0.8601 0.0692  -0.2194 498  TRP A CZ2   
2946 C  CZ3   . TRP A 395 ? 2.8213 3.2646 2.5066 -0.8147 0.0434  -0.1825 498  TRP A CZ3   
2947 C  CH2   . TRP A 395 ? 3.0320 3.4277 2.6883 -0.8406 0.0654  -0.2088 498  TRP A CH2   
2948 N  N     . SER A 396 ? 2.3943 3.1487 2.1353 -0.7526 -0.0601 -0.0717 499  SER A N     
2949 C  CA    . SER A 396 ? 2.2146 3.0356 1.9853 -0.7384 -0.0807 -0.0425 499  SER A CA    
2950 C  C     . SER A 396 ? 2.2621 3.1407 2.0178 -0.7635 -0.0971 -0.0322 499  SER A C     
2951 O  O     . SER A 396 ? 2.3762 3.3156 2.1466 -0.7752 -0.1137 -0.0137 499  SER A O     
2952 C  CB    . SER A 396 ? 2.3540 3.1672 2.1564 -0.6909 -0.0825 -0.0265 499  SER A CB    
2953 O  OG    . SER A 396 ? 2.3807 3.1779 2.1715 -0.6815 -0.0799 -0.0302 499  SER A OG    
2954 N  N     . VAL A 397 ? 2.0965 2.9572 1.8237 -0.7725 -0.0927 -0.0429 500  VAL A N     
2955 C  CA    . VAL A 397 ? 2.1388 3.0494 1.8449 -0.7996 -0.1084 -0.0340 500  VAL A CA    
2956 C  C     . VAL A 397 ? 2.3660 3.2776 2.0308 -0.8522 -0.1065 -0.0525 500  VAL A C     
2957 O  O     . VAL A 397 ? 2.4833 3.4507 2.1363 -0.8808 -0.1252 -0.0403 500  VAL A O     
2958 C  CB    . VAL A 397 ? 1.8431 2.7341 1.5341 -0.7870 -0.1042 -0.0365 500  VAL A CB    
2959 C  CG1   . VAL A 397 ? 1.7853 2.7251 1.4497 -0.8165 -0.1210 -0.0267 500  VAL A CG1   
2960 C  CG2   . VAL A 397 ? 1.5705 2.4633 1.3025 -0.7364 -0.1074 -0.0171 500  VAL A CG2   
2961 N  N     . SER A 398 ? 2.5394 3.3910 2.1828 -0.8666 -0.0847 -0.0807 501  SER A N     
2962 C  CA    . SER A 398 ? 2.5817 3.4286 2.1834 -0.9179 -0.0802 -0.1005 501  SER A CA    
2963 C  C     . SER A 398 ? 2.5254 3.4128 2.1429 -0.9355 -0.0919 -0.0912 501  SER A C     
2964 O  O     . SER A 398 ? 2.5468 3.4602 2.1357 -0.9803 -0.0994 -0.0965 501  SER A O     
2965 C  CB    . SER A 398 ? 2.6494 3.4142 2.2232 -0.9271 -0.0499 -0.1344 501  SER A CB    
2966 O  OG    . SER A 398 ? 3.0774 3.8086 2.6775 -0.9070 -0.0387 -0.1388 501  SER A OG    
2967 N  N     . ARG A 399 ? 2.3073 3.2003 1.9685 -0.9029 -0.0932 -0.0776 502  ARG A N     
2968 C  CA    . ARG A 399 ? 2.3267 3.2602 2.0075 -0.9168 -0.1031 -0.0671 502  ARG A CA    
2969 C  C     . ARG A 399 ? 2.3660 3.3860 2.0697 -0.9221 -0.1309 -0.0362 502  ARG A C     
2970 O  O     . ARG A 399 ? 2.4997 3.5622 2.2193 -0.9399 -0.1409 -0.0263 502  ARG A O     
2971 C  CB    . ARG A 399 ? 2.1604 3.0687 1.8782 -0.8805 -0.0938 -0.0625 502  ARG A CB    
2972 N  N     . GLU A 400 ? 2.2432 3.2901 1.9511 -0.9069 -0.1430 -0.0201 503  GLU A N     
2973 C  CA    . GLU A 400 ? 2.3219 3.4509 2.0547 -0.9090 -0.1698 0.0121  503  GLU A CA    
2974 C  C     . GLU A 400 ? 2.6789 3.8474 2.4685 -0.8808 -0.1766 0.0368  503  GLU A C     
2975 O  O     . GLU A 400 ? 2.4723 3.6233 2.2924 -0.8367 -0.1696 0.0454  503  GLU A O     
2976 C  CB    . GLU A 400 ? 1.9655 3.1348 1.6663 -0.9640 -0.1847 0.0100  503  GLU A CB    
2977 N  N     . LEU A 420 ? 2.1541 3.7307 2.1987 -0.5454 -0.3314 0.4078  523  LEU A N     
2978 C  CA    . LEU A 420 ? 2.2749 3.7992 2.2851 -0.5329 -0.3194 0.3928  523  LEU A CA    
2979 C  C     . LEU A 420 ? 2.4349 3.9931 2.4705 -0.5091 -0.3305 0.4287  523  LEU A C     
2980 O  O     . LEU A 420 ? 2.4327 3.9599 2.4409 -0.5018 -0.3250 0.4233  523  LEU A O     
2981 C  CB    . LEU A 420 ? 2.3325 3.8296 2.2728 -0.5767 -0.3211 0.3658  523  LEU A CB    
2982 C  CG    . LEU A 420 ? 2.3651 3.7914 2.2644 -0.5687 -0.3008 0.3372  523  LEU A CG    
2983 C  CD1   . LEU A 420 ? 2.3873 3.7541 2.3014 -0.5399 -0.2750 0.3112  523  LEU A CD1   
2984 C  CD2   . LEU A 420 ? 2.3004 3.7047 2.1319 -0.6159 -0.3015 0.3120  523  LEU A CD2   
2985 N  N     . ARG A 421 ? 2.5269 4.1488 2.6175 -0.4966 -0.3449 0.4660  524  ARG A N     
2986 C  CA    . ARG A 421 ? 2.5318 4.1900 2.6535 -0.4728 -0.3556 0.5037  524  ARG A CA    
2987 C  C     . ARG A 421 ? 2.3437 3.9544 2.4856 -0.4252 -0.3324 0.4995  524  ARG A C     
2988 O  O     . ARG A 421 ? 2.1912 3.7545 2.3393 -0.4064 -0.3105 0.4752  524  ARG A O     
2989 C  CB    . ARG A 421 ? 2.2674 3.9819 2.4458 -0.4645 -0.3651 0.5406  524  ARG A CB    
2990 C  CG    . ARG A 421 ? 2.0419 3.7669 2.2662 -0.4505 -0.3553 0.5377  524  ARG A CG    
2991 C  CD    . ARG A 421 ? 1.9932 3.7690 2.2644 -0.4503 -0.3637 0.5709  524  ARG A CD    
2992 N  NE    . ARG A 421 ? 2.0729 3.8587 2.3860 -0.4397 -0.3533 0.5674  524  ARG A NE    
2993 C  CZ    . ARG A 421 ? 2.1670 3.9940 2.5238 -0.4397 -0.3575 0.5913  524  ARG A CZ    
2994 N  NH1   . ARG A 421 ? 2.0471 3.9111 2.4139 -0.4497 -0.3733 0.6218  524  ARG A NH1   
2995 N  NH2   . ARG A 421 ? 2.0640 3.8954 2.4558 -0.4301 -0.3454 0.5851  524  ARG A NH2   
2996 N  N     . GLU A 422 ? 2.3411 3.9645 2.4919 -0.4070 -0.3380 0.5243  525  GLU A N     
2997 C  CA    . GLU A 422 ? 2.0993 3.6748 2.2611 -0.3659 -0.3169 0.5192  525  GLU A CA    
2998 C  C     . GLU A 422 ? 2.1217 3.7052 2.3467 -0.3263 -0.3041 0.5349  525  GLU A C     
2999 O  O     . GLU A 422 ? 2.1911 3.7224 2.4215 -0.2960 -0.2819 0.5193  525  GLU A O     
3000 C  CB    . GLU A 422 ? 2.0646 3.6519 2.2162 -0.3599 -0.3265 0.5419  525  GLU A CB    
3001 C  CG    . GLU A 422 ? 2.0995 3.6220 2.2317 -0.3343 -0.3054 0.5231  525  GLU A CG    
3002 C  CD    . GLU A 422 ? 2.1914 3.7045 2.3761 -0.2863 -0.2901 0.5388  525  GLU A CD    
3003 O  OE1   . GLU A 422 ? 2.3236 3.8867 2.5609 -0.2713 -0.2972 0.5713  525  GLU A OE1   
3004 O  OE2   . GLU A 422 ? 2.0765 3.5315 2.2502 -0.2642 -0.2702 0.5188  525  GLU A OE2   
3005 N  N     . ASN A 423 ? 2.2081 3.8553 2.4813 -0.3267 -0.3169 0.5656  526  ASN A N     
3006 C  CA    . ASN A 423 ? 2.0201 3.6756 2.3547 -0.2897 -0.3023 0.5817  526  ASN A CA    
3007 C  C     . ASN A 423 ? 1.9470 3.5587 2.2790 -0.2856 -0.2819 0.5496  526  ASN A C     
3008 O  O     . ASN A 423 ? 1.9748 3.5712 2.3447 -0.2529 -0.2633 0.5537  526  ASN A O     
3009 C  CB    . ASN A 423 ? 2.0437 3.7813 2.4342 -0.2925 -0.3207 0.6239  526  ASN A CB    
3010 C  CG    . ASN A 423 ? 2.0101 3.7706 2.3803 -0.3343 -0.3346 0.6162  526  ASN A CG    
3011 O  OD1   . ASN A 423 ? 2.0029 3.7748 2.3378 -0.3641 -0.3509 0.6206  526  ASN A OD1   
3012 N  ND2   . ASN A 423 ? 2.0263 3.7920 2.4174 -0.3374 -0.3271 0.6045  526  ASN A ND2   
3013 N  N     . ASP A 424 ? 2.0511 3.6405 2.3382 -0.3187 -0.2842 0.5182  527  ASP A N     
3014 C  CA    . ASP A 424 ? 2.1096 3.6540 2.3900 -0.3167 -0.2658 0.4872  527  ASP A CA    
3015 C  C     . ASP A 424 ? 2.0160 3.4816 2.2614 -0.3014 -0.2461 0.4551  527  ASP A C     
3016 O  O     . ASP A 424 ? 1.8441 3.2695 2.1007 -0.2805 -0.2272 0.4406  527  ASP A O     
3017 C  CB    . ASP A 424 ? 1.9661 3.5238 2.2183 -0.3595 -0.2766 0.4696  527  ASP A CB    
3018 C  CG    . ASP A 424 ? 2.0053 3.6327 2.3020 -0.3705 -0.2901 0.4962  527  ASP A CG    
3019 O  OD1   . ASP A 424 ? 2.2972 3.9856 2.6203 -0.3732 -0.3092 0.5313  527  ASP A OD1   
3020 O  OD2   . ASP A 424 ? 1.8133 3.4352 2.1199 -0.3767 -0.2818 0.4831  527  ASP A OD2   
3021 N  N     . LYS A 425 ? 2.0764 3.5192 2.2799 -0.3124 -0.2503 0.4443  528  LYS A N     
3022 C  CA    . LYS A 425 ? 1.8738 3.2441 2.0464 -0.2999 -0.2325 0.4144  528  LYS A CA    
3023 C  C     . LYS A 425 ? 1.8164 3.1635 2.0179 -0.2571 -0.2184 0.4256  528  LYS A C     
3024 O  O     . LYS A 425 ? 2.0199 3.3076 2.2093 -0.2415 -0.2015 0.4024  528  LYS A O     
3025 C  CB    . LYS A 425 ? 1.9701 3.3246 2.0923 -0.3241 -0.2392 0.4011  528  LYS A CB    
3026 C  CG    . LYS A 425 ? 2.2133 3.5881 2.3011 -0.3695 -0.2524 0.3893  528  LYS A CG    
3027 C  CD    . LYS A 425 ? 2.1323 3.4744 2.2105 -0.3809 -0.2412 0.3597  528  LYS A CD    
3028 C  CE    . LYS A 425 ? 2.0989 3.4716 2.1530 -0.4251 -0.2551 0.3535  528  LYS A CE    
3029 N  NZ    . LYS A 425 ? 2.1266 3.5736 2.2195 -0.4305 -0.2737 0.3873  528  LYS A NZ    
3030 N  N     . GLU A 426 ? 1.8684 3.2601 2.1081 -0.2386 -0.2250 0.4613  529  GLU A N     
3031 C  CA    . GLU A 426 ? 1.8803 3.2502 2.1488 -0.1983 -0.2099 0.4729  529  GLU A CA    
3032 C  C     . GLU A 426 ? 1.8263 3.1769 2.1246 -0.1772 -0.1925 0.4679  529  GLU A C     
3033 O  O     . GLU A 426 ? 1.8388 3.1548 2.1508 -0.1464 -0.1761 0.4684  529  GLU A O     
3034 C  CB    . GLU A 426 ? 2.0787 3.5025 2.3826 -0.1846 -0.2206 0.5141  529  GLU A CB    
3035 C  CG    . GLU A 426 ? 2.1281 3.5614 2.4011 -0.1988 -0.2348 0.5210  529  GLU A CG    
3036 C  CD    . GLU A 426 ? 2.0602 3.5449 2.3702 -0.1832 -0.2455 0.5640  529  GLU A CD    
3037 O  OE1   . GLU A 426 ? 2.0381 3.5624 2.4004 -0.1673 -0.2451 0.5901  529  GLU A OE1   
3038 O  OE2   . GLU A 426 ? 1.9680 3.4529 2.2560 -0.1866 -0.2533 0.5722  529  GLU A OE2   
3039 N  N     . GLN A 427 ? 1.8451 3.2157 2.1517 -0.1943 -0.1950 0.4629  530  GLN A N     
3040 C  CA    . GLN A 427 ? 1.7362 3.0862 2.0670 -0.1766 -0.1775 0.4571  530  GLN A CA    
3041 C  C     . GLN A 427 ? 1.7019 2.9799 1.9960 -0.1774 -0.1638 0.4198  530  GLN A C     
3042 O  O     . GLN A 427 ? 1.6883 2.9280 1.9928 -0.1539 -0.1463 0.4136  530  GLN A O     
3043 C  CB    . GLN A 427 ? 1.6846 3.0849 2.0410 -0.1944 -0.1847 0.4677  530  GLN A CB    
3044 C  CG    . GLN A 427 ? 1.7359 3.1180 2.1181 -0.1777 -0.1655 0.4634  530  GLN A CG    
3045 C  CD    . GLN A 427 ? 1.9946 3.3696 2.4144 -0.1391 -0.1486 0.4832  530  GLN A CD    
3046 O  OE1   . GLN A 427 ? 2.1005 3.4178 2.5089 -0.1196 -0.1301 0.4670  530  GLN A OE1   
3047 N  NE2   . GLN A 427 ? 1.8508 3.2839 2.3158 -0.1287 -0.1549 0.5192  530  GLN A NE2   
3048 N  N     . LEU A 428 ? 1.8305 3.0886 2.0818 -0.2049 -0.1713 0.3952  531  LEU A N     
3049 C  CA    . LEU A 428 ? 1.6758 2.8662 1.8953 -0.2052 -0.1593 0.3616  531  LEU A CA    
3050 C  C     . LEU A 428 ? 1.5822 2.7267 1.7968 -0.1781 -0.1485 0.3578  531  LEU A C     
3051 O  O     . LEU A 428 ? 1.5694 2.6608 1.7758 -0.1657 -0.1356 0.3396  531  LEU A O     
3052 C  CB    . LEU A 428 ? 1.5890 2.7680 1.7663 -0.2394 -0.1676 0.3378  531  LEU A CB    
3053 C  CG    . LEU A 428 ? 1.3608 2.5705 1.5329 -0.2712 -0.1763 0.3328  531  LEU A CG    
3054 C  CD1   . LEU A 428 ? 1.6571 2.9352 1.8379 -0.2903 -0.1954 0.3573  531  LEU A CD1   
3055 C  CD2   . LEU A 428 ? 1.6235 2.7891 1.7526 -0.2961 -0.1732 0.2987  531  LEU A CD2   
3056 N  N     . LYS A 429 ? 1.5732 2.7372 1.7921 -0.1696 -0.1544 0.3755  532  LYS A N     
3057 C  CA    . LYS A 429 ? 1.6664 2.7907 1.8845 -0.1430 -0.1439 0.3748  532  LYS A CA    
3058 C  C     . LYS A 429 ? 1.7191 2.8350 1.9710 -0.1119 -0.1299 0.3884  532  LYS A C     
3059 O  O     . LYS A 429 ? 1.8251 2.8903 2.0709 -0.0929 -0.1172 0.3772  532  LYS A O     
3060 C  CB    . LYS A 429 ? 1.5508 2.7007 1.7658 -0.1425 -0.1533 0.3924  532  LYS A CB    
3061 C  CG    . LYS A 429 ? 1.5977 2.7069 1.8094 -0.1177 -0.1430 0.3909  532  LYS A CG    
3062 C  CD    . LYS A 429 ? 1.5514 2.6878 1.7586 -0.1192 -0.1526 0.4094  532  LYS A CD    
3063 C  CE    . LYS A 429 ? 1.8105 2.9063 2.0152 -0.0950 -0.1415 0.4080  532  LYS A CE    
3064 N  NZ    . LYS A 429 ? 1.6162 2.7369 1.8154 -0.0964 -0.1501 0.4267  532  LYS A NZ    
3065 N  N     . ALA A 430 ? 1.5086 2.6728 1.7965 -0.1073 -0.1312 0.4124  533  ALA A N     
3066 C  CA    . ALA A 430 ? 1.4196 2.5752 1.7401 -0.0791 -0.1146 0.4250  533  ALA A CA    
3067 C  C     . ALA A 430 ? 1.5513 2.6650 1.8622 -0.0797 -0.1019 0.4027  533  ALA A C     
3068 O  O     . ALA A 430 ? 1.6686 2.7573 1.9948 -0.0573 -0.0850 0.4060  533  ALA A O     
3069 C  CB    . ALA A 430 ? 1.5653 2.7872 1.9321 -0.0740 -0.1184 0.4587  533  ALA A CB    
3070 N  N     . ILE A 431 ? 1.5858 2.6895 1.8701 -0.1057 -0.1089 0.3805  534  ILE A N     
3071 C  CA    . ILE A 431 ? 1.4934 2.5553 1.7656 -0.1079 -0.0982 0.3596  534  ILE A CA    
3072 C  C     . ILE A 431 ? 1.4213 2.4152 1.6624 -0.1012 -0.0921 0.3357  534  ILE A C     
3073 O  O     . ILE A 431 ? 1.4583 2.4091 1.6954 -0.0892 -0.0795 0.3264  534  ILE A O     
3074 C  CB    . ILE A 431 ? 1.6006 2.6831 1.8615 -0.1387 -0.1076 0.3481  534  ILE A CB    
3075 C  CG1   . ILE A 431 ? 1.4765 2.6281 1.7734 -0.1449 -0.1137 0.3736  534  ILE A CG1   
3076 C  CG2   . ILE A 431 ? 1.5927 2.6279 1.8374 -0.1422 -0.0972 0.3258  534  ILE A CG2   
3077 C  CD1   . ILE A 431 ? 1.4220 2.5975 1.7089 -0.1768 -0.1235 0.3637  534  ILE A CD1   
3078 N  N     . SER A 432 ? 1.3210 2.3041 1.5396 -0.1097 -0.1008 0.3261  535  SER A N     
3079 C  CA    . SER A 432 ? 1.5262 2.4483 1.7201 -0.1038 -0.0959 0.3049  535  SER A CA    
3080 C  C     . SER A 432 ? 1.5594 2.4549 1.7645 -0.0745 -0.0849 0.3142  535  SER A C     
3081 O  O     . SER A 432 ? 1.4578 2.2997 1.6483 -0.0664 -0.0782 0.2989  535  SER A O     
3082 C  CB    . SER A 432 ? 1.4644 2.3841 1.6352 -0.1197 -0.1054 0.2939  535  SER A CB    
3083 O  OG    . SER A 432 ? 1.5685 2.5239 1.7499 -0.1135 -0.1108 0.3140  535  SER A OG    
3084 N  N     . THR A 433 ? 1.4575 2.3892 1.6889 -0.0590 -0.0831 0.3397  536  THR A N     
3085 C  CA    . THR A 433 ? 1.5253 2.4325 1.7680 -0.0314 -0.0708 0.3495  536  THR A CA    
3086 C  C     . THR A 433 ? 1.7293 2.6150 1.9836 -0.0175 -0.0550 0.3511  536  THR A C     
3087 O  O     . THR A 433 ? 1.9326 2.7890 2.1915 0.0039  -0.0425 0.3559  536  THR A O     
3088 C  CB    . THR A 433 ? 1.2995 2.2520 1.5678 -0.0192 -0.0732 0.3776  536  THR A CB    
3089 O  OG1   . THR A 433 ? 1.4121 2.4197 1.7101 -0.0223 -0.0752 0.3982  536  THR A OG1   
3090 C  CG2   . THR A 433 ? 1.5868 2.5540 1.8381 -0.0330 -0.0874 0.3756  536  THR A CG2   
3091 N  N     . ARG A 434 ? 1.6674 2.5647 1.9245 -0.0299 -0.0542 0.3468  537  ARG A N     
3092 C  CA    . ARG A 434 ? 1.6456 2.5201 1.9100 -0.0190 -0.0376 0.3471  537  ARG A CA    
3093 C  C     . ARG A 434 ? 1.5675 2.3754 1.7983 -0.0221 -0.0338 0.3220  537  ARG A C     
3094 O  O     . ARG A 434 ? 1.4402 2.2288 1.6468 -0.0381 -0.0452 0.3033  537  ARG A O     
3095 C  CB    . ARG A 434 ? 1.5579 2.4731 1.8407 -0.0314 -0.0373 0.3539  537  ARG A CB    
3096 C  CG    . ARG A 434 ? 1.4429 2.4282 1.7638 -0.0293 -0.0425 0.3818  537  ARG A CG    
3097 C  CD    . ARG A 434 ? 1.6428 2.6599 1.9933 -0.0302 -0.0330 0.3938  537  ARG A CD    
3098 N  NE    . ARG A 434 ? 1.7458 2.7587 2.0778 -0.0546 -0.0386 0.3756  537  ARG A NE    
3099 C  CZ    . ARG A 434 ? 1.6556 2.7168 1.9949 -0.0770 -0.0533 0.3791  537  ARG A CZ    
3100 N  NH1   . ARG A 434 ? 1.4302 2.5498 1.7939 -0.0796 -0.0659 0.4009  537  ARG A NH1   
3101 N  NH2   . ARG A 434 ? 1.6689 2.7189 1.9893 -0.0983 -0.0559 0.3608  537  ARG A NH2   
3102 N  N     . ASP A 435 ? 1.6785 2.4506 1.9084 -0.0071 -0.0173 0.3223  538  ASP A N     
3103 C  CA    . ASP A 435 ? 1.6234 2.3320 1.8211 -0.0102 -0.0145 0.3014  538  ASP A CA    
3104 C  C     . ASP A 435 ? 1.5496 2.2531 1.7321 -0.0318 -0.0201 0.2865  538  ASP A C     
3105 O  O     . ASP A 435 ? 1.5650 2.3095 1.7643 -0.0405 -0.0194 0.2939  538  ASP A O     
3106 C  CB    . ASP A 435 ? 1.5763 2.2493 1.7734 0.0076  0.0056  0.3061  538  ASP A CB    
3107 C  CG    . ASP A 435 ? 1.7065 2.4082 1.9281 0.0120  0.0212  0.3200  538  ASP A CG    
3108 O  OD1   . ASP A 435 ? 1.8171 2.5113 2.0288 -0.0011 0.0236  0.3110  538  ASP A OD1   
3109 O  OD2   . ASP A 435 ? 1.7649 2.4967 2.0175 0.0288  0.0318  0.3407  538  ASP A OD2   
3110 N  N     . PRO A 436 ? 1.6156 2.2698 1.7682 -0.0410 -0.0260 0.2665  539  PRO A N     
3111 C  CA    . PRO A 436 ? 1.5457 2.1920 1.6832 -0.0616 -0.0312 0.2525  539  PRO A CA    
3112 C  C     . PRO A 436 ? 1.4358 2.0773 1.5744 -0.0622 -0.0173 0.2554  539  PRO A C     
3113 O  O     . PRO A 436 ? 1.5066 2.1504 1.6371 -0.0796 -0.0204 0.2468  539  PRO A O     
3114 C  CB    . PRO A 436 ? 1.5676 2.1570 1.6764 -0.0665 -0.0391 0.2340  539  PRO A CB    
3115 C  CG    . PRO A 436 ? 1.3128 1.8722 1.4192 -0.0472 -0.0331 0.2387  539  PRO A CG    
3116 C  CD    . PRO A 436 ? 1.6671 2.2721 1.8005 -0.0338 -0.0291 0.2568  539  PRO A CD    
3117 N  N     . LEU A 437 ? 1.4115 2.0444 1.5592 -0.0445 -0.0005 0.2668  540  LEU A N     
3118 C  CA    . LEU A 437 ? 1.5510 2.1795 1.7015 -0.0442 0.0165  0.2705  540  LEU A CA    
3119 C  C     . LEU A 437 ? 1.7695 2.4604 1.9606 -0.0391 0.0250  0.2905  540  LEU A C     
3120 O  O     . LEU A 437 ? 1.9238 2.6188 2.1235 -0.0396 0.0405  0.2948  540  LEU A O     
3121 C  CB    . LEU A 437 ? 1.5153 2.0905 1.6486 -0.0297 0.0332  0.2696  540  LEU A CB    
3122 C  CG    . LEU A 437 ? 1.6987 2.2085 1.7909 -0.0362 0.0254  0.2515  540  LEU A CG    
3123 C  CD1   . LEU A 437 ? 1.5232 1.9831 1.5963 -0.0251 0.0435  0.2518  540  LEU A CD1   
3124 C  CD2   . LEU A 437 ? 1.3978 1.8929 1.4690 -0.0577 0.0160  0.2372  540  LEU A CD2   
3125 N  N     . SER A 438 ? 1.6859 2.4256 1.9027 -0.0348 0.0154  0.3037  541  SER A N     
3126 C  CA    . SER A 438 ? 1.6947 2.4989 1.9536 -0.0313 0.0197  0.3255  541  SER A CA    
3127 C  C     . SER A 438 ? 1.8262 2.6612 2.0885 -0.0541 0.0124  0.3209  541  SER A C     
3128 O  O     . SER A 438 ? 1.8349 2.6741 2.0795 -0.0732 -0.0055 0.3083  541  SER A O     
3129 C  CB    . SER A 438 ? 1.5958 2.4427 1.8759 -0.0246 0.0074  0.3406  541  SER A CB    
3130 O  OG    . SER A 438 ? 1.5504 2.4620 1.8738 -0.0214 0.0093  0.3645  541  SER A OG    
3131 N  N     . GLU A 439 ? 1.9793 2.8343 2.2646 -0.0525 0.0277  0.3309  542  GLU A N     
3132 C  CA    . GLU A 439 ? 1.9909 2.8719 2.2797 -0.0744 0.0233  0.3264  542  GLU A CA    
3133 C  C     . GLU A 439 ? 1.7837 2.7314 2.0956 -0.0877 0.0037  0.3374  542  GLU A C     
3134 O  O     . GLU A 439 ? 1.8313 2.8303 2.1825 -0.0771 0.0040  0.3611  542  GLU A O     
3135 C  CB    . GLU A 439 ? 2.0621 2.9522 2.3754 -0.0679 0.0465  0.3369  542  GLU A CB    
3136 C  CG    . GLU A 439 ? 2.0677 2.8896 2.3532 -0.0578 0.0677  0.3257  542  GLU A CG    
3137 C  CD    . GLU A 439 ? 2.1820 2.9508 2.4191 -0.0764 0.0608  0.3004  542  GLU A CD    
3138 O  OE1   . GLU A 439 ? 2.3139 3.1030 2.5467 -0.0977 0.0473  0.2927  542  GLU A OE1   
3139 O  OE2   . GLU A 439 ? 2.1329 2.8392 2.3363 -0.0705 0.0685  0.2888  542  GLU A OE2   
3140 N  N     . ILE A 440 ? 1.3198 2.2653 1.6066 -0.1117 -0.0132 0.3206  543  ILE A N     
3141 C  CA    . ILE A 440 ? 1.5590 2.5624 1.8590 -0.1302 -0.0320 0.3274  543  ILE A CA    
3142 C  C     . ILE A 440 ? 1.8117 2.8561 2.1345 -0.1455 -0.0292 0.3341  543  ILE A C     
3143 O  O     . ILE A 440 ? 1.7092 2.7267 2.0115 -0.1602 -0.0250 0.3173  543  ILE A O     
3144 C  CB    . ILE A 440 ? 1.3896 2.3680 1.6509 -0.1498 -0.0486 0.3050  543  ILE A CB    
3145 C  CG1   . ILE A 440 ? 1.6049 2.5485 1.8492 -0.1344 -0.0515 0.3004  543  ILE A CG1   
3146 C  CG2   . ILE A 440 ? 1.3405 2.3749 1.6093 -0.1736 -0.0663 0.3096  543  ILE A CG2   
3147 N  N     . THR A 441 ? 1.7441 2.8542 2.1110 -0.1424 -0.0316 0.3598  544  THR A N     
3148 C  CA    . THR A 441 ? 1.4656 2.6210 1.8618 -0.1559 -0.0288 0.3695  544  THR A CA    
3149 C  C     . THR A 441 ? 1.5197 2.6917 1.8944 -0.1899 -0.0474 0.3551  544  THR A C     
3150 O  O     . THR A 441 ? 1.8126 2.9728 2.1566 -0.2024 -0.0633 0.3421  544  THR A O     
3151 C  CB    . THR A 441 ? 1.3899 2.6154 1.8431 -0.1444 -0.0294 0.4033  544  THR A CB    
3152 O  OG1   . THR A 441 ? 1.2831 2.5509 1.7378 -0.1555 -0.0538 0.4126  544  THR A OG1   
3153 C  CG2   . THR A 441 ? 1.8086 3.0150 2.2831 -0.1102 -0.0093 0.4174  544  THR A CG2   
3154 N  N     . GLU A 442 ? 1.3948 2.5933 1.7862 -0.2056 -0.0434 0.3570  545  GLU A N     
3155 C  CA    . GLU A 442 ? 1.3884 2.6019 1.7599 -0.2396 -0.0588 0.3431  545  GLU A CA    
3156 C  C     . GLU A 442 ? 1.5532 2.8270 1.9365 -0.2554 -0.0822 0.3567  545  GLU A C     
3157 O  O     . GLU A 442 ? 1.4800 2.7504 1.8312 -0.2818 -0.0972 0.3403  545  GLU A O     
3158 C  CB    . GLU A 442 ? 1.6829 2.9143 2.0733 -0.2523 -0.0484 0.3444  545  GLU A CB    
3159 C  CG    . GLU A 442 ? 1.8200 2.9923 2.1967 -0.2388 -0.0243 0.3323  545  GLU A CG    
3160 C  CD    . GLU A 442 ? 1.8051 2.9039 2.1255 -0.2451 -0.0255 0.3027  545  GLU A CD    
3161 O  OE1   . GLU A 442 ? 1.6184 2.7148 1.9124 -0.2686 -0.0414 0.2876  545  GLU A OE1   
3162 O  OE2   . GLU A 442 ? 1.8203 2.8632 2.1231 -0.2271 -0.0104 0.2952  545  GLU A OE2   
3163 N  N     . GLN A 443 ? 1.6926 3.0206 2.1207 -0.2407 -0.0852 0.3867  546  GLN A N     
3164 C  CA    . GLN A 443 ? 1.6331 3.0173 2.0700 -0.2554 -0.1091 0.4021  546  GLN A CA    
3165 C  C     . GLN A 443 ? 1.5671 2.9164 1.9625 -0.2545 -0.1191 0.3884  546  GLN A C     
3166 O  O     . GLN A 443 ? 1.7430 3.1136 2.1177 -0.2792 -0.1385 0.3845  546  GLN A O     
3167 C  CB    . GLN A 443 ? 1.5566 3.0032 2.0534 -0.2365 -0.1094 0.4398  546  GLN A CB    
3168 C  CG    . GLN A 443 ? 1.5477 3.0594 2.0571 -0.2536 -0.1363 0.4603  546  GLN A CG    
3169 C  CD    . GLN A 443 ? 1.6819 3.2346 2.1869 -0.2925 -0.1531 0.4566  546  GLN A CD    
3170 O  OE1   . GLN A 443 ? 1.6993 3.2706 2.2295 -0.2997 -0.1450 0.4593  546  GLN A OE1   
3171 N  NE2   . GLN A 443 ? 1.8703 3.4352 2.3414 -0.3192 -0.1755 0.4498  546  GLN A NE2   
3172 N  N     . GLU A 444 ? 1.3761 2.6711 1.7582 -0.2279 -0.1055 0.3806  547  GLU A N     
3173 C  CA    . GLU A 444 ? 1.3070 2.5639 1.6511 -0.2261 -0.1126 0.3661  547  GLU A CA    
3174 C  C     . GLU A 444 ? 1.5915 2.7972 1.8867 -0.2474 -0.1142 0.3325  547  GLU A C     
3175 O  O     . GLU A 444 ? 1.6635 2.8476 1.9276 -0.2547 -0.1227 0.3196  547  GLU A O     
3176 C  CB    . GLU A 444 ? 1.3389 2.5551 1.6870 -0.1913 -0.0976 0.3696  547  GLU A CB    
3177 C  CG    . GLU A 444 ? 1.3444 2.6049 1.7408 -0.1674 -0.0936 0.4028  547  GLU A CG    
3178 C  CD    . GLU A 444 ? 1.3905 2.6051 1.7894 -0.1342 -0.0749 0.4041  547  GLU A CD    
3179 O  OE1   . GLU A 444 ? 1.3955 2.5455 1.7592 -0.1308 -0.0662 0.3798  547  GLU A OE1   
3180 O  OE2   . GLU A 444 ? 1.4525 2.6954 1.8891 -0.1123 -0.0691 0.4300  547  GLU A OE2   
3181 N  N     . LYS A 445 ? 1.7353 2.9201 2.0241 -0.2571 -0.1049 0.3188  548  LYS A N     
3182 C  CA    . LYS A 445 ? 1.3873 2.5249 1.6331 -0.2778 -0.1061 0.2887  548  LYS A CA    
3183 C  C     . LYS A 445 ? 1.5310 2.6999 1.7598 -0.3111 -0.1234 0.2826  548  LYS A C     
3184 O  O     . LYS A 445 ? 1.2956 2.4339 1.4900 -0.3216 -0.1287 0.2645  548  LYS A O     
3185 C  CB    . LYS A 445 ? 1.4586 2.5729 1.7036 -0.2824 -0.0930 0.2787  548  LYS A CB    
3186 C  CG    . LYS A 445 ? 1.3901 2.4601 1.6396 -0.2541 -0.0744 0.2792  548  LYS A CG    
3187 C  CD    . LYS A 445 ? 1.2937 2.2956 1.5072 -0.2443 -0.0723 0.2596  548  LYS A CD    
3188 C  CE    . LYS A 445 ? 1.5221 2.4729 1.7299 -0.2251 -0.0550 0.2554  548  LYS A CE    
3189 N  NZ    . LYS A 445 ? 1.7163 2.6892 1.9581 -0.2004 -0.0428 0.2780  548  LYS A NZ    
3190 N  N     . ASP A 446 ? 1.6044 2.8338 1.8571 -0.3292 -0.1318 0.2975  549  ASP A N     
3191 C  CA    . ASP A 446 ? 1.5773 2.8380 1.8116 -0.3646 -0.1487 0.2921  549  ASP A CA    
3192 C  C     . ASP A 446 ? 1.3315 2.6162 1.5589 -0.3659 -0.1633 0.3026  549  ASP A C     
3193 O  O     . ASP A 446 ? 1.2931 2.5814 1.4892 -0.3945 -0.1747 0.2906  549  ASP A O     
3194 C  CB    . ASP A 446 ? 1.3128 2.6356 1.5777 -0.3839 -0.1552 0.3081  549  ASP A CB    
3195 C  CG    . ASP A 446 ? 1.4520 2.7518 1.7218 -0.3856 -0.1401 0.2972  549  ASP A CG    
3196 O  OD1   . ASP A 446 ? 1.5244 2.7606 1.7602 -0.3865 -0.1300 0.2712  549  ASP A OD1   
3197 O  OD2   . ASP A 446 ? 1.6188 2.9641 1.9276 -0.3863 -0.1381 0.3156  549  ASP A OD2   
3198 N  N     . PHE A 447 ? 1.1185 2.4176 1.3726 -0.3365 -0.1620 0.3245  550  PHE A N     
3199 C  CA    . PHE A 447 ? 1.3240 2.6424 1.5702 -0.3363 -0.1751 0.3352  550  PHE A CA    
3200 C  C     . PHE A 447 ? 1.6065 2.8643 1.8062 -0.3390 -0.1717 0.3080  550  PHE A C     
3201 O  O     . PHE A 447 ? 1.6646 2.9306 1.8373 -0.3598 -0.1833 0.3029  550  PHE A O     
3202 C  CB    . PHE A 447 ? 1.3961 2.7366 1.6822 -0.3017 -0.1716 0.3640  550  PHE A CB    
3203 C  CG    . PHE A 447 ? 1.2851 2.6559 1.5693 -0.3019 -0.1866 0.3811  550  PHE A CG    
3204 C  CD1   . PHE A 447 ? 1.3156 2.7201 1.5778 -0.3358 -0.2060 0.3812  550  PHE A CD1   
3205 C  CD2   . PHE A 447 ? 1.2942 2.6574 1.5958 -0.2696 -0.1807 0.3967  550  PHE A CD2   
3206 C  CE1   . PHE A 447 ? 1.7317 3.1623 1.9884 -0.3375 -0.2199 0.3974  550  PHE A CE1   
3207 C  CE2   . PHE A 447 ? 1.2941 2.6838 1.5929 -0.2700 -0.1943 0.4130  550  PHE A CE2   
3208 C  CZ    . PHE A 447 ? 1.7286 3.1522 2.0045 -0.3040 -0.2142 0.4138  550  PHE A CZ    
3209 N  N     . LEU A 448 ? 1.6618 2.8581 1.8517 -0.3191 -0.1557 0.2909  551  LEU A N     
3210 C  CA    . LEU A 448 ? 1.4110 2.5495 1.5628 -0.3203 -0.1517 0.2660  551  LEU A CA    
3211 C  C     . LEU A 448 ? 1.5682 2.6844 1.6856 -0.3531 -0.1526 0.2394  551  LEU A C     
3212 O  O     . LEU A 448 ? 1.7498 2.8390 1.8356 -0.3656 -0.1537 0.2223  551  LEU A O     
3213 C  CB    . LEU A 448 ? 1.1993 2.2812 1.3535 -0.2900 -0.1363 0.2582  551  LEU A CB    
3214 C  CG    . LEU A 448 ? 1.1477 2.2399 1.3312 -0.2564 -0.1318 0.2811  551  LEU A CG    
3215 C  CD1   . LEU A 448 ? 1.3376 2.3708 1.5184 -0.2317 -0.1167 0.2710  551  LEU A CD1   
3216 C  CD2   . LEU A 448 ? 1.3403 2.4457 1.5180 -0.2523 -0.1403 0.2898  551  LEU A CD2   
3217 N  N     . TRP A 449 ? 1.4368 2.5626 1.5604 -0.3676 -0.1505 0.2355  552  TRP A N     
3218 C  CA    . TRP A 449 ? 1.2421 2.3445 1.3337 -0.3990 -0.1498 0.2102  552  TRP A CA    
3219 C  C     . TRP A 449 ? 1.4557 2.6017 1.5313 -0.4336 -0.1644 0.2120  552  TRP A C     
3220 O  O     . TRP A 449 ? 1.3976 2.5161 1.4367 -0.4577 -0.1635 0.1895  552  TRP A O     
3221 C  CB    . TRP A 449 ? 1.1510 2.2472 1.2529 -0.4038 -0.1421 0.2055  552  TRP A CB    
3222 C  CG    . TRP A 449 ? 1.2622 2.3327 1.3328 -0.4354 -0.1401 0.1801  552  TRP A CG    
3223 C  CD1   . TRP A 449 ? 1.7827 2.8863 1.8515 -0.4662 -0.1456 0.1788  552  TRP A CD1   
3224 C  CD2   . TRP A 449 ? 1.5726 2.5783 1.6108 -0.4397 -0.1312 0.1529  552  TRP A CD2   
3225 N  NE1   . TRP A 449 ? 1.7868 2.8479 1.8219 -0.4895 -0.1396 0.1515  552  TRP A NE1   
3226 C  CE2   . TRP A 449 ? 1.5914 2.5922 1.6087 -0.4731 -0.1304 0.1358  552  TRP A CE2   
3227 C  CE3   . TRP A 449 ? 1.4950 2.4470 1.5225 -0.4187 -0.1237 0.1423  552  TRP A CE3   
3228 C  CZ2   . TRP A 449 ? 1.7844 2.7273 1.7716 -0.4848 -0.1209 0.1088  552  TRP A CZ2   
3229 C  CZ3   . TRP A 449 ? 1.3525 2.2499 1.3527 -0.4303 -0.1156 0.1165  552  TRP A CZ3   
3230 C  CH2   . TRP A 449 ? 1.7749 2.6675 1.7558 -0.4624 -0.1137 0.1002  552  TRP A CH2   
3231 N  N     . SER A 450 ? 1.6585 2.8716 1.7610 -0.4374 -0.1776 0.2389  553  SER A N     
3232 C  CA    . SER A 450 ? 1.5123 2.7695 1.5981 -0.4714 -0.1944 0.2436  553  SER A CA    
3233 C  C     . SER A 450 ? 1.6497 2.8963 1.7099 -0.4714 -0.1992 0.2419  553  SER A C     
3234 O  O     . SER A 450 ? 1.8631 3.1244 1.8924 -0.5039 -0.2093 0.2358  553  SER A O     
3235 C  CB    . SER A 450 ? 1.4218 2.7565 1.5483 -0.4743 -0.2090 0.2764  553  SER A CB    
3236 O  OG    . SER A 450 ? 1.6139 2.9691 1.7756 -0.4398 -0.2095 0.3027  553  SER A OG    
3237 N  N     . HIS A 451 ? 1.4838 2.7039 1.5542 -0.4372 -0.1917 0.2467  554  HIS A N     
3238 C  CA    . HIS A 451 ? 1.6269 2.8306 1.6744 -0.4337 -0.1933 0.2440  554  HIS A CA    
3239 C  C     . HIS A 451 ? 1.6956 2.8248 1.7217 -0.4199 -0.1762 0.2170  554  HIS A C     
3240 O  O     . HIS A 451 ? 1.7307 2.8375 1.7569 -0.3975 -0.1719 0.2192  554  HIS A O     
3241 C  CB    . HIS A 451 ? 1.7087 2.9484 1.7881 -0.4061 -0.2002 0.2754  554  HIS A CB    
3242 C  CG    . HIS A 451 ? 1.5911 2.9068 1.6942 -0.4194 -0.2190 0.3053  554  HIS A CG    
3243 N  ND1   . HIS A 451 ? 1.7121 3.0667 1.8468 -0.4243 -0.2226 0.3178  554  HIS A ND1   
3244 C  CD2   . HIS A 451 ? 1.6164 2.9773 1.7179 -0.4292 -0.2359 0.3267  554  HIS A CD2   
3245 C  CE1   . HIS A 451 ? 1.6800 3.1025 1.8348 -0.4362 -0.2414 0.3463  554  HIS A CE1   
3246 N  NE2   . HIS A 451 ? 1.8267 3.2542 1.9608 -0.4397 -0.2506 0.3527  554  HIS A NE2   
3247 N  N     . ARG A 452 ? 1.8130 2.9034 1.8223 -0.4335 -0.1665 0.1922  555  ARG A N     
3248 C  CA    . ARG A 452 ? 1.6544 2.6754 1.6488 -0.4205 -0.1511 0.1684  555  ARG A CA    
3249 C  C     . ARG A 452 ? 1.9006 2.8951 1.8614 -0.4338 -0.1480 0.1523  555  ARG A C     
3250 O  O     . ARG A 452 ? 1.8675 2.8166 1.8256 -0.4142 -0.1380 0.1426  555  ARG A O     
3251 C  CB    . ARG A 452 ? 1.5438 2.5322 1.5305 -0.4328 -0.1422 0.1482  555  ARG A CB    
3252 C  CG    . ARG A 452 ? 1.6094 2.6142 1.5709 -0.4742 -0.1463 0.1358  555  ARG A CG    
3253 C  CD    . ARG A 452 ? 1.6970 2.6720 1.6556 -0.4837 -0.1372 0.1191  555  ARG A CD    
3254 N  NE    . ARG A 452 ? 1.5812 2.5765 1.5186 -0.5238 -0.1414 0.1093  555  ARG A NE    
3255 C  CZ    . ARG A 452 ? 1.6042 2.6526 1.5565 -0.5388 -0.1519 0.1240  555  ARG A CZ    
3256 N  NH1   . ARG A 452 ? 1.6151 2.7026 1.6058 -0.5164 -0.1580 0.1496  555  ARG A NH1   
3257 N  NH2   . ARG A 452 ? 1.7546 2.8167 1.6838 -0.5777 -0.1555 0.1128  555  ARG A NH2   
3258 N  N     . HIS A 453 ? 1.8639 2.8851 1.7984 -0.4679 -0.1559 0.1493  556  HIS A N     
3259 C  CA    . HIS A 453 ? 1.7151 2.7106 1.6139 -0.4837 -0.1509 0.1333  556  HIS A CA    
3260 C  C     . HIS A 453 ? 1.7635 2.7788 1.6666 -0.4676 -0.1574 0.1518  556  HIS A C     
3261 O  O     . HIS A 453 ? 1.8288 2.8189 1.7043 -0.4760 -0.1511 0.1395  556  HIS A O     
3262 C  CB    . HIS A 453 ? 1.6832 2.6967 1.5464 -0.5294 -0.1560 0.1221  556  HIS A CB    
3263 C  CG    . HIS A 453 ? 1.9373 2.9245 1.7909 -0.5484 -0.1472 0.1005  556  HIS A CG    
3264 N  ND1   . HIS A 453 ? 1.7962 2.7421 1.6684 -0.5266 -0.1351 0.0906  556  HIS A ND1   
3265 C  CD2   . HIS A 453 ? 2.1980 3.1935 2.0239 -0.5881 -0.1488 0.0874  556  HIS A CD2   
3266 C  CE1   . HIS A 453 ? 1.8586 2.7884 1.7165 -0.5509 -0.1293 0.0728  556  HIS A CE1   
3267 N  NE2   . HIS A 453 ? 2.2343 3.1932 2.0643 -0.5884 -0.1367 0.0699  556  HIS A NE2   
3268 N  N     . TYR A 454 ? 2.0496 3.1076 1.9870 -0.4449 -0.1683 0.1811  557  TYR A N     
3269 C  CA    . TYR A 454 ? 2.1443 3.2186 2.0901 -0.4255 -0.1734 0.2006  557  TYR A CA    
3270 C  C     . TYR A 454 ? 2.1954 3.2295 2.1627 -0.3859 -0.1615 0.2002  557  TYR A C     
3271 O  O     . TYR A 454 ? 2.1636 3.1897 2.1280 -0.3721 -0.1600 0.2061  557  TYR A O     
3272 C  CB    . TYR A 454 ? 2.0728 3.2176 2.0463 -0.4229 -0.1916 0.2352  557  TYR A CB    
3273 C  CG    . TYR A 454 ? 2.3377 3.4982 2.3326 -0.3934 -0.1951 0.2597  557  TYR A CG    
3274 C  CD1   . TYR A 454 ? 2.5192 3.6878 2.4904 -0.4027 -0.2011 0.2653  557  TYR A CD1   
3275 C  CD2   . TYR A 454 ? 2.3636 3.5281 2.4004 -0.3570 -0.1910 0.2768  557  TYR A CD2   
3276 C  CE1   . TYR A 454 ? 2.4636 3.6451 2.4542 -0.3758 -0.2037 0.2881  557  TYR A CE1   
3277 C  CE2   . TYR A 454 ? 2.4370 3.6130 2.4932 -0.3302 -0.1926 0.2987  557  TYR A CE2   
3278 C  CZ    . TYR A 454 ? 2.4339 3.6192 2.4680 -0.3393 -0.1993 0.3047  557  TYR A CZ    
3279 O  OH    . TYR A 454 ? 2.5486 3.7443 2.6019 -0.3127 -0.2004 0.3271  557  TYR A OH    
3280 N  N     . CYS A 455 ? 1.9245 2.9317 1.9108 -0.3692 -0.1530 0.1931  558  CYS A N     
3281 C  CA    . CYS A 455 ? 1.7829 2.7543 1.7896 -0.3331 -0.1436 0.1948  558  CYS A CA    
3282 C  C     . CYS A 455 ? 1.7933 2.7118 1.7811 -0.3282 -0.1326 0.1752  558  CYS A C     
3283 O  O     . CYS A 455 ? 1.8480 2.7385 1.8511 -0.2997 -0.1265 0.1778  558  CYS A O     
3284 C  CB    . CYS A 455 ? 1.7705 2.7203 1.7937 -0.3224 -0.1371 0.1888  558  CYS A CB    
3285 S  SG    . CYS A 455 ? 1.7643 2.7723 1.8194 -0.3201 -0.1456 0.2139  558  CYS A SG    
3286 N  N     . VAL A 456 ? 1.7671 2.6702 1.7227 -0.3558 -0.1291 0.1558  559  VAL A N     
3287 C  CA    . VAL A 456 ? 1.8122 2.6680 1.7531 -0.3515 -0.1170 0.1385  559  VAL A CA    
3288 C  C     . VAL A 456 ? 1.8108 2.6813 1.7540 -0.3371 -0.1202 0.1545  559  VAL A C     
3289 O  O     . VAL A 456 ? 1.6824 2.5151 1.6250 -0.3232 -0.1101 0.1458  559  VAL A O     
3290 C  CB    . VAL A 456 ? 1.9243 2.7595 1.8294 -0.3861 -0.1093 0.1136  559  VAL A CB    
3291 C  CG1   . VAL A 456 ? 1.5133 2.3248 1.4176 -0.3975 -0.1036 0.0962  559  VAL A CG1   
3292 C  CG2   . VAL A 456 ? 1.9839 2.8665 1.8644 -0.4158 -0.1207 0.1224  559  VAL A CG2   
3293 N  N     . THR A 457 ? 1.8389 2.7642 1.7868 -0.3403 -0.1341 0.1790  560  THR A N     
3294 C  CA    . THR A 457 ? 1.8350 2.7758 1.7873 -0.3250 -0.1377 0.1972  560  THR A CA    
3295 C  C     . THR A 457 ? 1.8230 2.7499 1.8092 -0.2858 -0.1338 0.2097  560  THR A C     
3296 O  O     . THR A 457 ? 1.9632 2.8697 1.9511 -0.2687 -0.1281 0.2115  560  THR A O     
3297 C  CB    . THR A 457 ? 1.8563 2.8612 1.8071 -0.3394 -0.1551 0.2226  560  THR A CB    
3298 O  OG1   . THR A 457 ? 1.8620 2.8773 1.7763 -0.3793 -0.1592 0.2098  560  THR A OG1   
3299 C  CG2   . THR A 457 ? 1.9621 2.9819 1.9156 -0.3248 -0.1589 0.2425  560  THR A CG2   
3300 N  N     . ILE A 458 ? 1.6567 2.5929 1.6686 -0.2723 -0.1356 0.2178  561  ILE A N     
3301 C  CA    . ILE A 458 ? 1.8070 2.7256 1.8473 -0.2376 -0.1303 0.2276  561  ILE A CA    
3302 C  C     . ILE A 458 ? 1.6462 2.5177 1.6885 -0.2327 -0.1212 0.2073  561  ILE A C     
3303 O  O     . ILE A 458 ? 1.6257 2.5064 1.6806 -0.2316 -0.1224 0.2105  561  ILE A O     
3304 C  CB    . ILE A 458 ? 1.5784 2.5458 1.6483 -0.2237 -0.1380 0.2568  561  ILE A CB    
3305 C  CG1   . ILE A 458 ? 1.6693 2.6786 1.7396 -0.2478 -0.1473 0.2609  561  ILE A CG1   
3306 C  CG2   . ILE A 458 ? 1.8884 2.8874 1.9650 -0.2142 -0.1441 0.2802  561  ILE A CG2   
3307 N  N     . PRO A 459 ? 1.5828 2.4037 1.6143 -0.2298 -0.1121 0.1874  562  PRO A N     
3308 C  CA    . PRO A 459 ? 1.4048 2.1812 1.4377 -0.2278 -0.1053 0.1692  562  PRO A CA    
3309 C  C     . PRO A 459 ? 1.2855 2.0465 1.3404 -0.2009 -0.1037 0.1786  562  PRO A C     
3310 O  O     . PRO A 459 ? 1.2640 1.9933 1.3193 -0.2005 -0.1004 0.1670  562  PRO A O     
3311 C  CB    . PRO A 459 ? 1.4264 2.1578 1.4473 -0.2299 -0.0965 0.1498  562  PRO A CB    
3312 C  CG    . PRO A 459 ? 1.7052 2.4498 1.7270 -0.2192 -0.0970 0.1619  562  PRO A CG    
3313 C  CD    . PRO A 459 ? 1.5791 2.3816 1.5984 -0.2288 -0.1073 0.1816  562  PRO A CD    
3314 N  N     . GLU A 460 ? 1.3636 2.1435 1.4350 -0.1795 -0.1052 0.1991  563  GLU A N     
3315 C  CA    . GLU A 460 ? 1.3297 2.0931 1.4186 -0.1557 -0.1016 0.2076  563  GLU A CA    
3316 C  C     . GLU A 460 ? 1.4735 2.2619 1.5722 -0.1593 -0.1030 0.2157  563  GLU A C     
3317 O  O     . GLU A 460 ? 1.3299 2.0976 1.4378 -0.1440 -0.0979 0.2184  563  GLU A O     
3318 C  CB    . GLU A 460 ? 1.5744 2.3485 1.6781 -0.1322 -0.1002 0.2268  563  GLU A CB    
3319 C  CG    . GLU A 460 ? 1.7328 2.5651 1.8464 -0.1342 -0.1063 0.2493  563  GLU A CG    
3320 C  CD    . GLU A 460 ? 1.6786 2.5269 1.7759 -0.1496 -0.1113 0.2474  563  GLU A CD    
3321 O  OE1   . GLU A 460 ? 1.7470 2.5609 1.8260 -0.1593 -0.1078 0.2270  563  GLU A OE1   
3322 O  OE2   . GLU A 460 ? 1.8919 2.7866 1.9950 -0.1523 -0.1183 0.2672  563  GLU A OE2   
3323 N  N     . ILE A 461 ? 1.6763 2.5076 1.7722 -0.1802 -0.1094 0.2195  564  ILE A N     
3324 C  CA    . ILE A 461 ? 1.3615 2.2188 1.4688 -0.1859 -0.1104 0.2267  564  ILE A CA    
3325 C  C     . ILE A 461 ? 1.3701 2.1970 1.4625 -0.2023 -0.1079 0.2056  564  ILE A C     
3326 O  O     . ILE A 461 ? 1.3533 2.1977 1.4525 -0.2097 -0.1078 0.2087  564  ILE A O     
3327 C  CB    . ILE A 461 ? 1.1277 2.0490 1.2420 -0.2016 -0.1201 0.2431  564  ILE A CB    
3328 C  CG1   . ILE A 461 ? 1.2997 2.2572 1.4407 -0.1956 -0.1197 0.2613  564  ILE A CG1   
3329 C  CG2   . ILE A 461 ? 1.1388 2.0659 1.2280 -0.2348 -0.1258 0.2262  564  ILE A CG2   
3330 N  N     . LEU A 462 ? 1.3338 2.1152 1.4083 -0.2078 -0.1050 0.1849  565  LEU A N     
3331 C  CA    . LEU A 462 ? 1.3930 2.1424 1.4545 -0.2229 -0.1022 0.1654  565  LEU A CA    
3332 C  C     . LEU A 462 ? 1.3433 2.0728 1.4129 -0.2114 -0.0982 0.1679  565  LEU A C     
3333 O  O     . LEU A 462 ? 1.0296 1.7630 1.0948 -0.2267 -0.0978 0.1622  565  LEU A O     
3334 C  CB    . LEU A 462 ? 1.1743 1.8760 1.2224 -0.2254 -0.0985 0.1460  565  LEU A CB    
3335 C  CG    . LEU A 462 ? 1.4052 2.0664 1.4427 -0.2379 -0.0948 0.1267  565  LEU A CG    
3336 C  CD1   . LEU A 462 ? 1.2924 1.9777 1.3175 -0.2667 -0.0958 0.1188  565  LEU A CD1   
3337 C  CD2   . LEU A 462 ? 1.2860 1.9016 1.3185 -0.2360 -0.0902 0.1112  565  LEU A CD2   
3338 N  N     . PRO A 463 ? 1.3493 2.0551 1.4278 -0.1868 -0.0945 0.1755  566  PRO A N     
3339 C  CA    . PRO A 463 ? 1.2424 1.9297 1.3240 -0.1788 -0.0896 0.1781  566  PRO A CA    
3340 C  C     . PRO A 463 ? 1.2920 2.0257 1.3880 -0.1819 -0.0879 0.1928  566  PRO A C     
3341 O  O     . PRO A 463 ? 1.1711 1.8947 1.2653 -0.1859 -0.0835 0.1904  566  PRO A O     
3342 C  CB    . PRO A 463 ? 1.2407 1.8981 1.3272 -0.1532 -0.0858 0.1848  566  PRO A CB    
3343 C  CG    . PRO A 463 ? 1.3518 2.0315 1.4460 -0.1455 -0.0884 0.1929  566  PRO A CG    
3344 C  CD    . PRO A 463 ? 1.4307 2.1205 1.5139 -0.1670 -0.0936 0.1804  566  PRO A CD    
3345 N  N     . LYS A 464 ? 1.4688 2.2536 1.5803 -0.1803 -0.0914 0.2090  567  LYS A N     
3346 C  CA    . LYS A 464 ? 1.2354 2.0702 1.3661 -0.1848 -0.0910 0.2247  567  LYS A CA    
3347 C  C     . LYS A 464 ? 1.2679 2.1248 1.3895 -0.2145 -0.0969 0.2153  567  LYS A C     
3348 O  O     . LYS A 464 ? 1.4255 2.3037 1.5575 -0.2217 -0.0943 0.2203  567  LYS A O     
3349 C  CB    . LYS A 464 ? 1.2172 2.1011 1.3702 -0.1741 -0.0946 0.2476  567  LYS A CB    
3350 C  CG    . LYS A 464 ? 1.3531 2.2161 1.5148 -0.1455 -0.0881 0.2572  567  LYS A CG    
3351 C  CD    . LYS A 464 ? 1.3552 2.1982 1.5282 -0.1275 -0.0749 0.2634  567  LYS A CD    
3352 C  CE    . LYS A 464 ? 1.3985 2.2208 1.5789 -0.1007 -0.0675 0.2730  567  LYS A CE    
3353 N  NZ    . LYS A 464 ? 1.6681 2.4670 1.8554 -0.0847 -0.0524 0.2781  567  LYS A NZ    
3354 N  N     . LEU A 465 ? 1.4595 2.3105 1.5615 -0.2326 -0.1033 0.2011  568  LEU A N     
3355 C  CA    . LEU A 465 ? 1.3065 2.1752 1.3961 -0.2631 -0.1080 0.1905  568  LEU A CA    
3356 C  C     . LEU A 465 ? 1.2234 2.0507 1.3000 -0.2717 -0.1018 0.1729  568  LEU A C     
3357 O  O     . LEU A 465 ? 1.2879 2.1343 1.3628 -0.2919 -0.1026 0.1698  568  LEU A O     
3358 C  CB    . LEU A 465 ? 1.2851 2.1530 1.3541 -0.2804 -0.1135 0.1789  568  LEU A CB    
3359 C  CG    . LEU A 465 ? 1.2328 2.1087 1.2817 -0.3146 -0.1164 0.1635  568  LEU A CG    
3360 C  CD1   . LEU A 465 ? 1.2388 2.1764 1.3006 -0.3304 -0.1244 0.1789  568  LEU A CD1   
3361 C  CD2   . LEU A 465 ? 1.4535 2.3185 1.4791 -0.3293 -0.1179 0.1504  568  LEU A CD2   
3362 N  N     . LEU A 466 ? 1.2276 1.9989 1.2953 -0.2576 -0.0963 0.1625  569  LEU A N     
3363 C  CA    . LEU A 466 ? 1.2205 1.9495 1.2750 -0.2658 -0.0917 0.1472  569  LEU A CA    
3364 C  C     . LEU A 466 ? 1.4244 2.1626 1.4889 -0.2620 -0.0864 0.1564  569  LEU A C     
3365 O  O     . LEU A 466 ? 1.2818 2.0044 1.3364 -0.2769 -0.0837 0.1465  569  LEU A O     
3366 C  CB    . LEU A 466 ? 1.2042 1.8738 1.2495 -0.2511 -0.0893 0.1372  569  LEU A CB    
3367 C  CG    . LEU A 466 ? 1.3931 2.0457 1.4291 -0.2566 -0.0915 0.1248  569  LEU A CG    
3368 C  CD1   . LEU A 466 ? 1.1375 1.7385 1.1727 -0.2383 -0.0903 0.1201  569  LEU A CD1   
3369 C  CD2   . LEU A 466 ? 1.3298 1.9747 1.3505 -0.2841 -0.0905 0.1071  569  LEU A CD2   
3370 N  N     . LEU A 467 ? 1.3523 2.1142 1.4368 -0.2425 -0.0833 0.1753  570  LEU A N     
3371 C  CA    . LEU A 467 ? 1.1937 1.9676 1.2905 -0.2387 -0.0754 0.1851  570  LEU A CA    
3372 C  C     . LEU A 467 ? 1.2054 2.0388 1.3185 -0.2567 -0.0782 0.1940  570  LEU A C     
3373 O  O     . LEU A 467 ? 1.1879 2.0348 1.3138 -0.2568 -0.0707 0.2014  570  LEU A O     
3374 C  CB    . LEU A 467 ? 1.5724 2.3464 1.6861 -0.2108 -0.0679 0.2017  570  LEU A CB    
3375 C  CG    . LEU A 467 ? 1.2698 1.9824 1.3678 -0.1946 -0.0605 0.1955  570  LEU A CG    
3376 C  CD1   . LEU A 467 ? 0.9554 1.6279 1.0363 -0.1915 -0.0678 0.1831  570  LEU A CD1   
3377 C  CD2   . LEU A 467 ? 1.6200 2.3381 1.7350 -0.1706 -0.0498 0.2126  570  LEU A CD2   
3378 N  N     . SER A 468 ? 1.4048 2.2736 1.5172 -0.2732 -0.0887 0.1937  571  SER A N     
3379 C  CA    . SER A 468 ? 1.4258 2.3539 1.5526 -0.2934 -0.0945 0.2030  571  SER A CA    
3380 C  C     . SER A 468 ? 1.3074 2.2273 1.4116 -0.3251 -0.0978 0.1837  571  SER A C     
3381 O  O     . SER A 468 ? 1.4922 2.4579 1.5995 -0.3478 -0.1062 0.1872  571  SER A O     
3382 C  CB    . SER A 468 ? 1.3734 2.3514 1.5136 -0.2929 -0.1053 0.2188  571  SER A CB    
3383 O  OG    . SER A 468 ? 1.4550 2.4397 1.6172 -0.2632 -0.1012 0.2372  571  SER A OG    
3384 N  N     . VAL A 469 ? 1.3844 2.2466 1.4659 -0.3277 -0.0917 0.1642  572  VAL A N     
3385 C  CA    . VAL A 469 ? 1.4660 2.3111 1.5249 -0.3561 -0.0924 0.1443  572  VAL A CA    
3386 C  C     . VAL A 469 ? 1.4365 2.2548 1.4922 -0.3592 -0.0836 0.1386  572  VAL A C     
3387 O  O     . VAL A 469 ? 1.6797 2.4548 1.7319 -0.3403 -0.0769 0.1375  572  VAL A O     
3388 C  CB    . VAL A 469 ? 1.4523 2.2492 1.4871 -0.3582 -0.0927 0.1253  572  VAL A CB    
3389 C  CG1   . VAL A 469 ? 1.5261 2.3046 1.5390 -0.3879 -0.0910 0.1049  572  VAL A CG1   
3390 C  CG2   . VAL A 469 ? 1.6035 2.4237 1.6400 -0.3540 -0.0996 0.1311  572  VAL A CG2   
3391 N  N     . LYS A 470 ? 1.3761 2.2195 1.4313 -0.3845 -0.0840 0.1353  573  LYS A N     
3392 C  CA    . LYS A 470 ? 1.7053 2.5213 1.7533 -0.3922 -0.0753 0.1277  573  LYS A CA    
3393 C  C     . LYS A 470 ? 1.6230 2.3777 1.6419 -0.4012 -0.0730 0.1052  573  LYS A C     
3394 O  O     . LYS A 470 ? 1.7211 2.4752 1.7251 -0.4268 -0.0747 0.0912  573  LYS A O     
3395 C  CB    . LYS A 470 ? 1.5075 2.3717 1.5659 -0.4176 -0.0766 0.1315  573  LYS A CB    
3396 C  CG    . LYS A 470 ? 1.2605 2.1792 1.3541 -0.4066 -0.0753 0.1553  573  LYS A CG    
3397 C  CD    . LYS A 470 ? 1.3700 2.3368 1.4760 -0.4339 -0.0774 0.1590  573  LYS A CD    
3398 C  CE    . LYS A 470 ? 1.6084 2.6237 1.7544 -0.4215 -0.0725 0.1828  573  LYS A CE    
3399 N  NZ    . LYS A 470 ? 1.3344 2.3094 1.4814 -0.4024 -0.0558 0.1830  573  LYS A NZ    
3400 N  N     . TRP A 471 ? 1.3091 2.0112 1.3203 -0.3808 -0.0688 0.1023  574  TRP A N     
3401 C  CA    . TRP A 471 ? 1.3835 2.0265 1.3727 -0.3862 -0.0670 0.0842  574  TRP A CA    
3402 C  C     . TRP A 471 ? 1.7652 2.3890 1.7414 -0.4078 -0.0614 0.0734  574  TRP A C     
3403 O  O     . TRP A 471 ? 1.4573 2.0368 1.4170 -0.4169 -0.0596 0.0581  574  TRP A O     
3404 C  CB    . TRP A 471 ? 1.6625 2.2573 1.6487 -0.3601 -0.0660 0.0869  574  TRP A CB    
3405 C  CG    . TRP A 471 ? 1.6232 2.2278 1.6195 -0.3398 -0.0708 0.0947  574  TRP A CG    
3406 C  CD1   . TRP A 471 ? 1.5110 2.1409 1.5233 -0.3195 -0.0707 0.1116  574  TRP A CD1   
3407 C  CD2   . TRP A 471 ? 1.6010 2.1891 1.5928 -0.3381 -0.0748 0.0859  574  TRP A CD2   
3408 N  NE1   . TRP A 471 ? 1.4582 2.0883 1.4750 -0.3055 -0.0754 0.1140  574  TRP A NE1   
3409 C  CE2   . TRP A 471 ? 1.4015 2.0067 1.4060 -0.3167 -0.0780 0.0983  574  TRP A CE2   
3410 C  CE3   . TRP A 471 ? 1.3650 1.9240 1.3444 -0.3524 -0.0741 0.0687  574  TRP A CE3   
3411 C  CZ2   . TRP A 471 ? 1.3793 1.9746 1.3836 -0.3099 -0.0813 0.0940  574  TRP A CZ2   
3412 C  CZ3   . TRP A 471 ? 1.0096 1.5585 0.9901 -0.3453 -0.0761 0.0643  574  TRP A CZ3   
3413 C  CH2   . TRP A 471 ? 1.3365 1.9040 1.3289 -0.3245 -0.0800 0.0769  574  TRP A CH2   
3414 N  N     . ASN A 472 ? 1.7778 2.4332 1.7631 -0.4159 -0.0578 0.0816  575  ASN A N     
3415 C  CA    . ASN A 472 ? 1.6405 2.2839 1.6145 -0.4388 -0.0520 0.0721  575  ASN A CA    
3416 C  C     . ASN A 472 ? 1.7920 2.4670 1.7617 -0.4694 -0.0549 0.0624  575  ASN A C     
3417 O  O     . ASN A 472 ? 2.0128 2.6918 1.9772 -0.4912 -0.0504 0.0567  575  ASN A O     
3418 C  CB    . ASN A 472 ? 1.7255 2.3890 1.7120 -0.4351 -0.0451 0.0849  575  ASN A CB    
3419 C  CG    . ASN A 472 ? 1.6500 2.3849 1.6648 -0.4350 -0.0479 0.1013  575  ASN A CG    
3420 O  OD1   . ASN A 472 ? 1.7191 2.4952 1.7417 -0.4581 -0.0493 0.1016  575  ASN A OD1   
3421 N  ND2   . ASN A 472 ? 1.6524 2.4024 1.6840 -0.4095 -0.0490 0.1161  575  ASN A ND2   
3422 N  N     . SER A 473 ? 1.6512 2.3470 1.6208 -0.4729 -0.0618 0.0601  576  SER A N     
3423 C  CA    . SER A 473 ? 1.6586 2.3823 1.6189 -0.5040 -0.0650 0.0503  576  SER A CA    
3424 C  C     . SER A 473 ? 1.7309 2.4109 1.6700 -0.5103 -0.0627 0.0314  576  SER A C     
3425 O  O     . SER A 473 ? 1.8037 2.4745 1.7448 -0.4928 -0.0656 0.0332  576  SER A O     
3426 C  CB    . SER A 473 ? 1.8633 2.6558 1.8410 -0.5066 -0.0751 0.0658  576  SER A CB    
3427 O  OG    . SER A 473 ? 2.2213 3.0387 2.1850 -0.5392 -0.0796 0.0561  576  SER A OG    
3428 N  N     . ARG A 474 ? 1.7590 2.4113 1.6791 -0.5354 -0.0559 0.0134  577  ARG A N     
3429 C  CA    . ARG A 474 ? 1.6762 2.2853 1.5780 -0.5433 -0.0502 -0.0055 577  ARG A CA    
3430 C  C     . ARG A 474 ? 1.7417 2.3826 1.6361 -0.5566 -0.0547 -0.0089 577  ARG A C     
3431 O  O     . ARG A 474 ? 1.8533 2.4610 1.7358 -0.5573 -0.0492 -0.0221 577  ARG A O     
3432 C  CB    . ARG A 474 ? 1.6568 2.2305 1.5407 -0.5688 -0.0400 -0.0234 577  ARG A CB    
3433 C  CG    . ARG A 474 ? 2.1599 2.7760 2.0361 -0.6027 -0.0410 -0.0266 577  ARG A CG    
3434 C  CD    . ARG A 474 ? 2.1408 2.7178 2.0010 -0.6249 -0.0296 -0.0427 577  ARG A CD    
3435 N  NE    . ARG A 474 ? 2.1318 2.6569 1.9737 -0.6340 -0.0189 -0.0632 577  ARG A NE    
3436 C  CZ    . ARG A 474 ? 2.1191 2.6454 1.9401 -0.6658 -0.0128 -0.0801 577  ARG A CZ    
3437 N  NH1   . ARG A 474 ? 2.0269 2.6047 1.8407 -0.6935 -0.0188 -0.0789 577  ARG A NH1   
3438 N  NH2   . ARG A 474 ? 2.0726 2.5465 1.8800 -0.6707 0.0002  -0.0984 577  ARG A NH2   
3439 N  N     . ASP A 475 ? 1.9491 2.6532 1.8506 -0.5676 -0.0644 0.0036  578  ASP A N     
3440 C  CA    . ASP A 475 ? 2.0398 2.7779 1.9323 -0.5813 -0.0711 0.0034  578  ASP A CA    
3441 C  C     . ASP A 475 ? 1.9927 2.7460 1.9008 -0.5516 -0.0782 0.0189  578  ASP A C     
3442 O  O     . ASP A 475 ? 2.1205 2.8668 2.0166 -0.5532 -0.0781 0.0126  578  ASP A O     
3443 C  CB    . ASP A 475 ? 2.2127 3.0140 2.1063 -0.6093 -0.0806 0.0117  578  ASP A CB    
3444 C  CG    . ASP A 475 ? 2.2868 3.0751 2.1632 -0.6421 -0.0736 -0.0044 578  ASP A CG    
3445 O  OD1   . ASP A 475 ? 2.2326 2.9615 2.0962 -0.6421 -0.0606 -0.0216 578  ASP A OD1   
3446 O  OD2   . ASP A 475 ? 2.2942 3.1320 2.1712 -0.6681 -0.0814 0.0012  578  ASP A OD2   
3447 N  N     . GLU A 476 ? 1.7857 2.5577 1.7197 -0.5249 -0.0827 0.0386  579  GLU A N     
3448 C  CA    . GLU A 476 ? 1.9555 2.7404 1.9050 -0.4963 -0.0884 0.0538  579  GLU A CA    
3449 C  C     . GLU A 476 ? 1.8707 2.5957 1.8162 -0.4731 -0.0814 0.0449  579  GLU A C     
3450 O  O     . GLU A 476 ? 1.6322 2.3566 1.5795 -0.4592 -0.0838 0.0481  579  GLU A O     
3451 C  CB    . GLU A 476 ? 1.8946 2.7166 1.8733 -0.4760 -0.0929 0.0774  579  GLU A CB    
3452 C  CG    . GLU A 476 ? 1.6088 2.4976 1.6004 -0.4957 -0.1011 0.0908  579  GLU A CG    
3453 C  CD    . GLU A 476 ? 1.6436 2.5710 1.6695 -0.4722 -0.1037 0.1161  579  GLU A CD    
3454 O  OE1   . GLU A 476 ? 1.8671 2.7665 1.9022 -0.4417 -0.0983 0.1217  579  GLU A OE1   
3455 O  OE2   . GLU A 476 ? 1.4830 2.4685 1.5275 -0.4848 -0.1105 0.1308  579  GLU A OE2   
3456 N  N     . VAL A 477 ? 1.8388 2.5140 1.7801 -0.4692 -0.0734 0.0348  580  VAL A N     
3457 C  CA    . VAL A 477 ? 1.5806 2.1994 1.5206 -0.4492 -0.0684 0.0275  580  VAL A CA    
3458 C  C     . VAL A 477 ? 1.7225 2.3148 1.6461 -0.4638 -0.0621 0.0088  580  VAL A C     
3459 O  O     . VAL A 477 ? 1.8547 2.4134 1.7818 -0.4469 -0.0593 0.0052  580  VAL A O     
3460 C  CB    . VAL A 477 ? 1.4840 2.0577 1.4237 -0.4427 -0.0632 0.0241  580  VAL A CB    
3461 C  CG1   . VAL A 477 ? 1.7280 2.2764 1.6507 -0.4703 -0.0552 0.0058  580  VAL A CG1   
3462 C  CG2   . VAL A 477 ? 1.4879 2.0133 1.4333 -0.4163 -0.0627 0.0247  580  VAL A CG2   
3463 N  N     . ALA A 478 ? 1.4809 2.0872 1.3867 -0.4959 -0.0589 -0.0035 581  ALA A N     
3464 C  CA    . ALA A 478 ? 1.5619 2.1427 1.4493 -0.5122 -0.0499 -0.0224 581  ALA A CA    
3465 C  C     . ALA A 478 ? 1.6574 2.2726 1.5406 -0.5129 -0.0555 -0.0169 581  ALA A C     
3466 O  O     . ALA A 478 ? 1.6835 2.2716 1.5600 -0.5101 -0.0482 -0.0270 581  ALA A O     
3467 C  CB    . ALA A 478 ? 1.6002 2.1763 1.4657 -0.5486 -0.0423 -0.0394 581  ALA A CB    
3468 N  N     . GLN A 479 ? 1.5224 2.1975 1.4110 -0.5168 -0.0681 0.0000  582  GLN A N     
3469 C  CA    . GLN A 479 ? 1.4147 2.1249 1.2998 -0.5167 -0.0753 0.0086  582  GLN A CA    
3470 C  C     . GLN A 479 ? 1.6810 2.3823 1.5861 -0.4802 -0.0778 0.0213  582  GLN A C     
3471 O  O     . GLN A 479 ? 1.3660 2.0680 1.2649 -0.4767 -0.0775 0.0208  582  GLN A O     
3472 C  CB    . GLN A 479 ? 1.5054 2.2842 1.3945 -0.5315 -0.0895 0.0258  582  GLN A CB    
3473 C  CG    . GLN A 479 ? 1.9787 2.7726 1.8449 -0.5723 -0.0891 0.0136  582  GLN A CG    
3474 C  CD    . GLN A 479 ? 2.1968 2.9717 2.0285 -0.5990 -0.0820 -0.0061 582  GLN A CD    
3475 O  OE1   . GLN A 479 ? 2.4484 3.2281 2.2739 -0.5927 -0.0838 -0.0029 582  GLN A OE1   
3476 N  NE2   . GLN A 479 ? 1.9689 2.7195 1.7767 -0.6296 -0.0721 -0.0270 582  GLN A NE2   
3477 N  N     . MET A 480 ? 1.8191 2.5104 1.7461 -0.4541 -0.0795 0.0324  583  MET A N     
3478 C  CA    . MET A 480 ? 1.5156 2.1950 1.4599 -0.4207 -0.0814 0.0438  583  MET A CA    
3479 C  C     . MET A 480 ? 1.7032 2.3241 1.6436 -0.4114 -0.0718 0.0285  583  MET A C     
3480 O  O     . MET A 480 ? 1.7263 2.3396 1.6745 -0.3922 -0.0724 0.0333  583  MET A O     
3481 C  CB    . MET A 480 ? 1.3450 2.0280 1.3096 -0.3986 -0.0848 0.0591  583  MET A CB    
3482 C  CG    . MET A 480 ? 1.5542 2.2264 1.5352 -0.3653 -0.0868 0.0718  583  MET A CG    
3483 S  SD    . MET A 480 ? 1.6200 2.3340 1.6060 -0.3578 -0.0934 0.0851  583  MET A SD    
3484 C  CE    . MET A 480 ? 1.4009 2.1872 1.3962 -0.3713 -0.1026 0.1036  583  MET A CE    
3485 N  N     . TYR A 481 ? 1.6030 2.1828 1.5339 -0.4247 -0.0626 0.0108  584  TYR A N     
3486 C  CA    . TYR A 481 ? 1.4537 1.9792 1.3858 -0.4169 -0.0527 -0.0028 584  TYR A CA    
3487 C  C     . TYR A 481 ? 1.6274 2.1545 1.5474 -0.4274 -0.0461 -0.0126 584  TYR A C     
3488 O  O     . TYR A 481 ? 1.6776 2.1783 1.6070 -0.4108 -0.0416 -0.0145 584  TYR A O     
3489 C  CB    . TYR A 481 ? 1.4239 1.9075 1.3496 -0.4310 -0.0432 -0.0186 584  TYR A CB    
3490 C  CG    . TYR A 481 ? 1.4908 1.9489 1.4298 -0.4137 -0.0471 -0.0108 584  TYR A CG    
3491 C  CD1   . TYR A 481 ? 1.3997 1.8693 1.3536 -0.3877 -0.0569 0.0073  584  TYR A CD1   
3492 C  CD2   . TYR A 481 ? 1.3951 1.8151 1.3299 -0.4242 -0.0401 -0.0217 584  TYR A CD2   
3493 C  CE1   . TYR A 481 ? 1.3773 1.8208 1.3380 -0.3743 -0.0600 0.0138  584  TYR A CE1   
3494 C  CE2   . TYR A 481 ? 1.4270 1.8222 1.3703 -0.4101 -0.0444 -0.0139 584  TYR A CE2   
3495 C  CZ    . TYR A 481 ? 1.5415 1.9483 1.4962 -0.3859 -0.0544 0.0035  584  TYR A CZ    
3496 O  OH    . TYR A 481 ? 1.7194 2.0988 1.6774 -0.3742 -0.0583 0.0108  584  TYR A OH    
3497 N  N     . CYS A 482 ? 1.5880 2.1451 1.4859 -0.4564 -0.0455 -0.0187 585  CYS A N     
3498 C  CA    . CYS A 482 ? 1.6338 2.1907 1.5138 -0.4703 -0.0382 -0.0290 585  CYS A CA    
3499 C  C     . CYS A 482 ? 1.6338 2.2225 1.5216 -0.4523 -0.0476 -0.0120 585  CYS A C     
3500 O  O     . CYS A 482 ? 1.8272 2.4017 1.7082 -0.4514 -0.0401 -0.0185 585  CYS A O     
3501 C  CB    . CYS A 482 ? 1.6831 2.2631 1.5327 -0.5093 -0.0363 -0.0396 585  CYS A CB    
3502 S  SG    . CYS A 482 ? 1.7538 2.2891 1.5890 -0.5349 -0.0206 -0.0639 585  CYS A SG    
3503 N  N     . LEU A 483 ? 1.4886 2.1190 1.3914 -0.4379 -0.0623 0.0099  586  LEU A N     
3504 C  CA    . LEU A 483 ? 1.4759 2.1352 1.3888 -0.4189 -0.0705 0.0276  586  LEU A CA    
3505 C  C     . LEU A 483 ? 1.6827 2.3046 1.6159 -0.3868 -0.0666 0.0299  586  LEU A C     
3506 O  O     . LEU A 483 ? 1.5869 2.2095 1.5216 -0.3761 -0.0656 0.0337  586  LEU A O     
3507 C  CB    . LEU A 483 ? 1.6266 2.3401 1.5532 -0.4125 -0.0852 0.0510  586  LEU A CB    
3508 C  CG    . LEU A 483 ? 1.7629 2.5245 1.6744 -0.4435 -0.0930 0.0541  586  LEU A CG    
3509 C  CD1   . LEU A 483 ? 1.7160 2.5298 1.6507 -0.4322 -0.1060 0.0795  586  LEU A CD1   
3510 C  CD2   . LEU A 483 ? 1.5707 2.3498 1.4575 -0.4640 -0.0941 0.0506  586  LEU A CD2   
3511 N  N     . VAL A 484 ? 1.6955 2.2844 1.6433 -0.3726 -0.0648 0.0281  587  VAL A N     
3512 C  CA    . VAL A 484 ? 1.3023 1.8543 1.2689 -0.3446 -0.0628 0.0305  587  VAL A CA    
3513 C  C     . VAL A 484 ? 1.4996 2.0091 1.4630 -0.3494 -0.0497 0.0124  587  VAL A C     
3514 O  O     . VAL A 484 ? 1.9061 2.3959 1.8833 -0.3301 -0.0476 0.0147  587  VAL A O     
3515 C  CB    . VAL A 484 ? 1.3861 1.9150 1.3656 -0.3312 -0.0662 0.0348  587  VAL A CB    
3516 C  CG1   . VAL A 484 ? 1.5183 2.0084 1.5155 -0.3050 -0.0662 0.0378  587  VAL A CG1   
3517 C  CG2   . VAL A 484 ? 1.5279 2.0981 1.5122 -0.3258 -0.0758 0.0526  587  VAL A CG2   
3518 N  N     . LYS A 485 ? 1.4882 1.9825 1.4347 -0.3754 -0.0393 -0.0059 588  LYS A N     
3519 C  CA    . LYS A 485 ? 1.6617 2.1133 1.6071 -0.3807 -0.0232 -0.0240 588  LYS A CA    
3520 C  C     . LYS A 485 ? 1.4689 1.9322 1.4074 -0.3802 -0.0187 -0.0241 588  LYS A C     
3521 O  O     . LYS A 485 ? 1.6824 2.1130 1.6335 -0.3689 -0.0086 -0.0304 588  LYS A O     
3522 C  CB    . LYS A 485 ? 1.3384 1.7738 1.2634 -0.4114 -0.0109 -0.0437 588  LYS A CB    
3523 C  CG    . LYS A 485 ? 1.5370 1.9252 1.4620 -0.4183 0.0097  -0.0636 588  LYS A CG    
3524 C  CD    . LYS A 485 ? 1.6514 2.0236 1.5528 -0.4506 0.0236  -0.0836 588  LYS A CD    
3525 C  CE    . LYS A 485 ? 1.6437 2.0581 1.5097 -0.4798 0.0206  -0.0861 588  LYS A CE    
3526 N  NZ    . LYS A 485 ? 1.7853 2.1823 1.6249 -0.5140 0.0347  -0.1068 588  LYS A NZ    
3527 N  N     . ASP A 486 ? 1.6153 2.1253 1.5349 -0.3927 -0.0264 -0.0160 589  ASP A N     
3528 C  CA    . ASP A 486 ? 1.7813 2.3060 1.6892 -0.3950 -0.0236 -0.0144 589  ASP A CA    
3529 C  C     . ASP A 486 ? 1.6051 2.1711 1.5245 -0.3744 -0.0397 0.0102  589  ASP A C     
3530 O  O     . ASP A 486 ? 1.6080 2.2088 1.5119 -0.3833 -0.0447 0.0182  589  ASP A O     
3531 C  CB    . ASP A 486 ? 1.9701 2.5117 1.8412 -0.4315 -0.0180 -0.0263 589  ASP A CB    
3532 C  CG    . ASP A 486 ? 1.8696 2.3656 1.7273 -0.4527 0.0021  -0.0524 589  ASP A CG    
3533 O  OD1   . ASP A 486 ? 2.0612 2.5128 1.9419 -0.4372 0.0121  -0.0601 589  ASP A OD1   
3534 O  OD2   . ASP A 486 ? 1.9946 2.4987 1.8190 -0.4857 0.0080  -0.0647 589  ASP A OD2   
3535 N  N     . TRP A 487 ? 1.3957 1.9564 1.3415 -0.3472 -0.0477 0.0229  590  TRP A N     
3536 C  CA    . TRP A 487 ? 1.5109 2.1078 1.4686 -0.3272 -0.0604 0.0460  590  TRP A CA    
3537 C  C     . TRP A 487 ? 1.5928 2.1744 1.5609 -0.3075 -0.0564 0.0495  590  TRP A C     
3538 O  O     . TRP A 487 ? 1.4993 2.0373 1.4791 -0.2980 -0.0472 0.0388  590  TRP A O     
3539 C  CB    . TRP A 487 ? 1.5495 2.1469 1.5272 -0.3082 -0.0689 0.0581  590  TRP A CB    
3540 C  CG    . TRP A 487 ? 1.4638 2.1043 1.4520 -0.2929 -0.0802 0.0817  590  TRP A CG    
3541 C  CD1   . TRP A 487 ? 1.5767 2.2153 1.5820 -0.2656 -0.0830 0.0956  590  TRP A CD1   
3542 C  CD2   . TRP A 487 ? 1.3226 2.0143 1.3074 -0.3040 -0.0893 0.0949  590  TRP A CD2   
3543 N  NE1   . TRP A 487 ? 1.3156 1.9990 1.3284 -0.2581 -0.0917 0.1164  590  TRP A NE1   
3544 C  CE2   . TRP A 487 ? 1.3571 2.0753 1.3597 -0.2809 -0.0961 0.1172  590  TRP A CE2   
3545 C  CE3   . TRP A 487 ? 1.3267 2.0447 1.2966 -0.3318 -0.0921 0.0905  590  TRP A CE3   
3546 C  CZ2   . TRP A 487 ? 1.4462 2.2171 1.4561 -0.2832 -0.1051 0.1363  590  TRP A CZ2   
3547 C  CZ3   . TRP A 487 ? 1.3666 2.1385 1.3430 -0.3353 -0.1029 0.1095  590  TRP A CZ3   
3548 C  CH2   . TRP A 487 ? 1.4822 2.2806 1.4802 -0.3104 -0.1091 0.1327  590  TRP A CH2   
3549 N  N     . PRO A 488 ? 1.4533 2.0705 1.4190 -0.3015 -0.0632 0.0654  591  PRO A N     
3550 C  CA    . PRO A 488 ? 1.4703 2.0737 1.4450 -0.2833 -0.0590 0.0693  591  PRO A CA    
3551 C  C     . PRO A 488 ? 1.5213 2.0993 1.5239 -0.2536 -0.0614 0.0763  591  PRO A C     
3552 O  O     . PRO A 488 ? 1.6532 2.2369 1.6662 -0.2442 -0.0692 0.0850  591  PRO A O     
3553 C  CB    . PRO A 488 ? 1.6201 2.2728 1.5869 -0.2835 -0.0684 0.0888  591  PRO A CB    
3554 C  CG    . PRO A 488 ? 1.7052 2.3933 1.6517 -0.3112 -0.0746 0.0886  591  PRO A CG    
3555 C  CD    . PRO A 488 ? 1.5256 2.1978 1.4797 -0.3140 -0.0745 0.0803  591  PRO A CD    
3556 N  N     . PRO A 489 ? 1.7332 2.2817 1.7475 -0.2393 -0.0546 0.0729  592  PRO A N     
3557 C  CA    . PRO A 489 ? 1.7343 2.2575 1.7731 -0.2131 -0.0583 0.0798  592  PRO A CA    
3558 C  C     . PRO A 489 ? 1.6267 2.1787 1.6728 -0.1939 -0.0679 0.1018  592  PRO A C     
3559 O  O     . PRO A 489 ? 1.7410 2.3267 1.7794 -0.1953 -0.0698 0.1125  592  PRO A O     
3560 C  CB    . PRO A 489 ? 1.7924 2.2818 1.8416 -0.2067 -0.0478 0.0703  592  PRO A CB    
3561 C  CG    . PRO A 489 ? 1.8389 2.3485 1.8680 -0.2225 -0.0404 0.0666  592  PRO A CG    
3562 C  CD    . PRO A 489 ? 1.7800 2.3155 1.7850 -0.2480 -0.0425 0.0620  592  PRO A CD    
3563 N  N     . ILE A 490 ? 1.3412 1.8779 1.4018 -0.1765 -0.0733 0.1088  593  ILE A N     
3564 C  CA    . ILE A 490 ? 1.0229 1.5789 1.0919 -0.1569 -0.0794 0.1284  593  ILE A CA    
3565 C  C     . ILE A 490 ? 1.1255 1.6452 1.2099 -0.1358 -0.0790 0.1302  593  ILE A C     
3566 O  O     . ILE A 490 ? 1.1980 1.6809 1.2891 -0.1365 -0.0759 0.1179  593  ILE A O     
3567 C  CB    . ILE A 490 ? 1.3109 1.8849 1.3794 -0.1574 -0.0851 0.1366  593  ILE A CB    
3568 C  CG1   . ILE A 490 ? 1.6507 2.1858 1.7211 -0.1585 -0.0856 0.1259  593  ILE A CG1   
3569 C  CG2   . ILE A 490 ? 1.1345 1.7505 1.1905 -0.1785 -0.0871 0.1376  593  ILE A CG2   
3570 C  CD1   . ILE A 490 ? 0.8877 1.4358 0.9558 -0.1600 -0.0892 0.1325  593  ILE A CD1   
3571 N  N     . LYS A 491 ? 1.4252 1.9557 1.5164 -0.1174 -0.0819 0.1465  594  LYS A N     
3572 C  CA    . LYS A 491 ? 1.3205 1.8183 1.4236 -0.0986 -0.0820 0.1495  594  LYS A CA    
3573 C  C     . LYS A 491 ? 1.2933 1.7545 1.3990 -0.0968 -0.0862 0.1434  594  LYS A C     
3574 O  O     . LYS A 491 ? 1.3848 1.8517 1.4832 -0.1041 -0.0887 0.1430  594  LYS A O     
3575 C  CB    . LYS A 491 ? 1.2076 1.7241 1.3150 -0.0806 -0.0823 0.1682  594  LYS A CB    
3576 C  CG    . LYS A 491 ? 1.4580 2.0092 1.5641 -0.0803 -0.0796 0.1774  594  LYS A CG    
3577 C  CD    . LYS A 491 ? 1.6785 2.2109 1.7863 -0.0822 -0.0748 0.1680  594  LYS A CD    
3578 C  CE    . LYS A 491 ? 1.8469 2.4116 1.9493 -0.0831 -0.0722 0.1778  594  LYS A CE    
3579 N  NZ    . LYS A 491 ? 1.5527 2.1564 1.6406 -0.1022 -0.0748 0.1791  594  LYS A NZ    
3580 N  N     . PRO A 492 ? 1.2786 1.7019 1.3947 -0.0883 -0.0876 0.1394  595  PRO A N     
3581 C  CA    . PRO A 492 ? 1.3203 1.7078 1.4376 -0.0877 -0.0939 0.1357  595  PRO A CA    
3582 C  C     . PRO A 492 ? 1.2863 1.6743 1.3944 -0.0792 -0.0972 0.1467  595  PRO A C     
3583 O  O     . PRO A 492 ? 1.2506 1.6233 1.3508 -0.0853 -0.1010 0.1439  595  PRO A O     
3584 C  CB    . PRO A 492 ? 1.1963 1.5499 1.3293 -0.0790 -0.0960 0.1333  595  PRO A CB    
3585 C  CG    . PRO A 492 ? 1.2400 1.6088 1.3805 -0.0809 -0.0878 0.1292  595  PRO A CG    
3586 C  CD    . PRO A 492 ? 1.3518 1.7632 1.4796 -0.0812 -0.0840 0.1378  595  PRO A CD    
3587 N  N     . GLU A 493 ? 1.5416 1.9447 1.6502 -0.0654 -0.0942 0.1592  596  GLU A N     
3588 C  CA    . GLU A 493 ? 1.4271 1.8299 1.5274 -0.0571 -0.0934 0.1694  596  GLU A CA    
3589 C  C     . GLU A 493 ? 1.2629 1.6981 1.3567 -0.0663 -0.0910 0.1719  596  GLU A C     
3590 O  O     . GLU A 493 ? 1.3488 1.7758 1.4345 -0.0653 -0.0901 0.1753  596  GLU A O     
3591 C  CB    . GLU A 493 ? 1.3812 1.7933 1.4862 -0.0399 -0.0882 0.1825  596  GLU A CB    
3592 C  CG    . GLU A 493 ? 1.4119 1.7870 1.5211 -0.0300 -0.0906 0.1817  596  GLU A CG    
3593 C  CD    . GLU A 493 ? 1.5942 1.9687 1.7161 -0.0323 -0.0914 0.1750  596  GLU A CD    
3594 O  OE1   . GLU A 493 ? 1.4399 1.8431 1.5639 -0.0409 -0.0885 0.1716  596  GLU A OE1   
3595 O  OE2   . GLU A 493 ? 1.3489 1.6934 1.4780 -0.0266 -0.0945 0.1732  596  GLU A OE2   
3596 N  N     . GLN A 494 ? 1.2730 1.7444 1.3692 -0.0765 -0.0896 0.1703  597  GLN A N     
3597 C  CA    . GLN A 494 ? 1.4533 1.9576 1.5449 -0.0880 -0.0888 0.1724  597  GLN A CA    
3598 C  C     . GLN A 494 ? 1.3707 1.8570 1.4540 -0.1053 -0.0918 0.1580  597  GLN A C     
3599 O  O     . GLN A 494 ? 1.2953 1.7944 1.3731 -0.1134 -0.0914 0.1590  597  GLN A O     
3600 C  CB    . GLN A 494 ? 1.4811 2.0324 1.5761 -0.0945 -0.0878 0.1778  597  GLN A CB    
3601 C  CG    . GLN A 494 ? 1.5492 2.1234 1.6538 -0.0776 -0.0848 0.1950  597  GLN A CG    
3602 C  CD    . GLN A 494 ? 1.5462 2.1641 1.6518 -0.0857 -0.0860 0.2011  597  GLN A CD    
3603 O  OE1   . GLN A 494 ? 1.4257 2.0471 1.5223 -0.1033 -0.0879 0.1891  597  GLN A OE1   
3604 N  NE2   . GLN A 494 ? 1.7032 2.3534 1.8189 -0.0738 -0.0845 0.2203  597  GLN A NE2   
3605 N  N     . ALA A 495 ? 1.4174 1.8738 1.5018 -0.1110 -0.0940 0.1451  598  ALA A N     
3606 C  CA    . ALA A 495 ? 1.3777 1.8132 1.4566 -0.1263 -0.0960 0.1321  598  ALA A CA    
3607 C  C     . ALA A 495 ? 1.4650 1.8660 1.5379 -0.1224 -0.1003 0.1333  598  ALA A C     
3608 O  O     . ALA A 495 ? 1.4429 1.8338 1.5084 -0.1350 -0.1016 0.1265  598  ALA A O     
3609 C  CB    . ALA A 495 ? 1.3853 1.7978 1.4716 -0.1320 -0.0951 0.1194  598  ALA A CB    
3610 N  N     . MET A 496 ? 1.2972 1.6781 1.3708 -0.1067 -0.1023 0.1416  599  MET A N     
3611 C  CA    . MET A 496 ? 1.2375 1.5839 1.3000 -0.1050 -0.1065 0.1433  599  MET A CA    
3612 C  C     . MET A 496 ? 1.4353 1.8000 1.4861 -0.1093 -0.1017 0.1481  599  MET A C     
3613 O  O     . MET A 496 ? 1.2875 1.6264 1.3254 -0.1153 -0.1041 0.1459  599  MET A O     
3614 C  CB    . MET A 496 ? 1.2121 1.5337 1.2743 -0.0893 -0.1087 0.1509  599  MET A CB    
3615 C  CG    . MET A 496 ? 1.1425 1.4436 1.2187 -0.0847 -0.1140 0.1471  599  MET A CG    
3616 S  SD    . MET A 496 ? 1.2462 1.5148 1.3189 -0.0695 -0.1179 0.1558  599  MET A SD    
3617 C  CE    . MET A 496 ? 1.4339 1.7375 1.5025 -0.0569 -0.1053 0.1675  599  MET A CE    
3618 N  N     . GLU A 497 ? 1.2788 1.6878 1.3351 -0.1066 -0.0949 0.1558  600  GLU A N     
3619 C  CA    . GLU A 497 ? 1.1870 1.6183 1.2382 -0.1106 -0.0892 0.1616  600  GLU A CA    
3620 C  C     . GLU A 497 ? 1.1774 1.6102 1.2217 -0.1302 -0.0913 0.1515  600  GLU A C     
3621 O  O     . GLU A 497 ? 1.3383 1.7687 1.3737 -0.1354 -0.0880 0.1530  600  GLU A O     
3622 C  CB    . GLU A 497 ? 1.2532 1.7365 1.3178 -0.1046 -0.0834 0.1737  600  GLU A CB    
3623 C  CG    . GLU A 497 ? 1.3930 1.9048 1.4595 -0.1072 -0.0765 0.1822  600  GLU A CG    
3624 C  CD    . GLU A 497 ? 1.3143 1.8803 1.3991 -0.1012 -0.0728 0.1968  600  GLU A CD    
3625 O  OE1   . GLU A 497 ? 1.5293 2.1066 1.6219 -0.0933 -0.0749 0.2011  600  GLU A OE1   
3626 O  OE2   . GLU A 497 ? 1.5264 2.1244 1.6192 -0.1047 -0.0679 0.2050  600  GLU A OE2   
3627 N  N     . LEU A 498 ? 1.2741 1.7083 1.3217 -0.1417 -0.0950 0.1407  601  LEU A N     
3628 C  CA    . LEU A 498 ? 1.1365 1.5686 1.1772 -0.1613 -0.0957 0.1297  601  LEU A CA    
3629 C  C     . LEU A 498 ? 1.2073 1.5884 1.2395 -0.1649 -0.1005 0.1222  601  LEU A C     
3630 O  O     . LEU A 498 ? 1.3162 1.6885 1.3441 -0.1805 -0.1008 0.1123  601  LEU A O     
3631 C  CB    . LEU A 498 ? 1.1554 1.6075 1.2012 -0.1735 -0.0951 0.1206  601  LEU A CB    
3632 C  CG    . LEU A 498 ? 1.1072 1.6107 1.1592 -0.1732 -0.0928 0.1287  601  LEU A CG    
3633 C  CD1   . LEU A 498 ? 1.1923 1.7089 1.2421 -0.1895 -0.0918 0.1176  601  LEU A CD1   
3634 C  CD2   . LEU A 498 ? 1.2435 1.7841 1.2955 -0.1774 -0.0908 0.1386  601  LEU A CD2   
3635 N  N     . LEU A 499 ? 1.1695 1.5164 1.1987 -0.1519 -0.1046 0.1272  602  LEU A N     
3636 C  CA    . LEU A 499 ? 1.2053 1.5038 1.2262 -0.1555 -0.1119 0.1231  602  LEU A CA    
3637 C  C     . LEU A 499 ? 1.1828 1.4595 1.1847 -0.1526 -0.1121 0.1301  602  LEU A C     
3638 O  O     . LEU A 499 ? 1.4759 1.7100 1.4676 -0.1545 -0.1201 0.1296  602  LEU A O     
3639 C  CB    . LEU A 499 ? 1.1325 1.4030 1.1653 -0.1465 -0.1193 0.1222  602  LEU A CB    
3640 C  CG    . LEU A 499 ? 1.0795 1.3557 1.1303 -0.1515 -0.1183 0.1128  602  LEU A CG    
3641 C  CD1   . LEU A 499 ? 1.0897 1.3366 1.1554 -0.1414 -0.1251 0.1139  602  LEU A CD1   
3642 C  CD2   . LEU A 499 ? 1.0622 1.3287 1.1111 -0.1685 -0.1172 0.1024  602  LEU A CD2   
3643 N  N     . ASP A 500 ? 1.2011 1.5050 1.1984 -0.1486 -0.1031 0.1373  603  ASP A N     
3644 C  CA    . ASP A 500 ? 1.3591 1.6413 1.3367 -0.1467 -0.0993 0.1431  603  ASP A CA    
3645 C  C     . ASP A 500 ? 1.6475 1.9322 1.6143 -0.1626 -0.0958 0.1389  603  ASP A C     
3646 O  O     . ASP A 500 ? 1.4053 1.6956 1.3772 -0.1754 -0.0992 0.1305  603  ASP A O     
3647 C  CB    . ASP A 500 ? 1.6376 1.9438 1.6193 -0.1322 -0.0887 0.1538  603  ASP A CB    
3648 C  CG    . ASP A 500 ? 1.7122 2.0759 1.7117 -0.1333 -0.0805 0.1577  603  ASP A CG    
3649 O  OD1   . ASP A 500 ? 1.6266 2.0109 1.6314 -0.1473 -0.0831 0.1509  603  ASP A OD1   
3650 O  OD2   . ASP A 500 ? 1.4947 1.8826 1.5031 -0.1208 -0.0717 0.1682  603  ASP A OD2   
3651 N  N     . CYS A 501 ? 1.6721 1.9508 1.6234 -0.1625 -0.0874 0.1441  604  CYS A N     
3652 C  CA    . CYS A 501 ? 1.4916 1.7687 1.4310 -0.1777 -0.0831 0.1406  604  CYS A CA    
3653 C  C     . CYS A 501 ? 1.6049 1.9362 1.5615 -0.1852 -0.0757 0.1401  604  CYS A C     
3654 O  O     . CYS A 501 ? 1.7124 2.0460 1.6631 -0.2008 -0.0741 0.1347  604  CYS A O     
3655 C  CB    . CYS A 501 ? 1.5549 1.8064 1.4711 -0.1758 -0.0742 0.1462  604  CYS A CB    
3656 S  SG    . CYS A 501 ? 1.8397 2.1204 1.7661 -0.1579 -0.0576 0.1580  604  CYS A SG    
3657 N  N     . ASN A 502 ? 1.6854 2.0599 1.6627 -0.1755 -0.0720 0.1464  605  ASN A N     
3658 C  CA    . ASN A 502 ? 1.5521 1.9813 1.5460 -0.1835 -0.0668 0.1487  605  ASN A CA    
3659 C  C     . ASN A 502 ? 1.5201 1.9635 1.5189 -0.1993 -0.0742 0.1379  605  ASN A C     
3660 O  O     . ASN A 502 ? 1.7167 2.1985 1.7229 -0.2124 -0.0716 0.1373  605  ASN A O     
3661 C  CB    . ASN A 502 ? 1.6349 2.1058 1.6497 -0.1682 -0.0617 0.1614  605  ASN A CB    
3662 C  CG    . ASN A 502 ? 1.6936 2.1521 1.7055 -0.1526 -0.0503 0.1720  605  ASN A CG    
3663 O  OD1   . ASN A 502 ? 1.7951 2.2324 1.7926 -0.1569 -0.0425 0.1717  605  ASN A OD1   
3664 N  ND2   . ASN A 502 ? 1.6754 2.1446 1.6994 -0.1350 -0.0478 0.1813  605  ASN A ND2   
3665 N  N     . TYR A 503 ? 1.2619 1.6749 1.2575 -0.1993 -0.0826 0.1295  606  TYR A N     
3666 C  CA    . TYR A 503 ? 1.1958 1.6176 1.1962 -0.2133 -0.0866 0.1182  606  TYR A CA    
3667 C  C     . TYR A 503 ? 1.1194 1.4909 1.1089 -0.2211 -0.0916 0.1077  606  TYR A C     
3668 O  O     . TYR A 503 ? 1.0596 1.4040 1.0536 -0.2148 -0.0973 0.1042  606  TYR A O     
3669 C  CB    . TYR A 503 ? 1.0072 1.4470 1.0209 -0.2045 -0.0893 0.1192  606  TYR A CB    
3670 C  CG    . TYR A 503 ? 1.2275 1.7131 1.2533 -0.1938 -0.0856 0.1327  606  TYR A CG    
3671 C  CD1   . TYR A 503 ? 1.3427 1.8201 1.3718 -0.1736 -0.0835 0.1438  606  TYR A CD1   
3672 C  CD2   . TYR A 503 ? 1.1771 1.7137 1.2113 -0.2047 -0.0845 0.1350  606  TYR A CD2   
3673 C  CE1   . TYR A 503 ? 1.1966 1.7147 1.2398 -0.1626 -0.0791 0.1575  606  TYR A CE1   
3674 C  CE2   . TYR A 503 ? 1.0878 1.6678 1.1364 -0.1945 -0.0824 0.1500  606  TYR A CE2   
3675 C  CZ    . TYR A 503 ? 1.1668 1.7370 1.2213 -0.1725 -0.0791 0.1614  606  TYR A CZ    
3676 O  OH    . TYR A 503 ? 1.1660 1.7782 1.2378 -0.1611 -0.0758 0.1776  606  TYR A OH    
3677 N  N     . PRO A 504 ? 1.2211 1.5795 1.1985 -0.2349 -0.0896 0.1036  607  PRO A N     
3678 C  CA    . PRO A 504 ? 1.1650 1.4751 1.1332 -0.2425 -0.0946 0.0958  607  PRO A CA    
3679 C  C     . PRO A 504 ? 1.1888 1.4989 1.1631 -0.2578 -0.0938 0.0827  607  PRO A C     
3680 O  O     . PRO A 504 ? 1.4941 1.7642 1.4655 -0.2631 -0.0971 0.0770  607  PRO A O     
3681 C  CB    . PRO A 504 ? 1.4976 1.7958 1.4483 -0.2509 -0.0908 0.0983  607  PRO A CB    
3682 C  CG    . PRO A 504 ? 1.2459 1.5966 1.2027 -0.2575 -0.0822 0.1007  607  PRO A CG    
3683 C  CD    . PRO A 504 ? 1.1453 1.5318 1.1184 -0.2432 -0.0821 0.1078  607  PRO A CD    
3684 N  N     . ASP A 505 ? 1.1883 1.5402 1.1703 -0.2655 -0.0892 0.0784  608  ASP A N     
3685 C  CA    . ASP A 505 ? 1.2049 1.5552 1.1882 -0.2830 -0.0857 0.0644  608  ASP A CA    
3686 C  C     . ASP A 505 ? 1.1861 1.5062 1.1805 -0.2753 -0.0878 0.0588  608  ASP A C     
3687 O  O     . ASP A 505 ? 1.3189 1.6459 1.3229 -0.2599 -0.0907 0.0645  608  ASP A O     
3688 C  CB    . ASP A 505 ? 1.1166 1.5198 1.1017 -0.2951 -0.0813 0.0622  608  ASP A CB    
3689 C  CG    . ASP A 505 ? 1.4364 1.8375 1.4156 -0.3185 -0.0755 0.0464  608  ASP A CG    
3690 O  OD1   . ASP A 505 ? 1.5381 1.9157 1.5216 -0.3194 -0.0729 0.0367  608  ASP A OD1   
3691 O  OD2   . ASP A 505 ? 1.8393 2.2611 1.8101 -0.3367 -0.0723 0.0433  608  ASP A OD2   
3692 N  N     . PRO A 506 ? 1.1197 1.4055 1.1152 -0.2854 -0.0855 0.0483  609  PRO A N     
3693 C  CA    . PRO A 506 ? 1.3398 1.5967 1.3513 -0.2776 -0.0859 0.0437  609  PRO A CA    
3694 C  C     . PRO A 506 ? 1.3124 1.5953 1.3311 -0.2803 -0.0789 0.0363  609  PRO A C     
3695 O  O     . PRO A 506 ? 1.5912 1.8632 1.6246 -0.2672 -0.0801 0.0377  609  PRO A O     
3696 C  CB    . PRO A 506 ? 1.1852 1.4031 1.1974 -0.2900 -0.0825 0.0347  609  PRO A CB    
3697 C  CG    . PRO A 506 ? 1.1730 1.4104 1.1676 -0.3098 -0.0766 0.0292  609  PRO A CG    
3698 C  CD    . PRO A 506 ? 1.1844 1.4542 1.1689 -0.3036 -0.0815 0.0410  609  PRO A CD    
3699 N  N     . MET A 507 ? 1.3661 1.6825 1.3738 -0.2983 -0.0718 0.0289  610  MET A N     
3700 C  CA    . MET A 507 ? 1.1377 1.4791 1.1466 -0.3032 -0.0657 0.0226  610  MET A CA    
3701 C  C     . MET A 507 ? 1.1546 1.5279 1.1683 -0.2863 -0.0720 0.0359  610  MET A C     
3702 O  O     . MET A 507 ? 1.3887 1.7677 1.4087 -0.2813 -0.0692 0.0340  610  MET A O     
3703 C  CB    . MET A 507 ? 1.2099 1.5797 1.2021 -0.3295 -0.0587 0.0125  610  MET A CB    
3704 C  CG    . MET A 507 ? 1.5322 1.8687 1.5189 -0.3483 -0.0491 -0.0033 610  MET A CG    
3705 S  SD    . MET A 507 ? 1.7474 2.0444 1.7464 -0.3483 -0.0364 -0.0180 610  MET A SD    
3706 C  CE    . MET A 507 ? 1.9215 2.1759 1.9173 -0.3664 -0.0260 -0.0318 610  MET A CE    
3707 N  N     . VAL A 508 ? 1.3273 1.7198 1.3383 -0.2775 -0.0788 0.0494  611  VAL A N     
3708 C  CA    . VAL A 508 ? 1.2955 1.7138 1.3130 -0.2594 -0.0834 0.0632  611  VAL A CA    
3709 C  C     . VAL A 508 ? 1.2978 1.6809 1.3271 -0.2386 -0.0876 0.0677  611  VAL A C     
3710 O  O     . VAL A 508 ? 1.3812 1.7733 1.4190 -0.2269 -0.0879 0.0716  611  VAL A O     
3711 C  CB    . VAL A 508 ? 1.1283 1.5748 1.1418 -0.2561 -0.0864 0.0761  611  VAL A CB    
3712 C  CG1   . VAL A 508 ? 1.1102 1.5744 1.1324 -0.2346 -0.0895 0.0912  611  VAL A CG1   
3713 C  CG2   . VAL A 508 ? 1.1263 1.6161 1.1328 -0.2767 -0.0837 0.0741  611  VAL A CG2   
3714 N  N     . ARG A 509 ? 1.3894 1.7319 1.4190 -0.2347 -0.0917 0.0678  612  ARG A N     
3715 C  CA    . ARG A 509 ? 1.0984 1.4071 1.1391 -0.2172 -0.0980 0.0731  612  ARG A CA    
3716 C  C     . ARG A 509 ? 1.2067 1.4973 1.2636 -0.2169 -0.0945 0.0641  612  ARG A C     
3717 O  O     . ARG A 509 ? 1.5204 1.8011 1.5904 -0.2020 -0.0978 0.0691  612  ARG A O     
3718 C  CB    . ARG A 509 ? 1.2493 1.5192 1.2839 -0.2163 -0.1049 0.0765  612  ARG A CB    
3719 C  CG    . ARG A 509 ? 1.1013 1.3818 1.1200 -0.2129 -0.1071 0.0866  612  ARG A CG    
3720 C  CD    . ARG A 509 ? 1.1267 1.3644 1.1349 -0.2131 -0.1142 0.0902  612  ARG A CD    
3721 N  NE    . ARG A 509 ? 1.1914 1.4311 1.1846 -0.2053 -0.1154 0.1009  612  ARG A NE    
3722 C  CZ    . ARG A 509 ? 1.1158 1.3413 1.1079 -0.1903 -0.1205 0.1096  612  ARG A CZ    
3723 N  NH1   . ARG A 509 ? 1.1127 1.3222 1.1193 -0.1811 -0.1269 0.1099  612  ARG A NH1   
3724 N  NH2   . ARG A 509 ? 1.6710 1.8972 1.6472 -0.1850 -0.1180 0.1178  612  ARG A NH2   
3725 N  N     . GLY A 510 ? 1.3856 1.6702 1.4425 -0.2335 -0.0861 0.0507  613  GLY A N     
3726 C  CA    . GLY A 510 ? 1.4133 1.6811 1.4865 -0.2341 -0.0787 0.0411  613  GLY A CA    
3727 C  C     . GLY A 510 ? 1.3174 1.6151 1.3918 -0.2305 -0.0736 0.0409  613  GLY A C     
3728 O  O     . GLY A 510 ? 1.3399 1.6230 1.4308 -0.2229 -0.0697 0.0381  613  GLY A O     
3729 N  N     . PHE A 511 ? 1.4417 1.7819 1.5001 -0.2360 -0.0738 0.0449  614  PHE A N     
3730 C  CA    . PHE A 511 ? 1.4181 1.7887 1.4757 -0.2325 -0.0709 0.0475  614  PHE A CA    
3731 C  C     . PHE A 511 ? 1.2322 1.5996 1.3024 -0.2087 -0.0779 0.0608  614  PHE A C     
3732 O  O     . PHE A 511 ? 1.6350 2.0031 1.7141 -0.2017 -0.0742 0.0604  614  PHE A O     
3733 C  CB    . PHE A 511 ? 1.1938 1.6124 1.2339 -0.2446 -0.0716 0.0516  614  PHE A CB    
3734 C  CG    . PHE A 511 ? 0.9763 1.4295 1.0149 -0.2400 -0.0714 0.0587  614  PHE A CG    
3735 C  CD1   . PHE A 511 ? 1.1135 1.5741 1.1442 -0.2538 -0.0629 0.0484  614  PHE A CD1   
3736 C  CD2   . PHE A 511 ? 0.9255 1.4018 0.9691 -0.2225 -0.0786 0.0761  614  PHE A CD2   
3737 C  CE1   . PHE A 511 ? 1.4375 1.9290 1.4644 -0.2506 -0.0635 0.0561  614  PHE A CE1   
3738 C  CE2   . PHE A 511 ? 1.0288 1.5363 1.0721 -0.2177 -0.0787 0.0843  614  PHE A CE2   
3739 C  CZ    . PHE A 511 ? 1.2020 1.7177 1.2364 -0.2320 -0.0721 0.0748  614  PHE A CZ    
3740 N  N     . ALA A 512 ? 1.0614 1.4237 1.1307 -0.1973 -0.0868 0.0722  615  ALA A N     
3741 C  CA    . ALA A 512 ? 1.0308 1.3880 1.1087 -0.1764 -0.0927 0.0845  615  ALA A CA    
3742 C  C     . ALA A 512 ? 1.0159 1.3336 1.1119 -0.1674 -0.0947 0.0815  615  ALA A C     
3743 O  O     . ALA A 512 ? 1.3687 1.6858 1.4752 -0.1541 -0.0955 0.0868  615  ALA A O     
3744 C  CB    . ALA A 512 ? 1.3005 1.6557 1.3695 -0.1689 -0.0995 0.0955  615  ALA A CB    
3745 N  N     . VAL A 513 ? 1.1240 1.4091 1.2264 -0.1746 -0.0955 0.0740  616  VAL A N     
3746 C  CA    . VAL A 513 ? 1.1961 1.4455 1.3217 -0.1668 -0.0979 0.0727  616  VAL A CA    
3747 C  C     . VAL A 513 ? 1.3456 1.6010 1.4852 -0.1683 -0.0862 0.0639  616  VAL A C     
3748 O  O     . VAL A 513 ? 1.4859 1.7298 1.6444 -0.1562 -0.0872 0.0673  616  VAL A O     
3749 C  CB    . VAL A 513 ? 1.3802 1.5949 1.5117 -0.1747 -0.1012 0.0685  616  VAL A CB    
3750 C  CG1   . VAL A 513 ? 1.2501 1.4309 1.4117 -0.1667 -0.1040 0.0690  616  VAL A CG1   
3751 C  CG2   . VAL A 513 ? 1.1815 1.3872 1.2958 -0.1735 -0.1126 0.0778  616  VAL A CG2   
3752 N  N     . ARG A 514 ? 1.2144 1.4870 1.3432 -0.1846 -0.0743 0.0523  617  ARG A N     
3753 C  CA    . ARG A 514 ? 1.1436 1.4208 1.2795 -0.1889 -0.0608 0.0427  617  ARG A CA    
3754 C  C     . ARG A 514 ? 1.0581 1.3640 1.1894 -0.1791 -0.0614 0.0508  617  ARG A C     
3755 O  O     . ARG A 514 ? 1.2959 1.6004 1.4361 -0.1782 -0.0516 0.0456  617  ARG A O     
3756 C  CB    . ARG A 514 ? 1.2323 1.5201 1.3510 -0.2117 -0.0481 0.0280  617  ARG A CB    
3757 C  CG    . ARG A 514 ? 1.3591 1.6140 1.4853 -0.2222 -0.0431 0.0179  617  ARG A CG    
3758 C  CD    . ARG A 514 ? 1.1024 1.3641 1.2103 -0.2463 -0.0276 0.0013  617  ARG A CD    
3759 N  NE    . ARG A 514 ? 1.3538 1.6538 1.4324 -0.2589 -0.0324 0.0035  617  ARG A NE    
3760 C  CZ    . ARG A 514 ? 1.6902 1.9925 1.7568 -0.2687 -0.0373 0.0035  617  ARG A CZ    
3761 N  NH1   . ARG A 514 ? 1.6093 1.8766 1.6874 -0.2677 -0.0385 0.0015  617  ARG A NH1   
3762 N  NH2   . ARG A 514 ? 1.5710 1.9122 1.6151 -0.2801 -0.0413 0.0067  617  ARG A NH2   
3763 N  N     . CYS A 515 ? 1.1810 1.5116 1.2996 -0.1716 -0.0710 0.0636  618  CYS A N     
3764 C  CA    . CYS A 515 ? 1.2909 1.6449 1.4085 -0.1593 -0.0723 0.0739  618  CYS A CA    
3765 C  C     . CYS A 515 ? 1.2711 1.6018 1.4067 -0.1394 -0.0794 0.0831  618  CYS A C     
3766 O  O     . CYS A 515 ? 1.2798 1.6222 1.4190 -0.1286 -0.0783 0.0899  618  CYS A O     
3767 C  CB    . CYS A 515 ? 1.1307 1.5228 1.2302 -0.1596 -0.0775 0.0848  618  CYS A CB    
3768 S  SG    . CYS A 515 ? 1.2883 1.7203 1.3665 -0.1833 -0.0711 0.0780  618  CYS A SG    
3769 N  N     . LEU A 516 ? 1.2498 1.5476 1.3957 -0.1356 -0.0873 0.0839  619  LEU A N     
3770 C  CA    . LEU A 516 ? 1.3551 1.6282 1.5174 -0.1199 -0.0958 0.0923  619  LEU A CA    
3771 C  C     . LEU A 516 ? 1.2571 1.5062 1.4475 -0.1183 -0.0909 0.0857  619  LEU A C     
3772 O  O     . LEU A 516 ? 1.5254 1.7724 1.7296 -0.1073 -0.0904 0.0900  619  LEU A O     
3773 C  CB    . LEU A 516 ? 1.3425 1.5917 1.4996 -0.1182 -0.1086 0.0984  619  LEU A CB    
3774 C  CG    . LEU A 516 ? 1.1695 1.4371 1.3015 -0.1177 -0.1121 0.1060  619  LEU A CG    
3775 C  CD1   . LEU A 516 ? 1.1799 1.4171 1.3047 -0.1173 -0.1236 0.1111  619  LEU A CD1   
3776 C  CD2   . LEU A 516 ? 1.1822 1.4716 1.3094 -0.1048 -0.1106 0.1160  619  LEU A CD2   
3777 N  N     . GLU A 517 ? 1.4035 1.6341 1.6046 -0.1289 -0.0860 0.0755  620  GLU A N     
3778 C  CA    . GLU A 517 ? 1.5186 1.7259 1.7516 -0.1273 -0.0789 0.0695  620  GLU A CA    
3779 C  C     . GLU A 517 ? 1.5640 1.7874 1.7987 -0.1305 -0.0616 0.0609  620  GLU A C     
3780 O  O     . GLU A 517 ? 1.9378 2.1430 2.2001 -0.1289 -0.0521 0.0551  620  GLU A O     
3781 C  CB    . GLU A 517 ? 1.6637 1.8462 1.9086 -0.1377 -0.0759 0.0614  620  GLU A CB    
3782 C  CG    . GLU A 517 ? 1.4546 1.6517 1.6748 -0.1554 -0.0651 0.0497  620  GLU A CG    
3783 C  CD    . GLU A 517 ? 1.5170 1.6865 1.7471 -0.1648 -0.0635 0.0435  620  GLU A CD    
3784 O  OE1   . GLU A 517 ? 1.7883 1.9281 2.0481 -0.1572 -0.0700 0.0488  620  GLU A OE1   
3785 O  OE2   . GLU A 517 ? 1.5915 1.7694 1.8007 -0.1804 -0.0561 0.0342  620  GLU A OE2   
3786 N  N     . LYS A 518 ? 1.2800 1.5367 1.4871 -0.1353 -0.0573 0.0606  621  LYS A N     
3787 C  CA    . LYS A 518 ? 1.3852 1.6581 1.5878 -0.1395 -0.0426 0.0543  621  LYS A CA    
3788 C  C     . LYS A 518 ? 1.2776 1.5741 1.4719 -0.1275 -0.0469 0.0661  621  LYS A C     
3789 O  O     . LYS A 518 ? 1.6152 1.9198 1.8099 -0.1281 -0.0358 0.0631  621  LYS A O     
3790 C  CB    . LYS A 518 ? 1.2784 1.5710 1.4537 -0.1602 -0.0320 0.0429  621  LYS A CB    
3791 C  CG    . LYS A 518 ? 1.4547 1.7222 1.6373 -0.1744 -0.0215 0.0279  621  LYS A CG    
3792 C  CD    . LYS A 518 ? 1.8679 2.1552 2.0188 -0.1971 -0.0118 0.0167  621  LYS A CD    
3793 C  CE    . LYS A 518 ? 1.7734 2.0818 1.9073 -0.2044 -0.0003 0.0127  621  LYS A CE    
3794 N  NZ    . LYS A 518 ? 1.8788 2.2076 1.9784 -0.2292 0.0069  0.0026  621  LYS A NZ    
3795 N  N     . TYR A 519 ? 1.0405 1.3463 1.2265 -0.1171 -0.0609 0.0795  622  TYR A N     
3796 C  CA    . TYR A 519 ? 1.0241 1.3518 1.2025 -0.1053 -0.0635 0.0915  622  TYR A CA    
3797 C  C     . TYR A 519 ? 1.0689 1.3826 1.2549 -0.0887 -0.0761 0.1042  622  TYR A C     
3798 O  O     . TYR A 519 ? 1.4881 1.8138 1.6717 -0.0774 -0.0765 0.1140  622  TYR A O     
3799 C  CB    . TYR A 519 ? 1.0737 1.4406 1.2248 -0.1126 -0.0635 0.0961  622  TYR A CB    
3800 C  CG    . TYR A 519 ? 1.2552 1.6389 1.3920 -0.1317 -0.0522 0.0846  622  TYR A CG    
3801 C  CD1   . TYR A 519 ? 1.2194 1.6184 1.3501 -0.1343 -0.0431 0.0840  622  TYR A CD1   
3802 C  CD2   . TYR A 519 ? 1.3292 1.7114 1.4560 -0.1488 -0.0503 0.0741  622  TYR A CD2   
3803 C  CE1   . TYR A 519 ? 1.3976 1.8093 1.5100 -0.1546 -0.0326 0.0729  622  TYR A CE1   
3804 C  CE2   . TYR A 519 ? 1.5008 1.8957 1.6110 -0.1688 -0.0395 0.0625  622  TYR A CE2   
3805 C  CZ    . TYR A 519 ? 1.3949 1.8042 1.4967 -0.1722 -0.0308 0.0618  622  TYR A CZ    
3806 O  OH    . TYR A 519 ? 1.3554 1.7748 1.4354 -0.1947 -0.0199 0.0498  622  TYR A OH    
3807 N  N     . LEU A 520 ? 1.0660 1.3534 1.2591 -0.0877 -0.0860 0.1048  623  LEU A N     
3808 C  CA    . LEU A 520 ? 1.2349 1.5055 1.4297 -0.0752 -0.0981 0.1161  623  LEU A CA    
3809 C  C     . LEU A 520 ? 1.3649 1.6081 1.5876 -0.0677 -0.1011 0.1167  623  LEU A C     
3810 O  O     . LEU A 520 ? 1.2975 1.5196 1.5414 -0.0729 -0.1015 0.1102  623  LEU A O     
3811 C  CB    . LEU A 520 ? 1.1891 1.4447 1.3729 -0.0800 -0.1084 0.1175  623  LEU A CB    
3812 C  CG    . LEU A 520 ? 0.9627 1.1961 1.1412 -0.0708 -0.1209 0.1281  623  LEU A CG    
3813 C  CD1   . LEU A 520 ? 0.9405 1.1947 1.1008 -0.0615 -0.1180 0.1375  623  LEU A CD1   
3814 C  CD2   . LEU A 520 ? 0.9793 1.1925 1.1474 -0.0788 -0.1303 0.1277  623  LEU A CD2   
3815 N  N     . THR A 521 ? 1.3904 1.6341 1.6155 -0.0557 -0.1028 0.1252  624  THR A N     
3816 C  CA    . THR A 521 ? 1.4469 1.6669 1.6993 -0.0489 -0.1065 0.1272  624  THR A CA    
3817 C  C     . THR A 521 ? 1.4340 1.6240 1.6894 -0.0470 -0.1239 0.1340  624  THR A C     
3818 O  O     . THR A 521 ? 1.2464 1.4337 1.4779 -0.0486 -0.1313 0.1383  624  THR A O     
3819 C  CB    . THR A 521 ? 1.3075 1.5385 1.5599 -0.0380 -0.1010 0.1335  624  THR A CB    
3820 O  OG1   . THR A 521 ? 1.0598 1.2951 1.2891 -0.0307 -0.1068 0.1436  624  THR A OG1   
3821 C  CG2   . THR A 521 ? 1.2018 1.4616 1.4481 -0.0413 -0.0852 0.1282  624  THR A CG2   
3822 N  N     . ASP A 522 ? 1.4904 1.6575 1.7760 -0.0447 -0.1302 0.1355  625  ASP A N     
3823 C  CA    . ASP A 522 ? 1.3183 1.4561 1.6077 -0.0449 -0.1491 0.1435  625  ASP A CA    
3824 C  C     . ASP A 522 ? 1.2305 1.3626 1.4966 -0.0381 -0.1562 0.1528  625  ASP A C     
3825 O  O     . ASP A 522 ? 1.2105 1.3199 1.4635 -0.0411 -0.1711 0.1589  625  ASP A O     
3826 C  CB    . ASP A 522 ? 1.5039 1.6222 1.8361 -0.0442 -0.1549 0.1448  625  ASP A CB    
3827 C  CG    . ASP A 522 ? 1.6504 1.7661 2.0076 -0.0513 -0.1483 0.1365  625  ASP A CG    
3828 O  OD1   . ASP A 522 ? 1.4722 1.5997 1.8098 -0.0580 -0.1402 0.1290  625  ASP A OD1   
3829 O  OD2   . ASP A 522 ? 1.5493 1.6508 1.9471 -0.0503 -0.1504 0.1378  625  ASP A OD2   
3830 N  N     . ASP A 523 ? 1.2466 1.3970 1.5059 -0.0298 -0.1451 0.1541  626  ASP A N     
3831 C  CA    . ASP A 523 ? 1.2686 1.4132 1.5044 -0.0230 -0.1481 0.1624  626  ASP A CA    
3832 C  C     . ASP A 523 ? 1.2835 1.4361 1.4849 -0.0250 -0.1465 0.1639  626  ASP A C     
3833 O  O     . ASP A 523 ? 1.2455 1.3767 1.4263 -0.0263 -0.1553 0.1690  626  ASP A O     
3834 C  CB    . ASP A 523 ? 1.2530 1.4152 1.4931 -0.0130 -0.1353 0.1644  626  ASP A CB    
3835 C  CG    . ASP A 523 ? 1.3302 1.4910 1.5439 -0.0052 -0.1332 0.1725  626  ASP A CG    
3836 O  OD1   . ASP A 523 ? 1.6231 1.7555 1.8279 -0.0057 -0.1440 0.1773  626  ASP A OD1   
3837 O  OD2   . ASP A 523 ? 1.0803 1.2674 1.2821 0.0009  -0.1206 0.1747  626  ASP A OD2   
3838 N  N     . LYS A 524 ? 1.3408 1.5239 1.5351 -0.0265 -0.1350 0.1596  627  LYS A N     
3839 C  CA    . LYS A 524 ? 1.3278 1.5223 1.4945 -0.0288 -0.1326 0.1614  627  LYS A CA    
3840 C  C     . LYS A 524 ? 1.3504 1.5248 1.5095 -0.0397 -0.1432 0.1584  627  LYS A C     
3841 O  O     . LYS A 524 ? 1.3197 1.4889 1.4541 -0.0417 -0.1448 0.1616  627  LYS A O     
3842 C  CB    . LYS A 524 ? 1.2068 1.4414 1.3707 -0.0297 -0.1196 0.1586  627  LYS A CB    
3843 C  CG    . LYS A 524 ? 1.1926 1.4492 1.3632 -0.0202 -0.1093 0.1627  627  LYS A CG    
3844 C  CD    . LYS A 524 ? 1.1919 1.4589 1.3458 -0.0095 -0.1042 0.1737  627  LYS A CD    
3845 C  CE    . LYS A 524 ? 1.2405 1.4778 1.3947 -0.0006 -0.1077 0.1793  627  LYS A CE    
3846 N  NZ    . LYS A 524 ? 1.5333 1.7784 1.6725 0.0104  -0.0992 0.1897  627  LYS A NZ    
3847 N  N     . LEU A 525 ? 1.2698 1.4319 1.4507 -0.0466 -0.1494 0.1527  628  LEU A N     
3848 C  CA    . LEU A 525 ? 1.3006 1.4413 1.4763 -0.0568 -0.1604 0.1514  628  LEU A CA    
3849 C  C     . LEU A 525 ? 1.2892 1.3957 1.4513 -0.0573 -0.1756 0.1595  628  LEU A C     
3850 O  O     . LEU A 525 ? 1.3914 1.4853 1.5273 -0.0633 -0.1806 0.1615  628  LEU A O     
3851 C  CB    . LEU A 525 ? 1.0324 1.1662 1.2395 -0.0626 -0.1622 0.1450  628  LEU A CB    
3852 C  CG    . LEU A 525 ? 0.9639 1.0718 1.1723 -0.0723 -0.1751 0.1456  628  LEU A CG    
3853 C  CD1   . LEU A 525 ? 1.2472 1.3628 1.4249 -0.0798 -0.1722 0.1432  628  LEU A CD1   
3854 C  CD2   . LEU A 525 ? 1.0528 1.1563 1.2967 -0.0763 -0.1725 0.1395  628  LEU A CD2   
3855 N  N     . SER A 526 ? 1.4059 1.4961 1.5839 -0.0525 -0.1830 0.1642  629  SER A N     
3856 C  CA    . SER A 526 ? 1.2801 1.3379 1.4405 -0.0548 -0.1975 0.1721  629  SER A CA    
3857 C  C     . SER A 526 ? 1.2112 1.2703 1.3352 -0.0504 -0.1890 0.1750  629  SER A C     
3858 O  O     . SER A 526 ? 1.3203 1.3513 1.4169 -0.0560 -0.1977 0.1794  629  SER A O     
3859 C  CB    . SER A 526 ? 1.2363 1.2801 1.4234 -0.0513 -0.2064 0.1766  629  SER A CB    
3860 O  OG    . SER A 526 ? 1.5677 1.5777 1.7376 -0.0573 -0.2236 0.1844  629  SER A OG    
3861 N  N     . GLN A 527 ? 1.2765 1.3668 1.3998 -0.0411 -0.1717 0.1733  630  GLN A N     
3862 C  CA    . GLN A 527 ? 1.3882 1.4831 1.4824 -0.0355 -0.1609 0.1771  630  GLN A CA    
3863 C  C     . GLN A 527 ? 1.4384 1.5367 1.5091 -0.0425 -0.1579 0.1755  630  GLN A C     
3864 O  O     . GLN A 527 ? 1.2673 1.3464 1.3090 -0.0441 -0.1565 0.1788  630  GLN A O     
3865 C  CB    . GLN A 527 ? 1.4080 1.5379 1.5128 -0.0235 -0.1445 0.1782  630  GLN A CB    
3866 C  CG    . GLN A 527 ? 1.3556 1.4943 1.4377 -0.0154 -0.1311 0.1840  630  GLN A CG    
3867 C  CD    . GLN A 527 ? 1.5174 1.6335 1.5919 -0.0077 -0.1289 0.1895  630  GLN A CD    
3868 O  OE1   . GLN A 527 ? 1.4311 1.5266 1.4797 -0.0071 -0.1246 0.1929  630  GLN A OE1   
3869 N  NE2   . GLN A 527 ? 1.6056 1.7241 1.7020 -0.0025 -0.1302 0.1899  630  GLN A NE2   
3870 N  N     . TYR A 528 ? 1.3198 1.4409 1.4018 -0.0475 -0.1557 0.1699  631  TYR A N     
3871 C  CA    . TYR A 528 ? 1.4290 1.5581 1.4922 -0.0547 -0.1518 0.1679  631  TYR A CA    
3872 C  C     . TYR A 528 ? 1.3411 1.4427 1.3995 -0.0678 -0.1658 0.1652  631  TYR A C     
3873 O  O     . TYR A 528 ? 1.1822 1.2926 1.2319 -0.0756 -0.1631 0.1617  631  TYR A O     
3874 C  CB    . TYR A 528 ? 1.1318 1.3048 1.2071 -0.0540 -0.1400 0.1638  631  TYR A CB    
3875 C  CG    . TYR A 528 ? 1.0890 1.2926 1.1710 -0.0419 -0.1275 0.1684  631  TYR A CG    
3876 C  CD1   . TYR A 528 ? 1.2420 1.4401 1.3105 -0.0319 -0.1210 0.1764  631  TYR A CD1   
3877 C  CD2   . TYR A 528 ? 1.0655 1.3017 1.1662 -0.0411 -0.1216 0.1651  631  TYR A CD2   
3878 C  CE1   . TYR A 528 ? 1.2350 1.4607 1.3117 -0.0200 -0.1097 0.1824  631  TYR A CE1   
3879 C  CE2   . TYR A 528 ? 1.0496 1.3137 1.1553 -0.0307 -0.1116 0.1711  631  TYR A CE2   
3880 C  CZ    . TYR A 528 ? 1.2854 1.5448 1.3808 -0.0195 -0.1061 0.1804  631  TYR A CZ    
3881 O  OH    . TYR A 528 ? 1.1714 1.4582 1.2738 -0.0084 -0.0962 0.1880  631  TYR A OH    
3882 N  N     . LEU A 529 ? 1.2857 1.3549 1.3509 -0.0709 -0.1813 0.1679  632  LEU A N     
3883 C  CA    . LEU A 529 ? 1.1800 1.2242 1.2458 -0.0829 -0.1963 0.1676  632  LEU A CA    
3884 C  C     . LEU A 529 ? 1.2813 1.3032 1.3086 -0.0919 -0.1992 0.1701  632  LEU A C     
3885 O  O     . LEU A 529 ? 1.3892 1.4024 1.4120 -0.1021 -0.2050 0.1684  632  LEU A O     
3886 C  CB    . LEU A 529 ? 1.2301 1.2473 1.3156 -0.0841 -0.2138 0.1727  632  LEU A CB    
3887 C  CG    . LEU A 529 ? 0.9835 0.9767 1.0794 -0.0951 -0.2310 0.1752  632  LEU A CG    
3888 C  CD1   . LEU A 529 ? 1.2805 1.2950 1.4044 -0.0963 -0.2233 0.1675  632  LEU A CD1   
3889 C  CD2   . LEU A 529 ? 1.3845 1.3527 1.5009 -0.0961 -0.2500 0.1833  632  LEU A CD2   
3890 N  N     . ILE A 530 ? 1.4997 1.5103 1.4985 -0.0888 -0.1938 0.1739  633  ILE A N     
3891 C  CA    . ILE A 530 ? 1.5293 1.5146 1.4886 -0.0982 -0.1942 0.1757  633  ILE A CA    
3892 C  C     . ILE A 530 ? 1.5448 1.5561 1.4975 -0.1003 -0.1801 0.1711  633  ILE A C     
3893 O  O     . ILE A 530 ? 1.6424 1.6369 1.5752 -0.1118 -0.1842 0.1705  633  ILE A O     
3894 C  CB    . ILE A 530 ? 1.5467 1.5121 1.4772 -0.0943 -0.1876 0.1796  633  ILE A CB    
3895 C  CG1   . ILE A 530 ? 1.6317 1.5738 1.5192 -0.1035 -0.1814 0.1799  633  ILE A CG1   
3896 C  CG2   . ILE A 530 ? 1.6432 1.6423 1.5884 -0.0784 -0.1689 0.1792  633  ILE A CG2   
3897 C  CD1   . ILE A 530 ? 2.0091 1.9116 1.8750 -0.1206 -0.2011 0.1822  633  ILE A CD1   
3898 N  N     . GLN A 531 ? 1.4833 1.5364 1.4527 -0.0904 -0.1643 0.1686  634  GLN A N     
3899 C  CA    . GLN A 531 ? 1.2783 1.3605 1.2450 -0.0936 -0.1523 0.1651  634  GLN A CA    
3900 C  C     . GLN A 531 ? 1.2628 1.3551 1.2479 -0.1025 -0.1587 0.1589  634  GLN A C     
3901 O  O     . GLN A 531 ? 1.2794 1.3789 1.2546 -0.1114 -0.1546 0.1558  634  GLN A O     
3902 C  CB    . GLN A 531 ? 1.3922 1.5174 1.3714 -0.0814 -0.1353 0.1667  634  GLN A CB    
3903 C  CG    . GLN A 531 ? 1.3396 1.4577 1.3011 -0.0720 -0.1236 0.1731  634  GLN A CG    
3904 C  CD    . GLN A 531 ? 1.1973 1.3012 1.1654 -0.0624 -0.1270 0.1765  634  GLN A CD    
3905 O  OE1   . GLN A 531 ? 1.2721 1.3781 1.2623 -0.0613 -0.1370 0.1745  634  GLN A OE1   
3906 N  NE2   . GLN A 531 ? 1.4478 1.5360 1.3976 -0.0557 -0.1170 0.1814  634  GLN A NE2   
3907 N  N     . LEU A 532 ? 1.4424 1.5344 1.4548 -0.1008 -0.1671 0.1568  635  LEU A N     
3908 C  CA    . LEU A 532 ? 1.3519 1.4493 1.3830 -0.1092 -0.1707 0.1502  635  LEU A CA    
3909 C  C     . LEU A 532 ? 1.4428 1.5020 1.4628 -0.1207 -0.1850 0.1522  635  LEU A C     
3910 O  O     . LEU A 532 ? 1.4873 1.5480 1.5074 -0.1304 -0.1842 0.1476  635  LEU A O     
3911 C  CB    . LEU A 532 ? 1.2259 1.3325 1.2912 -0.1034 -0.1722 0.1473  635  LEU A CB    
3912 C  CG    . LEU A 532 ? 1.2103 1.3595 1.2901 -0.0999 -0.1574 0.1412  635  LEU A CG    
3913 C  CD1   . LEU A 532 ? 1.5048 1.6797 1.5712 -0.0908 -0.1468 0.1461  635  LEU A CD1   
3914 C  CD2   . LEU A 532 ? 1.2875 1.4389 1.3983 -0.0951 -0.1577 0.1381  635  LEU A CD2   
3915 N  N     . VAL A 533 ? 1.4710 1.4950 1.4805 -0.1209 -0.1989 0.1596  636  VAL A N     
3916 C  CA    . VAL A 533 ? 1.4403 1.4268 1.4335 -0.1330 -0.2142 0.1640  636  VAL A CA    
3917 C  C     . VAL A 533 ? 1.3808 1.3624 1.3366 -0.1411 -0.2065 0.1632  636  VAL A C     
3918 O  O     . VAL A 533 ? 1.3551 1.3193 1.3005 -0.1527 -0.2126 0.1633  636  VAL A O     
3919 C  CB    . VAL A 533 ? 1.4051 1.3566 1.3920 -0.1332 -0.2319 0.1732  636  VAL A CB    
3920 C  CG1   . VAL A 533 ? 1.1869 1.0982 1.1419 -0.1473 -0.2468 0.1798  636  VAL A CG1   
3921 C  CG2   . VAL A 533 ? 1.4027 1.3546 1.4327 -0.1286 -0.2427 0.1752  636  VAL A CG2   
3922 N  N     . GLN A 534 ? 1.4816 1.4790 1.4192 -0.1350 -0.1915 0.1627  637  GLN A N     
3923 C  CA    . GLN A 534 ? 1.4103 1.4014 1.3137 -0.1420 -0.1820 0.1626  637  GLN A CA    
3924 C  C     . GLN A 534 ? 1.4613 1.4808 1.3727 -0.1478 -0.1722 0.1562  637  GLN A C     
3925 O  O     . GLN A 534 ? 1.6413 1.6463 1.5294 -0.1589 -0.1708 0.1558  637  GLN A O     
3926 C  CB    . GLN A 534 ? 1.4618 1.4629 1.3498 -0.1323 -0.1663 0.1647  637  GLN A CB    
3927 C  CG    . GLN A 534 ? 1.6977 1.6784 1.5463 -0.1397 -0.1568 0.1661  637  GLN A CG    
3928 C  CD    . GLN A 534 ? 1.6841 1.6106 1.4993 -0.1519 -0.1724 0.1702  637  GLN A CD    
3929 O  OE1   . GLN A 534 ? 1.9938 1.8980 1.7798 -0.1644 -0.1720 0.1702  637  GLN A OE1   
3930 N  NE2   . GLN A 534 ? 1.6260 1.5308 1.4444 -0.1496 -0.1869 0.1743  637  GLN A NE2   
3931 N  N     . VAL A 535 ? 1.4712 1.5300 1.4129 -0.1420 -0.1650 0.1510  638  VAL A N     
3932 C  CA    . VAL A 535 ? 1.2789 1.3662 1.2270 -0.1495 -0.1558 0.1444  638  VAL A CA    
3933 C  C     . VAL A 535 ? 1.5174 1.5871 1.4749 -0.1608 -0.1655 0.1401  638  VAL A C     
3934 O  O     . VAL A 535 ? 1.3463 1.4364 1.3096 -0.1688 -0.1582 0.1333  638  VAL A O     
3935 C  CB    . VAL A 535 ? 1.1380 1.2738 1.1104 -0.1419 -0.1445 0.1406  638  VAL A CB    
3936 C  CG1   . VAL A 535 ? 1.1379 1.2950 1.1034 -0.1306 -0.1330 0.1466  638  VAL A CG1   
3937 C  CG2   . VAL A 535 ? 1.2650 1.4011 1.2651 -0.1362 -0.1512 0.1382  638  VAL A CG2   
3938 N  N     . LEU A 536 ? 1.4521 1.4847 1.4127 -0.1622 -0.1818 0.1446  639  LEU A N     
3939 C  CA    . LEU A 536 ? 1.4263 1.4378 1.3958 -0.1727 -0.1910 0.1431  639  LEU A CA    
3940 C  C     . LEU A 536 ? 1.3145 1.3093 1.2536 -0.1858 -0.1899 0.1436  639  LEU A C     
3941 O  O     . LEU A 536 ? 1.4916 1.4810 1.4370 -0.1956 -0.1904 0.1398  639  LEU A O     
3942 C  CB    . LEU A 536 ? 1.3463 1.3229 1.3284 -0.1709 -0.2104 0.1511  639  LEU A CB    
3943 C  CG    . LEU A 536 ? 1.2721 1.2566 1.2977 -0.1650 -0.2129 0.1484  639  LEU A CG    
3944 C  CD1   . LEU A 536 ? 1.6810 1.7034 1.7222 -0.1541 -0.1990 0.1421  639  LEU A CD1   
3945 C  CD2   . LEU A 536 ? 1.5315 1.4836 1.5703 -0.1626 -0.2331 0.1592  639  LEU A CD2   
3946 N  N     . LYS A 537 ? 1.2991 1.2839 1.2051 -0.1865 -0.1867 0.1480  640  LYS A N     
3947 C  CA    . LYS A 537 ? 1.4178 1.3861 1.2925 -0.1993 -0.1833 0.1484  640  LYS A CA    
3948 C  C     . LYS A 537 ? 1.5061 1.5117 1.3867 -0.2039 -0.1664 0.1400  640  LYS A C     
3949 O  O     . LYS A 537 ? 1.9638 1.9588 1.8304 -0.2166 -0.1645 0.1380  640  LYS A O     
3950 C  CB    . LYS A 537 ? 1.3499 1.2981 1.1876 -0.1989 -0.1802 0.1541  640  LYS A CB    
3951 C  CG    . LYS A 537 ? 1.4842 1.3976 1.3128 -0.1958 -0.1966 0.1621  640  LYS A CG    
3952 C  CD    . LYS A 537 ? 1.7295 1.6253 1.5206 -0.1951 -0.1888 0.1654  640  LYS A CD    
3953 C  CE    . LYS A 537 ? 1.9495 1.8093 1.7285 -0.1948 -0.2060 0.1728  640  LYS A CE    
3954 N  NZ    . LYS A 537 ? 2.1497 1.9881 1.8889 -0.1954 -0.1961 0.1746  640  LYS A NZ    
3955 N  N     . TYR A 538 ? 1.3637 1.4130 1.2642 -0.1949 -0.1547 0.1358  641  TYR A N     
3956 C  CA    . TYR A 538 ? 1.4930 1.5816 1.4004 -0.2007 -0.1405 0.1290  641  TYR A CA    
3957 C  C     . TYR A 538 ? 1.3999 1.4931 1.3262 -0.2102 -0.1425 0.1207  641  TYR A C     
3958 O  O     . TYR A 538 ? 1.6463 1.7648 1.5733 -0.2199 -0.1326 0.1144  641  TYR A O     
3959 C  CB    . TYR A 538 ? 1.5614 1.6954 1.4841 -0.1890 -0.1297 0.1292  641  TYR A CB    
3960 C  CG    . TYR A 538 ? 1.3799 1.5142 1.2856 -0.1800 -0.1220 0.1368  641  TYR A CG    
3961 C  CD1   . TYR A 538 ? 1.4706 1.5780 1.3463 -0.1866 -0.1184 0.1400  641  TYR A CD1   
3962 C  CD2   . TYR A 538 ? 1.5184 1.6777 1.4375 -0.1652 -0.1166 0.1408  641  TYR A CD2   
3963 C  CE1   . TYR A 538 ? 1.8111 1.9154 1.6708 -0.1788 -0.1080 0.1459  641  TYR A CE1   
3964 C  CE2   . TYR A 538 ? 1.7181 1.8754 1.6233 -0.1565 -0.1071 0.1477  641  TYR A CE2   
3965 C  CZ    . TYR A 538 ? 1.7911 1.9203 1.6668 -0.1633 -0.1020 0.1497  641  TYR A CZ    
3966 O  OH    . TYR A 538 ? 2.0411 2.1649 1.9024 -0.1551 -0.0893 0.1556  641  TYR A OH    
3967 N  N     . GLU A 539 ? 1.3990 1.4686 1.3421 -0.2083 -0.1540 0.1206  642  GLU A N     
3968 C  CA    . GLU A 539 ? 1.4139 1.4809 1.3751 -0.2174 -0.1536 0.1127  642  GLU A CA    
3969 C  C     . GLU A 539 ? 1.5859 1.6237 1.5286 -0.2315 -0.1566 0.1133  642  GLU A C     
3970 O  O     . GLU A 539 ? 1.9550 1.9551 1.8814 -0.2325 -0.1686 0.1222  642  GLU A O     
3971 C  CB    . GLU A 539 ? 1.3953 1.4438 1.3840 -0.2100 -0.1635 0.1139  642  GLU A CB    
3972 C  CG    . GLU A 539 ? 1.5277 1.6044 1.5365 -0.1974 -0.1591 0.1120  642  GLU A CG    
3973 C  CD    . GLU A 539 ? 1.6021 1.7176 1.6225 -0.2023 -0.1444 0.1005  642  GLU A CD    
3974 O  OE1   . GLU A 539 ? 1.7421 1.8561 1.7631 -0.2155 -0.1387 0.0925  642  GLU A OE1   
3975 O  OE2   . GLU A 539 ? 1.3224 1.4687 1.3498 -0.1941 -0.1386 0.0999  642  GLU A OE2   
3976 N  N     . GLN A 540 ? 1.5446 1.5990 1.4881 -0.2438 -0.1460 0.1043  643  GLN A N     
3977 C  CA    . GLN A 540 ? 1.5485 1.5778 1.4740 -0.2581 -0.1465 0.1042  643  GLN A CA    
3978 C  C     . GLN A 540 ? 1.3539 1.3441 1.2930 -0.2621 -0.1565 0.1056  643  GLN A C     
3979 O  O     . GLN A 540 ? 1.5359 1.4981 1.4595 -0.2730 -0.1595 0.1082  643  GLN A O     
3980 C  CB    . GLN A 540 ? 1.7299 1.7915 1.6521 -0.2711 -0.1313 0.0939  643  GLN A CB    
3981 C  CG    . GLN A 540 ? 1.7497 1.8398 1.6967 -0.2734 -0.1233 0.0826  643  GLN A CG    
3982 C  CD    . GLN A 540 ? 1.6160 1.7375 1.5569 -0.2893 -0.1102 0.0731  643  GLN A CD    
3983 O  OE1   . GLN A 540 ? 1.6762 1.7959 1.5978 -0.2989 -0.1068 0.0747  643  GLN A OE1   
3984 N  NE2   . GLN A 540 ? 1.5180 1.6680 1.4741 -0.2937 -0.1025 0.0631  643  GLN A NE2   
3985 N  N     . TYR A 541 ? 1.3107 1.2981 1.2800 -0.2533 -0.1609 0.1049  644  TYR A N     
3986 C  CA    . TYR A 541 ? 1.5673 1.5197 1.5575 -0.2550 -0.1692 0.1078  644  TYR A CA    
3987 C  C     . TYR A 541 ? 1.5738 1.5097 1.5837 -0.2412 -0.1843 0.1182  644  TYR A C     
3988 O  O     . TYR A 541 ? 1.7291 1.6848 1.7409 -0.2303 -0.1847 0.1193  644  TYR A O     
3989 C  CB    . TYR A 541 ? 1.5440 1.5082 1.5593 -0.2610 -0.1549 0.0942  644  TYR A CB    
3990 C  CG    . TYR A 541 ? 1.3605 1.3460 1.3576 -0.2763 -0.1397 0.0827  644  TYR A CG    
3991 C  CD1   . TYR A 541 ? 1.4599 1.4251 1.4346 -0.2888 -0.1405 0.0850  644  TYR A CD1   
3992 C  CD2   . TYR A 541 ? 1.6557 1.6815 1.6574 -0.2797 -0.1252 0.0702  644  TYR A CD2   
3993 C  CE1   . TYR A 541 ? 1.4539 1.4394 1.4137 -0.3038 -0.1268 0.0747  644  TYR A CE1   
3994 C  CE2   . TYR A 541 ? 1.6096 1.6567 1.5957 -0.2955 -0.1131 0.0606  644  TYR A CE2   
3995 C  CZ    . TYR A 541 ? 1.4414 1.4687 1.4078 -0.3073 -0.1136 0.0626  644  TYR A CZ    
3996 O  OH    . TYR A 541 ? 1.6446 1.6940 1.5970 -0.3240 -0.1016 0.0532  644  TYR A OH    
3997 N  N     . LEU A 542 ? 1.2889 1.1883 1.3151 -0.2420 -0.1971 0.1270  645  LEU A N     
3998 C  CA    . LEU A 542 ? 1.4535 1.3368 1.5034 -0.2305 -0.2132 0.1384  645  LEU A CA    
3999 C  C     . LEU A 542 ? 1.3975 1.3019 1.4875 -0.2207 -0.2033 0.1302  645  LEU A C     
4000 O  O     . LEU A 542 ? 1.4767 1.3980 1.5732 -0.2099 -0.2050 0.1312  645  LEU A O     
4001 C  CB    . LEU A 542 ? 1.3754 1.2162 1.4359 -0.2348 -0.2306 0.1523  645  LEU A CB    
4002 C  CG    . LEU A 542 ? 1.3550 1.1676 1.3738 -0.2453 -0.2437 0.1631  645  LEU A CG    
4003 C  CD1   . LEU A 542 ? 1.3768 1.1494 1.4116 -0.2496 -0.2616 0.1783  645  LEU A CD1   
4004 C  CD2   . LEU A 542 ? 1.1824 0.9947 1.1706 -0.2415 -0.2542 0.1703  645  LEU A CD2   
4005 N  N     . ASP A 543 ? 1.3865 1.2880 1.5023 -0.2251 -0.1914 0.1216  646  ASP A N     
4006 C  CA    . ASP A 543 ? 1.4630 1.3803 1.6152 -0.2180 -0.1788 0.1124  646  ASP A CA    
4007 C  C     . ASP A 543 ? 1.4640 1.4212 1.6000 -0.2218 -0.1595 0.0962  646  ASP A C     
4008 O  O     . ASP A 543 ? 1.5315 1.4970 1.6499 -0.2347 -0.1474 0.0861  646  ASP A O     
4009 C  CB    . ASP A 543 ? 1.2250 1.1182 1.4113 -0.2219 -0.1718 0.1099  646  ASP A CB    
4010 C  CG    . ASP A 543 ? 1.2999 1.2018 1.5273 -0.2138 -0.1586 0.1021  646  ASP A CG    
4011 O  OD1   . ASP A 543 ? 1.4671 1.3911 1.6979 -0.2044 -0.1586 0.1011  646  ASP A OD1   
4012 O  OD2   . ASP A 543 ? 1.5500 1.4347 1.8062 -0.2171 -0.1467 0.0968  646  ASP A OD2   
4013 N  N     . ASN A 544 ? 1.4505 1.4324 1.5924 -0.2115 -0.1573 0.0947  647  ASN A N     
4014 C  CA    . ASN A 544 ? 1.1684 1.1900 1.2970 -0.2144 -0.1415 0.0822  647  ASN A CA    
4015 C  C     . ASN A 544 ? 1.4613 1.4982 1.6137 -0.2027 -0.1372 0.0801  647  ASN A C     
4016 O  O     . ASN A 544 ? 1.6544 1.6716 1.8352 -0.1928 -0.1453 0.0875  647  ASN A O     
4017 C  CB    . ASN A 544 ? 1.2578 1.3004 1.3498 -0.2157 -0.1450 0.0861  647  ASN A CB    
4018 C  CG    . ASN A 544 ? 1.1477 1.1806 1.2328 -0.2034 -0.1607 0.1000  647  ASN A CG    
4019 O  OD1   . ASN A 544 ? 1.2384 1.2880 1.3312 -0.1923 -0.1607 0.1017  647  ASN A OD1   
4020 N  ND2   . ASN A 544 ? 1.6192 1.6231 1.6871 -0.2067 -0.1739 0.1100  647  ASN A ND2   
4021 N  N     . LEU A 545 ? 1.3128 1.3861 1.4541 -0.2046 -0.1247 0.0709  648  LEU A N     
4022 C  CA    . LEU A 545 ? 0.9949 1.0837 1.1553 -0.1952 -0.1183 0.0679  648  LEU A CA    
4023 C  C     . LEU A 545 ? 1.2551 1.3471 1.4153 -0.1798 -0.1315 0.0807  648  LEU A C     
4024 O  O     . LEU A 545 ? 1.1662 1.2526 1.3519 -0.1695 -0.1330 0.0834  648  LEU A O     
4025 C  CB    . LEU A 545 ? 1.0350 1.1612 1.1804 -0.2039 -0.1023 0.0556  648  LEU A CB    
4026 C  CG    . LEU A 545 ? 0.9747 1.0977 1.1300 -0.2169 -0.0841 0.0395  648  LEU A CG    
4027 C  CD1   . LEU A 545 ? 1.9173 2.0212 2.1083 -0.2080 -0.0783 0.0376  648  LEU A CD1   
4028 C  CD2   . LEU A 545 ? 1.4988 1.5995 1.6488 -0.2307 -0.0813 0.0345  648  LEU A CD2   
4029 N  N     . LEU A 546 ? 1.1551 1.2551 1.2871 -0.1787 -0.1397 0.0883  649  LEU A N     
4030 C  CA    . LEU A 546 ? 1.0903 1.1913 1.2180 -0.1653 -0.1501 0.0994  649  LEU A CA    
4031 C  C     . LEU A 546 ? 1.3796 1.4433 1.5240 -0.1593 -0.1666 0.1100  649  LEU A C     
4032 O  O     . LEU A 546 ? 1.4126 1.4736 1.5697 -0.1483 -0.1730 0.1164  649  LEU A O     
4033 C  CB    . LEU A 546 ? 1.1539 1.2681 1.2475 -0.1665 -0.1519 0.1044  649  LEU A CB    
4034 C  CG    . LEU A 546 ? 1.2456 1.3580 1.3292 -0.1541 -0.1598 0.1152  649  LEU A CG    
4035 C  CD1   . LEU A 546 ? 1.0617 1.1971 1.1619 -0.1430 -0.1537 0.1142  649  LEU A CD1   
4036 C  CD2   . LEU A 546 ? 1.0158 1.1407 1.0677 -0.1562 -0.1567 0.1188  649  LEU A CD2   
4037 N  N     . VAL A 547 ? 1.5518 1.5866 1.6968 -0.1672 -0.1745 0.1130  650  VAL A N     
4038 C  CA    . VAL A 547 ? 1.2743 1.2746 1.4368 -0.1633 -0.1927 0.1254  650  VAL A CA    
4039 C  C     . VAL A 547 ? 1.2830 1.2779 1.4919 -0.1571 -0.1896 0.1238  650  VAL A C     
4040 O  O     . VAL A 547 ? 1.2512 1.2352 1.4811 -0.1483 -0.2015 0.1333  650  VAL A O     
4041 C  CB    . VAL A 547 ? 1.3697 1.3409 1.5192 -0.1741 -0.2024 0.1308  650  VAL A CB    
4042 C  CG1   . VAL A 547 ? 1.2977 1.2343 1.4700 -0.1713 -0.2229 0.1454  650  VAL A CG1   
4043 C  CG2   . VAL A 547 ? 1.5866 1.5597 1.6901 -0.1796 -0.2053 0.1336  650  VAL A CG2   
4044 N  N     . ARG A 548 ? 1.3288 1.3306 1.5546 -0.1625 -0.1724 0.1114  651  ARG A N     
4045 C  CA    . ARG A 548 ? 1.4874 1.4833 1.7581 -0.1570 -0.1647 0.1083  651  ARG A CA    
4046 C  C     . ARG A 548 ? 1.4659 1.4839 1.7460 -0.1465 -0.1591 0.1063  651  ARG A C     
4047 O  O     . ARG A 548 ? 1.2418 1.2513 1.5600 -0.1386 -0.1592 0.1094  651  ARG A O     
4048 C  CB    . ARG A 548 ? 1.1637 1.1610 1.4435 -0.1669 -0.1435 0.0930  651  ARG A CB    
4049 C  CG    . ARG A 548 ? 1.1598 1.1292 1.4420 -0.1761 -0.1472 0.0956  651  ARG A CG    
4050 C  CD    . ARG A 548 ? 1.5042 1.4741 1.7930 -0.1869 -0.1234 0.0786  651  ARG A CD    
4051 N  NE    . ARG A 548 ? 1.3616 1.3021 1.6565 -0.1950 -0.1252 0.0813  651  ARG A NE    
4052 C  CZ    . ARG A 548 ? 1.3971 1.3098 1.7345 -0.1922 -0.1221 0.0849  651  ARG A CZ    
4053 N  NH1   . ARG A 548 ? 1.4415 1.3519 1.8208 -0.1817 -0.1163 0.0859  651  ARG A NH1   
4054 N  NH2   . ARG A 548 ? 1.3192 1.2056 1.6591 -0.1999 -0.1239 0.0884  651  ARG A NH2   
4055 N  N     . PHE A 549 ? 1.3256 1.3722 1.5737 -0.1461 -0.1538 0.1021  652  PHE A N     
4056 C  CA    . PHE A 549 ? 1.2719 1.3391 1.5259 -0.1361 -0.1490 0.1015  652  PHE A CA    
4057 C  C     . PHE A 549 ? 1.2801 1.3349 1.5375 -0.1256 -0.1676 0.1161  652  PHE A C     
4058 O  O     . PHE A 549 ? 1.2322 1.2838 1.5186 -0.1170 -0.1688 0.1193  652  PHE A O     
4059 C  CB    . PHE A 549 ? 1.1840 1.2865 1.4050 -0.1391 -0.1380 0.0946  652  PHE A CB    
4060 C  CG    . PHE A 549 ? 1.2860 1.4086 1.5055 -0.1279 -0.1368 0.0982  652  PHE A CG    
4061 C  CD1   . PHE A 549 ? 1.1701 1.3025 1.4119 -0.1238 -0.1248 0.0922  652  PHE A CD1   
4062 C  CD2   . PHE A 549 ? 1.4141 1.5437 1.6093 -0.1217 -0.1458 0.1075  652  PHE A CD2   
4063 C  CE1   . PHE A 549 ? 1.2265 1.3762 1.4663 -0.1137 -0.1235 0.0962  652  PHE A CE1   
4064 C  CE2   . PHE A 549 ? 1.0568 1.2031 1.2514 -0.1111 -0.1436 0.1113  652  PHE A CE2   
4065 C  CZ    . PHE A 549 ? 1.1622 1.3190 1.3791 -0.1070 -0.1332 0.1061  652  PHE A CZ    
4066 N  N     . LEU A 550 ? 1.2230 1.2692 1.4497 -0.1275 -0.1812 0.1244  653  LEU A N     
4067 C  CA    . LEU A 550 ? 1.0755 1.1064 1.2985 -0.1206 -0.1986 0.1374  653  LEU A CA    
4068 C  C     . LEU A 550 ? 1.3471 1.3469 1.6019 -0.1203 -0.2156 0.1478  653  LEU A C     
4069 O  O     . LEU A 550 ? 1.2940 1.2820 1.5548 -0.1151 -0.2301 0.1583  653  LEU A O     
4070 C  CB    . LEU A 550 ? 0.9445 0.9705 1.1229 -0.1247 -0.2061 0.1426  653  LEU A CB    
4071 C  CG    . LEU A 550 ? 1.3532 1.4107 1.5033 -0.1223 -0.1920 0.1370  653  LEU A CG    
4072 C  CD1   . LEU A 550 ? 1.0949 1.1421 1.2053 -0.1259 -0.1981 0.1430  653  LEU A CD1   
4073 C  CD2   . LEU A 550 ? 1.3325 1.4082 1.4941 -0.1105 -0.1862 0.1374  653  LEU A CD2   
4074 N  N     . LEU A 551 ? 1.3836 1.3697 1.6600 -0.1263 -0.2144 0.1461  654  LEU A N     
4075 C  CA    . LEU A 551 ? 1.2714 1.2303 1.5851 -0.1253 -0.2307 0.1583  654  LEU A CA    
4076 C  C     . LEU A 551 ? 1.3580 1.3233 1.7226 -0.1166 -0.2215 0.1559  654  LEU A C     
4077 O  O     . LEU A 551 ? 1.3330 1.2877 1.7257 -0.1109 -0.2359 0.1677  654  LEU A O     
4078 C  CB    . LEU A 551 ? 1.3234 1.2622 1.6412 -0.1347 -0.2332 0.1597  654  LEU A CB    
4079 C  CG    . LEU A 551 ? 1.2361 1.1469 1.5957 -0.1339 -0.2514 0.1752  654  LEU A CG    
4080 C  CD1   . LEU A 551 ? 1.2110 1.1040 1.5537 -0.1351 -0.2799 0.1929  654  LEU A CD1   
4081 C  CD2   . LEU A 551 ? 1.2498 1.1425 1.6167 -0.1421 -0.2492 0.1753  654  LEU A CD2   
4082 N  N     . LYS A 552 ? 1.5008 1.4826 1.8771 -0.1170 -0.1970 0.1407  655  LYS A N     
4083 C  CA    . LYS A 552 ? 1.2808 1.2671 1.7035 -0.1097 -0.1841 0.1367  655  LYS A CA    
4084 C  C     . LYS A 552 ? 1.3201 1.3216 1.7424 -0.1004 -0.1859 0.1392  655  LYS A C     
4085 O  O     . LYS A 552 ? 1.6022 1.5989 2.0662 -0.0931 -0.1878 0.1448  655  LYS A O     
4086 C  CB    . LYS A 552 ? 1.2480 1.2470 1.6726 -0.1148 -0.1557 0.1180  655  LYS A CB    
4087 C  CG    . LYS A 552 ? 1.1628 1.1646 1.6314 -0.1087 -0.1376 0.1116  655  LYS A CG    
4088 C  CD    . LYS A 552 ? 1.7904 1.8011 2.2528 -0.1171 -0.1086 0.0920  655  LYS A CD    
4089 C  CE    . LYS A 552 ? 1.8061 1.7962 2.2751 -0.1263 -0.1039 0.0885  655  LYS A CE    
4090 N  NZ    . LYS A 552 ? 1.7093 1.7049 2.1701 -0.1368 -0.0746 0.0681  655  LYS A NZ    
4091 N  N     . LYS A 553 ? 1.2803 1.3003 1.6584 -0.1003 -0.1846 0.1360  656  LYS A N     
4092 C  CA    . LYS A 553 ? 1.4503 1.4833 1.8259 -0.0913 -0.1855 0.1389  656  LYS A CA    
4093 C  C     . LYS A 553 ? 1.3237 1.3370 1.7033 -0.0882 -0.2105 0.1551  656  LYS A C     
4094 O  O     . LYS A 553 ? 1.4962 1.5109 1.8970 -0.0809 -0.2136 0.1599  656  LYS A O     
4095 C  CB    . LYS A 553 ? 1.5104 1.5689 1.8406 -0.0916 -0.1760 0.1322  656  LYS A CB    
4096 C  CG    . LYS A 553 ? 1.2531 1.3344 1.5883 -0.0838 -0.1619 0.1273  656  LYS A CG    
4097 C  CD    . LYS A 553 ? 1.4971 1.5881 1.8563 -0.0863 -0.1406 0.1145  656  LYS A CD    
4098 C  CE    . LYS A 553 ? 1.5329 1.6462 1.8916 -0.0801 -0.1264 0.1100  656  LYS A CE    
4099 N  NZ    . LYS A 553 ? 2.0650 2.1855 2.4403 -0.0850 -0.1038 0.0964  656  LYS A NZ    
4100 N  N     . ALA A 554 ? 1.5023 1.4960 1.8599 -0.0952 -0.2285 0.1637  657  ALA A N     
4101 C  CA    . ALA A 554 ? 1.4940 1.4654 1.8519 -0.0957 -0.2540 0.1796  657  ALA A CA    
4102 C  C     . ALA A 554 ? 1.2989 1.2538 1.7116 -0.0947 -0.2665 0.1902  657  ALA A C     
4103 O  O     . ALA A 554 ? 1.2970 1.2398 1.7227 -0.0937 -0.2858 0.2032  657  ALA A O     
4104 C  CB    . ALA A 554 ? 1.4878 1.4415 1.8008 -0.1054 -0.2686 0.1854  657  ALA A CB    
4105 N  N     . LEU A 555 ? 1.3142 1.2679 1.7603 -0.0955 -0.2557 0.1856  658  LEU A N     
4106 C  CA    . LEU A 555 ? 1.4477 1.3881 1.9543 -0.0928 -0.2634 0.1959  658  LEU A CA    
4107 C  C     . LEU A 555 ? 1.3426 1.2980 1.8937 -0.0831 -0.2461 0.1899  658  LEU A C     
4108 O  O     . LEU A 555 ? 1.2658 1.2126 1.8736 -0.0794 -0.2501 0.1988  658  LEU A O     
4109 C  CB    . LEU A 555 ? 1.5057 1.4337 2.0300 -0.0979 -0.2578 0.1944  658  LEU A CB    
4110 C  CG    . LEU A 555 ? 1.2555 1.1621 1.7488 -0.1079 -0.2787 0.2048  658  LEU A CG    
4111 C  CD1   . LEU A 555 ? 1.3269 1.2217 1.8414 -0.1121 -0.2696 0.2024  658  LEU A CD1   
4112 C  CD2   . LEU A 555 ? 1.3835 1.2710 1.8881 -0.1099 -0.3116 0.2270  658  LEU A CD2   
4113 N  N     . THR A 556 ? 1.4054 1.3828 1.9335 -0.0792 -0.2266 0.1762  659  THR A N     
4114 C  CA    . THR A 556 ? 1.4697 1.4607 2.0327 -0.0709 -0.2098 0.1705  659  THR A CA    
4115 C  C     . THR A 556 ? 1.2201 1.2207 1.7655 -0.0657 -0.2165 0.1742  659  THR A C     
4116 O  O     . THR A 556 ? 1.2473 1.2574 1.8220 -0.0589 -0.2051 0.1717  659  THR A O     
4117 C  CB    . THR A 556 ? 1.3459 1.3539 1.9008 -0.0717 -0.1781 0.1507  659  THR A CB    
4118 O  OG1   . THR A 556 ? 1.2958 1.3182 1.7918 -0.0763 -0.1742 0.1427  659  THR A OG1   
4119 C  CG2   . THR A 556 ? 1.3430 1.3382 1.9269 -0.0763 -0.1669 0.1459  659  THR A CG2   
4120 N  N     . ASN A 557 ? 0.9971 0.9936 1.4957 -0.0691 -0.2328 0.1799  660  ASN A N     
4121 C  CA    . ASN A 557 ? 1.1327 1.1340 1.6113 -0.0649 -0.2390 0.1839  660  ASN A CA    
4122 C  C     . ASN A 557 ? 1.1852 1.1639 1.6394 -0.0717 -0.2676 0.1981  660  ASN A C     
4123 O  O     . ASN A 557 ? 1.1076 1.0811 1.5144 -0.0775 -0.2715 0.1968  660  ASN A O     
4124 C  CB    . ASN A 557 ? 1.2388 1.2622 1.6739 -0.0620 -0.2201 0.1718  660  ASN A CB    
4125 C  CG    . ASN A 557 ? 1.4664 1.4947 1.8859 -0.0560 -0.2221 0.1754  660  ASN A CG    
4126 O  OD1   . ASN A 557 ? 1.1334 1.1449 1.5368 -0.0585 -0.2413 0.1857  660  ASN A OD1   
4127 N  ND2   . ASN A 557 ? 1.4778 1.5276 1.9001 -0.0491 -0.2017 0.1669  660  ASN A ND2   
4128 N  N     . GLN A 558 ? 1.0329 0.9979 1.5192 -0.0722 -0.2872 0.2117  661  GLN A N     
4129 C  CA    . GLN A 558 ? 1.2513 1.1917 1.7153 -0.0818 -0.3167 0.2263  661  GLN A CA    
4130 C  C     . GLN A 558 ? 1.1955 1.1321 1.6012 -0.0840 -0.3188 0.2245  661  GLN A C     
4131 O  O     . GLN A 558 ? 1.4579 1.3735 1.8241 -0.0939 -0.3360 0.2313  661  GLN A O     
4132 C  CB    . GLN A 558 ? 1.2317 1.1612 1.7465 -0.0830 -0.3381 0.2424  661  GLN A CB    
4133 C  CG    . GLN A 558 ? 1.2485 1.1510 1.7464 -0.0960 -0.3718 0.2598  661  GLN A CG    
4134 C  CD    . GLN A 558 ? 1.5216 1.4170 2.0792 -0.0980 -0.3943 0.2778  661  GLN A CD    
4135 O  OE1   . GLN A 558 ? 1.8327 1.7208 2.3895 -0.1027 -0.4121 0.2875  661  GLN A OE1   
4136 N  NE2   . GLN A 558 ? 1.4152 1.3127 2.0266 -0.0950 -0.3933 0.2830  661  GLN A NE2   
4137 N  N     . ARG A 559 ? 1.2164 1.1709 1.6153 -0.0751 -0.3005 0.2158  662  ARG A N     
4138 C  CA    . ARG A 559 ? 1.2896 1.2412 1.6345 -0.0755 -0.2977 0.2133  662  ARG A CA    
4139 C  C     . ARG A 559 ? 1.4168 1.3712 1.7161 -0.0787 -0.2886 0.2062  662  ARG A C     
4140 O  O     . ARG A 559 ? 1.3798 1.3190 1.6323 -0.0844 -0.2946 0.2085  662  ARG A O     
4141 C  CB    . ARG A 559 ? 1.4021 1.3744 1.7533 -0.0643 -0.2781 0.2063  662  ARG A CB    
4142 C  CG    . ARG A 559 ? 1.4000 1.3730 1.7000 -0.0619 -0.2694 0.2030  662  ARG A CG    
4143 C  CD    . ARG A 559 ? 1.3225 1.3140 1.6334 -0.0507 -0.2522 0.1988  662  ARG A CD    
4144 N  NE    . ARG A 559 ? 1.5993 1.6170 1.9438 -0.0437 -0.2340 0.1906  662  ARG A NE    
4145 C  CZ    . ARG A 559 ? 1.7202 1.7604 2.0493 -0.0402 -0.2153 0.1813  662  ARG A CZ    
4146 N  NH1   . ARG A 559 ? 1.5679 1.6111 1.8536 -0.0415 -0.2117 0.1797  662  ARG A NH1   
4147 N  NH2   . ARG A 559 ? 1.5543 1.6143 1.9122 -0.0364 -0.1994 0.1737  662  ARG A NH2   
4148 N  N     . ILE A 560 ? 1.3684 1.3410 1.6806 -0.0762 -0.2731 0.1972  663  ILE A N     
4149 C  CA    . ILE A 560 ? 1.4333 1.4098 1.7075 -0.0806 -0.2655 0.1910  663  ILE A CA    
4150 C  C     . ILE A 560 ? 1.5273 1.4776 1.7922 -0.0923 -0.2852 0.1989  663  ILE A C     
4151 O  O     . ILE A 560 ? 1.6175 1.5572 1.8382 -0.0992 -0.2879 0.1992  663  ILE A O     
4152 C  CB    . ILE A 560 ? 1.2393 1.2441 1.5284 -0.0763 -0.2426 0.1783  663  ILE A CB    
4153 C  CG1   . ILE A 560 ? 1.2281 1.2580 1.5217 -0.0659 -0.2243 0.1721  663  ILE A CG1   
4154 C  CG2   . ILE A 560 ? 1.1419 1.1525 1.3946 -0.0822 -0.2356 0.1724  663  ILE A CG2   
4155 C  CD1   . ILE A 560 ? 1.1474 1.2036 1.4551 -0.0639 -0.2028 0.1600  663  ILE A CD1   
4156 N  N     . GLY A 561 ? 1.2040 1.1430 1.5116 -0.0949 -0.2987 0.2066  664  GLY A N     
4157 C  CA    . GLY A 561 ? 1.4127 1.3271 1.7152 -0.1059 -0.3183 0.2161  664  GLY A CA    
4158 C  C     . GLY A 561 ? 1.2550 1.1410 1.5220 -0.1159 -0.3424 0.2284  664  GLY A C     
4159 O  O     . GLY A 561 ? 1.4587 1.3235 1.6983 -0.1270 -0.3556 0.2343  664  GLY A O     
4160 N  N     . HIS A 562 ? 1.6206 1.5037 1.8851 -0.1136 -0.3481 0.2322  665  HIS A N     
4161 C  CA    . HIS A 562 ? 1.5224 1.3757 1.7479 -0.1255 -0.3698 0.2426  665  HIS A CA    
4162 C  C     . HIS A 562 ? 1.4166 1.2608 1.5771 -0.1307 -0.3602 0.2358  665  HIS A C     
4163 O  O     . HIS A 562 ? 1.3181 1.1357 1.4437 -0.1442 -0.3751 0.2423  665  HIS A O     
4164 C  CB    . HIS A 562 ? 1.3758 1.2287 1.6111 -0.1221 -0.3740 0.2458  665  HIS A CB    
4165 C  CG    . HIS A 562 ? 1.4415 1.2638 1.6272 -0.1350 -0.3906 0.2528  665  HIS A CG    
4166 N  ND1   . HIS A 562 ? 1.6554 1.4478 1.8312 -0.1513 -0.4209 0.2676  665  HIS A ND1   
4167 C  CD2   . HIS A 562 ? 1.5978 1.4126 1.7393 -0.1349 -0.3804 0.2472  665  HIS A CD2   
4168 C  CE1   . HIS A 562 ? 1.6942 1.4608 1.8183 -0.1624 -0.4284 0.2695  665  HIS A CE1   
4169 N  NE2   . HIS A 562 ? 1.5502 1.3291 1.6536 -0.1521 -0.4031 0.2568  665  HIS A NE2   
4170 N  N     . PHE A 563 ? 1.5387 1.4048 1.6833 -0.1205 -0.3349 0.2235  666  PHE A N     
4171 C  CA    . PHE A 563 ? 1.4226 1.2842 1.5128 -0.1236 -0.3223 0.2173  666  PHE A CA    
4172 C  C     . PHE A 563 ? 1.4809 1.3496 1.5652 -0.1270 -0.3156 0.2126  666  PHE A C     
4173 O  O     . PHE A 563 ? 1.4095 1.2682 1.4493 -0.1333 -0.3100 0.2101  666  PHE A O     
4174 C  CB    . PHE A 563 ? 1.3923 1.2782 1.4742 -0.1106 -0.2977 0.2081  666  PHE A CB    
4175 C  CG    . PHE A 563 ? 1.3226 1.1990 1.4047 -0.1076 -0.3017 0.2119  666  PHE A CG    
4176 C  CD1   . PHE A 563 ? 1.5461 1.3948 1.5813 -0.1148 -0.3046 0.2145  666  PHE A CD1   
4177 C  CD2   . PHE A 563 ? 1.3405 1.2338 1.4689 -0.0985 -0.3011 0.2124  666  PHE A CD2   
4178 C  CE1   . PHE A 563 ? 1.3517 1.1896 1.3856 -0.1133 -0.3075 0.2174  666  PHE A CE1   
4179 C  CE2   . PHE A 563 ? 1.4495 1.3338 1.5785 -0.0965 -0.3045 0.2159  666  PHE A CE2   
4180 C  CZ    . PHE A 563 ? 1.4888 1.3453 1.5703 -0.1041 -0.3081 0.2183  666  PHE A CZ    
4181 N  N     . PHE A 564 ? 1.3930 1.2775 1.5214 -0.1235 -0.3144 0.2109  667  PHE A N     
4182 C  CA    . PHE A 564 ? 1.3105 1.1975 1.4344 -0.1287 -0.3097 0.2070  667  PHE A CA    
4183 C  C     . PHE A 564 ? 1.2860 1.1376 1.3886 -0.1436 -0.3326 0.2183  667  PHE A C     
4184 O  O     . PHE A 564 ? 1.5295 1.3751 1.6058 -0.1509 -0.3287 0.2156  667  PHE A O     
4185 C  CB    . PHE A 564 ? 1.4308 1.3387 1.6070 -0.1223 -0.3014 0.2021  667  PHE A CB    
4186 C  CG    . PHE A 564 ? 1.3059 1.2133 1.4815 -0.1288 -0.2971 0.1982  667  PHE A CG    
4187 C  CD1   . PHE A 564 ? 1.1638 1.0890 1.3113 -0.1297 -0.2783 0.1871  667  PHE A CD1   
4188 C  CD2   . PHE A 564 ? 1.6014 1.4909 1.8070 -0.1341 -0.3117 0.2066  667  PHE A CD2   
4189 C  CE1   . PHE A 564 ? 1.3692 1.2931 1.5155 -0.1369 -0.2739 0.1831  667  PHE A CE1   
4190 C  CE2   . PHE A 564 ? 1.4741 1.3608 1.6789 -0.1402 -0.3065 0.2029  667  PHE A CE2   
4191 C  CZ    . PHE A 564 ? 1.3901 1.2934 1.5638 -0.1422 -0.2874 0.1904  667  PHE A CZ    
4192 N  N     . PHE A 565 ? 1.5147 1.3429 1.6277 -0.1493 -0.3570 0.2316  668  PHE A N     
4193 C  CA    . PHE A 565 ? 1.4742 1.2675 1.5649 -0.1651 -0.3818 0.2448  668  PHE A CA    
4194 C  C     . PHE A 565 ? 1.7523 1.5203 1.7759 -0.1761 -0.3844 0.2452  668  PHE A C     
4195 O  O     . PHE A 565 ? 1.9061 1.6544 1.8917 -0.1877 -0.3875 0.2468  668  PHE A O     
4196 C  CB    . PHE A 565 ? 1.3341 1.1139 1.4647 -0.1684 -0.4091 0.2610  668  PHE A CB    
4197 C  CG    . PHE A 565 ? 1.5361 1.2782 1.6376 -0.1867 -0.4390 0.2774  668  PHE A CG    
4198 C  CD1   . PHE A 565 ? 1.7552 1.4846 1.8656 -0.1942 -0.4511 0.2862  668  PHE A CD1   
4199 C  CD2   . PHE A 565 ? 1.6857 1.4036 1.7492 -0.1977 -0.4552 0.2845  668  PHE A CD2   
4200 C  CE1   . PHE A 565 ? 1.7128 1.4070 1.7943 -0.2122 -0.4799 0.3029  668  PHE A CE1   
4201 C  CE2   . PHE A 565 ? 1.7441 1.4259 1.7760 -0.2171 -0.4837 0.3000  668  PHE A CE2   
4202 C  CZ    . PHE A 565 ? 1.7475 1.4182 1.7885 -0.2243 -0.4969 0.3098  668  PHE A CZ    
4203 N  N     . TRP A 566 ? 1.5786 1.3445 1.5860 -0.1733 -0.3814 0.2436  669  TRP A N     
4204 C  CA    . TRP A 566 ? 1.7395 1.4757 1.6831 -0.1850 -0.3830 0.2442  669  TRP A CA    
4205 C  C     . TRP A 566 ? 1.5847 1.3295 1.4905 -0.1823 -0.3563 0.2318  669  TRP A C     
4206 O  O     . TRP A 566 ? 1.6124 1.3285 1.4643 -0.1951 -0.3568 0.2326  669  TRP A O     
4207 C  CB    . TRP A 566 ? 1.5905 1.3215 1.5289 -0.1823 -0.3840 0.2447  669  TRP A CB    
4208 C  CG    . TRP A 566 ? 1.5905 1.2992 1.5440 -0.1933 -0.4157 0.2597  669  TRP A CG    
4209 C  CD1   . TRP A 566 ? 1.5496 1.2741 1.5587 -0.1857 -0.4257 0.2653  669  TRP A CD1   
4210 C  CD2   . TRP A 566 ? 1.9704 1.6373 1.8832 -0.2152 -0.4424 0.2721  669  TRP A CD2   
4211 N  NE1   . TRP A 566 ? 1.6395 1.3371 1.6487 -0.2011 -0.4578 0.2813  669  TRP A NE1   
4212 C  CE2   . TRP A 566 ? 1.9945 1.6562 1.9433 -0.2201 -0.4697 0.2859  669  TRP A CE2   
4213 C  CE3   . TRP A 566 ? 1.8579 1.4909 1.7066 -0.2323 -0.4458 0.2731  669  TRP A CE3   
4214 C  CZ2   . TRP A 566 ? 1.9958 1.6210 1.9181 -0.2421 -0.5022 0.3017  669  TRP A CZ2   
4215 C  CZ3   . TRP A 566 ? 1.8318 1.4258 1.6503 -0.2546 -0.4767 0.2877  669  TRP A CZ3   
4216 C  CH2   . TRP A 566 ? 2.0703 1.6614 1.9253 -0.2597 -0.5057 0.3023  669  TRP A CH2   
4217 N  N     . HIS A 567 ? 1.5033 1.2870 1.4357 -0.1670 -0.3327 0.2209  670  HIS A N     
4218 C  CA    . HIS A 567 ? 1.5999 1.3962 1.5033 -0.1650 -0.3091 0.2111  670  HIS A CA    
4219 C  C     . HIS A 567 ? 1.7222 1.5093 1.6150 -0.1756 -0.3135 0.2121  670  HIS A C     
4220 O  O     . HIS A 567 ? 1.6023 1.3891 1.4612 -0.1793 -0.2984 0.2065  670  HIS A O     
4221 C  CB    . HIS A 567 ? 1.7088 1.5508 1.6437 -0.1477 -0.2855 0.2010  670  HIS A CB    
4222 C  CG    . HIS A 567 ? 1.7316 1.5828 1.6644 -0.1370 -0.2743 0.1989  670  HIS A CG    
4223 N  ND1   . HIS A 567 ? 1.6872 1.5552 1.6598 -0.1266 -0.2762 0.1995  670  HIS A ND1   
4224 C  CD2   . HIS A 567 ? 1.5949 1.4392 1.4914 -0.1350 -0.2597 0.1966  670  HIS A CD2   
4225 C  CE1   . HIS A 567 ? 1.7837 1.6550 1.7435 -0.1188 -0.2644 0.1978  670  HIS A CE1   
4226 N  NE2   . HIS A 567 ? 1.6615 1.5184 1.5762 -0.1234 -0.2538 0.1962  670  HIS A NE2   
4227 N  N     . LEU A 568 ? 1.4994 1.2789 1.4224 -0.1805 -0.3330 0.2198  671  LEU A N     
4228 C  CA    . LEU A 568 ? 1.5753 1.3412 1.4882 -0.1914 -0.3392 0.2226  671  LEU A CA    
4229 C  C     . LEU A 568 ? 1.7914 1.5113 1.6642 -0.2098 -0.3631 0.2353  671  LEU A C     
4230 O  O     . LEU A 568 ? 1.9562 1.6584 1.7941 -0.2212 -0.3620 0.2357  671  LEU A O     
4231 C  CB    . LEU A 568 ? 1.5295 1.3112 1.4987 -0.1864 -0.3446 0.2242  671  LEU A CB    
4232 C  CG    . LEU A 568 ? 1.6512 1.4753 1.6542 -0.1725 -0.3200 0.2105  671  LEU A CG    
4233 C  CD1   . LEU A 568 ? 1.3230 1.1548 1.3768 -0.1702 -0.3235 0.2115  671  LEU A CD1   
4234 C  CD2   . LEU A 568 ? 1.4757 1.3147 1.4463 -0.1741 -0.2981 0.1995  671  LEU A CD2   
4235 N  N     . LYS A 569 ? 1.6220 1.3220 1.4977 -0.2144 -0.3851 0.2462  672  LYS A N     
4236 C  CA    . LYS A 569 ? 1.7456 1.4007 1.5778 -0.2345 -0.4096 0.2592  672  LYS A CA    
4237 C  C     . LYS A 569 ? 1.8246 1.4567 1.5884 -0.2435 -0.3965 0.2528  672  LYS A C     
4238 O  O     . LYS A 569 ? 2.0040 1.5988 1.7183 -0.2621 -0.4078 0.2592  672  LYS A O     
4239 C  CB    . LYS A 569 ? 1.6581 1.3005 1.5144 -0.2384 -0.4381 0.2734  672  LYS A CB    
4240 C  CG    . LYS A 569 ? 1.7547 1.3521 1.5717 -0.2615 -0.4691 0.2900  672  LYS A CG    
4241 C  CD    . LYS A 569 ? 2.3692 1.9573 2.2108 -0.2664 -0.4977 0.3045  672  LYS A CD    
4242 C  CE    . LYS A 569 ? 2.0582 1.6017 1.8569 -0.2920 -0.5309 0.3224  672  LYS A CE    
4243 N  NZ    . LYS A 569 ? 1.8659 1.4007 1.6752 -0.2988 -0.5450 0.3339  672  LYS A NZ    
4244 N  N     . SER A 570 ? 1.5239 1.1765 1.2839 -0.2309 -0.3716 0.2407  673  SER A N     
4245 C  CA    . SER A 570 ? 1.6435 1.2757 1.3439 -0.2370 -0.3540 0.2339  673  SER A CA    
4246 C  C     . SER A 570 ? 2.0413 1.6743 1.7135 -0.2408 -0.3350 0.2270  673  SER A C     
4247 O  O     . SER A 570 ? 2.2547 1.8658 1.8752 -0.2482 -0.3200 0.2223  673  SER A O     
4248 C  CB    . SER A 570 ? 1.7347 1.3912 1.4461 -0.2203 -0.3315 0.2245  673  SER A CB    
4249 O  OG    . SER A 570 ? 1.8331 1.5376 1.5892 -0.2018 -0.3124 0.2162  673  SER A OG    
4250 N  N     . GLU A 571 ? 1.8689 1.5255 1.5741 -0.2364 -0.3338 0.2258  674  GLU A N     
4251 C  CA    . GLU A 571 ? 1.9549 1.6138 1.6374 -0.2411 -0.3173 0.2197  674  GLU A CA    
4252 C  C     . GLU A 571 ? 2.1043 1.7310 1.7676 -0.2591 -0.3378 0.2295  674  GLU A C     
4253 O  O     . GLU A 571 ? 2.0096 1.6365 1.6564 -0.2644 -0.3260 0.2253  674  GLU A O     
4254 C  CB    . GLU A 571 ? 1.7396 1.4486 1.4681 -0.2249 -0.2979 0.2099  674  GLU A CB    
4255 C  CG    . GLU A 571 ? 1.6792 1.4234 1.4248 -0.2074 -0.2756 0.2010  674  GLU A CG    
4256 C  CD    . GLU A 571 ? 1.8829 1.6308 1.5927 -0.2068 -0.2490 0.1937  674  GLU A CD    
4257 O  OE1   . GLU A 571 ? 1.8152 1.5318 1.4801 -0.2213 -0.2477 0.1950  674  GLU A OE1   
4258 O  OE2   . GLU A 571 ? 1.6869 1.4691 1.4146 -0.1919 -0.2289 0.1874  674  GLU A OE2   
4259 N  N     . MET A 572 ? 2.1014 1.7011 1.7677 -0.2690 -0.3687 0.2435  675  MET A N     
4260 C  CA    . MET A 572 ? 1.9061 1.4762 1.5589 -0.2855 -0.3909 0.2558  675  MET A CA    
4261 C  C     . MET A 572 ? 1.9616 1.4891 1.5403 -0.3059 -0.3891 0.2570  675  MET A C     
4262 O  O     . MET A 572 ? 1.8669 1.3730 1.4280 -0.3192 -0.3995 0.2643  675  MET A O     
4263 C  CB    . MET A 572 ? 1.9820 1.5371 1.6618 -0.2905 -0.4260 0.2730  675  MET A CB    
4264 C  CG    . MET A 572 ? 1.9160 1.5080 1.6732 -0.2730 -0.4290 0.2739  675  MET A CG    
4265 S  SD    . MET A 572 ? 1.8969 1.5089 1.6860 -0.2680 -0.4166 0.2692  675  MET A SD    
4266 C  CE    . MET A 572 ? 1.7858 1.4361 1.6608 -0.2480 -0.4170 0.2686  675  MET A CE    
4267 N  N     . HIS A 573 ? 2.3036 1.8161 1.8377 -0.3091 -0.3747 0.2502  676  HIS A N     
4268 C  CA    . HIS A 573 ? 2.1551 1.6251 1.6160 -0.3288 -0.3681 0.2494  676  HIS A CA    
4269 C  C     . HIS A 573 ? 2.1289 1.6127 1.5783 -0.3264 -0.3391 0.2384  676  HIS A C     
4270 O  O     . HIS A 573 ? 2.4531 1.9023 1.8436 -0.3428 -0.3304 0.2371  676  HIS A O     
4271 C  CB    . HIS A 573 ? 2.4287 1.8771 1.8471 -0.3324 -0.3571 0.2440  676  HIS A CB    
4272 C  CG    . HIS A 573 ? 2.3192 1.8012 1.7506 -0.3131 -0.3203 0.2284  676  HIS A CG    
4273 N  ND1   . HIS A 573 ? 2.1567 1.6854 1.6476 -0.2902 -0.3133 0.2238  676  HIS A ND1   
4274 C  CD2   . HIS A 573 ? 2.3451 1.8210 1.7393 -0.3133 -0.2883 0.2177  676  HIS A CD2   
4275 C  CE1   . HIS A 573 ? 2.3900 1.9409 1.8795 -0.2773 -0.2806 0.2121  676  HIS A CE1   
4276 N  NE2   . HIS A 573 ? 2.6091 2.1295 2.0429 -0.2903 -0.2645 0.2083  676  HIS A NE2   
4277 N  N     . ASN A 574 ? 2.0503 1.5826 1.5527 -0.3079 -0.3238 0.2305  677  ASN A N     
4278 C  CA    . ASN A 574 ? 2.0834 1.6350 1.5826 -0.3055 -0.2977 0.2206  677  ASN A CA    
4279 C  C     . ASN A 574 ? 2.2760 1.8434 1.8140 -0.3049 -0.3088 0.2243  677  ASN A C     
4280 O  O     . ASN A 574 ? 2.2147 1.8145 1.8094 -0.2910 -0.3145 0.2241  677  ASN A O     
4281 C  CB    . ASN A 574 ? 2.1343 1.7311 1.6593 -0.2856 -0.2674 0.2075  677  ASN A CB    
4282 C  CG    . ASN A 574 ? 2.3085 1.9328 1.8399 -0.2828 -0.2428 0.1985  677  ASN A CG    
4283 O  OD1   . ASN A 574 ? 2.4365 2.0991 2.0143 -0.2732 -0.2405 0.1950  677  ASN A OD1   
4284 N  ND2   . ASN A 574 ? 2.4434 2.0477 1.9278 -0.2923 -0.2234 0.1946  677  ASN A ND2   
4285 N  N     . LYS A 575 ? 2.3638 1.9061 1.8702 -0.3206 -0.3103 0.2275  678  LYS A N     
4286 C  CA    . LYS A 575 ? 2.1730 1.7213 1.7104 -0.3228 -0.3219 0.2326  678  LYS A CA    
4287 C  C     . LYS A 575 ? 2.1324 1.7284 1.7107 -0.3097 -0.2983 0.2196  678  LYS A C     
4288 O  O     . LYS A 575 ? 2.2088 1.8144 1.8216 -0.3088 -0.3054 0.2218  678  LYS A O     
4289 C  CB    . LYS A 575 ? 2.1017 1.6050 1.5887 -0.3450 -0.3309 0.2410  678  LYS A CB    
4290 C  CG    . LYS A 575 ? 2.1338 1.5878 1.5823 -0.3617 -0.3611 0.2571  678  LYS A CG    
4291 C  CD    . LYS A 575 ? 2.5203 1.9310 1.9213 -0.3842 -0.3715 0.2669  678  LYS A CD    
4292 C  CE    . LYS A 575 ? 2.7514 2.1136 2.1134 -0.4031 -0.4049 0.2850  678  LYS A CE    
4293 N  NZ    . LYS A 575 ? 2.6174 1.9360 1.9312 -0.4261 -0.4168 0.2963  678  LYS A NZ    
4294 N  N     . THR A 576 ? 1.9271 1.5525 1.5031 -0.3003 -0.2707 0.2070  679  THR A N     
4295 C  CA    . THR A 576 ? 1.8408 1.5136 1.4543 -0.2899 -0.2502 0.1956  679  THR A CA    
4296 C  C     . THR A 576 ? 2.0906 1.7992 1.7633 -0.2737 -0.2555 0.1934  679  THR A C     
4297 O  O     . THR A 576 ? 1.9354 1.6787 1.6413 -0.2681 -0.2438 0.1853  679  THR A O     
4298 C  CB    . THR A 576 ? 1.7704 1.4666 1.3679 -0.2845 -0.2206 0.1854  679  THR A CB    
4299 O  OG1   . THR A 576 ? 2.3400 2.0545 1.9521 -0.2697 -0.2163 0.1835  679  THR A OG1   
4300 C  CG2   . THR A 576 ? 1.8689 1.5248 1.4053 -0.3001 -0.2129 0.1874  679  THR A CG2   
4301 N  N     . VAL A 577 ? 2.1795 1.8795 1.8646 -0.2675 -0.2721 0.2000  680  VAL A N     
4302 C  CA    . VAL A 577 ? 1.9337 1.6647 1.6740 -0.2525 -0.2761 0.1981  680  VAL A CA    
4303 C  C     . VAL A 577 ? 1.8329 1.5370 1.5906 -0.2555 -0.3055 0.2116  680  VAL A C     
4304 O  O     . VAL A 577 ? 1.7198 1.4421 1.5223 -0.2439 -0.3117 0.2124  680  VAL A O     
4305 C  CB    . VAL A 577 ? 1.6321 1.3907 1.3801 -0.2379 -0.2623 0.1918  680  VAL A CB    
4306 C  CG1   . VAL A 577 ? 1.9757 1.7668 1.7160 -0.2336 -0.2340 0.1808  680  VAL A CG1   
4307 C  CG2   . VAL A 577 ? 1.5932 1.3182 1.3049 -0.2420 -0.2721 0.1989  680  VAL A CG2   
4308 N  N     . SER A 578 ? 1.8126 1.4735 1.5359 -0.2716 -0.3239 0.2233  681  SER A N     
4309 C  CA    . SER A 578 ? 1.8310 1.4659 1.5705 -0.2760 -0.3547 0.2394  681  SER A CA    
4310 C  C     . SER A 578 ? 1.9045 1.5511 1.6981 -0.2713 -0.3614 0.2427  681  SER A C     
4311 O  O     . SER A 578 ? 1.9184 1.5672 1.7547 -0.2646 -0.3779 0.2513  681  SER A O     
4312 C  CB    . SER A 578 ? 1.9537 1.5386 1.6377 -0.2966 -0.3734 0.2523  681  SER A CB    
4313 O  OG    . SER A 578 ? 2.1799 1.7483 1.8151 -0.3017 -0.3685 0.2498  681  SER A OG    
4314 N  N     . GLN A 579 ? 1.7897 1.4430 1.5835 -0.2750 -0.3475 0.2359  682  GLN A N     
4315 C  CA    . GLN A 579 ? 1.7747 1.4343 1.6171 -0.2718 -0.3510 0.2383  682  GLN A CA    
4316 C  C     . GLN A 579 ? 1.7271 1.4275 1.6230 -0.2547 -0.3367 0.2270  682  GLN A C     
4317 O  O     . GLN A 579 ? 1.6429 1.3448 1.5878 -0.2484 -0.3459 0.2328  682  GLN A O     
4318 C  CB    . GLN A 579 ? 1.9843 1.6386 1.8090 -0.2819 -0.3382 0.2328  682  GLN A CB    
4319 C  CG    . GLN A 579 ? 2.1105 1.7606 1.9787 -0.2817 -0.3427 0.2372  682  GLN A CG    
4320 C  CD    . GLN A 579 ? 2.2864 1.9299 2.1350 -0.2928 -0.3291 0.2311  682  GLN A CD    
4321 O  OE1   . GLN A 579 ? 2.3944 2.0173 2.2593 -0.2984 -0.3374 0.2396  682  GLN A OE1   
4322 N  NE2   . GLN A 579 ? 2.2513 1.9128 2.0671 -0.2959 -0.3075 0.2171  682  GLN A NE2   
4323 N  N     . ARG A 580 ? 1.6267 1.3600 1.5150 -0.2474 -0.3137 0.2116  683  ARG A N     
4324 C  CA    . ARG A 580 ? 1.4951 1.2666 1.4283 -0.2328 -0.2999 0.2008  683  ARG A CA    
4325 C  C     . ARG A 580 ? 1.5078 1.2795 1.4667 -0.2227 -0.3138 0.2082  683  ARG A C     
4326 O  O     . ARG A 580 ? 1.5531 1.3360 1.5613 -0.2141 -0.3152 0.2084  683  ARG A O     
4327 C  CB    . ARG A 580 ? 1.5611 1.3679 1.4777 -0.2285 -0.2745 0.1856  683  ARG A CB    
4328 C  CG    . ARG A 580 ? 1.6169 1.4624 1.5711 -0.2142 -0.2619 0.1760  683  ARG A CG    
4329 C  CD    . ARG A 580 ? 1.5726 1.4531 1.5093 -0.2103 -0.2402 0.1646  683  ARG A CD    
4330 N  NE    . ARG A 580 ? 1.2981 1.1936 1.2275 -0.2188 -0.2250 0.1554  683  ARG A NE    
4331 C  CZ    . ARG A 580 ? 1.3913 1.3134 1.3484 -0.2181 -0.2127 0.1450  683  ARG A CZ    
4332 N  NH1   . ARG A 580 ? 1.6621 1.5982 1.6563 -0.2088 -0.2120 0.1420  683  ARG A NH1   
4333 N  NH2   . ARG A 580 ? 1.3758 1.3096 1.3220 -0.2282 -0.2000 0.1371  683  ARG A NH2   
4334 N  N     . PHE A 581 ? 1.5666 1.3246 1.4925 -0.2243 -0.3226 0.2140  684  PHE A N     
4335 C  CA    . PHE A 581 ? 1.5586 1.3167 1.5061 -0.2161 -0.3356 0.2207  684  PHE A CA    
4336 C  C     . PHE A 581 ? 1.7394 1.4687 1.7102 -0.2213 -0.3643 0.2385  684  PHE A C     
4337 O  O     . PHE A 581 ? 1.7570 1.4935 1.7693 -0.2127 -0.3736 0.2438  684  PHE A O     
4338 C  CB    . PHE A 581 ? 1.6674 1.4168 1.5701 -0.2176 -0.3349 0.2208  684  PHE A CB    
4339 C  CG    . PHE A 581 ? 1.7332 1.5157 1.6252 -0.2085 -0.3073 0.2060  684  PHE A CG    
4340 C  CD1   . PHE A 581 ? 1.7016 1.5220 1.6257 -0.1995 -0.2884 0.1943  684  PHE A CD1   
4341 C  CD2   . PHE A 581 ? 1.6046 1.3795 1.4546 -0.2096 -0.3002 0.2045  684  PHE A CD2   
4342 C  CE1   . PHE A 581 ? 1.6593 1.5122 1.5753 -0.1919 -0.2657 0.1834  684  PHE A CE1   
4343 C  CE2   . PHE A 581 ? 1.4830 1.2897 1.3282 -0.2002 -0.2753 0.1934  684  PHE A CE2   
4344 C  CZ    . PHE A 581 ? 1.5076 1.3547 1.3866 -0.1913 -0.2594 0.1838  684  PHE A CZ    
4345 N  N     . GLY A 582 ? 1.8186 1.5161 1.7651 -0.2355 -0.3788 0.2490  685  GLY A N     
4346 C  CA    . GLY A 582 ? 1.4064 1.0783 1.3787 -0.2409 -0.4075 0.2686  685  GLY A CA    
4347 C  C     . GLY A 582 ? 1.7377 1.4258 1.7773 -0.2306 -0.4037 0.2688  685  GLY A C     
4348 O  O     . GLY A 582 ? 1.6941 1.3807 1.7793 -0.2251 -0.4198 0.2807  685  GLY A O     
4349 N  N     . LEU A 583 ? 1.6978 1.4007 1.7448 -0.2288 -0.3811 0.2554  686  LEU A N     
4350 C  CA    . LEU A 583 ? 1.7865 1.5035 1.8942 -0.2197 -0.3717 0.2522  686  LEU A CA    
4351 C  C     . LEU A 583 ? 1.6776 1.4257 1.8241 -0.2045 -0.3594 0.2427  686  LEU A C     
4352 O  O     . LEU A 583 ? 1.4409 1.1930 1.6438 -0.1964 -0.3606 0.2468  686  LEU A O     
4353 C  CB    . LEU A 583 ? 1.6226 1.3478 1.7218 -0.2237 -0.3484 0.2377  686  LEU A CB    
4354 C  CG    . LEU A 583 ? 1.5765 1.2707 1.6454 -0.2384 -0.3575 0.2464  686  LEU A CG    
4355 C  CD1   . LEU A 583 ? 1.5224 1.2301 1.5774 -0.2428 -0.3313 0.2290  686  LEU A CD1   
4356 C  CD2   . LEU A 583 ? 1.6404 1.3092 1.7509 -0.2393 -0.3776 0.2657  686  LEU A CD2   
4357 N  N     . LEU A 584 ? 1.5658 1.3353 1.6841 -0.2004 -0.3464 0.2306  687  LEU A N     
4358 C  CA    . LEU A 584 ? 1.4716 1.2701 1.6225 -0.1866 -0.3343 0.2219  687  LEU A CA    
4359 C  C     . LEU A 584 ? 1.5389 1.3274 1.7130 -0.1823 -0.3563 0.2365  687  LEU A C     
4360 O  O     . LEU A 584 ? 1.7804 1.5827 2.0049 -0.1718 -0.3530 0.2362  687  LEU A O     
4361 C  CB    . LEU A 584 ? 1.3793 1.2037 1.4942 -0.1834 -0.3146 0.2069  687  LEU A CB    
4362 C  CG    . LEU A 584 ? 1.3834 1.2404 1.5261 -0.1699 -0.2990 0.1966  687  LEU A CG    
4363 C  CD1   . LEU A 584 ? 1.2295 1.0996 1.4216 -0.1649 -0.2857 0.1892  687  LEU A CD1   
4364 C  CD2   . LEU A 584 ? 1.1937 1.0767 1.3009 -0.1679 -0.2795 0.1838  687  LEU A CD2   
4365 N  N     . LEU A 585 ? 1.5157 1.2792 1.6526 -0.1915 -0.3783 0.2493  688  LEU A N     
4366 C  CA    . LEU A 585 ? 1.4283 1.1802 1.5854 -0.1906 -0.4023 0.2647  688  LEU A CA    
4367 C  C     . LEU A 585 ? 1.7195 1.4579 1.9302 -0.1911 -0.4213 0.2817  688  LEU A C     
4368 O  O     . LEU A 585 ? 1.5015 1.2444 1.7574 -0.1846 -0.4327 0.2909  688  LEU A O     
4369 C  CB    . LEU A 585 ? 1.3073 1.0321 1.4055 -0.2037 -0.4211 0.2738  688  LEU A CB    
4370 C  CG    . LEU A 585 ? 1.5382 1.2745 1.5946 -0.2006 -0.4053 0.2610  688  LEU A CG    
4371 C  CD1   . LEU A 585 ? 1.5277 1.2312 1.5299 -0.2148 -0.4246 0.2710  688  LEU A CD1   
4372 C  CD2   . LEU A 585 ? 1.6595 1.4243 1.7560 -0.1852 -0.3950 0.2545  688  LEU A CD2   
4373 N  N     . GLU A 586 ? 1.6382 1.3601 1.8472 -0.1985 -0.4243 0.2867  689  GLU A N     
4374 C  CA    . GLU A 586 ? 1.3759 1.0860 1.6417 -0.1973 -0.4392 0.3034  689  GLU A CA    
4375 C  C     . GLU A 586 ? 1.4818 1.2171 1.8133 -0.1818 -0.4176 0.2935  689  GLU A C     
4376 O  O     . GLU A 586 ? 1.6407 1.3755 2.0311 -0.1754 -0.4290 0.3068  689  GLU A O     
4377 C  CB    . GLU A 586 ? 1.6429 1.3300 1.8906 -0.2080 -0.4429 0.3092  689  GLU A CB    
4378 C  CG    . GLU A 586 ? 1.7216 1.3971 2.0317 -0.2052 -0.4534 0.3257  689  GLU A CG    
4379 C  CD    . GLU A 586 ? 1.8723 1.5245 2.1632 -0.2155 -0.4545 0.3306  689  GLU A CD    
4380 O  OE1   . GLU A 586 ? 1.7165 1.3569 1.9418 -0.2274 -0.4543 0.3255  689  GLU A OE1   
4381 O  OE2   . GLU A 586 ? 1.8646 1.5094 2.2071 -0.2115 -0.4541 0.3395  689  GLU A OE2   
4382 N  N     . SER A 587 ? 1.5323 1.2897 1.8548 -0.1765 -0.3859 0.2705  690  SER A N     
4383 C  CA    . SER A 587 ? 1.3110 1.0904 1.6878 -0.1640 -0.3625 0.2588  690  SER A CA    
4384 C  C     . SER A 587 ? 1.4227 1.2204 1.8237 -0.1537 -0.3629 0.2581  690  SER A C     
4385 O  O     . SER A 587 ? 1.5365 1.3425 1.9971 -0.1441 -0.3558 0.2592  690  SER A O     
4386 C  CB    . SER A 587 ? 1.3723 1.1705 1.7255 -0.1641 -0.3306 0.2347  690  SER A CB    
4387 O  OG    . SER A 587 ? 1.4571 1.2704 1.7566 -0.1660 -0.3247 0.2242  690  SER A OG    
4388 N  N     . TYR A 588 ? 1.3505 1.1532 1.7071 -0.1557 -0.3693 0.2562  691  TYR A N     
4389 C  CA    . TYR A 588 ? 1.5285 1.3465 1.9047 -0.1468 -0.3702 0.2561  691  TYR A CA    
4390 C  C     . TYR A 588 ? 1.6644 1.4674 2.0838 -0.1470 -0.3985 0.2786  691  TYR A C     
4391 O  O     . TYR A 588 ? 1.4267 1.2419 1.9027 -0.1371 -0.3942 0.2805  691  TYR A O     
4392 C  CB    . TYR A 588 ? 1.4953 1.3182 1.8118 -0.1495 -0.3698 0.2497  691  TYR A CB    
4393 C  CG    . TYR A 588 ? 1.3591 1.1942 1.6904 -0.1417 -0.3721 0.2506  691  TYR A CG    
4394 C  CD1   . TYR A 588 ? 1.4524 1.3159 1.8045 -0.1298 -0.3474 0.2358  691  TYR A CD1   
4395 C  CD2   . TYR A 588 ? 1.3126 1.1293 1.6347 -0.1477 -0.3991 0.2665  691  TYR A CD2   
4396 C  CE1   . TYR A 588 ? 1.7842 1.6577 2.1494 -0.1228 -0.3487 0.2369  691  TYR A CE1   
4397 C  CE2   . TYR A 588 ? 1.3830 1.2097 1.7182 -0.1414 -0.4007 0.2670  691  TYR A CE2   
4398 C  CZ    . TYR A 588 ? 1.7829 1.6380 2.1406 -0.1283 -0.3750 0.2523  691  TYR A CZ    
4399 O  OH    . TYR A 588 ? 1.3471 1.2111 1.7177 -0.1222 -0.3758 0.2530  691  TYR A OH    
4400 N  N     . CYS A 589 ? 1.6169 1.3933 2.0104 -0.1594 -0.4279 0.2966  692  CYS A N     
4401 C  CA    . CYS A 589 ? 1.4351 1.1978 1.8672 -0.1623 -0.4591 0.3207  692  CYS A CA    
4402 C  C     . CYS A 589 ? 1.3751 1.1379 1.8824 -0.1554 -0.4592 0.3312  692  CYS A C     
4403 O  O     . CYS A 589 ? 1.3263 1.0890 1.8871 -0.1524 -0.4773 0.3487  692  CYS A O     
4404 C  CB    . CYS A 589 ? 1.3947 1.1268 1.7765 -0.1799 -0.4906 0.3378  692  CYS A CB    
4405 S  SG    . CYS A 589 ? 1.4926 1.2176 1.7858 -0.1895 -0.4903 0.3273  692  CYS A SG    
4406 N  N     . ARG A 590 ? 1.3427 1.1052 1.8571 -0.1532 -0.4384 0.3213  693  ARG A N     
4407 C  CA    . ARG A 590 ? 1.1963 0.9563 1.7828 -0.1461 -0.4337 0.3298  693  ARG A CA    
4408 C  C     . ARG A 590 ? 1.5281 1.3110 2.1756 -0.1312 -0.4128 0.3213  693  ARG A C     
4409 O  O     . ARG A 590 ? 1.4575 1.2383 2.1762 -0.1243 -0.4156 0.3345  693  ARG A O     
4410 C  CB    . ARG A 590 ? 1.7178 1.4705 2.2914 -0.1484 -0.4124 0.3179  693  ARG A CB    
4411 C  CG    . ARG A 590 ? 1.6825 1.4243 2.3245 -0.1432 -0.4090 0.3292  693  ARG A CG    
4412 C  CD    . ARG A 590 ? 1.8833 1.5987 2.5341 -0.1519 -0.4457 0.3595  693  ARG A CD    
4413 N  NE    . ARG A 590 ? 1.8319 1.5284 2.4116 -0.1664 -0.4550 0.3593  693  ARG A NE    
4414 C  CZ    . ARG A 590 ? 1.7796 1.4500 2.3470 -0.1776 -0.4859 0.3833  693  ARG A CZ    
4415 N  NH1   . ARG A 590 ? 1.6178 1.2792 2.2405 -0.1764 -0.5133 0.4115  693  ARG A NH1   
4416 N  NH2   . ARG A 590 ? 1.7905 1.4439 2.2892 -0.1910 -0.4897 0.3799  693  ARG A NH2   
4417 N  N     . ALA A 591 ? 1.5223 1.3268 2.1443 -0.1261 -0.3913 0.3002  694  ALA A N     
4418 C  CA    . ALA A 591 ? 1.5030 1.3283 2.1766 -0.1132 -0.3681 0.2899  694  ALA A CA    
4419 C  C     . ALA A 591 ? 1.3976 1.2401 2.0522 -0.1097 -0.3687 0.2841  694  ALA A C     
4420 O  O     . ALA A 591 ? 1.3717 1.2333 2.0527 -0.1000 -0.3449 0.2709  694  ALA A O     
4421 C  CB    . ALA A 591 ? 1.5184 1.3541 2.1904 -0.1093 -0.3297 0.2656  694  ALA A CB    
4422 N  N     . CYS A 592 ? 1.6007 1.4349 2.2086 -0.1181 -0.3939 0.2933  695  CYS A N     
4423 C  CA    . CYS A 592 ? 1.4561 1.3037 2.0463 -0.1150 -0.3940 0.2884  695  CYS A CA    
4424 C  C     . CYS A 592 ? 1.4241 1.2764 2.0770 -0.1093 -0.4067 0.3027  695  CYS A C     
4425 O  O     . CYS A 592 ? 1.5771 1.4414 2.2246 -0.1056 -0.4039 0.2981  695  CYS A O     
4426 C  CB    . CYS A 592 ? 1.2595 1.0930 1.7788 -0.1268 -0.4144 0.2929  695  CYS A CB    
4427 S  SG    . CYS A 592 ? 1.7052 1.5084 2.2251 -0.1414 -0.4604 0.3230  695  CYS A SG    
4428 N  N     . GLY A 593 ? 1.4763 1.3197 2.1903 -0.1085 -0.4204 0.3207  696  GLY A N     
4429 C  CA    . GLY A 593 ? 1.7735 1.6241 2.5566 -0.1025 -0.4307 0.3352  696  GLY A CA    
4430 C  C     . GLY A 593 ? 1.6846 1.5235 2.4608 -0.1133 -0.4713 0.3585  696  GLY A C     
4431 O  O     . GLY A 593 ? 1.6973 1.5155 2.4366 -0.1263 -0.4975 0.3718  696  GLY A O     
4432 N  N     . MET A 594 ? 1.7044 1.5553 2.5140 -0.1095 -0.4767 0.3636  697  MET A N     
4433 C  CA    . MET A 594 ? 1.6964 1.5371 2.5045 -0.1214 -0.5159 0.3862  697  MET A CA    
4434 C  C     . MET A 594 ? 1.6857 1.5131 2.4037 -0.1343 -0.5275 0.3800  697  MET A C     
4435 O  O     . MET A 594 ? 1.7400 1.5505 2.4375 -0.1494 -0.5623 0.3984  697  MET A O     
4436 C  CB    . MET A 594 ? 2.1809 2.0392 3.0521 -0.1141 -0.5162 0.3922  697  MET A CB    
4437 C  CG    . MET A 594 ? 2.2794 2.1537 3.2367 -0.0982 -0.4916 0.3906  697  MET A CG    
4438 S  SD    . MET A 594 ? 2.6053 2.4930 3.5420 -0.0847 -0.4382 0.3555  697  MET A SD    
4439 C  CE    . MET A 594 ? 1.7578 1.6573 2.6385 -0.0847 -0.4286 0.3384  697  MET A CE    
4440 N  N     . TYR A 595 ? 1.7541 1.5881 2.4184 -0.1296 -0.4988 0.3552  698  TYR A N     
4441 C  CA    . TYR A 595 ? 1.5423 1.3641 2.1252 -0.1398 -0.5046 0.3482  698  TYR A CA    
4442 C  C     . TYR A 595 ? 1.5447 1.3387 2.0730 -0.1564 -0.5277 0.3582  698  TYR A C     
4443 O  O     . TYR A 595 ? 1.6718 1.4491 2.1354 -0.1684 -0.5386 0.3574  698  TYR A O     
4444 C  CB    . TYR A 595 ? 1.4546 1.2925 2.0000 -0.1296 -0.4677 0.3214  698  TYR A CB    
4445 C  CG    . TYR A 595 ? 1.7123 1.5405 2.1835 -0.1369 -0.4685 0.3138  698  TYR A CG    
4446 C  CD1   . TYR A 595 ? 1.4759 1.3043 1.9445 -0.1383 -0.4759 0.3165  698  TYR A CD1   
4447 C  CD2   . TYR A 595 ? 1.6760 1.4940 2.0816 -0.1424 -0.4603 0.3040  698  TYR A CD2   
4448 C  CE1   . TYR A 595 ? 1.5409 1.3575 1.9426 -0.1447 -0.4741 0.3093  698  TYR A CE1   
4449 C  CE2   . TYR A 595 ? 1.6460 1.4537 1.9870 -0.1482 -0.4582 0.2973  698  TYR A CE2   
4450 C  CZ    . TYR A 595 ? 1.6151 1.4212 1.9541 -0.1492 -0.4645 0.2998  698  TYR A CZ    
4451 O  OH    . TYR A 595 ? 1.5008 1.2938 1.7762 -0.1548 -0.4599 0.2928  698  TYR A OH    
4452 N  N     . LEU A 596 ? 1.4035 1.1900 1.9551 -0.1577 -0.5339 0.3675  699  LEU A N     
4453 C  CA    . LEU A 596 ? 1.5667 1.3250 2.0689 -0.1746 -0.5580 0.3796  699  LEU A CA    
4454 C  C     . LEU A 596 ? 1.6427 1.3812 2.1339 -0.1918 -0.5987 0.4028  699  LEU A C     
4455 O  O     . LEU A 596 ? 1.7123 1.4247 2.1354 -0.2092 -0.6161 0.4072  699  LEU A O     
4456 C  CB    . LEU A 596 ? 1.6124 1.3664 2.1527 -0.1721 -0.5586 0.3884  699  LEU A CB    
4457 C  CG    . LEU A 596 ? 1.4666 1.1911 1.9594 -0.1888 -0.5808 0.4010  699  LEU A CG    
4458 C  CD1   . LEU A 596 ? 1.3097 1.0257 1.7179 -0.1944 -0.5628 0.3807  699  LEU A CD1   
4459 C  CD2   . LEU A 596 ? 1.7450 1.4670 2.2882 -0.1840 -0.5798 0.4109  699  LEU A CD2   
4460 N  N     . LYS A 597 ? 1.6359 1.3860 2.1922 -0.1886 -0.6139 0.4176  700  LYS A N     
4461 C  CA    . LYS A 597 ? 1.6569 1.3907 2.2064 -0.2066 -0.6545 0.4406  700  LYS A CA    
4462 C  C     . LYS A 597 ? 1.8563 1.5792 2.3344 -0.2167 -0.6537 0.4287  700  LYS A C     
4463 O  O     . LYS A 597 ? 1.8841 1.5786 2.3017 -0.2378 -0.6792 0.4381  700  LYS A O     
4464 C  CB    . LYS A 597 ? 1.7363 1.4895 2.3787 -0.1994 -0.6676 0.4582  700  LYS A CB    
4465 C  CG    . LYS A 597 ? 1.9991 1.7640 2.7207 -0.1865 -0.6620 0.4686  700  LYS A CG    
4466 C  CD    . LYS A 597 ? 2.0466 1.8352 2.8645 -0.1752 -0.6638 0.4804  700  LYS A CD    
4467 C  CE    . LYS A 597 ? 1.8448 1.6434 2.7425 -0.1604 -0.6510 0.4878  700  LYS A CE    
4468 N  NZ    . LYS A 597 ? 2.0445 1.8667 3.0392 -0.1477 -0.6464 0.4972  700  LYS A NZ    
4469 N  N     . HIS A 598 ? 1.8164 1.5596 2.2989 -0.2023 -0.6236 0.4081  701  HIS A N     
4470 C  CA    . HIS A 598 ? 1.7140 1.4468 2.1315 -0.2096 -0.6185 0.3959  701  HIS A CA    
4471 C  C     . HIS A 598 ? 1.9147 1.6281 2.2473 -0.2160 -0.6047 0.3813  701  HIS A C     
4472 O  O     . HIS A 598 ? 2.1042 1.7947 2.3705 -0.2302 -0.6111 0.3783  701  HIS A O     
4473 C  CB    . HIS A 598 ? 1.5998 1.3599 2.0459 -0.1913 -0.5883 0.3786  701  HIS A CB    
4474 C  CG    . HIS A 598 ? 1.5887 1.3715 2.1250 -0.1814 -0.5930 0.3894  701  HIS A CG    
4475 N  ND1   . HIS A 598 ? 1.8650 1.6681 2.4677 -0.1658 -0.5776 0.3890  701  HIS A ND1   
4476 C  CD2   . HIS A 598 ? 1.5029 1.2907 2.0751 -0.1852 -0.6097 0.4008  701  HIS A CD2   
4477 C  CE1   . HIS A 598 ? 1.5861 1.4055 2.2631 -0.1597 -0.5835 0.3998  701  HIS A CE1   
4478 N  NE2   . HIS A 598 ? 1.4733 1.2852 2.1345 -0.1712 -0.6037 0.4075  701  HIS A NE2   
4479 N  N     . LEU A 599 ? 1.9208 1.6421 2.2548 -0.2065 -0.5844 0.3717  702  LEU A N     
4480 C  CA    . LEU A 599 ? 1.9154 1.6222 2.1748 -0.2114 -0.5685 0.3574  702  LEU A CA    
4481 C  C     . LEU A 599 ? 1.7439 1.4136 1.9497 -0.2348 -0.5980 0.3724  702  LEU A C     
4482 O  O     . LEU A 599 ? 1.8252 1.4736 1.9565 -0.2452 -0.5914 0.3633  702  LEU A O     
4483 C  CB    . LEU A 599 ? 1.8126 1.5394 2.0912 -0.1963 -0.5398 0.3437  702  LEU A CB    
4484 C  CG    . LEU A 599 ? 1.6387 1.3629 1.8529 -0.1957 -0.5141 0.3245  702  LEU A CG    
4485 C  CD1   . LEU A 599 ? 1.4831 1.2158 1.6659 -0.1898 -0.4943 0.3095  702  LEU A CD1   
4486 C  CD2   . LEU A 599 ? 1.4784 1.2247 1.7203 -0.1825 -0.4888 0.3127  702  LEU A CD2   
4487 N  N     . ASN A 600 ? 1.8908 1.5516 2.1335 -0.2438 -0.6299 0.3960  703  ASN A N     
4488 C  CA    . ASN A 600 ? 2.1450 1.7693 2.3360 -0.2682 -0.6612 0.4128  703  ASN A CA    
4489 C  C     . ASN A 600 ? 1.9898 1.5907 2.1378 -0.2882 -0.6855 0.4209  703  ASN A C     
4490 O  O     . ASN A 600 ? 1.7540 1.3197 1.8310 -0.3105 -0.7017 0.4262  703  ASN A O     
4491 C  CB    . ASN A 600 ? 1.7352 1.3583 1.9822 -0.2713 -0.6887 0.4379  703  ASN A CB    
4492 C  CG    . ASN A 600 ? 1.8094 1.4447 2.0822 -0.2570 -0.6661 0.4302  703  ASN A CG    
4493 O  OD1   . ASN A 600 ? 1.9374 1.5549 2.1563 -0.2643 -0.6590 0.4240  703  ASN A OD1   
4494 N  ND2   . ASN A 600 ? 2.1628 1.8269 2.5175 -0.2377 -0.6535 0.4300  703  ASN A ND2   
4495 N  N     . ARG A 601 ? 1.7532 1.3712 1.9407 -0.2822 -0.6876 0.4217  704  ARG A N     
4496 C  CA    . ARG A 601 ? 1.9122 1.5075 2.0565 -0.3018 -0.7078 0.4270  704  ARG A CA    
4497 C  C     . ARG A 601 ? 1.8635 1.4406 1.9247 -0.3053 -0.6812 0.4040  704  ARG A C     
4498 O  O     . ARG A 601 ? 1.8476 1.3891 1.8401 -0.3287 -0.6965 0.4072  704  ARG A O     
4499 C  CB    . ARG A 601 ? 1.6879 1.3076 1.8981 -0.2934 -0.7136 0.4323  704  ARG A CB    
4500 C  CG    . ARG A 601 ? 1.8616 1.4998 2.1607 -0.2899 -0.7395 0.4568  704  ARG A CG    
4501 C  CD    . ARG A 601 ? 1.7975 1.4466 2.1415 -0.2940 -0.7589 0.4687  704  ARG A CD    
4502 N  NE    . ARG A 601 ? 2.2698 1.8858 2.5495 -0.3232 -0.7887 0.4781  704  ARG A NE    
4503 C  CZ    . ARG A 601 ? 2.2835 1.9008 2.5855 -0.3349 -0.8126 0.4908  704  ARG A CZ    
4504 N  NH1   . ARG A 601 ? 2.2997 1.9506 2.6896 -0.3192 -0.8107 0.4965  704  ARG A NH1   
4505 N  NH2   . ARG A 601 ? 2.2380 1.8209 2.4714 -0.3642 -0.8384 0.4976  704  ARG A NH2   
4506 N  N     . GLN A 602 ? 1.7934 1.3939 1.8599 -0.2829 -0.6409 0.3814  705  GLN A N     
4507 C  CA    . GLN A 602 ? 1.7255 1.3121 1.7205 -0.2835 -0.6130 0.3608  705  GLN A CA    
4508 C  C     . GLN A 602 ? 2.0895 1.6443 2.0141 -0.2991 -0.6141 0.3598  705  GLN A C     
4509 O  O     . GLN A 602 ? 1.9675 1.4917 1.8186 -0.3133 -0.6081 0.3522  705  GLN A O     
4510 C  CB    . GLN A 602 ? 1.7315 1.3545 1.7550 -0.2560 -0.5723 0.3400  705  GLN A CB    
4511 C  CG    . GLN A 602 ? 1.7607 1.4169 1.8589 -0.2390 -0.5682 0.3406  705  GLN A CG    
4512 C  CD    . GLN A 602 ? 1.6444 1.3361 1.7704 -0.2138 -0.5300 0.3217  705  GLN A CD    
4513 O  OE1   . GLN A 602 ? 1.6296 1.3220 1.7147 -0.2089 -0.5055 0.3072  705  GLN A OE1   
4514 N  NE2   . GLN A 602 ? 1.7993 1.5208 1.9955 -0.1986 -0.5247 0.3224  705  GLN A NE2   
4515 N  N     . VAL A 603 ? 1.8565 1.4163 1.8021 -0.2971 -0.6199 0.3670  706  VAL A N     
4516 C  CA    . VAL A 603 ? 1.7589 1.2889 1.6404 -0.3122 -0.6209 0.3669  706  VAL A CA    
4517 C  C     . VAL A 603 ? 2.0750 1.5610 1.9034 -0.3432 -0.6571 0.3845  706  VAL A C     
4518 O  O     . VAL A 603 ? 1.9823 1.4332 1.7304 -0.3604 -0.6519 0.3781  706  VAL A O     
4519 C  CB    . VAL A 603 ? 2.0088 1.5539 1.9298 -0.3032 -0.6199 0.3719  706  VAL A CB    
4520 C  CG1   . VAL A 603 ? 1.7554 1.2673 1.6105 -0.3209 -0.6238 0.3740  706  VAL A CG1   
4521 C  CG2   . VAL A 603 ? 1.9353 1.5205 1.8972 -0.2761 -0.5822 0.3523  706  VAL A CG2   
4522 N  N     . GLU A 604 ? 2.0781 1.5649 1.9505 -0.3519 -0.6941 0.4074  707  GLU A N     
4523 C  CA    . GLU A 604 ? 2.0504 1.4972 1.8741 -0.3837 -0.7324 0.4261  707  GLU A CA    
4524 C  C     . GLU A 604 ? 2.2273 1.6524 1.9954 -0.3962 -0.7269 0.4154  707  GLU A C     
4525 O  O     . GLU A 604 ? 2.2722 1.6536 1.9617 -0.4239 -0.7404 0.4185  707  GLU A O     
4526 C  CB    . GLU A 604 ? 2.2994 1.7582 2.1928 -0.3884 -0.7733 0.4546  707  GLU A CB    
4527 C  CG    . GLU A 604 ? 2.2043 1.6259 2.0544 -0.4230 -0.8183 0.4774  707  GLU A CG    
4528 C  CD    . GLU A 604 ? 2.5484 1.9307 2.3292 -0.4462 -0.8334 0.4865  707  GLU A CD    
4529 O  OE1   . GLU A 604 ? 2.6799 2.0334 2.3781 -0.4553 -0.8110 0.4683  707  GLU A OE1   
4530 O  OE2   . GLU A 604 ? 2.5642 1.9439 2.3746 -0.4553 -0.8672 0.5127  707  GLU A OE2   
4531 N  N     . ALA A 605 ? 1.9768 1.4298 1.7826 -0.3769 -0.7057 0.4025  708  ALA A N     
4532 C  CA    . ALA A 605 ? 1.6876 1.1203 1.4433 -0.3865 -0.6961 0.3909  708  ALA A CA    
4533 C  C     . ALA A 605 ? 2.0239 1.4326 1.7008 -0.3879 -0.6613 0.3692  708  ALA A C     
4534 O  O     . ALA A 605 ? 1.8486 1.2156 1.4505 -0.4106 -0.6633 0.3656  708  ALA A O     
4535 C  CB    . ALA A 605 ? 2.0093 1.4791 1.8281 -0.3637 -0.6800 0.3827  708  ALA A CB    
4536 N  N     . MET A 606 ? 2.1450 1.5788 1.8381 -0.3648 -0.6285 0.3548  709  MET A N     
4537 C  CA    . MET A 606 ? 2.2941 1.7102 1.9212 -0.3639 -0.5937 0.3352  709  MET A CA    
4538 C  C     . MET A 606 ? 2.2233 1.5955 1.7788 -0.3899 -0.6062 0.3412  709  MET A C     
4539 O  O     . MET A 606 ? 2.2372 1.5741 1.7175 -0.4031 -0.5890 0.3300  709  MET A O     
4540 C  CB    . MET A 606 ? 2.0936 1.5517 1.7616 -0.3337 -0.5583 0.3203  709  MET A CB    
4541 C  CG    . MET A 606 ? 1.9729 1.4682 1.6909 -0.3092 -0.5366 0.3096  709  MET A CG    
4542 S  SD    . MET A 606 ? 2.1252 1.5964 1.7832 -0.3126 -0.5109 0.2940  709  MET A SD    
4543 C  CE    . MET A 606 ? 2.6247 2.0826 2.2225 -0.3110 -0.4764 0.2788  709  MET A CE    
4544 N  N     . GLU A 607 ? 2.5314 1.9036 2.1090 -0.3977 -0.6349 0.3592  710  GLU A N     
4545 C  CA    . GLU A 607 ? 2.5598 1.8890 2.0691 -0.4238 -0.6493 0.3670  710  GLU A CA    
4546 C  C     . GLU A 607 ? 2.6445 1.9252 2.0879 -0.4575 -0.6763 0.3766  710  GLU A C     
4547 O  O     . GLU A 607 ? 2.6834 1.9192 2.0438 -0.4806 -0.6734 0.3734  710  GLU A O     
4548 C  CB    . GLU A 607 ? 2.5470 1.8883 2.1007 -0.4235 -0.6751 0.3862  710  GLU A CB    
4549 C  CG    . GLU A 607 ? 2.7289 2.0416 2.2265 -0.4371 -0.6717 0.3868  710  GLU A CG    
4550 C  CD    . GLU A 607 ? 2.9327 2.1898 2.3504 -0.4747 -0.7011 0.4004  710  GLU A CD    
4551 O  OE1   . GLU A 607 ? 3.0748 2.3208 2.4987 -0.4912 -0.7368 0.4178  710  GLU A OE1   
4552 O  OE2   . GLU A 607 ? 2.8371 2.0612 2.1847 -0.4889 -0.6883 0.3939  710  GLU A OE2   
4553 N  N     . LYS A 608 ? 2.4850 1.7731 1.9626 -0.4622 -0.7018 0.3879  711  LYS A N     
4554 C  CA    . LYS A 608 ? 2.3786 1.6221 1.7942 -0.4954 -0.7269 0.3958  711  LYS A CA    
4555 C  C     . LYS A 608 ? 2.5521 1.7684 1.9008 -0.4997 -0.6927 0.3725  711  LYS A C     
4556 O  O     . LYS A 608 ? 2.8212 1.9911 2.1004 -0.5305 -0.7070 0.3748  711  LYS A O     
4557 C  CB    . LYS A 608 ? 2.2586 1.5219 1.7364 -0.4982 -0.7626 0.4144  711  LYS A CB    
4558 C  CG    . LYS A 608 ? 2.1973 1.4684 1.7193 -0.5080 -0.8079 0.4443  711  LYS A CG    
4559 C  CD    . LYS A 608 ? 2.4876 1.7054 1.9267 -0.5476 -0.8393 0.4593  711  LYS A CD    
4560 C  CE    . LYS A 608 ? 2.4354 1.6617 1.9199 -0.5560 -0.8839 0.4911  711  LYS A CE    
4561 N  NZ    . LYS A 608 ? 2.4066 1.6602 1.9374 -0.5305 -0.8665 0.4895  711  LYS A NZ    
4562 N  N     . LEU A 609 ? 2.3918 1.6349 1.7599 -0.4704 -0.6482 0.3509  712  LEU A N     
4563 C  CA    . LEU A 609 ? 2.5262 1.7446 1.8352 -0.4713 -0.6114 0.3292  712  LEU A CA    
4564 C  C     . LEU A 609 ? 2.6820 1.8748 1.9269 -0.4748 -0.5811 0.3159  712  LEU A C     
4565 O  O     . LEU A 609 ? 2.6075 1.7618 1.7828 -0.4869 -0.5572 0.3020  712  LEU A O     
4566 C  CB    . LEU A 609 ? 2.4878 1.7505 1.8560 -0.4375 -0.5801 0.3149  712  LEU A CB    
4567 C  CG    . LEU A 609 ? 2.3760 1.6641 1.8065 -0.4315 -0.6012 0.3240  712  LEU A CG    
4568 C  CD1   . LEU A 609 ? 2.1587 1.4899 1.6428 -0.3974 -0.5663 0.3090  712  LEU A CD1   
4569 C  CD2   . LEU A 609 ? 2.2461 1.4894 1.6220 -0.4624 -0.6211 0.3283  712  LEU A CD2   
4570 N  N     . ILE A 610 ? 2.6290 1.8412 1.8967 -0.4650 -0.5802 0.3197  713  ILE A N     
4571 C  CA    . ILE A 610 ? 2.7099 1.9009 1.9219 -0.4678 -0.5508 0.3075  713  ILE A CA    
4572 C  C     . ILE A 610 ? 2.9553 2.0839 2.0781 -0.5069 -0.5707 0.3154  713  ILE A C     
4573 O  O     . ILE A 610 ? 3.0114 2.1010 2.0602 -0.5192 -0.5434 0.3017  713  ILE A O     
4574 C  CB    . ILE A 610 ? 2.5380 1.7702 1.8039 -0.4457 -0.5433 0.3086  713  ILE A CB    
4575 C  CG1   . ILE A 610 ? 2.6231 1.9149 1.9720 -0.4095 -0.5232 0.3001  713  ILE A CG1   
4576 C  CG2   . ILE A 610 ? 2.6493 1.8617 1.8604 -0.4490 -0.5125 0.2962  713  ILE A CG2   
4577 C  CD1   . ILE A 610 ? 2.4032 1.7356 1.8067 -0.3892 -0.5161 0.3005  713  ILE A CD1   
4578 N  N     . ASN A 611 ? 3.2287 2.3463 2.3572 -0.5275 -0.6181 0.3383  714  ASN A N     
4579 C  CA    . ASN A 611 ? 3.2665 2.3251 2.3092 -0.5668 -0.6408 0.3484  714  ASN A CA    
4580 C  C     . ASN A 611 ? 3.3678 2.3768 2.3358 -0.5937 -0.6396 0.3414  714  ASN A C     
4581 O  O     . ASN A 611 ? 3.4707 2.4244 2.3468 -0.6216 -0.6315 0.3360  714  ASN A O     
4582 C  CB    . ASN A 611 ? 3.3995 2.4624 2.4736 -0.5811 -0.6940 0.3776  714  ASN A CB    
4583 C  CG    . ASN A 611 ? 3.5336 2.6156 2.6603 -0.5824 -0.7277 0.3922  714  ASN A CG    
4584 O  OD1   . ASN A 611 ? 3.2158 2.3288 2.3889 -0.5601 -0.7095 0.3809  714  ASN A OD1   
4585 N  ND2   . ASN A 611 ? 3.4976 2.5619 2.6184 -0.6092 -0.7775 0.4185  714  ASN A ND2   
4586 N  N     . LEU A 612 ? 3.0233 2.0491 2.0274 -0.5869 -0.6459 0.3409  715  LEU A N     
4587 C  CA    . LEU A 612 ? 3.0165 1.9947 1.9512 -0.6128 -0.6435 0.3334  715  LEU A CA    
4588 C  C     . LEU A 612 ? 3.1547 2.1070 2.0321 -0.6069 -0.5886 0.3064  715  LEU A C     
4589 O  O     . LEU A 612 ? 3.0753 1.9672 1.8606 -0.6374 -0.5805 0.2990  715  LEU A O     
4590 C  CB    . LEU A 612 ? 2.8936 1.8998 1.8867 -0.6035 -0.6585 0.3376  715  LEU A CB    
4591 C  CG    . LEU A 612 ? 3.0232 2.0463 2.0652 -0.6161 -0.7153 0.3658  715  LEU A CG    
4592 C  CD1   . LEU A 612 ? 2.5296 1.5702 1.6134 -0.6123 -0.7254 0.3671  715  LEU A CD1   
4593 C  CD2   . LEU A 612 ? 3.2099 2.1791 2.1747 -0.6611 -0.7538 0.3829  715  LEU A CD2   
4594 N  N     . THR A 613 ? 3.1897 2.1863 2.1205 -0.5686 -0.5498 0.2920  716  THR A N     
4595 C  CA    . THR A 613 ? 3.0282 2.0053 1.9138 -0.5603 -0.4968 0.2688  716  THR A CA    
4596 C  C     . THR A 613 ? 3.0717 2.0114 1.8895 -0.5778 -0.4846 0.2657  716  THR A C     
4597 O  O     . THR A 613 ? 3.0514 1.9490 1.8005 -0.5878 -0.4487 0.2495  716  THR A O     
4598 C  CB    . THR A 613 ? 2.7793 1.8174 1.7428 -0.5159 -0.4624 0.2575  716  THR A CB    
4599 O  OG1   . THR A 613 ? 2.8582 1.9420 1.8829 -0.4979 -0.4746 0.2668  716  THR A OG1   
4600 C  CG2   . THR A 613 ? 2.6337 1.7011 1.6526 -0.5001 -0.4673 0.2575  716  THR A CG2   
4601 N  N     . ASP A 614 ? 3.0895 2.0423 1.9259 -0.5816 -0.5122 0.2811  717  ASP A N     
4602 C  CA    . ASP A 614 ? 3.1403 2.0542 1.9092 -0.6014 -0.5043 0.2801  717  ASP A CA    
4603 C  C     . ASP A 614 ? 3.2318 2.0734 1.9018 -0.6481 -0.5266 0.2862  717  ASP A C     
4604 O  O     . ASP A 614 ? 3.4338 2.2251 2.0214 -0.6681 -0.5024 0.2756  717  ASP A O     
4605 C  CB    . ASP A 614 ? 3.1536 2.1013 1.9721 -0.5923 -0.5279 0.2956  717  ASP A CB    
4606 C  CG    . ASP A 614 ? 3.0021 2.0137 1.9025 -0.5502 -0.4995 0.2865  717  ASP A CG    
4607 O  OD1   . ASP A 614 ? 3.1275 2.1469 2.0234 -0.5326 -0.4542 0.2669  717  ASP A OD1   
4608 O  OD2   . ASP A 614 ? 2.9595 2.0129 1.9288 -0.5355 -0.5223 0.2995  717  ASP A OD2   
4609 N  N     . ILE A 615 ? 3.0960 1.9308 1.7721 -0.6673 -0.5725 0.3034  718  ILE A N     
4610 C  CA    . ILE A 615 ? 3.1874 1.9537 1.7678 -0.7144 -0.5964 0.3097  718  ILE A CA    
4611 C  C     . ILE A 615 ? 3.3218 2.0461 1.8402 -0.7246 -0.5606 0.2878  718  ILE A C     
4612 O  O     . ILE A 615 ? 3.5843 2.2407 2.0019 -0.7622 -0.5572 0.2829  718  ILE A O     
4613 C  CB    . ILE A 615 ? 3.0836 1.8596 1.6952 -0.7320 -0.6582 0.3367  718  ILE A CB    
4614 C  CG1   . ILE A 615 ? 3.3376 2.1520 2.0115 -0.7212 -0.6907 0.3591  718  ILE A CG1   
4615 C  CG2   . ILE A 615 ? 3.3036 2.0092 1.8137 -0.7839 -0.6865 0.3448  718  ILE A CG2   
4616 C  CD1   . ILE A 615 ? 3.1105 1.8869 1.7184 -0.7429 -0.6926 0.3641  718  ILE A CD1   
4617 N  N     . LEU A 616 ? 3.2758 2.0370 1.8508 -0.6923 -0.5317 0.2742  719  LEU A N     
4618 C  CA    . LEU A 616 ? 3.1151 1.8388 1.6391 -0.6979 -0.4937 0.2533  719  LEU A CA    
4619 C  C     . LEU A 616 ? 3.2702 1.9745 1.7552 -0.6866 -0.4348 0.2313  719  LEU A C     
4620 O  O     . LEU A 616 ? 3.3011 1.9595 1.7256 -0.6978 -0.4005 0.2140  719  LEU A O     
4621 C  CB    . LEU A 616 ? 3.0027 1.7727 1.6038 -0.6684 -0.4874 0.2493  719  LEU A CB    
4622 C  CG    . LEU A 616 ? 2.9692 1.7486 1.5996 -0.6831 -0.5380 0.2671  719  LEU A CG    
4623 C  CD1   . LEU A 616 ? 2.7011 1.5257 1.4065 -0.6514 -0.5240 0.2606  719  LEU A CD1   
4624 C  CD2   . LEU A 616 ? 2.8948 1.6011 1.4255 -0.7328 -0.5576 0.2689  719  LEU A CD2   
4625 N  N     . LYS A 617 ? 3.4854 2.2228 2.0046 -0.6651 -0.4214 0.2317  720  LYS A N     
4626 C  CA    . LYS A 617 ? 3.5120 2.2368 2.0023 -0.6533 -0.3666 0.2128  720  LYS A CA    
4627 C  C     . LYS A 617 ? 3.7214 2.3988 2.1353 -0.6825 -0.3681 0.2152  720  LYS A C     
4628 O  O     . LYS A 617 ? 3.7602 2.3785 2.0903 -0.7034 -0.3352 0.2009  720  LYS A O     
4629 C  CB    . LYS A 617 ? 3.3902 2.1899 1.9770 -0.6058 -0.3435 0.2091  720  LYS A CB    
4630 C  CG    . LYS A 617 ? 3.4741 2.3146 2.1253 -0.5749 -0.3264 0.2019  720  LYS A CG    
4631 C  CD    . LYS A 617 ? 3.3202 2.2319 2.0590 -0.5310 -0.3028 0.1982  720  LYS A CD    
4632 C  CE    . LYS A 617 ? 3.3776 2.2812 2.0941 -0.5179 -0.2465 0.1810  720  LYS A CE    
4633 N  NZ    . LYS A 617 ? 3.4096 2.2874 2.0784 -0.5342 -0.2401 0.1810  720  LYS A NZ    
4634 N  N     . GLN A 618 ? 3.8712 2.5715 2.3119 -0.6848 -0.4040 0.2330  721  GLN A N     
4635 C  CA    . GLN A 618 ? 3.8869 2.5421 2.2552 -0.7132 -0.4076 0.2370  721  GLN A CA    
4636 C  C     . GLN A 618 ? 3.9160 2.4969 2.1842 -0.7636 -0.4353 0.2435  721  GLN A C     
4637 O  O     . GLN A 618 ? 4.0124 2.5313 2.1875 -0.7918 -0.4141 0.2346  721  GLN A O     
4638 C  CB    . GLN A 618 ? 3.7032 2.4018 2.1292 -0.7024 -0.4404 0.2558  721  GLN A CB    
4639 C  CG    . GLN A 618 ? 3.6492 2.4167 2.1646 -0.6571 -0.4124 0.2486  721  GLN A CG    
4640 C  CD    . GLN A 618 ? 3.8579 2.6604 2.4217 -0.6496 -0.4412 0.2656  721  GLN A CD    
4641 O  OE1   . GLN A 618 ? 3.9502 2.7265 2.4837 -0.6768 -0.4828 0.2843  721  GLN A OE1   
4642 N  NE2   . GLN A 618 ? 3.7593 2.6205 2.3981 -0.6133 -0.4194 0.2598  721  GLN A NE2   
4643 N  N     . GLU A 619 ? 3.8938 2.4793 2.1788 -0.7766 -0.4821 0.2593  722  GLU A N     
4644 C  CA    . GLU A 619 ? 3.9101 2.4291 2.1045 -0.8255 -0.5125 0.2668  722  GLU A CA    
4645 C  C     . GLU A 619 ? 3.9976 2.4932 2.1687 -0.8308 -0.4938 0.2517  722  GLU A C     
4646 O  O     . GLU A 619 ? 3.9939 2.5340 2.2345 -0.7948 -0.4692 0.2412  722  GLU A O     
4647 C  CB    . GLU A 619 ? 3.9127 2.4502 2.1391 -0.8410 -0.5814 0.2976  722  GLU A CB    
4648 C  CG    . GLU A 619 ? 3.9095 2.4745 2.1717 -0.8333 -0.6019 0.3139  722  GLU A CG    
4649 C  CD    . GLU A 619 ? 3.8281 2.4229 2.1532 -0.8418 -0.6617 0.3393  722  GLU A CD    
4650 O  OE1   . GLU A 619 ? 3.8423 2.4270 2.1674 -0.8609 -0.6893 0.3461  722  GLU A OE1   
4651 O  OE2   . GLU A 619 ? 3.6768 2.3047 2.0533 -0.8294 -0.6794 0.3533  722  GLU A OE2   
4652 N  N     . LYS A 620 ? 4.1410 2.5641 2.2104 -0.8776 -0.5055 0.2508  723  LYS A N     
4653 C  CA    . LYS A 620 ? 4.2968 2.6851 2.3283 -0.8918 -0.4918 0.2372  723  LYS A CA    
4654 C  C     . LYS A 620 ? 4.2557 2.6457 2.2951 -0.8611 -0.4215 0.2090  723  LYS A C     
4655 O  O     . LYS A 620 ? 4.3514 2.7119 2.3430 -0.8627 -0.3810 0.1957  723  LYS A O     
4656 C  CB    . LYS A 620 ? 4.0916 2.5253 2.1977 -0.8838 -0.5375 0.2539  723  LYS A CB    
4657 C  CG    . LYS A 620 ? 4.1546 2.5936 2.2674 -0.9105 -0.6059 0.2841  723  LYS A CG    
4658 C  CD    . LYS A 620 ? 3.8627 2.3502 2.0561 -0.8997 -0.6481 0.3011  723  LYS A CD    
4659 C  CE    . LYS A 620 ? 3.9523 2.4590 2.1918 -0.9173 -0.7044 0.3297  723  LYS A CE    
4660 N  NZ    . LYS A 620 ? 3.8658 2.4105 2.1556 -0.8974 -0.7135 0.3413  723  LYS A NZ    
4661 N  N     . LYS A 621 ? 4.2236 2.6466 2.3219 -0.8335 -0.4047 0.2004  724  LYS A N     
4662 C  CA    . LYS A 621 ? 4.2420 2.6742 2.3610 -0.8007 -0.3408 0.1770  724  LYS A CA    
4663 C  C     . LYS A 621 ? 4.2928 2.6420 2.3030 -0.8287 -0.2942 0.1553  724  LYS A C     
4664 O  O     . LYS A 621 ? 4.4994 2.8487 2.5191 -0.8039 -0.2367 0.1361  724  LYS A O     
4665 C  CB    . LYS A 621 ? 4.1776 2.6698 2.3696 -0.7583 -0.3160 0.1757  724  LYS A CB    
4666 C  CG    . LYS A 621 ? 4.1583 2.6975 2.4231 -0.7120 -0.2702 0.1616  724  LYS A CG    
4667 C  CD    . LYS A 621 ? 4.0956 2.6907 2.4243 -0.6754 -0.2477 0.1611  724  LYS A CD    
4668 C  CE    . LYS A 621 ? 4.0953 2.6441 2.3516 -0.6924 -0.2163 0.1518  724  LYS A CE    
4669 N  NZ    . LYS A 621 ? 3.8046 2.4085 2.1234 -0.6586 -0.1955 0.1517  724  LYS A NZ    
4670 N  N     . ASP A 622 ? 4.1509 2.4280 2.0579 -0.8806 -0.3167 0.1583  725  ASP A N     
4671 C  CA    . ASP A 622 ? 4.1810 2.3730 1.9780 -0.9107 -0.2711 0.1366  725  ASP A CA    
4672 C  C     . ASP A 622 ? 4.1631 2.3304 1.9483 -0.9116 -0.2469 0.1214  725  ASP A C     
4673 O  O     . ASP A 622 ? 4.0962 2.2387 1.8634 -0.8980 -0.1855 0.0995  725  ASP A O     
4674 C  CB    . ASP A 622 ? 4.3838 2.5047 2.0698 -0.9687 -0.3048 0.1451  725  ASP A CB    
4675 C  CG    . ASP A 622 ? 4.4399 2.4788 2.0269 -0.9964 -0.2523 0.1195  725  ASP A CG    
4676 O  OD1   . ASP A 622 ? 4.5954 2.6233 2.1748 -0.9735 -0.1897 0.1007  725  ASP A OD1   
4677 O  OD2   . ASP A 622 ? 4.4238 2.4128 1.9550 -1.0391 -0.2707 0.1199  725  ASP A OD2   
4678 N  N     . GLU A 623 ? 4.2539 2.4281 2.0516 -0.9272 -0.2938 0.1335  726  GLU A N     
4679 C  CA    . GLU A 623 ? 4.2816 2.4352 2.0722 -0.9297 -0.2773 0.1213  726  GLU A CA    
4680 C  C     . GLU A 623 ? 4.2453 2.4837 2.1595 -0.8864 -0.2955 0.1313  726  GLU A C     
4681 O  O     . GLU A 623 ? 4.3466 2.6447 2.3311 -0.8739 -0.3431 0.1529  726  GLU A O     
4682 C  CB    . GLU A 623 ? 4.1821 2.2672 1.8773 -0.9887 -0.3152 0.1256  726  GLU A CB    
4683 C  CG    . GLU A 623 ? 4.3746 2.4105 2.0259 -1.0024 -0.2849 0.1065  726  GLU A CG    
4684 C  CD    . GLU A 623 ? 4.5538 2.6239 2.2586 -1.0032 -0.3300 0.1195  726  GLU A CD    
4685 O  OE1   . GLU A 623 ? 4.2768 2.4279 2.0871 -0.9710 -0.3646 0.1382  726  GLU A OE1   
4686 O  OE2   . GLU A 623 ? 4.7038 2.7182 2.3443 -1.0372 -0.3301 0.1108  726  GLU A OE2   
4687 N  N     . THR A 624 ? 4.1846 2.4267 2.1251 -0.8635 -0.2553 0.1157  727  THR A N     
4688 C  CA    . THR A 624 ? 4.3655 2.6855 2.4210 -0.8192 -0.2618 0.1221  727  THR A CA    
4689 C  C     . THR A 624 ? 4.3552 2.6526 2.4002 -0.8324 -0.2660 0.1170  727  THR A C     
4690 O  O     . THR A 624 ? 4.2992 2.6185 2.3924 -0.8009 -0.2313 0.1066  727  THR A O     
4691 C  CB    . THR A 624 ? 4.3821 2.7451 2.5014 -0.7682 -0.2061 0.1103  727  THR A CB    
4692 O  OG1   . THR A 624 ? 4.5788 2.8816 2.6354 -0.7735 -0.1456 0.0873  727  THR A OG1   
4693 C  CG2   . THR A 624 ? 4.0118 2.4046 2.1508 -0.7541 -0.2055 0.1167  727  THR A CG2   
4694 N  N     . GLN A 625 ? 4.3182 2.5714 2.2995 -0.8806 -0.3102 0.1253  728  GLN A N     
4695 C  CA    . GLN A 625 ? 4.3905 2.6254 2.3644 -0.8970 -0.3229 0.1232  728  GLN A CA    
4696 C  C     . GLN A 625 ? 4.3674 2.6282 2.3664 -0.9203 -0.3978 0.1487  728  GLN A C     
4697 O  O     . GLN A 625 ? 4.2205 2.5425 2.3111 -0.8955 -0.4213 0.1599  728  GLN A O     
4698 C  CB    . GLN A 625 ? 4.4616 2.5977 2.3129 -0.9400 -0.2905 0.1024  728  GLN A CB    
4699 C  CG    . GLN A 625 ? 4.5553 2.6652 2.3899 -0.9611 -0.3012 0.0984  728  GLN A CG    
4700 C  CD    . GLN A 625 ? 4.4518 2.5202 2.2164 -1.0197 -0.3611 0.1120  728  GLN A CD    
4701 O  OE1   . GLN A 625 ? 4.2881 2.3268 1.9836 -1.0472 -0.3725 0.1197  728  GLN A OE1   
4702 N  NE2   . GLN A 625 ? 4.4243 2.5147 2.2237 -1.0259 -0.3941 0.1220  728  GLN A NE2   
4703 N  N     . LYS A 626 ? 4.3951 2.6098 2.3145 -0.9682 -0.4352 0.1589  729  LYS A N     
4704 C  CA    . LYS A 626 ? 4.3210 2.5637 2.2683 -0.9897 -0.5088 0.1872  729  LYS A CA    
4705 C  C     . LYS A 626 ? 4.1179 2.4182 2.1283 -0.9676 -0.5367 0.2072  729  LYS A C     
4706 O  O     . LYS A 626 ? 4.0492 2.4116 2.1462 -0.9532 -0.5826 0.2295  729  LYS A O     
4707 C  CB    . LYS A 626 ? 4.1812 2.3654 2.0308 -1.0414 -0.5309 0.1985  729  LYS A CB    
4708 C  CG    . LYS A 626 ? 4.1036 2.2611 1.9240 -1.0597 -0.5263 0.1935  729  LYS A CG    
4709 C  CD    . LYS A 626 ? 4.1201 2.2314 1.8583 -1.1057 -0.5467 0.2117  729  LYS A CD    
4710 C  CE    . LYS A 626 ? 4.3776 2.4640 2.0859 -1.1250 -0.5436 0.2067  729  LYS A CE    
4711 N  NZ    . LYS A 626 ? 4.3338 2.3731 1.9619 -1.1725 -0.5641 0.2255  729  LYS A NZ    
4712 N  N     . VAL A 627 ? 4.0025 2.2823 1.9721 -0.9646 -0.5080 0.1994  730  VAL A N     
4713 C  CA    . VAL A 627 ? 4.0536 2.3832 2.0773 -0.9450 -0.5312 0.2171  730  VAL A CA    
4714 C  C     . VAL A 627 ? 4.0013 2.4198 2.1552 -0.8856 -0.5198 0.2197  730  VAL A C     
4715 O  O     . VAL A 627 ? 3.8401 2.3160 2.0686 -0.8689 -0.5571 0.2405  730  VAL A O     
4716 C  CB    . VAL A 627 ? 4.1624 2.4473 2.1106 -0.9549 -0.4966 0.2055  730  VAL A CB    
4717 C  CG1   . VAL A 627 ? 3.9632 2.2939 1.9600 -0.9397 -0.5238 0.2247  730  VAL A CG1   
4718 C  CG2   . VAL A 627 ? 3.7613 1.9546 1.5783 -1.0140 -0.5016 0.2014  730  VAL A CG2   
4719 N  N     . GLN A 628 ? 4.0130 2.4435 2.1959 -0.8534 -0.4681 0.1992  731  GLN A N     
4720 C  CA    . GLN A 628 ? 4.0910 2.6040 2.3933 -0.7994 -0.4576 0.2015  731  GLN A CA    
4721 C  C     . GLN A 628 ? 3.9179 2.4767 2.2948 -0.7948 -0.5038 0.2189  731  GLN A C     
4722 O  O     . GLN A 628 ? 4.0324 2.6633 2.5116 -0.7554 -0.5098 0.2271  731  GLN A O     
4723 C  CB    . GLN A 628 ? 4.1211 2.6328 2.4328 -0.7687 -0.3927 0.1773  731  GLN A CB    
4724 C  CG    . GLN A 628 ? 3.9860 2.4644 2.2720 -0.7821 -0.3819 0.1668  731  GLN A CG    
4725 C  CD    . GLN A 628 ? 3.9438 2.4425 2.2722 -0.7414 -0.3248 0.1489  731  GLN A CD    
4726 O  OE1   . GLN A 628 ? 3.8933 2.4373 2.2771 -0.7021 -0.2963 0.1458  731  GLN A OE1   
4727 N  NE2   . GLN A 628 ? 3.9929 2.4582 2.2958 -0.7516 -0.3086 0.1380  731  GLN A NE2   
4728 N  N     . MET A 629 ? 3.8345 2.3524 2.1620 -0.8352 -0.5358 0.2247  732  MET A N     
4729 C  CA    . MET A 629 ? 3.8162 2.3740 2.2117 -0.8346 -0.5798 0.2417  732  MET A CA    
4730 C  C     . MET A 629 ? 3.9655 2.5075 2.3338 -0.8776 -0.6459 0.2670  732  MET A C     
4731 O  O     . MET A 629 ? 4.0650 2.6295 2.4763 -0.8865 -0.6860 0.2823  732  MET A O     
4732 C  CB    . MET A 629 ? 3.9694 2.5027 2.3487 -0.8393 -0.5572 0.2263  732  MET A CB    
4733 C  CG    . MET A 629 ? 3.9056 2.5042 2.3918 -0.8092 -0.5717 0.2348  732  MET A CG    
4734 S  SD    . MET A 629 ? 3.9394 2.6216 2.5401 -0.7418 -0.5382 0.2312  732  MET A SD    
4735 C  CE    . MET A 629 ? 3.8010 2.4425 2.3441 -0.7261 -0.4612 0.2005  732  MET A CE    
4736 N  N     . LYS A 630 ? 3.9969 2.5011 2.2957 -0.9051 -0.6586 0.2729  733  LYS A N     
4737 C  CA    . LYS A 630 ? 4.0380 2.5315 2.3154 -0.9444 -0.7239 0.3007  733  LYS A CA    
4738 C  C     . LYS A 630 ? 3.9729 2.5345 2.3449 -0.9156 -0.7538 0.3235  733  LYS A C     
4739 O  O     . LYS A 630 ? 3.9659 2.5784 2.4225 -0.9059 -0.7941 0.3444  733  LYS A O     
4740 C  CB    . LYS A 630 ? 4.1165 2.5399 2.2840 -0.9816 -0.7113 0.3009  733  LYS A CB    
4741 C  CG    . LYS A 630 ? 4.1123 2.5378 2.2880 -1.0064 -0.7581 0.3363  733  LYS A CG    
4742 C  CD    . LYS A 630 ? 4.2940 2.6509 2.3678 -1.0418 -0.7414 0.3342  733  LYS A CD    
4743 C  CE    . LYS A 630 ? 4.2416 2.6005 2.3298 -1.0671 -0.7886 0.3683  733  LYS A CE    
4744 N  NZ    . LYS A 630 ? 4.1420 2.4338 2.1338 -1.1033 -0.7733 0.3655  733  LYS A NZ    
4745 N  N     . PHE A 631 ? 3.8158 2.3777 2.1751 -0.9019 -0.7322 0.3194  734  PHE A N     
4746 C  CA    . PHE A 631 ? 3.6191 2.2408 2.0628 -0.8748 -0.7556 0.3390  734  PHE A CA    
4747 C  C     . PHE A 631 ? 3.5544 2.2534 2.1210 -0.8225 -0.7413 0.3370  734  PHE A C     
4748 O  O     . PHE A 631 ? 3.6835 2.4368 2.3351 -0.8033 -0.7714 0.3572  734  PHE A O     
4749 C  CB    . PHE A 631 ? 3.6163 2.2195 2.0171 -0.8700 -0.7276 0.3308  734  PHE A CB    
4750 C  CG    . PHE A 631 ? 3.6671 2.3220 2.1412 -0.8482 -0.7523 0.3511  734  PHE A CG    
4751 C  CD1   . PHE A 631 ? 3.7077 2.3579 2.1869 -0.8728 -0.7967 0.3765  734  PHE A CD1   
4752 C  CD2   . PHE A 631 ? 3.6554 2.3684 2.2127 -0.7988 -0.7206 0.3425  734  PHE A CD2   
4753 C  CE1   . PHE A 631 ? 3.7430 2.4396 2.2951 -0.8516 -0.8149 0.3933  734  PHE A CE1   
4754 C  CE2   . PHE A 631 ? 3.7118 2.4689 2.3342 -0.7800 -0.7413 0.3598  734  PHE A CE2   
4755 C  CZ    . PHE A 631 ? 3.7833 2.5277 2.3914 -0.8087 -0.7940 0.3873  734  PHE A CZ    
4756 N  N     . LEU A 632 ? 3.3768 2.0805 1.9540 -0.7996 -0.6955 0.3137  735  LEU A N     
4757 C  CA    . LEU A 632 ? 3.2523 2.0269 1.9407 -0.7515 -0.6806 0.3113  735  LEU A CA    
4758 C  C     . LEU A 632 ? 3.3546 2.1626 2.1102 -0.7552 -0.7257 0.3308  735  LEU A C     
4759 O  O     . LEU A 632 ? 3.3953 2.2648 2.2485 -0.7278 -0.7446 0.3454  735  LEU A O     
4760 C  CB    . LEU A 632 ? 3.2721 2.0396 1.9498 -0.7284 -0.6208 0.2831  735  LEU A CB    
4761 C  CG    . LEU A 632 ? 3.2838 2.1205 2.0676 -0.6794 -0.6002 0.2786  735  LEU A CG    
4762 C  CD1   . LEU A 632 ? 2.8224 1.6713 1.6104 -0.6456 -0.5428 0.2580  735  LEU A CD1   
4763 C  CD2   . LEU A 632 ? 3.4735 2.3088 2.2726 -0.6818 -0.6002 0.2742  735  LEU A CD2   
4764 N  N     . VAL A 633 ? 3.2892 2.0567 1.9942 -0.7897 -0.7427 0.3312  736  VAL A N     
4765 C  CA    . VAL A 633 ? 3.3262 2.1249 2.0950 -0.7950 -0.7851 0.3498  736  VAL A CA    
4766 C  C     . VAL A 633 ? 3.2362 2.0431 2.0208 -0.8203 -0.8483 0.3822  736  VAL A C     
4767 O  O     . VAL A 633 ? 3.2651 2.1159 2.1314 -0.8145 -0.8847 0.4023  736  VAL A O     
4768 C  CB    . VAL A 633 ? 3.4280 2.1817 2.1397 -0.8244 -0.7821 0.3393  736  VAL A CB    
4769 C  CG1   . VAL A 633 ? 3.4075 2.1465 2.0972 -0.8008 -0.7175 0.3080  736  VAL A CG1   
4770 C  CG2   . VAL A 633 ? 3.3964 2.0780 1.9947 -0.8819 -0.8100 0.3453  736  VAL A CG2   
4771 N  N     . GLU A 634 ? 3.3244 2.0906 2.0353 -0.8481 -0.8620 0.3889  737  GLU A N     
4772 C  CA    . GLU A 634 ? 3.3221 2.1010 2.0657 -0.8620 -0.9062 0.4226  737  GLU A CA    
4773 C  C     . GLU A 634 ? 3.4051 2.2478 2.2492 -0.8266 -0.9194 0.4365  737  GLU A C     
4774 O  O     . GLU A 634 ? 3.4907 2.3672 2.4104 -0.8247 -0.9538 0.4641  737  GLU A O     
4775 C  CB    . GLU A 634 ? 3.4710 2.1885 2.1181 -0.8966 -0.9023 0.4254  737  GLU A CB    
4776 C  CG    . GLU A 634 ? 3.7000 2.3552 2.2553 -0.9370 -0.8990 0.4220  737  GLU A CG    
4777 C  CD    . GLU A 634 ? 3.9563 2.5494 2.4154 -0.9716 -0.8921 0.4234  737  GLU A CD    
4778 O  OE1   . GLU A 634 ? 3.9554 2.5554 2.4232 -0.9643 -0.8917 0.4271  737  GLU A OE1   
4779 O  OE2   . GLU A 634 ? 3.9673 2.5043 2.3422 -1.0065 -0.8862 0.4204  737  GLU A OE2   
4780 N  N     . GLN A 635 ? 3.4206 2.2818 2.2745 -0.7946 -0.8840 0.4181  738  GLN A N     
4781 C  CA    . GLN A 635 ? 3.2746 2.1963 2.2258 -0.7576 -0.8879 0.4297  738  GLN A CA    
4782 C  C     . GLN A 635 ? 3.1773 2.1617 2.2404 -0.7220 -0.8846 0.4308  738  GLN A C     
4783 O  O     . GLN A 635 ? 3.2020 2.2339 2.3542 -0.7057 -0.9119 0.4518  738  GLN A O     
4784 C  CB    . GLN A 635 ? 3.3165 2.2376 2.2476 -0.7329 -0.8399 0.4093  738  GLN A CB    
4785 C  CG    . GLN A 635 ? 3.4461 2.3077 2.2720 -0.7657 -0.8408 0.4085  738  GLN A CG    
4786 C  CD    . GLN A 635 ? 3.6778 2.5386 2.5177 -0.7869 -0.8878 0.4378  738  GLN A CD    
4787 O  OE1   . GLN A 635 ? 3.7350 2.5472 2.5102 -0.8241 -0.8980 0.4427  738  GLN A OE1   
4788 N  NE2   . GLN A 635 ? 3.7148 2.6322 2.6546 -0.7593 -0.9046 0.4544  738  GLN A NE2   
4789 N  N     . MET A 636 ? 2.9590 1.9429 2.0192 -0.7099 -0.8502 0.4089  739  MET A N     
4790 C  CA    . MET A 636 ? 2.8513 1.8913 2.0120 -0.6778 -0.8450 0.4090  739  MET A CA    
4791 C  C     . MET A 636 ? 3.0132 2.0666 2.2185 -0.6981 -0.8974 0.4346  739  MET A C     
4792 O  O     . MET A 636 ? 2.7783 1.8858 2.0842 -0.6720 -0.9047 0.4435  739  MET A O     
4793 C  CB    . MET A 636 ? 3.0164 2.0479 2.1568 -0.6626 -0.7963 0.3805  739  MET A CB    
4794 C  CG    . MET A 636 ? 2.6735 1.6991 1.7826 -0.6386 -0.7422 0.3561  739  MET A CG    
4795 S  SD    . MET A 636 ? 3.2710 2.2971 2.3771 -0.6146 -0.6863 0.3272  739  MET A SD    
4796 C  CE    . MET A 636 ? 3.2252 2.1882 2.2494 -0.6618 -0.7050 0.3265  739  MET A CE    
4797 N  N     . ARG A 637 ? 3.0710 2.0764 2.2041 -0.7447 -0.9333 0.4468  740  ARG A N     
4798 C  CA    . ARG A 637 ? 3.1512 2.1691 2.3276 -0.7647 -0.9811 0.4743  740  ARG A CA    
4799 C  C     . ARG A 637 ? 3.2504 2.2828 2.4705 -0.7673 -1.0093 0.5045  740  ARG A C     
4800 O  O     . ARG A 637 ? 3.1865 2.2351 2.4603 -0.7763 -1.0396 0.5298  740  ARG A O     
4801 C  CB    . ARG A 637 ? 3.0839 2.0453 2.1732 -0.8045 -0.9845 0.4717  740  ARG A CB    
4802 C  CG    . ARG A 637 ? 3.1841 2.0870 2.1766 -0.8386 -0.9881 0.4779  740  ARG A CG    
4803 C  CD    . ARG A 637 ? 3.2300 2.0753 2.1296 -0.8763 -0.9853 0.4720  740  ARG A CD    
4804 N  NE    . ARG A 637 ? 3.3940 2.1814 2.1992 -0.9106 -0.9871 0.4777  740  ARG A NE    
4805 C  CZ    . ARG A 637 ? 3.4819 2.2102 2.1905 -0.9471 -0.9818 0.4729  740  ARG A CZ    
4806 N  NH1   . ARG A 637 ? 3.1889 1.9067 1.8792 -0.9543 -0.9739 0.4615  740  ARG A NH1   
4807 N  NH2   . ARG A 637 ? 3.6269 2.3046 2.2555 -0.9777 -0.9832 0.4790  740  ARG A NH2   
4808 N  N     . ARG A 638 ? 3.3348 2.3610 2.5341 -0.7605 -0.9993 0.5019  741  ARG A N     
4809 C  CA    . ARG A 638 ? 3.0202 2.0597 2.2639 -0.7632 -1.0238 0.5276  741  ARG A CA    
4810 C  C     . ARG A 638 ? 2.9471 2.0549 2.3228 -0.7288 -1.0355 0.5426  741  ARG A C     
4811 O  O     . ARG A 638 ? 2.8897 2.0344 2.3111 -0.6946 -1.0147 0.5286  741  ARG A O     
4812 C  CB    . ARG A 638 ? 2.9317 1.9491 2.1220 -0.7625 -1.0063 0.5180  741  ARG A CB    
4813 C  CG    . ARG A 638 ? 3.0276 2.0619 2.2680 -0.7621 -1.0283 0.5410  741  ARG A CG    
4814 C  CD    . ARG A 638 ? 3.2366 2.2329 2.3992 -0.7743 -1.0140 0.5321  741  ARG A CD    
4815 N  NE    . ARG A 638 ? 3.4400 2.3776 2.5155 -0.8192 -1.0277 0.5389  741  ARG A NE    
4816 C  CZ    . ARG A 638 ? 3.6822 2.5653 2.6527 -0.8438 -1.0090 0.5209  741  ARG A CZ    
4817 N  NH1   . ARG A 638 ? 3.5625 2.4413 2.5001 -0.8285 -0.9761 0.4944  741  ARG A NH1   
4818 N  NH2   . ARG A 638 ? 3.6823 2.5129 2.5788 -0.8852 -1.0227 0.5298  741  ARG A NH2   
4819 N  N     . PRO A 639 ? 2.7408 1.8653 2.1793 -0.7374 -1.0674 0.5714  742  PRO A N     
4820 C  CA    . PRO A 639 ? 2.7884 1.9756 2.3551 -0.7057 -1.0758 0.5854  742  PRO A CA    
4821 C  C     . PRO A 639 ? 2.9545 2.1764 2.5711 -0.6705 -1.0567 0.5780  742  PRO A C     
4822 O  O     . PRO A 639 ? 2.9065 2.1743 2.5998 -0.6368 -1.0433 0.5723  742  PRO A O     
4823 C  CB    . PRO A 639 ? 2.7385 1.9252 2.3437 -0.7278 -1.1128 0.6181  742  PRO A CB    
4824 C  CG    . PRO A 639 ? 2.8231 1.9519 2.3261 -0.7708 -1.1254 0.6206  742  PRO A CG    
4825 C  CD    . PRO A 639 ? 2.8323 1.9188 2.2284 -0.7775 -1.0967 0.5930  742  PRO A CD    
4826 N  N     . ASP A 640 ? 2.8641 2.0646 2.4384 -0.6776 -1.0542 0.5781  743  ASP A N     
4827 C  CA    . ASP A 640 ? 2.8684 2.1005 2.4892 -0.6452 -1.0366 0.5730  743  ASP A CA    
4828 C  C     . ASP A 640 ? 2.9274 2.1657 2.5196 -0.6196 -1.0005 0.5460  743  ASP A C     
4829 O  O     . ASP A 640 ? 2.8525 2.1262 2.4999 -0.5866 -0.9835 0.5421  743  ASP A O     
4830 C  CB    . ASP A 640 ? 2.9538 2.1591 2.5321 -0.6614 -1.0434 0.5800  743  ASP A CB    
4831 C  CG    . ASP A 640 ? 3.1242 2.2682 2.5746 -0.6931 -1.0354 0.5664  743  ASP A CG    
4832 O  OD1   . ASP A 640 ? 3.0995 2.2297 2.4926 -0.6829 -1.0046 0.5424  743  ASP A OD1   
4833 O  OD2   . ASP A 640 ? 3.1233 2.2317 2.5303 -0.7287 -1.0588 0.5803  743  ASP A OD2   
4834 N  N     . PHE A 641 ? 3.0003 2.2038 2.5075 -0.6344 -0.9875 0.5279  744  PHE A N     
4835 C  CA    . PHE A 641 ? 2.6061 1.8161 2.0928 -0.6085 -0.9424 0.4990  744  PHE A CA    
4836 C  C     . PHE A 641 ? 2.6408 1.8873 2.1932 -0.5853 -0.9249 0.4885  744  PHE A C     
4837 O  O     . PHE A 641 ? 2.5633 1.8368 2.1455 -0.5515 -0.8811 0.4665  744  PHE A O     
4838 C  CB    . PHE A 641 ? 2.5718 1.7240 1.9375 -0.6324 -0.9197 0.4779  744  PHE A CB    
4839 C  CG    . PHE A 641 ? 2.5152 1.6741 1.8674 -0.6040 -0.8605 0.4445  744  PHE A CG    
4840 C  CD1   . PHE A 641 ? 2.5056 1.6787 1.8636 -0.5795 -0.8282 0.4322  744  PHE A CD1   
4841 C  CD2   . PHE A 641 ? 2.9080 2.0597 2.2431 -0.6023 -0.8378 0.4266  744  PHE A CD2   
4842 C  CE1   . PHE A 641 ? 2.6251 1.8072 1.9740 -0.5540 -0.7759 0.4039  744  PHE A CE1   
4843 C  CE2   . PHE A 641 ? 2.7024 1.8616 2.0284 -0.5758 -0.7845 0.3985  744  PHE A CE2   
4844 C  CZ    . PHE A 641 ? 2.4481 1.6236 1.7819 -0.5517 -0.7544 0.3878  744  PHE A CZ    
4845 N  N     . MET A 642 ? 2.7932 2.0416 2.3685 -0.6035 -0.9585 0.5043  745  MET A N     
4846 C  CA    . MET A 642 ? 2.4666 1.7488 2.1053 -0.5829 -0.9429 0.4954  745  MET A CA    
4847 C  C     . MET A 642 ? 2.3065 1.6484 2.0588 -0.5430 -0.9315 0.4995  745  MET A C     
4848 O  O     . MET A 642 ? 2.4628 1.8308 2.2457 -0.5115 -0.8896 0.4776  745  MET A O     
4849 C  CB    . MET A 642 ? 2.6797 1.9530 2.3243 -0.6130 -0.9855 0.5146  745  MET A CB    
4850 C  CG    . MET A 642 ? 2.8724 2.0865 2.4051 -0.6513 -0.9887 0.5047  745  MET A CG    
4851 S  SD    . MET A 642 ? 3.6754 2.8840 3.2242 -0.6796 -1.0227 0.5209  745  MET A SD    
4852 C  CE    . MET A 642 ? 3.0027 2.2285 2.6211 -0.6865 -1.0585 0.5597  745  MET A CE    
4853 N  N     . ASP A 643 ? 2.6157 1.9786 2.4308 -0.5443 -0.9679 0.5278  746  ASP A N     
4854 C  CA    . ASP A 643 ? 2.5158 1.9318 2.4401 -0.5085 -0.9572 0.5327  746  ASP A CA    
4855 C  C     . ASP A 643 ? 2.4429 1.8702 2.3637 -0.4792 -0.9132 0.5110  746  ASP A C     
4856 O  O     . ASP A 643 ? 2.3510 1.8203 2.3507 -0.4468 -0.8907 0.5052  746  ASP A O     
4857 C  CB    . ASP A 643 ? 2.7367 2.1667 2.7260 -0.5165 -0.9949 0.5643  746  ASP A CB    
4858 C  CG    . ASP A 643 ? 2.7584 2.1514 2.6847 -0.5405 -1.0076 0.5721  746  ASP A CG    
4859 O  OD1   . ASP A 643 ? 2.8084 2.1950 2.7034 -0.5292 -0.9897 0.5621  746  ASP A OD1   
4860 O  OD2   . ASP A 643 ? 2.8825 2.2523 2.7906 -0.5713 -1.0354 0.5891  746  ASP A OD2   
4861 N  N     . ALA A 644 ? 2.4375 1.8279 2.2686 -0.4911 -0.8999 0.4988  747  ALA A N     
4862 C  CA    . ALA A 644 ? 2.3890 1.7900 2.2128 -0.4651 -0.8571 0.4773  747  ALA A CA    
4863 C  C     . ALA A 644 ? 1.7749 1.1941 1.6033 -0.4402 -0.8105 0.4486  747  ALA A C     
4864 O  O     . ALA A 644 ? 2.0750 1.5210 1.9323 -0.4117 -0.7765 0.4336  747  ALA A O     
4865 C  CB    . ALA A 644 ? 2.4634 1.8189 2.1888 -0.4859 -0.8541 0.4719  747  ALA A CB    
4866 N  N     . LEU A 645 ? 2.0335 1.4381 1.8333 -0.4513 -0.8087 0.4413  748  LEU A N     
4867 C  CA    . LEU A 645 ? 2.2360 1.6566 2.0410 -0.4284 -0.7663 0.4165  748  LEU A CA    
4868 C  C     . LEU A 645 ? 2.0922 1.5414 1.9677 -0.4206 -0.7752 0.4226  748  LEU A C     
4869 O  O     . LEU A 645 ? 2.0325 1.4707 1.8829 -0.4244 -0.7625 0.4110  748  LEU A O     
4870 C  CB    . LEU A 645 ? 2.3496 1.7250 2.0546 -0.4453 -0.7462 0.3982  748  LEU A CB    
4871 C  CG    . LEU A 645 ? 2.1366 1.4789 1.7633 -0.4546 -0.7317 0.3892  748  LEU A CG    
4872 C  CD1   . LEU A 645 ? 2.7463 2.0436 2.2815 -0.4706 -0.7090 0.3710  748  LEU A CD1   
4873 C  CD2   . LEU A 645 ? 2.4971 1.8729 2.1577 -0.4222 -0.6977 0.3766  748  LEU A CD2   
4874 N  N     . GLN A 646 ? 2.2094 1.6944 2.1745 -0.4094 -0.7954 0.4408  749  GLN A N     
4875 C  CA    . GLN A 646 ? 2.1516 1.6659 2.1919 -0.4020 -0.8049 0.4488  749  GLN A CA    
4876 C  C     . GLN A 646 ? 2.2647 1.8276 2.4010 -0.3689 -0.7886 0.4493  749  GLN A C     
4877 O  O     . GLN A 646 ? 2.4543 2.0280 2.6274 -0.3652 -0.8029 0.4636  749  GLN A O     
4878 C  CB    . GLN A 646 ? 2.3209 1.8234 2.3751 -0.4320 -0.8578 0.4777  749  GLN A CB    
4879 C  CG    . GLN A 646 ? 2.6131 2.0677 2.5762 -0.4677 -0.8750 0.4769  749  GLN A CG    
4880 C  CD    . GLN A 646 ? 2.5559 2.0080 2.5056 -0.4643 -0.8513 0.4587  749  GLN A CD    
4881 O  OE1   . GLN A 646 ? 2.5100 1.9986 2.5345 -0.4439 -0.8412 0.4576  749  GLN A OE1   
4882 N  NE2   . GLN A 646 ? 2.5358 1.9429 2.3893 -0.4846 -0.8407 0.4441  749  GLN A NE2   
4883 N  N     . GLY A 647 ? 2.0389 1.6288 2.2137 -0.3460 -0.7578 0.4338  750  GLY A N     
4884 C  CA    . GLY A 647 ? 2.1007 1.7350 2.3672 -0.3169 -0.7414 0.4336  750  GLY A CA    
4885 C  C     . GLY A 647 ? 2.0746 1.7212 2.3447 -0.2974 -0.7165 0.4234  750  GLY A C     
4886 O  O     . GLY A 647 ? 2.0336 1.6988 2.3639 -0.2892 -0.7263 0.4363  750  GLY A O     
4887 N  N     . PHE A 648 ? 2.0535 1.6901 2.2617 -0.2901 -0.6836 0.4007  751  PHE A N     
4888 C  CA    . PHE A 648 ? 1.9575 1.6082 2.1673 -0.2715 -0.6567 0.3886  751  PHE A CA    
4889 C  C     . PHE A 648 ? 1.9790 1.6431 2.1690 -0.2518 -0.6130 0.3631  751  PHE A C     
4890 O  O     . PHE A 648 ? 1.8882 1.5358 2.0310 -0.2578 -0.6036 0.3536  751  PHE A O     
4891 C  CB    . PHE A 648 ? 1.8793 1.4988 2.0236 -0.2881 -0.6680 0.3920  751  PHE A CB    
4892 C  CG    . PHE A 648 ? 1.6801 1.2650 1.7300 -0.3019 -0.6562 0.3783  751  PHE A CG    
4893 C  CD1   . PHE A 648 ? 1.8378 1.3888 1.8403 -0.3284 -0.6805 0.3862  751  PHE A CD1   
4894 C  CD2   . PHE A 648 ? 1.7882 1.3738 1.7973 -0.2895 -0.6203 0.3578  751  PHE A CD2   
4895 C  CE1   . PHE A 648 ? 1.9890 1.5046 1.9040 -0.3415 -0.6663 0.3726  751  PHE A CE1   
4896 C  CE2   . PHE A 648 ? 1.7320 1.2852 1.6586 -0.3012 -0.6068 0.3457  751  PHE A CE2   
4897 C  CZ    . PHE A 648 ? 1.8801 1.3968 1.7588 -0.3270 -0.6285 0.3525  751  PHE A CZ    
4898 N  N     . LEU A 649 ? 1.8533 1.5471 2.0800 -0.2290 -0.5865 0.3527  752  LEU A N     
4899 C  CA    . LEU A 649 ? 1.6087 1.3204 1.8239 -0.2095 -0.5464 0.3309  752  LEU A CA    
4900 C  C     . LEU A 649 ? 1.5089 1.1964 1.6400 -0.2158 -0.5307 0.3181  752  LEU A C     
4901 O  O     . LEU A 649 ? 1.5491 1.2156 1.6407 -0.2280 -0.5410 0.3220  752  LEU A O     
4902 C  CB    . LEU A 649 ? 1.7691 1.5157 2.0383 -0.1874 -0.5241 0.3236  752  LEU A CB    
4903 C  CG    . LEU A 649 ? 1.5496 1.3196 1.9065 -0.1796 -0.5344 0.3353  752  LEU A CG    
4904 C  CD1   . LEU A 649 ? 1.7540 1.5538 2.1538 -0.1591 -0.5068 0.3245  752  LEU A CD1   
4905 C  CD2   . LEU A 649 ? 1.5701 1.3480 1.9557 -0.1777 -0.5357 0.3370  752  LEU A CD2   
4906 N  N     . SER A 650 ? 1.7694 1.4595 1.8748 -0.2071 -0.5045 0.3036  753  SER A N     
4907 C  CA    . SER A 650 ? 1.8875 1.5548 1.9176 -0.2116 -0.4862 0.2918  753  SER A CA    
4908 C  C     . SER A 650 ? 1.7805 1.4648 1.8048 -0.1991 -0.4643 0.2822  753  SER A C     
4909 O  O     . SER A 650 ? 1.7058 1.4260 1.7761 -0.1793 -0.4455 0.2755  753  SER A O     
4910 C  CB    . SER A 650 ? 1.8755 1.5441 1.8885 -0.2028 -0.4617 0.2801  753  SER A CB    
4911 O  OG    . SER A 650 ? 1.7604 1.4086 1.7066 -0.2049 -0.4404 0.2689  753  SER A OG    
4912 N  N     . PRO A 651 ? 1.7757 1.4345 1.7435 -0.2114 -0.4658 0.2812  754  PRO A N     
4913 C  CA    . PRO A 651 ? 1.7200 1.3957 1.6803 -0.2002 -0.4431 0.2712  754  PRO A CA    
4914 C  C     . PRO A 651 ? 1.8432 1.5405 1.7950 -0.1817 -0.4063 0.2554  754  PRO A C     
4915 O  O     . PRO A 651 ? 1.8346 1.5608 1.8046 -0.1675 -0.3869 0.2476  754  PRO A O     
4916 C  CB    . PRO A 651 ? 1.6430 1.2802 1.5378 -0.2207 -0.4535 0.2743  754  PRO A CB    
4917 C  CG    . PRO A 651 ? 1.8240 1.4299 1.7094 -0.2430 -0.4901 0.2903  754  PRO A CG    
4918 C  CD    . PRO A 651 ? 1.7669 1.3805 1.6780 -0.2382 -0.4905 0.2902  754  PRO A CD    
4919 N  N     . LEU A 652 ? 1.7825 1.4663 1.7074 -0.1821 -0.3965 0.2511  755  LEU A N     
4920 C  CA    . LEU A 652 ? 1.5555 1.2607 1.4768 -0.1636 -0.3624 0.2387  755  LEU A CA    
4921 C  C     . LEU A 652 ? 1.6047 1.3507 1.5894 -0.1443 -0.3532 0.2367  755  LEU A C     
4922 O  O     . LEU A 652 ? 1.7905 1.5654 1.7847 -0.1272 -0.3268 0.2278  755  LEU A O     
4923 C  CB    . LEU A 652 ? 1.5984 1.2733 1.4720 -0.1701 -0.3533 0.2353  755  LEU A CB    
4924 C  CG    . LEU A 652 ? 1.8332 1.4671 1.6352 -0.1866 -0.3501 0.2329  755  LEU A CG    
4925 C  CD1   . LEU A 652 ? 1.9329 1.5330 1.6918 -0.1945 -0.3416 0.2297  755  LEU A CD1   
4926 C  CD2   . LEU A 652 ? 1.8180 1.4693 1.6060 -0.1749 -0.3229 0.2242  755  LEU A CD2   
4927 N  N     . ASN A 653 ? 1.5384 1.2874 1.5667 -0.1475 -0.3744 0.2454  756  ASN A N     
4928 C  CA    . ASN A 653 ? 1.3825 1.1668 1.4718 -0.1309 -0.3655 0.2437  756  ASN A CA    
4929 C  C     . ASN A 653 ? 1.6180 1.4039 1.7589 -0.1374 -0.3927 0.2557  756  ASN A C     
4930 O  O     . ASN A 653 ? 1.5138 1.2778 1.6539 -0.1509 -0.4159 0.2657  756  ASN A O     
4931 C  CB    . ASN A 653 ? 1.5352 1.3207 1.6211 -0.1235 -0.3511 0.2396  756  ASN A CB    
4932 C  CG    . ASN A 653 ? 1.8071 1.6313 1.9442 -0.1040 -0.3327 0.2346  756  ASN A CG    
4933 O  OD1   . ASN A 653 ? 1.5914 1.4363 1.7777 -0.0995 -0.3379 0.2368  756  ASN A OD1   
4934 N  ND2   . ASN A 653 ? 1.5292 1.3615 1.6540 -0.0928 -0.3099 0.2282  756  ASN A ND2   
4935 N  N     . PRO A 654 ? 1.6978 1.5089 1.8853 -0.1288 -0.3904 0.2556  757  PRO A N     
4936 C  CA    . PRO A 654 ? 1.4129 1.2250 1.6543 -0.1341 -0.4150 0.2686  757  PRO A CA    
4937 C  C     . PRO A 654 ? 1.5985 1.4204 1.8871 -0.1298 -0.4192 0.2732  757  PRO A C     
4938 O  O     . PRO A 654 ? 1.4606 1.2783 1.7904 -0.1373 -0.4438 0.2871  757  PRO A O     
4939 C  CB    . PRO A 654 ? 1.3736 1.2106 1.6506 -0.1233 -0.4023 0.2637  757  PRO A CB    
4940 C  CG    . PRO A 654 ? 1.6907 1.5500 1.9496 -0.1090 -0.3692 0.2475  757  PRO A CG    
4941 C  CD    . PRO A 654 ? 1.8867 1.7260 2.0808 -0.1146 -0.3647 0.2441  757  PRO A CD    
4942 N  N     . ALA A 655 ? 1.6801 1.5155 1.9661 -0.1181 -0.3962 0.2633  758  ALA A N     
4943 C  CA    . ALA A 655 ? 1.3649 1.2085 1.6930 -0.1144 -0.3982 0.2671  758  ALA A CA    
4944 C  C     . ALA A 655 ? 1.5578 1.3721 1.8577 -0.1302 -0.4185 0.2751  758  ALA A C     
4945 O  O     . ALA A 655 ? 1.6420 1.4600 1.9788 -0.1311 -0.4261 0.2809  758  ALA A O     
4946 C  CB    . ALA A 655 ? 1.3933 1.2621 1.7287 -0.0963 -0.3653 0.2540  758  ALA A CB    
4947 N  N     . HIS A 656 ? 1.6150 1.3994 1.8502 -0.1439 -0.4263 0.2751  759  HIS A N     
4948 C  CA    . HIS A 656 ? 1.5778 1.3290 1.7767 -0.1625 -0.4452 0.2816  759  HIS A CA    
4949 C  C     . HIS A 656 ? 1.7737 1.5046 1.9760 -0.1834 -0.4834 0.2981  759  HIS A C     
4950 O  O     . HIS A 656 ? 1.8169 1.5394 1.9983 -0.1891 -0.4909 0.3005  759  HIS A O     
4951 C  CB    . HIS A 656 ? 1.6813 1.4073 1.8036 -0.1665 -0.4286 0.2713  759  HIS A CB    
4952 C  CG    . HIS A 656 ? 1.5304 1.2733 1.6480 -0.1476 -0.3939 0.2584  759  HIS A CG    
4953 N  ND1   . HIS A 656 ? 1.5432 1.2699 1.6025 -0.1460 -0.3725 0.2490  759  HIS A ND1   
4954 C  CD2   . HIS A 656 ? 1.4510 1.2251 1.6156 -0.1297 -0.3766 0.2543  759  HIS A CD2   
4955 C  CE1   . HIS A 656 ? 2.0186 1.7672 2.0911 -0.1274 -0.3451 0.2411  759  HIS A CE1   
4956 N  NE2   . HIS A 656 ? 1.7601 1.5371 1.8937 -0.1179 -0.3474 0.2439  759  HIS A NE2   
4957 N  N     . GLN A 657 ? 1.9036 1.6272 2.1325 -0.1954 -0.5080 0.3104  760  GLN A N     
4958 C  CA    . GLN A 657 ? 1.8003 1.5061 2.0363 -0.2169 -0.5481 0.3295  760  GLN A CA    
4959 C  C     . GLN A 657 ? 1.6611 1.3238 1.8232 -0.2424 -0.5647 0.3318  760  GLN A C     
4960 O  O     . GLN A 657 ? 1.7695 1.4211 1.9167 -0.2478 -0.5614 0.3284  760  GLN A O     
4961 C  CB    . GLN A 657 ? 1.7131 1.4396 2.0294 -0.2160 -0.5672 0.3440  760  GLN A CB    
4962 C  CG    . GLN A 657 ? 2.0231 1.7883 2.4143 -0.1929 -0.5504 0.3420  760  GLN A CG    
4963 C  CD    . GLN A 657 ? 1.9945 1.7776 2.4682 -0.1933 -0.5702 0.3584  760  GLN A CD    
4964 O  OE1   . GLN A 657 ? 2.0924 1.8610 2.5699 -0.2122 -0.6013 0.3738  760  GLN A OE1   
4965 N  NE2   . GLN A 657 ? 1.8320 1.6464 2.3727 -0.1734 -0.5516 0.3555  760  GLN A NE2   
4966 N  N     . LEU A 658 ? 1.6297 1.2660 1.7435 -0.2591 -0.5812 0.3372  761  LEU A N     
4967 C  CA    . LEU A 658 ? 1.8761 1.4666 1.9144 -0.2871 -0.5986 0.3401  761  LEU A CA    
4968 C  C     . LEU A 658 ? 1.9793 1.5600 2.0426 -0.3105 -0.6444 0.3631  761  LEU A C     
4969 O  O     . LEU A 658 ? 2.3103 1.8887 2.3851 -0.3199 -0.6705 0.3783  761  LEU A O     
4970 C  CB    . LEU A 658 ? 1.8314 1.3968 1.8019 -0.2945 -0.5915 0.3340  761  LEU A CB    
4971 C  CG    . LEU A 658 ? 1.8678 1.4185 1.7761 -0.2869 -0.5533 0.3131  761  LEU A CG    
4972 C  CD1   . LEU A 658 ? 1.8706 1.4598 1.8218 -0.2562 -0.5179 0.2998  761  LEU A CD1   
4973 C  CD2   . LEU A 658 ? 1.7628 1.2972 1.6205 -0.2909 -0.5454 0.3085  761  LEU A CD2   
4974 N  N     . GLY A 659 ? 1.7900 1.3656 1.8634 -0.3202 -0.6549 0.3669  762  GLY A N     
4975 C  CA    . GLY A 659 ? 1.9599 1.5323 2.0665 -0.3417 -0.6988 0.3900  762  GLY A CA    
4976 C  C     . GLY A 659 ? 2.3736 1.8979 2.4032 -0.3785 -0.7281 0.3979  762  GLY A C     
4977 O  O     . GLY A 659 ? 2.3545 1.8527 2.3294 -0.3923 -0.7372 0.4003  762  GLY A O     
4978 N  N     . ASN A 660 ? 2.4445 1.9551 2.4670 -0.3962 -0.7425 0.4017  763  ASN A N     
4979 C  CA    . ASN A 660 ? 2.2952 1.7589 2.2454 -0.4352 -0.7733 0.4103  763  ASN A CA    
4980 C  C     . ASN A 660 ? 2.2514 1.6711 2.0992 -0.4435 -0.7447 0.3887  763  ASN A C     
4981 O  O     . ASN A 660 ? 2.2844 1.7083 2.1213 -0.4230 -0.7034 0.3678  763  ASN A O     
4982 C  CB    . ASN A 660 ? 2.6304 2.0934 2.6052 -0.4525 -0.7961 0.4201  763  ASN A CB    
4983 C  CG    . ASN A 660 ? 2.5894 2.0930 2.6656 -0.4485 -0.8284 0.4448  763  ASN A CG    
4984 O  OD1   . ASN A 660 ? 2.3355 1.8519 2.4437 -0.4478 -0.8504 0.4616  763  ASN A OD1   
4985 N  ND2   . ASN A 660 ? 2.7404 2.2639 2.8699 -0.4455 -0.8302 0.4476  763  ASN A ND2   
4986 N  N     . LEU A 661 ? 2.2537 1.6304 2.0270 -0.4740 -0.7664 0.3947  764  LEU A N     
4987 C  CA    . LEU A 661 ? 2.1980 1.5266 1.8702 -0.4864 -0.7407 0.3756  764  LEU A CA    
4988 C  C     . LEU A 661 ? 2.7363 2.0294 2.3606 -0.5101 -0.7417 0.3693  764  LEU A C     
4989 O  O     . LEU A 661 ? 3.0009 2.2940 2.6483 -0.5308 -0.7769 0.3851  764  LEU A O     
4990 C  CB    . LEU A 661 ? 2.4200 1.7129 2.0269 -0.5118 -0.7620 0.3839  764  LEU A CB    
4991 C  CG    . LEU A 661 ? 2.2692 1.5793 1.8854 -0.4907 -0.7457 0.3808  764  LEU A CG    
4992 C  CD1   . LEU A 661 ? 2.1768 1.4536 1.7399 -0.5201 -0.7775 0.3954  764  LEU A CD1   
4993 C  CD2   . LEU A 661 ? 2.2907 1.5932 1.8657 -0.4701 -0.6928 0.3539  764  LEU A CD2   
4994 N  N     . ARG A 662 ? 2.7226 1.9850 2.2811 -0.5070 -0.7018 0.3464  765  ARG A N     
4995 C  CA    . ARG A 662 ? 2.8288 2.0480 2.3274 -0.5302 -0.6953 0.3368  765  ARG A CA    
4996 C  C     . ARG A 662 ? 2.7573 1.9163 2.1466 -0.5541 -0.6823 0.3252  765  ARG A C     
4997 O  O     . ARG A 662 ? 2.7623 1.9074 2.1145 -0.5379 -0.6371 0.3048  765  ARG A O     
4998 C  CB    . ARG A 662 ? 2.6678 1.9063 2.1969 -0.5015 -0.6542 0.3197  765  ARG A CB    
4999 C  CG    . ARG A 662 ? 2.8034 2.0957 2.4347 -0.4819 -0.6663 0.3305  765  ARG A CG    
5000 C  CD    . ARG A 662 ? 3.0900 2.3745 2.7361 -0.5142 -0.7143 0.3499  765  ARG A CD    
5001 N  NE    . ARG A 662 ? 2.8708 2.2083 2.6206 -0.4960 -0.7273 0.3623  765  ARG A NE    
5002 C  CZ    . ARG A 662 ? 3.0649 2.4097 2.8524 -0.5172 -0.7676 0.3814  765  ARG A CZ    
5003 N  NH1   . ARG A 662 ? 3.1907 2.4941 2.9197 -0.5592 -0.8020 0.3912  765  ARG A NH1   
5004 N  NH2   . ARG A 662 ? 2.8727 2.2674 2.7589 -0.4970 -0.7733 0.3912  765  ARG A NH2   
5005 N  N     . LEU A 663 ? 2.5948 1.7179 1.9334 -0.5935 -0.7220 0.3393  766  LEU A N     
5006 C  CA    . LEU A 663 ? 2.5056 1.5695 1.7387 -0.6198 -0.7134 0.3304  766  LEU A CA    
5007 C  C     . LEU A 663 ? 2.9956 2.0054 2.1485 -0.6364 -0.6826 0.3096  766  LEU A C     
5008 O  O     . LEU A 663 ? 3.1285 2.0888 2.1946 -0.6518 -0.6615 0.2969  766  LEU A O     
5009 C  CB    . LEU A 663 ? 2.5010 1.5403 1.7009 -0.6604 -0.7675 0.3530  766  LEU A CB    
5010 C  CG    . LEU A 663 ? 2.5157 1.6032 1.7937 -0.6484 -0.8027 0.3771  766  LEU A CG    
5011 C  CD1   . LEU A 663 ? 2.8064 1.8633 2.0414 -0.6912 -0.8555 0.4004  766  LEU A CD1   
5012 C  CD2   . LEU A 663 ? 2.5480 1.6609 1.8469 -0.6138 -0.7708 0.3679  766  LEU A CD2   
5013 N  N     . GLU A 664 ? 3.1678 2.1841 2.3474 -0.6340 -0.6776 0.3056  767  GLU A N     
5014 C  CA    . GLU A 664 ? 3.1012 2.0639 2.2062 -0.6495 -0.6463 0.2857  767  GLU A CA    
5015 C  C     . GLU A 664 ? 3.1193 2.0805 2.2104 -0.6162 -0.5856 0.2627  767  GLU A C     
5016 O  O     . GLU A 664 ? 3.2298 2.1362 2.2408 -0.6301 -0.5541 0.2453  767  GLU A O     
5017 C  CB    . GLU A 664 ? 2.9550 1.9270 2.0968 -0.6546 -0.6567 0.2882  767  GLU A CB    
5018 C  CG    . GLU A 664 ? 2.8607 1.9039 2.1166 -0.6137 -0.6525 0.2939  767  GLU A CG    
5019 C  CD    . GLU A 664 ? 2.8184 1.9060 2.1501 -0.6177 -0.7044 0.3204  767  GLU A CD    
5020 O  OE1   . GLU A 664 ? 2.9105 1.9777 2.2091 -0.6491 -0.7441 0.3358  767  GLU A OE1   
5021 O  OE2   . GLU A 664 ? 2.9824 2.1245 2.4072 -0.5896 -0.7047 0.3264  767  GLU A OE2   
5022 N  N     . GLU A 665 ? 3.1931 2.2128 2.3609 -0.5731 -0.5681 0.2628  768  GLU A N     
5023 C  CA    . GLU A 665 ? 3.1149 2.1398 2.2760 -0.5410 -0.5141 0.2443  768  GLU A CA    
5024 C  C     . GLU A 665 ? 2.9757 2.0035 2.1177 -0.5336 -0.5065 0.2438  768  GLU A C     
5025 O  O     . GLU A 665 ? 2.8551 1.8733 1.9703 -0.5161 -0.4625 0.2283  768  GLU A O     
5026 C  CB    . GLU A 665 ? 2.9530 2.0394 2.2063 -0.4979 -0.4941 0.2427  768  GLU A CB    
5027 C  CG    . GLU A 665 ? 2.9359 2.0178 2.2048 -0.4985 -0.4870 0.2385  768  GLU A CG    
5028 C  CD    . GLU A 665 ? 2.9698 2.0779 2.2958 -0.5110 -0.5333 0.2566  768  GLU A CD    
5029 O  OE1   . GLU A 665 ? 3.0110 2.1518 2.3817 -0.5101 -0.5667 0.2728  768  GLU A OE1   
5030 O  OE2   . GLU A 665 ? 2.9445 2.0404 2.2728 -0.5215 -0.5356 0.2551  768  GLU A OE2   
5031 N  N     . CYS A 666 ? 2.9434 1.9845 2.1006 -0.5464 -0.5476 0.2612  769  CYS A N     
5032 C  CA    . CYS A 666 ? 2.9907 2.0329 2.1288 -0.5415 -0.5422 0.2615  769  CYS A CA    
5033 C  C     . CYS A 666 ? 3.0796 2.0517 2.1080 -0.5716 -0.5260 0.2500  769  CYS A C     
5034 O  O     . CYS A 666 ? 3.2034 2.1263 2.1690 -0.6120 -0.5516 0.2546  769  CYS A O     
5035 C  CB    . CYS A 666 ? 2.9101 1.9784 2.0889 -0.5507 -0.5918 0.2845  769  CYS A CB    
5036 S  SG    . CYS A 666 ? 2.5430 1.6933 1.8536 -0.5136 -0.6064 0.2974  769  CYS A SG    
5037 N  N     . ARG A 667 ? 2.7550 1.7223 1.7600 -0.5529 -0.4830 0.2353  770  ARG A N     
5038 C  CA    . ARG A 667 ? 2.8912 1.7925 1.7954 -0.5770 -0.4582 0.2219  770  ARG A CA    
5039 C  C     . ARG A 667 ? 2.7486 1.6637 1.6513 -0.5568 -0.4308 0.2160  770  ARG A C     
5040 O  O     . ARG A 667 ? 2.4965 1.4709 1.4736 -0.5252 -0.4315 0.2217  770  ARG A O     
5041 C  CB    . ARG A 667 ? 2.9776 1.8434 1.8443 -0.5765 -0.4173 0.2034  770  ARG A CB    
5042 C  CG    . ARG A 667 ? 2.7662 1.6743 1.6897 -0.5303 -0.3709 0.1922  770  ARG A CG    
5043 C  CD    . ARG A 667 ? 2.9253 1.7995 1.8190 -0.5290 -0.3330 0.1767  770  ARG A CD    
5044 N  NE    . ARG A 667 ? 2.7886 1.7042 1.7371 -0.4849 -0.2900 0.1685  770  ARG A NE    
5045 C  CZ    . ARG A 667 ? 2.7859 1.7582 1.8174 -0.4554 -0.2929 0.1739  770  ARG A CZ    
5046 N  NH1   . ARG A 667 ? 2.9592 1.9552 2.0336 -0.4631 -0.3344 0.1867  770  ARG A NH1   
5047 N  NH2   . ARG A 667 ? 2.4737 1.4797 1.5467 -0.4178 -0.2531 0.1670  770  ARG A NH2   
5048 N  N     . ILE A 668 ? 3.0451 1.9034 1.8609 -0.5763 -0.4054 0.2040  771  ILE A N     
5049 C  CA    . ILE A 668 ? 2.8410 1.7043 1.6453 -0.5605 -0.3743 0.1965  771  ILE A CA    
5050 C  C     . ILE A 668 ? 2.8669 1.7105 1.6469 -0.5436 -0.3149 0.1760  771  ILE A C     
5051 O  O     . ILE A 668 ? 3.0864 1.8730 1.8016 -0.5655 -0.2980 0.1654  771  ILE A O     
5052 C  CB    . ILE A 668 ? 2.8999 1.7143 1.6257 -0.5969 -0.3928 0.2010  771  ILE A CB    
5053 C  CG1   . ILE A 668 ? 2.8775 1.6915 1.5856 -0.5819 -0.3547 0.1910  771  ILE A CG1   
5054 C  CG2   . ILE A 668 ? 3.5313 2.2673 2.1583 -0.6414 -0.3962 0.1948  771  ILE A CG2   
5055 C  CD1   . ILE A 668 ? 3.1102 1.8829 1.7495 -0.6145 -0.3734 0.1968  771  ILE A CD1   
5056 N  N     . MET A 669 ? 2.8416 1.7320 1.6749 -0.5051 -0.2831 0.1713  772  MET A N     
5057 C  CA    . MET A 669 ? 2.6851 1.5669 1.5107 -0.4839 -0.2271 0.1551  772  MET A CA    
5058 C  C     . MET A 669 ? 2.9486 1.7701 1.6883 -0.5034 -0.1945 0.1429  772  MET A C     
5059 O  O     . MET A 669 ? 3.1034 1.9022 1.7999 -0.5262 -0.2123 0.1470  772  MET A O     
5060 C  CB    . MET A 669 ? 2.7047 1.6592 1.6168 -0.4380 -0.2066 0.1561  772  MET A CB    
5061 C  CG    . MET A 669 ? 2.6836 1.6939 1.6785 -0.4148 -0.2250 0.1642  772  MET A CG    
5062 S  SD    . MET A 669 ? 2.7547 1.8461 1.8415 -0.3647 -0.2000 0.1649  772  MET A SD    
5063 C  CE    . MET A 669 ? 2.5766 1.7090 1.7348 -0.3459 -0.2135 0.1705  772  MET A CE    
5064 N  N     . SER A 670 ? 2.9882 1.7826 1.7042 -0.4938 -0.1446 0.1280  773  SER A N     
5065 C  CA    . SER A 670 ? 3.3726 2.1113 2.0147 -0.5069 -0.1032 0.1144  773  SER A CA    
5066 C  C     . SER A 670 ? 3.3202 2.0999 2.0076 -0.4694 -0.0607 0.1101  773  SER A C     
5067 O  O     . SER A 670 ? 3.1970 1.9405 1.8456 -0.4677 -0.0121 0.0974  773  SER A O     
5068 C  CB    . SER A 670 ? 3.1244 1.7955 1.7020 -0.5258 -0.0735 0.1005  773  SER A CB    
5069 O  OG    . SER A 670 ? 2.9725 1.6736 1.6067 -0.4940 -0.0481 0.0973  773  SER A OG    
5070 N  N     . SER A 671 ? 3.2626 2.1168 2.0320 -0.4402 -0.0776 0.1207  774  SER A N     
5071 C  CA    . SER A 671 ? 3.2912 2.1920 2.1100 -0.4052 -0.0428 0.1188  774  SER A CA    
5072 C  C     . SER A 671 ? 3.3894 2.2873 2.1838 -0.4162 -0.0483 0.1207  774  SER A C     
5073 O  O     . SER A 671 ? 3.5089 2.3533 2.2315 -0.4520 -0.0656 0.1200  774  SER A O     
5074 C  CB    . SER A 671 ? 3.2325 2.2137 2.1507 -0.3689 -0.0558 0.1281  774  SER A CB    
5075 O  OG    . SER A 671 ? 3.3195 2.3003 2.2570 -0.3604 -0.0506 0.1266  774  SER A OG    
5076 N  N     . ALA A 672 ? 3.2703 2.2249 2.1223 -0.3868 -0.0342 0.1235  775  ALA A N     
5077 C  CA    . ALA A 672 ? 3.2460 2.2023 2.0810 -0.3952 -0.0384 0.1254  775  ALA A CA    
5078 C  C     . ALA A 672 ? 3.2157 2.1894 2.0635 -0.4098 -0.0944 0.1384  775  ALA A C     
5079 O  O     . ALA A 672 ? 3.1814 2.2029 2.0926 -0.3950 -0.1231 0.1475  775  ALA A O     
5080 C  CB    . ALA A 672 ? 3.1101 2.1254 2.0073 -0.3599 -0.0085 0.1253  775  ALA A CB    
5081 N  N     . LYS A 673 ? 3.3813 2.3138 2.1678 -0.4398 -0.1088 0.1398  776  LYS A N     
5082 C  CA    . LYS A 673 ? 3.4461 2.3877 2.2375 -0.4567 -0.1608 0.1537  776  LYS A CA    
5083 C  C     . LYS A 673 ? 3.2777 2.2056 2.0660 -0.4744 -0.2024 0.1621  776  LYS A C     
5084 O  O     . LYS A 673 ? 3.4951 2.4321 2.2945 -0.4879 -0.2484 0.1761  776  LYS A O     
5085 C  CB    . LYS A 673 ? 3.1157 2.1329 1.9927 -0.4268 -0.1719 0.1618  776  LYS A CB    
5086 N  N     . ARG A 674 ? 2.8555 1.7615 1.6307 -0.4745 -0.1862 0.1546  777  ARG A N     
5087 C  CA    . ARG A 674 ? 2.8037 1.6922 1.5715 -0.4929 -0.2205 0.1608  777  ARG A CA    
5088 C  C     . ARG A 674 ? 2.7969 1.7484 1.6495 -0.4763 -0.2619 0.1762  777  ARG A C     
5089 O  O     . ARG A 674 ? 2.8724 1.8213 1.7217 -0.4963 -0.3066 0.1900  777  ARG A O     
5090 C  CB    . ARG A 674 ? 3.1894 2.0076 1.8652 -0.5404 -0.2459 0.1635  777  ARG A CB    
5091 C  CG    . ARG A 674 ? 3.2400 1.9905 1.8253 -0.5602 -0.2038 0.1476  777  ARG A CG    
5092 C  CD    . ARG A 674 ? 3.2466 1.9257 1.7360 -0.6104 -0.2311 0.1507  777  ARG A CD    
5093 N  NE    . ARG A 674 ? 3.4619 2.1171 1.9334 -0.6328 -0.2610 0.1551  777  ARG A NE    
5094 C  CZ    . ARG A 674 ? 3.5808 2.1905 2.0075 -0.6441 -0.2352 0.1417  777  ARG A CZ    
5095 N  NH1   . ARG A 674 ? 3.5726 2.1547 1.9694 -0.6338 -0.1774 0.1235  777  ARG A NH1   
5096 N  NH2   . ARG A 674 ? 3.6956 2.2870 2.1092 -0.6663 -0.2674 0.1473  777  ARG A NH2   
5097 N  N     . PRO A 675 ? 2.7234 1.7312 1.6531 -0.4404 -0.2480 0.1751  778  PRO A N     
5098 C  CA    . PRO A 675 ? 2.4644 1.5302 1.4750 -0.4245 -0.2836 0.1884  778  PRO A CA    
5099 C  C     . PRO A 675 ? 2.4477 1.4948 1.4533 -0.4461 -0.3213 0.1971  778  PRO A C     
5100 O  O     . PRO A 675 ? 2.8749 1.8687 1.8197 -0.4700 -0.3172 0.1914  778  PRO A O     
5101 C  CB    . PRO A 675 ? 2.3124 1.4326 1.3920 -0.3840 -0.2519 0.1824  778  PRO A CB    
5102 C  CG    . PRO A 675 ? 2.5437 1.6441 1.5868 -0.3758 -0.2020 0.1688  778  PRO A CG    
5103 C  CD    . PRO A 675 ? 2.8023 1.8249 1.7508 -0.4119 -0.1977 0.1625  778  PRO A CD    
5104 N  N     . LEU A 676 ? 2.1601 1.2519 1.2324 -0.4378 -0.3580 0.2112  779  LEU A N     
5105 C  CA    . LEU A 676 ? 2.3463 1.4310 1.4297 -0.4559 -0.3980 0.2226  779  LEU A CA    
5106 C  C     . LEU A 676 ? 2.5048 1.6357 1.6622 -0.4276 -0.3908 0.2217  779  LEU A C     
5107 O  O     . LEU A 676 ? 2.5062 1.6949 1.7382 -0.3987 -0.3904 0.2255  779  LEU A O     
5108 C  CB    . LEU A 676 ? 2.1486 1.2470 1.2552 -0.4695 -0.4465 0.2417  779  LEU A CB    
5109 C  CG    . LEU A 676 ? 2.2601 1.3095 1.2913 -0.5029 -0.4630 0.2467  779  LEU A CG    
5110 C  CD1   . LEU A 676 ? 2.6489 1.7137 1.7119 -0.5160 -0.5152 0.2690  779  LEU A CD1   
5111 C  CD2   . LEU A 676 ? 2.5357 1.5146 1.4738 -0.5381 -0.4590 0.2395  779  LEU A CD2   
5112 N  N     . TRP A 677 ? 2.4828 1.5861 1.6171 -0.4371 -0.3843 0.2163  780  TRP A N     
5113 C  CA    . TRP A 677 ? 2.5114 1.6516 1.7097 -0.4152 -0.3807 0.2165  780  TRP A CA    
5114 C  C     . TRP A 677 ? 2.5360 1.6901 1.7726 -0.4296 -0.4305 0.2334  780  TRP A C     
5115 O  O     . TRP A 677 ? 2.5806 1.6918 1.7704 -0.4634 -0.4566 0.2387  780  TRP A O     
5116 C  CB    . TRP A 677 ? 2.6210 1.7237 1.7776 -0.4188 -0.3492 0.2031  780  TRP A CB    
5117 C  CG    . TRP A 677 ? 2.5467 1.6886 1.7672 -0.3907 -0.3346 0.2010  780  TRP A CG    
5118 C  CD1   . TRP A 677 ? 2.6160 1.7884 1.8689 -0.3568 -0.2941 0.1923  780  TRP A CD1   
5119 C  CD2   . TRP A 677 ? 2.6396 1.7947 1.8995 -0.3949 -0.3607 0.2089  780  TRP A CD2   
5120 N  NE1   . TRP A 677 ? 2.3946 1.5963 1.7013 -0.3399 -0.2932 0.1940  780  TRP A NE1   
5121 C  CE2   . TRP A 677 ? 2.5016 1.6933 1.8141 -0.3625 -0.3327 0.2035  780  TRP A CE2   
5122 C  CE3   . TRP A 677 ? 2.8975 2.0380 2.1547 -0.4233 -0.4055 0.2211  780  TRP A CE3   
5123 C  CZ2   . TRP A 677 ? 2.4902 1.7021 1.8503 -0.3578 -0.3463 0.2085  780  TRP A CZ2   
5124 C  CZ3   . TRP A 677 ? 2.9930 2.1560 2.3014 -0.4182 -0.4193 0.2265  780  TRP A CZ3   
5125 C  CH2   . TRP A 677 ? 2.7532 1.9505 2.1115 -0.3857 -0.3888 0.2196  780  TRP A CH2   
5126 N  N     . LEU A 678 ? 2.4510 1.6643 1.7724 -0.4052 -0.4433 0.2422  781  LEU A N     
5127 C  CA    . LEU A 678 ? 2.1994 1.4327 1.5697 -0.4149 -0.4889 0.2599  781  LEU A CA    
5128 C  C     . LEU A 678 ? 2.0844 1.3525 1.5203 -0.3960 -0.4858 0.2602  781  LEU A C     
5129 O  O     . LEU A 678 ? 2.2414 1.5302 1.6978 -0.3694 -0.4494 0.2483  781  LEU A O     
5130 C  CB    . LEU A 678 ? 2.3500 1.6202 1.7678 -0.4045 -0.5079 0.2713  781  LEU A CB    
5131 C  CG    . LEU A 678 ? 2.5316 1.7726 1.8903 -0.4195 -0.5077 0.2708  781  LEU A CG    
5132 C  CD1   . LEU A 678 ? 2.5296 1.8093 1.9415 -0.4069 -0.5244 0.2817  781  LEU A CD1   
5133 C  CD2   . LEU A 678 ? 2.0833 1.2648 1.3659 -0.4619 -0.5360 0.2779  781  LEU A CD2   
5134 N  N     . ASN A 679 ? 2.2480 1.5229 1.7178 -0.4104 -0.5250 0.2753  782  ASN A N     
5135 C  CA    . ASN A 679 ? 2.2084 1.5122 1.7386 -0.3973 -0.5260 0.2771  782  ASN A CA    
5136 C  C     . ASN A 679 ? 2.0271 1.3646 1.6287 -0.3997 -0.5677 0.2971  782  ASN A C     
5137 O  O     . ASN A 679 ? 2.2195 1.5379 1.8031 -0.4262 -0.6053 0.3118  782  ASN A O     
5138 C  CB    . ASN A 679 ? 2.3453 1.6048 1.8252 -0.4201 -0.5244 0.2716  782  ASN A CB    
5139 C  CG    . ASN A 679 ? 2.3551 1.6421 1.8903 -0.4021 -0.5130 0.2690  782  ASN A CG    
5140 O  OD1   . ASN A 679 ? 2.4438 1.7770 2.0582 -0.3867 -0.5280 0.2789  782  ASN A OD1   
5141 N  ND2   . ASN A 679 ? 2.5248 1.7814 2.0178 -0.4041 -0.4844 0.2554  782  ASN A ND2   
5142 N  N     . TRP A 680 ? 2.0891 1.4760 1.7718 -0.3722 -0.5600 0.2982  783  TRP A N     
5143 C  CA    . TRP A 680 ? 2.1854 1.6081 1.9467 -0.3700 -0.5932 0.3162  783  TRP A CA    
5144 C  C     . TRP A 680 ? 2.2081 1.6552 2.0254 -0.3584 -0.5885 0.3160  783  TRP A C     
5145 O  O     . TRP A 680 ? 2.3831 1.8191 2.1770 -0.3520 -0.5603 0.3022  783  TRP A O     
5146 C  CB    . TRP A 680 ? 2.1097 1.5733 1.9232 -0.3454 -0.5872 0.3186  783  TRP A CB    
5147 C  CG    . TRP A 680 ? 2.1487 1.5958 1.9344 -0.3616 -0.6105 0.3288  783  TRP A CG    
5148 C  CD1   . TRP A 680 ? 2.1803 1.6285 1.9932 -0.3787 -0.6533 0.3502  783  TRP A CD1   
5149 C  CD2   . TRP A 680 ? 2.2242 1.6518 1.9516 -0.3619 -0.5921 0.3192  783  TRP A CD2   
5150 N  NE1   . TRP A 680 ? 2.0539 1.4828 1.8261 -0.3901 -0.6630 0.3546  783  TRP A NE1   
5151 C  CE2   . TRP A 680 ? 2.1456 1.5613 1.8643 -0.3803 -0.6254 0.3350  783  TRP A CE2   
5152 C  CE3   . TRP A 680 ? 2.2571 1.6767 1.9411 -0.3484 -0.5507 0.2998  783  TRP A CE3   
5153 C  CZ2   . TRP A 680 ? 2.2686 1.6635 1.9344 -0.3862 -0.6177 0.3309  783  TRP A CZ2   
5154 C  CZ3   . TRP A 680 ? 2.3320 1.7328 1.9666 -0.3540 -0.5429 0.2959  783  TRP A CZ3   
5155 C  CH2   . TRP A 680 ? 2.3258 1.7137 1.9503 -0.3730 -0.5758 0.3107  783  TRP A CH2   
5156 N  N     . GLU A 681 ? 2.1991 1.6790 2.0930 -0.3556 -0.6153 0.3320  784  GLU A N     
5157 C  CA    . GLU A 681 ? 2.2325 1.7412 2.1915 -0.3432 -0.6118 0.3335  784  GLU A CA    
5158 C  C     . GLU A 681 ? 2.1155 1.6765 2.1548 -0.3101 -0.5956 0.3328  784  GLU A C     
5159 O  O     . GLU A 681 ? 2.1230 1.6986 2.1764 -0.3013 -0.5972 0.3357  784  GLU A O     
5160 C  CB    . GLU A 681 ? 2.4338 1.9373 2.4207 -0.3690 -0.6560 0.3535  784  GLU A CB    
5161 C  CG    . GLU A 681 ? 2.5331 1.9843 2.4417 -0.4052 -0.6737 0.3542  784  GLU A CG    
5162 C  CD    . GLU A 681 ? 2.9145 2.3520 2.8047 -0.4048 -0.6504 0.3408  784  GLU A CD    
5163 O  OE1   . GLU A 681 ? 2.8832 2.3259 2.7618 -0.3805 -0.6078 0.3226  784  GLU A OE1   
5164 O  OE2   . GLU A 681 ? 3.0669 2.4887 2.9553 -0.4293 -0.6753 0.3495  784  GLU A OE2   
5165 N  N     . ASN A 682 ? 2.1053 1.6925 2.1952 -0.2930 -0.5789 0.3284  785  ASN A N     
5166 C  CA    . ASN A 682 ? 1.9162 1.5510 2.0830 -0.2641 -0.5630 0.3275  785  ASN A CA    
5167 C  C     . ASN A 682 ? 1.9234 1.5807 2.1691 -0.2690 -0.5922 0.3456  785  ASN A C     
5168 O  O     . ASN A 682 ? 2.0743 1.7369 2.3478 -0.2705 -0.5921 0.3468  785  ASN A O     
5169 C  CB    . ASN A 682 ? 2.0170 1.6671 2.1878 -0.2405 -0.5218 0.3105  785  ASN A CB    
5170 C  CG    . ASN A 682 ? 1.9516 1.6480 2.1929 -0.2124 -0.5027 0.3078  785  ASN A CG    
5171 O  OD1   . ASN A 682 ? 1.9605 1.6749 2.2360 -0.2074 -0.5123 0.3142  785  ASN A OD1   
5172 N  ND2   . ASN A 682 ? 2.0902 1.8038 2.3515 -0.1947 -0.4745 0.2981  785  ASN A ND2   
5173 N  N     . PRO A 683 ? 1.6315 1.3024 1.9179 -0.2716 -0.6168 0.3607  786  PRO A N     
5174 C  CA    . PRO A 683 ? 1.6320 1.3244 1.9988 -0.2765 -0.6454 0.3804  786  PRO A CA    
5175 C  C     . PRO A 683 ? 1.7979 1.5306 2.2450 -0.2506 -0.6216 0.3761  786  PRO A C     
5176 O  O     . PRO A 683 ? 1.8223 1.5761 2.3446 -0.2516 -0.6408 0.3920  786  PRO A O     
5177 C  CB    . PRO A 683 ? 1.6739 1.3692 2.0587 -0.2821 -0.6714 0.3962  786  PRO A CB    
5178 C  CG    . PRO A 683 ? 1.6169 1.3098 1.9592 -0.2672 -0.6431 0.3800  786  PRO A CG    
5179 C  CD    . PRO A 683 ? 1.8089 1.4754 2.0713 -0.2701 -0.6190 0.3612  786  PRO A CD    
5180 N  N     . ASP A 684 ? 1.6629 1.4071 2.0976 -0.2280 -0.5806 0.3560  787  ASP A N     
5181 C  CA    . ASP A 684 ? 1.7315 1.5102 2.2342 -0.2057 -0.5564 0.3508  787  ASP A CA    
5182 C  C     . ASP A 684 ? 1.8282 1.6049 2.3542 -0.2151 -0.5647 0.3559  787  ASP A C     
5183 O  O     . ASP A 684 ? 1.7551 1.5028 2.2241 -0.2312 -0.5695 0.3526  787  ASP A O     
5184 C  CB    . ASP A 684 ? 1.6721 1.4600 2.1454 -0.1831 -0.5130 0.3292  787  ASP A CB    
5185 C  CG    . ASP A 684 ? 1.7124 1.5373 2.2543 -0.1594 -0.4871 0.3237  787  ASP A CG    
5186 O  OD1   . ASP A 684 ? 1.9197 1.7580 2.5202 -0.1597 -0.4931 0.3314  787  ASP A OD1   
5187 O  OD2   . ASP A 684 ? 1.7042 1.5443 2.2403 -0.1416 -0.4601 0.3116  787  ASP A OD2   
5188 N  N     . ILE A 685 ? 1.7270 1.5337 2.3380 -0.2057 -0.5650 0.3639  788  ILE A N     
5189 C  CA    . ILE A 685 ? 1.9056 1.7145 2.5478 -0.2137 -0.5715 0.3692  788  ILE A CA    
5190 C  C     . ILE A 685 ? 1.9257 1.7288 2.5310 -0.2033 -0.5368 0.3504  788  ILE A C     
5191 O  O     . ILE A 685 ? 2.1648 1.9568 2.7661 -0.2149 -0.5419 0.3519  788  ILE A O     
5192 C  CB    . ILE A 685 ? 2.0343 1.8786 2.7808 -0.2036 -0.5748 0.3813  788  ILE A CB    
5193 C  CG1   . ILE A 685 ? 1.7151 1.5862 2.4946 -0.1750 -0.5380 0.3685  788  ILE A CG1   
5194 C  CG2   . ILE A 685 ? 1.7839 1.6301 2.5710 -0.2196 -0.6171 0.4056  788  ILE A CG2   
5195 C  CD1   . ILE A 685 ? 1.6884 1.5911 2.5691 -0.1642 -0.5365 0.3788  788  ILE A CD1   
5196 N  N     . MET A 686 ? 1.5174 1.3278 2.0960 -0.1824 -0.5020 0.3335  789  MET A N     
5197 C  CA    . MET A 686 ? 1.4147 1.2198 1.9555 -0.1711 -0.4685 0.3172  789  MET A CA    
5198 C  C     . MET A 686 ? 1.7241 1.4967 2.1736 -0.1778 -0.4620 0.3074  789  MET A C     
5199 O  O     . MET A 686 ? 1.8896 1.6638 2.3065 -0.1617 -0.4296 0.2933  789  MET A O     
5200 C  CB    . MET A 686 ? 1.8743 1.7115 2.4498 -0.1435 -0.4330 0.3062  789  MET A CB    
5201 C  CG    . MET A 686 ? 1.5112 1.3793 2.1771 -0.1355 -0.4343 0.3141  789  MET A CG    
5202 S  SD    . MET A 686 ? 1.5985 1.4691 2.3108 -0.1433 -0.4393 0.3211  789  MET A SD    
5203 C  CE    . MET A 686 ? 1.4264 1.2970 2.1010 -0.1259 -0.3956 0.3022  789  MET A CE    
5204 N  N     . SER A 687 ? 1.6423 1.3848 2.0502 -0.2019 -0.4919 0.3156  790  SER A N     
5205 C  CA    . SER A 687 ? 1.7600 1.4682 2.0806 -0.2101 -0.4850 0.3064  790  SER A CA    
5206 C  C     . SER A 687 ? 2.1493 1.8343 2.4248 -0.2118 -0.4641 0.2958  790  SER A C     
5207 O  O     . SER A 687 ? 2.1789 1.8399 2.3878 -0.2112 -0.4463 0.2852  790  SER A O     
5208 C  CB    . SER A 687 ? 1.8075 1.4863 2.0933 -0.2386 -0.5230 0.3183  790  SER A CB    
5209 O  OG    . SER A 687 ? 2.0685 1.7091 2.2669 -0.2492 -0.5147 0.3087  790  SER A OG    
5210 N  N     . GLU A 688 ? 2.1207 1.8117 2.4327 -0.2138 -0.4645 0.2987  791  GLU A N     
5211 C  CA    . GLU A 688 ? 1.9207 1.5873 2.1913 -0.2163 -0.4447 0.2893  791  GLU A CA    
5212 C  C     . GLU A 688 ? 2.0217 1.7027 2.2825 -0.1881 -0.4017 0.2753  791  GLU A C     
5213 O  O     . GLU A 688 ? 1.8865 1.5421 2.0950 -0.1874 -0.3805 0.2661  791  GLU A O     
5214 C  CB    . GLU A 688 ? 1.9572 1.6283 2.2736 -0.2262 -0.4568 0.2967  791  GLU A CB    
5215 C  CG    . GLU A 688 ? 2.2264 1.8926 2.5686 -0.2529 -0.5019 0.3140  791  GLU A CG    
5216 C  CD    . GLU A 688 ? 2.4700 2.0894 2.7356 -0.2833 -0.5245 0.3157  791  GLU A CD    
5217 O  OE1   . GLU A 688 ? 2.7092 2.2950 2.9074 -0.2873 -0.5041 0.3031  791  GLU A OE1   
5218 O  OE2   . GLU A 688 ? 2.2350 1.8500 2.5073 -0.3036 -0.5620 0.3301  791  GLU A OE2   
5219 N  N     . LEU A 689 ? 1.9020 1.6224 2.2119 -0.1655 -0.3882 0.2742  792  LEU A N     
5220 C  CA    . LEU A 689 ? 1.7478 1.4860 2.0524 -0.1398 -0.3500 0.2630  792  LEU A CA    
5221 C  C     . LEU A 689 ? 1.8659 1.5990 2.1205 -0.1318 -0.3364 0.2557  792  LEU A C     
5222 O  O     . LEU A 689 ? 2.0179 1.7508 2.2435 -0.1170 -0.3067 0.2472  792  LEU A O     
5223 C  CB    . LEU A 689 ? 1.7386 1.5199 2.1152 -0.1213 -0.3400 0.2642  792  LEU A CB    
5224 C  CG    . LEU A 689 ? 1.6217 1.4125 2.0571 -0.1270 -0.3503 0.2716  792  LEU A CG    
5225 C  CD1   . LEU A 689 ? 1.5406 1.3711 2.0425 -0.1079 -0.3346 0.2708  792  LEU A CD1   
5226 C  CD2   . LEU A 689 ? 1.8208 1.5902 2.2311 -0.1311 -0.3378 0.2679  792  LEU A CD2   
5227 N  N     . LEU A 690 ? 1.8330 1.5629 2.0789 -0.1412 -0.3572 0.2600  793  LEU A N     
5228 C  CA    . LEU A 690 ? 1.7503 1.4732 1.9482 -0.1366 -0.3466 0.2538  793  LEU A CA    
5229 C  C     . LEU A 690 ? 2.1032 1.7796 2.2340 -0.1600 -0.3608 0.2542  793  LEU A C     
5230 O  O     . LEU A 690 ? 2.5687 2.2179 2.6851 -0.1782 -0.3742 0.2575  793  LEU A O     
5231 C  CB    . LEU A 690 ? 1.9238 1.6736 2.1555 -0.1308 -0.3568 0.2572  793  LEU A CB    
5232 C  CG    . LEU A 690 ? 1.9183 1.6799 2.1232 -0.1168 -0.3366 0.2492  793  LEU A CG    
5233 C  CD1   . LEU A 690 ? 1.4682 1.2580 1.6878 -0.0928 -0.3028 0.2412  793  LEU A CD1   
5234 C  CD2   . LEU A 690 ? 1.5296 1.3082 1.7622 -0.1177 -0.3527 0.2538  793  LEU A CD2   
5235 N  N     . PHE A 691 ? 1.9933 1.6588 2.0807 -0.1609 -0.3571 0.2505  794  PHE A N     
5236 C  CA    . PHE A 691 ? 2.0558 1.6750 2.0756 -0.1842 -0.3687 0.2501  794  PHE A CA    
5237 C  C     . PHE A 691 ? 2.0992 1.7043 2.1283 -0.2102 -0.4108 0.2626  794  PHE A C     
5238 O  O     . PHE A 691 ? 1.9796 1.6132 2.0652 -0.2073 -0.4299 0.2718  794  PHE A O     
5239 C  CB    . PHE A 691 ? 2.2310 1.8449 2.2075 -0.1785 -0.3541 0.2437  794  PHE A CB    
5240 C  CG    . PHE A 691 ? 2.5856 2.2117 2.5494 -0.1550 -0.3144 0.2335  794  PHE A CG    
5241 C  CD1   . PHE A 691 ? 2.4934 2.0851 2.4029 -0.1582 -0.2932 0.2265  794  PHE A CD1   
5242 C  CD2   . PHE A 691 ? 2.6672 2.3382 2.6733 -0.1306 -0.2981 0.2315  794  PHE A CD2   
5243 C  CE1   . PHE A 691 ? 2.2775 1.8819 2.1801 -0.1357 -0.2574 0.2198  794  PHE A CE1   
5244 C  CE2   . PHE A 691 ? 2.3356 2.0200 2.3313 -0.1101 -0.2643 0.2246  794  PHE A CE2   
5245 C  CZ    . PHE A 691 ? 2.1510 1.8033 2.0973 -0.1118 -0.2443 0.2197  794  PHE A CZ    
5246 N  N     . GLN A 692 ? 2.2576 1.8171 2.2302 -0.2365 -0.4248 0.2636  795  GLN A N     
5247 C  CA    . GLN A 692 ? 2.1680 1.7099 2.1403 -0.2651 -0.4671 0.2770  795  GLN A CA    
5248 C  C     . GLN A 692 ? 2.1646 1.6703 2.0702 -0.2863 -0.4811 0.2780  795  GLN A C     
5249 O  O     . GLN A 692 ? 2.2907 1.7900 2.2026 -0.3068 -0.5181 0.2916  795  GLN A O     
5250 C  CB    . GLN A 692 ? 2.1288 1.6461 2.0932 -0.2853 -0.4797 0.2801  795  GLN A CB    
5251 C  CG    . GLN A 692 ? 2.2308 1.7824 2.2667 -0.2696 -0.4733 0.2824  795  GLN A CG    
5252 C  CD    . GLN A 692 ? 2.4512 1.9771 2.4762 -0.2905 -0.4841 0.2846  795  GLN A CD    
5253 O  OE1   . GLN A 692 ? 2.4353 1.9148 2.3902 -0.3125 -0.4853 0.2798  795  GLN A OE1   
5254 N  NE2   . GLN A 692 ? 2.3246 1.8792 2.4183 -0.2846 -0.4908 0.2915  795  GLN A NE2   
5255 N  N     . ASN A 693 ? 2.4303 1.9124 2.2742 -0.2822 -0.4527 0.2651  796  ASN A N     
5256 C  CA    . ASN A 693 ? 2.6028 2.0471 2.3778 -0.3024 -0.4609 0.2641  796  ASN A CA    
5257 C  C     . ASN A 693 ? 2.4489 1.9160 2.2263 -0.2808 -0.4400 0.2584  796  ASN A C     
5258 O  O     . ASN A 693 ? 2.3719 1.8389 2.1264 -0.2636 -0.4035 0.2460  796  ASN A O     
5259 C  CB    . ASN A 693 ? 2.6498 2.0404 2.3454 -0.3196 -0.4438 0.2534  796  ASN A CB    
5260 C  CG    . ASN A 693 ? 2.6054 1.9674 2.2889 -0.3473 -0.4682 0.2593  796  ASN A CG    
5261 O  OD1   . ASN A 693 ? 2.4819 1.8704 2.2257 -0.3485 -0.4931 0.2708  796  ASN A OD1   
5262 N  ND2   . ASN A 693 ? 2.5865 1.8934 2.1922 -0.3704 -0.4602 0.2512  796  ASN A ND2   
5263 N  N     . ASN A 694 ? 2.1127 1.6000 1.9202 -0.2819 -0.4634 0.2683  797  ASN A N     
5264 C  CA    . ASN A 694 ? 1.9771 1.4828 1.7834 -0.2660 -0.4479 0.2637  797  ASN A CA    
5265 C  C     . ASN A 694 ? 1.9786 1.4387 1.7023 -0.2852 -0.4445 0.2589  797  ASN A C     
5266 O  O     . ASN A 694 ? 2.4011 1.8348 2.0962 -0.3107 -0.4747 0.2682  797  ASN A O     
5267 C  CB    . ASN A 694 ? 2.1884 1.7269 2.0539 -0.2621 -0.4732 0.2760  797  ASN A CB    
5268 C  CG    . ASN A 694 ? 1.7768 1.3671 1.7158 -0.2322 -0.4559 0.2733  797  ASN A CG    
5269 O  OD1   . ASN A 694 ? 1.5978 1.2043 1.5347 -0.2113 -0.4219 0.2613  797  ASN A OD1   
5270 N  ND2   . ASN A 694 ? 1.9497 1.5657 1.9542 -0.2306 -0.4789 0.2852  797  ASN A ND2   
5271 N  N     . GLU A 695 ? 1.9438 1.3941 1.6295 -0.2732 -0.4069 0.2450  798  GLU A N     
5272 C  CA    . GLU A 695 ? 2.0723 1.4768 1.6783 -0.2896 -0.3954 0.2380  798  GLU A CA    
5273 C  C     . GLU A 695 ? 2.1357 1.5604 1.7412 -0.2740 -0.3776 0.2336  798  GLU A C     
5274 O  O     . GLU A 695 ? 2.2122 1.6750 1.8536 -0.2459 -0.3508 0.2277  798  GLU A O     
5275 C  CB    . GLU A 695 ? 2.3576 1.7315 1.9201 -0.2889 -0.3634 0.2260  798  GLU A CB    
5276 C  CG    . GLU A 695 ? 2.4202 1.7813 1.9927 -0.2996 -0.3758 0.2289  798  GLU A CG    
5277 C  CD    . GLU A 695 ? 2.5933 1.9344 2.1393 -0.2909 -0.3388 0.2169  798  GLU A CD    
5278 O  OE1   . GLU A 695 ? 2.7009 2.0373 2.2209 -0.2767 -0.3038 0.2073  798  GLU A OE1   
5279 O  OE2   . GLU A 695 ? 2.7235 2.0539 2.2770 -0.2981 -0.3443 0.2178  798  GLU A OE2   
5280 N  N     . ILE A 696 ? 2.1422 1.5416 1.7066 -0.2934 -0.3933 0.2372  799  ILE A N     
5281 C  CA    . ILE A 696 ? 2.0914 1.5068 1.6530 -0.2827 -0.3802 0.2341  799  ILE A CA    
5282 C  C     . ILE A 696 ? 2.1716 1.5349 1.6498 -0.3047 -0.3722 0.2288  799  ILE A C     
5283 O  O     . ILE A 696 ? 2.3648 1.6850 1.7971 -0.3349 -0.3974 0.2345  799  ILE A O     
5284 C  CB    . ILE A 696 ? 1.7754 1.2206 1.3857 -0.2821 -0.4105 0.2463  799  ILE A CB    
5285 C  CG1   . ILE A 696 ? 2.0342 1.5300 1.7279 -0.2598 -0.4141 0.2502  799  ILE A CG1   
5286 C  CG2   . ILE A 696 ? 1.8081 1.2648 1.4087 -0.2743 -0.3969 0.2424  799  ILE A CG2   
5287 C  CD1   . ILE A 696 ? 2.0072 1.4990 1.7306 -0.2736 -0.4479 0.2626  799  ILE A CD1   
5288 N  N     . ILE A 697 ? 2.1767 1.5440 1.6355 -0.2906 -0.3371 0.2184  800  ILE A N     
5289 C  CA    . ILE A 697 ? 2.3302 1.6510 1.7136 -0.3088 -0.3239 0.2123  800  ILE A CA    
5290 C  C     . ILE A 697 ? 2.3474 1.6797 1.7333 -0.3123 -0.3377 0.2177  800  ILE A C     
5291 O  O     . ILE A 697 ? 2.1560 1.5364 1.5941 -0.2893 -0.3302 0.2179  800  ILE A O     
5292 C  CB    . ILE A 697 ? 2.3509 1.6681 1.7139 -0.2914 -0.2756 0.1988  800  ILE A CB    
5293 C  CG1   . ILE A 697 ? 2.2272 1.5274 1.5839 -0.2892 -0.2610 0.1938  800  ILE A CG1   
5294 C  CG2   . ILE A 697 ? 2.2289 1.5000 1.5184 -0.3090 -0.2586 0.1920  800  ILE A CG2   
5295 C  CD1   . ILE A 697 ? 2.2900 1.5967 1.6448 -0.2662 -0.2135 0.1834  800  ILE A CD1   
5296 N  N     . PHE A 698 ? 2.3911 1.6778 1.7186 -0.3425 -0.3577 0.2221  801  PHE A N     
5297 C  CA    . PHE A 698 ? 1.9940 1.2831 1.3150 -0.3498 -0.3721 0.2281  801  PHE A CA    
5298 C  C     . PHE A 698 ? 2.2245 1.4783 1.4777 -0.3579 -0.3413 0.2172  801  PHE A C     
5299 O  O     . PHE A 698 ? 2.6122 1.8096 1.7924 -0.3872 -0.3470 0.2165  801  PHE A O     
5300 C  CB    . PHE A 698 ? 1.9171 1.1827 1.2256 -0.3783 -0.4199 0.2440  801  PHE A CB    
5301 C  CG    . PHE A 698 ? 2.1038 1.3761 1.4161 -0.3838 -0.4376 0.2527  801  PHE A CG    
5302 C  CD1   . PHE A 698 ? 1.9848 1.3063 1.3724 -0.3659 -0.4536 0.2617  801  PHE A CD1   
5303 C  CD2   . PHE A 698 ? 2.2466 1.4737 1.4860 -0.4074 -0.4367 0.2517  801  PHE A CD2   
5304 C  CE1   . PHE A 698 ? 1.9879 1.3137 1.3796 -0.3709 -0.4686 0.2698  801  PHE A CE1   
5305 C  CE2   . PHE A 698 ? 2.2102 1.4423 1.4527 -0.4126 -0.4526 0.2603  801  PHE A CE2   
5306 C  CZ    . PHE A 698 ? 1.9819 1.2634 1.3013 -0.3940 -0.4687 0.2695  801  PHE A CZ    
5307 N  N     . LYS A 699 ? 2.2575 1.5445 1.5350 -0.3328 -0.3082 0.2089  802  LYS A N     
5308 C  CA    . LYS A 699 ? 2.2789 1.5405 1.5040 -0.3363 -0.2752 0.1989  802  LYS A CA    
5309 C  C     . LYS A 699 ? 2.1185 1.3767 1.3295 -0.3486 -0.2917 0.2048  802  LYS A C     
5310 O  O     . LYS A 699 ? 2.2117 1.5167 1.4771 -0.3315 -0.2972 0.2087  802  LYS A O     
5311 C  CB    . LYS A 699 ? 2.3406 1.6430 1.6033 -0.3040 -0.2340 0.1896  802  LYS A CB    
5312 C  CG    . LYS A 699 ? 2.2350 1.5033 1.4521 -0.3036 -0.1941 0.1781  802  LYS A CG    
5313 C  CD    . LYS A 699 ? 2.6132 1.8336 1.7592 -0.3240 -0.1777 0.1724  802  LYS A CD    
5314 C  CE    . LYS A 699 ? 2.8959 2.0860 2.0047 -0.3199 -0.1316 0.1605  802  LYS A CE    
5315 N  NZ    . LYS A 699 ? 3.0374 2.1793 2.0769 -0.3398 -0.1117 0.1539  802  LYS A NZ    
5316 N  N     . ASN A 700 ? 2.2571 1.4578 1.3928 -0.3792 -0.2986 0.2051  803  ASN A N     
5317 C  CA    . ASN A 700 ? 2.1583 1.3482 1.2730 -0.3948 -0.3170 0.2123  803  ASN A CA    
5318 C  C     . ASN A 700 ? 2.4557 1.6468 1.5497 -0.3871 -0.2799 0.2021  803  ASN A C     
5319 O  O     . ASN A 700 ? 2.2161 1.4479 1.3528 -0.3717 -0.2786 0.2041  803  ASN A O     
5320 C  CB    . ASN A 700 ? 2.4370 1.5637 1.4785 -0.4342 -0.3460 0.2196  803  ASN A CB    
5321 C  CG    . ASN A 700 ? 2.6980 1.8081 1.7110 -0.4525 -0.3649 0.2281  803  ASN A CG    
5322 O  OD1   . ASN A 700 ? 2.5621 1.7134 1.6253 -0.4365 -0.3701 0.2329  803  ASN A OD1   
5323 N  ND2   . ASN A 700 ? 2.9624 2.0097 1.8918 -0.4875 -0.3746 0.2299  803  ASN A ND2   
5324 N  N     . GLY A 701 ? 2.7929 1.9388 1.8224 -0.3983 -0.2484 0.1910  804  GLY A N     
5325 C  CA    . GLY A 701 ? 2.5855 1.7251 1.5890 -0.3951 -0.2131 0.1822  804  GLY A CA    
5326 C  C     . GLY A 701 ? 2.6035 1.8032 1.6712 -0.3595 -0.1814 0.1763  804  GLY A C     
5327 O  O     . GLY A 701 ? 2.2455 1.4752 1.3374 -0.3510 -0.1775 0.1775  804  GLY A O     
5328 N  N     . ASP A 702 ? 2.8532 2.0707 1.9483 -0.3395 -0.1591 0.1707  805  ASP A N     
5329 C  CA    . ASP A 702 ? 2.7300 2.0022 1.8816 -0.3070 -0.1275 0.1663  805  ASP A CA    
5330 C  C     . ASP A 702 ? 2.6363 1.9731 1.8639 -0.2879 -0.1503 0.1738  805  ASP A C     
5331 O  O     . ASP A 702 ? 2.6223 1.9692 1.8764 -0.2900 -0.1837 0.1813  805  ASP A O     
5332 C  CB    . ASP A 702 ? 2.8668 2.1396 2.0285 -0.2912 -0.1007 0.1605  805  ASP A CB    
5333 C  CG    . ASP A 702 ? 3.0982 2.4311 2.3226 -0.2574 -0.0719 0.1589  805  ASP A CG    
5334 O  OD1   . ASP A 702 ? 3.2318 2.5720 2.4513 -0.2512 -0.0427 0.1550  805  ASP A OD1   
5335 O  OD2   . ASP A 702 ? 3.0388 2.4120 2.3176 -0.2377 -0.0787 0.1624  805  ASP A OD2   
5336 N  N     . ASP A 703 ? 2.3157 1.6956 1.5783 -0.2700 -0.1309 0.1718  806  ASP A N     
5337 C  CA    . ASP A 703 ? 2.3065 1.7472 1.6386 -0.2521 -0.1471 0.1770  806  ASP A CA    
5338 C  C     . ASP A 703 ? 2.4449 1.9254 1.8308 -0.2282 -0.1422 0.1773  806  ASP A C     
5339 O  O     . ASP A 703 ? 2.3492 1.8338 1.7363 -0.2146 -0.1118 0.1726  806  ASP A O     
5340 C  CB    . ASP A 703 ? 2.1881 1.6620 1.5380 -0.2422 -0.1264 0.1741  806  ASP A CB    
5341 C  CG    . ASP A 703 ? 2.2764 1.8080 1.6909 -0.2277 -0.1429 0.1783  806  ASP A CG    
5342 O  OD1   . ASP A 703 ? 2.3397 1.8785 1.7798 -0.2291 -0.1733 0.1841  806  ASP A OD1   
5343 O  OD2   . ASP A 703 ? 2.0718 1.6412 1.5121 -0.2158 -0.1246 0.1758  806  ASP A OD2   
5344 N  N     . LEU A 704 ? 2.3939 1.9030 1.8257 -0.2230 -0.1713 0.1835  807  LEU A N     
5345 C  CA    . LEU A 704 ? 2.2648 1.8111 1.7482 -0.2021 -0.1699 0.1845  807  LEU A CA    
5346 C  C     . LEU A 704 ? 2.0471 1.6566 1.5935 -0.1816 -0.1679 0.1853  807  LEU A C     
5347 O  O     . LEU A 704 ? 2.0699 1.7109 1.6633 -0.1692 -0.1789 0.1880  807  LEU A O     
5348 C  CB    . LEU A 704 ? 2.1402 1.6683 1.6284 -0.2123 -0.2022 0.1904  807  LEU A CB    
5349 C  CG    . LEU A 704 ? 2.3668 1.8341 1.7947 -0.2336 -0.2063 0.1897  807  LEU A CG    
5350 C  CD1   . LEU A 704 ? 2.2882 1.7510 1.7361 -0.2387 -0.2357 0.1962  807  LEU A CD1   
5351 C  CD2   . LEU A 704 ? 2.2042 1.6557 1.6052 -0.2257 -0.1676 0.1814  807  LEU A CD2   
5352 N  N     . ARG A 705 ? 2.0463 1.6737 1.5926 -0.1792 -0.1533 0.1828  808  ARG A N     
5353 C  CA    . ARG A 705 ? 1.9422 1.6288 1.5428 -0.1615 -0.1480 0.1826  808  ARG A CA    
5354 C  C     . ARG A 705 ? 1.9559 1.6767 1.5784 -0.1404 -0.1165 0.1804  808  ARG A C     
5355 O  O     . ARG A 705 ? 1.7476 1.5181 1.4189 -0.1240 -0.1148 0.1815  808  ARG A O     
5356 C  CB    . ARG A 705 ? 2.1345 1.8267 1.7279 -0.1706 -0.1497 0.1817  808  ARG A CB    
5357 C  CG    . ARG A 705 ? 1.9760 1.6467 1.5632 -0.1877 -0.1828 0.1863  808  ARG A CG    
5358 C  CD    . ARG A 705 ? 2.0174 1.6849 1.5883 -0.1986 -0.1818 0.1853  808  ARG A CD    
5359 N  NE    . ARG A 705 ? 2.4277 2.0744 1.9954 -0.2141 -0.2136 0.1916  808  ARG A NE    
5360 C  CZ    . ARG A 705 ? 2.5345 2.1297 2.0562 -0.2348 -0.2316 0.1966  808  ARG A CZ    
5361 N  NH1   . ARG A 705 ? 2.6641 2.2195 2.1341 -0.2442 -0.2200 0.1943  808  ARG A NH1   
5362 N  NH2   . ARG A 705 ? 2.3289 1.9110 1.8561 -0.2470 -0.2618 0.2048  808  ARG A NH2   
5363 N  N     . GLN A 706 ? 2.2294 1.9233 1.8165 -0.1410 -0.0910 0.1778  809  GLN A N     
5364 C  CA    . GLN A 706 ? 1.9465 1.6702 1.5566 -0.1201 -0.0608 0.1781  809  GLN A CA    
5365 C  C     . GLN A 706 ? 1.8086 1.5427 1.4445 -0.1071 -0.0644 0.1806  809  GLN A C     
5366 O  O     . GLN A 706 ? 1.8360 1.6126 1.5105 -0.0870 -0.0493 0.1835  809  GLN A O     
5367 C  CB    . GLN A 706 ? 2.1709 1.8579 1.7373 -0.1243 -0.0305 0.1748  809  GLN A CB    
5368 C  CG    . GLN A 706 ? 2.2952 1.9719 1.8356 -0.1364 -0.0217 0.1721  809  GLN A CG    
5369 C  CD    . GLN A 706 ? 2.4093 2.0338 1.8993 -0.1631 -0.0446 0.1699  809  GLN A CD    
5370 O  OE1   . GLN A 706 ? 2.4532 2.0507 1.9298 -0.1731 -0.0691 0.1713  809  GLN A OE1   
5371 N  NE2   . GLN A 706 ? 2.3193 1.9299 1.7820 -0.1754 -0.0373 0.1676  809  GLN A NE2   
5372 N  N     . ASP A 707 ? 1.8352 1.5317 1.4508 -0.1192 -0.0848 0.1806  810  ASP A N     
5373 C  CA    . ASP A 707 ? 1.9172 1.6205 1.5560 -0.1085 -0.0883 0.1828  810  ASP A CA    
5374 C  C     . ASP A 707 ? 1.8028 1.5566 1.4982 -0.0967 -0.1051 0.1860  810  ASP A C     
5375 O  O     . ASP A 707 ? 1.7699 1.5544 1.4990 -0.0791 -0.0956 0.1882  810  ASP A O     
5376 C  CB    . ASP A 707 ? 2.0865 1.7354 1.6875 -0.1272 -0.1067 0.1822  810  ASP A CB    
5377 C  CG    . ASP A 707 ? 2.2794 1.8742 1.8207 -0.1393 -0.0863 0.1777  810  ASP A CG    
5378 O  OD1   . ASP A 707 ? 2.0864 1.6868 1.6271 -0.1255 -0.0532 0.1759  810  ASP A OD1   
5379 O  OD2   . ASP A 707 ? 2.5430 2.0889 2.0378 -0.1630 -0.1029 0.1765  810  ASP A OD2   
5380 N  N     . MET A 708 ? 1.7448 1.5060 1.4505 -0.1066 -0.1288 0.1864  811  MET A N     
5381 C  CA    . MET A 708 ? 1.7020 1.5054 1.4592 -0.0975 -0.1435 0.1882  811  MET A CA    
5382 C  C     . MET A 708 ? 1.3978 1.2551 1.1902 -0.0786 -0.1234 0.1882  811  MET A C     
5383 O  O     . MET A 708 ? 1.5003 1.3892 1.3298 -0.0656 -0.1236 0.1898  811  MET A O     
5384 C  CB    . MET A 708 ? 1.6207 1.4206 1.3818 -0.1113 -0.1680 0.1887  811  MET A CB    
5385 C  CG    . MET A 708 ? 1.4175 1.1724 1.1563 -0.1295 -0.1948 0.1921  811  MET A CG    
5386 S  SD    . MET A 708 ? 1.6549 1.4164 1.4179 -0.1400 -0.2241 0.1956  811  MET A SD    
5387 C  CE    . MET A 708 ? 2.0623 1.8337 1.8059 -0.1434 -0.2086 0.1913  811  MET A CE    
5388 N  N     . LEU A 709 ? 1.5436 1.4125 1.3249 -0.0778 -0.1063 0.1869  812  LEU A N     
5389 C  CA    . LEU A 709 ? 1.4952 1.4175 1.3101 -0.0619 -0.0892 0.1886  812  LEU A CA    
5390 C  C     . LEU A 709 ? 1.7270 1.6605 1.5521 -0.0448 -0.0688 0.1929  812  LEU A C     
5391 O  O     . LEU A 709 ? 1.6660 1.6438 1.5276 -0.0305 -0.0637 0.1965  812  LEU A O     
5392 C  CB    . LEU A 709 ? 1.2205 1.1515 1.0221 -0.0663 -0.0759 0.1874  812  LEU A CB    
5393 C  CG    . LEU A 709 ? 1.3973 1.3871 1.2349 -0.0538 -0.0628 0.1901  812  LEU A CG    
5394 C  CD1   . LEU A 709 ? 1.3621 1.3851 1.2332 -0.0543 -0.0812 0.1883  812  LEU A CD1   
5395 C  CD2   . LEU A 709 ? 1.4520 1.4469 1.2754 -0.0595 -0.0488 0.1893  812  LEU A CD2   
5396 N  N     . THR A 710 ? 1.5388 1.4308 1.3305 -0.0468 -0.0564 0.1927  813  THR A N     
5397 C  CA    . THR A 710 ? 1.3574 1.2550 1.1585 -0.0305 -0.0357 0.1971  813  THR A CA    
5398 C  C     . THR A 710 ? 1.7559 1.6539 1.5760 -0.0257 -0.0494 0.1984  813  THR A C     
5399 O  O     . THR A 710 ? 1.7294 1.6605 1.5806 -0.0090 -0.0401 0.2035  813  THR A O     
5400 C  CB    . THR A 710 ? 1.6731 1.5216 1.4306 -0.0354 -0.0155 0.1953  813  THR A CB    
5401 O  OG1   . THR A 710 ? 1.6136 1.4610 1.3542 -0.0405 -0.0014 0.1938  813  THR A OG1   
5402 C  CG2   . THR A 710 ? 1.5605 1.4154 1.3307 -0.0169 0.0095  0.2006  813  THR A CG2   
5403 N  N     . LEU A 711 ? 1.6769 1.5393 1.4800 -0.0406 -0.0722 0.1949  814  LEU A N     
5404 C  CA    . LEU A 711 ? 1.4734 1.3362 1.2975 -0.0374 -0.0862 0.1963  814  LEU A CA    
5405 C  C     . LEU A 711 ? 1.4995 1.4121 1.3709 -0.0286 -0.0962 0.1977  814  LEU A C     
5406 O  O     . LEU A 711 ? 1.5794 1.5034 1.4755 -0.0207 -0.0999 0.1997  814  LEU A O     
5407 C  CB    . LEU A 711 ? 1.7121 1.5286 1.5109 -0.0570 -0.1106 0.1939  814  LEU A CB    
5408 C  CG    . LEU A 711 ? 1.6693 1.4332 1.4271 -0.0657 -0.1051 0.1927  814  LEU A CG    
5409 C  CD1   . LEU A 711 ? 1.8784 1.6502 1.6550 -0.0508 -0.0924 0.1951  814  LEU A CD1   
5410 C  CD2   . LEU A 711 ? 1.8786 1.6135 1.5920 -0.0711 -0.0832 0.1898  814  LEU A CD2   
5411 N  N     . GLN A 712 ? 1.4290 1.3695 1.3119 -0.0308 -0.0995 0.1963  815  GLN A N     
5412 C  CA    . GLN A 712 ? 1.6061 1.5915 1.5297 -0.0244 -0.1064 0.1963  815  GLN A CA    
5413 C  C     . GLN A 712 ? 1.5628 1.5931 1.5082 -0.0075 -0.0862 0.2011  815  GLN A C     
5414 O  O     . GLN A 712 ? 1.7229 1.7818 1.6977 0.0014  -0.0872 0.2030  815  GLN A O     
5415 C  CB    . GLN A 712 ? 1.6882 1.6818 1.6141 -0.0360 -0.1192 0.1923  815  GLN A CB    
5416 C  CG    . GLN A 712 ? 1.7259 1.7599 1.6902 -0.0323 -0.1257 0.1905  815  GLN A CG    
5417 C  CD    . GLN A 712 ? 1.4338 1.4867 1.3999 -0.0400 -0.1276 0.1868  815  GLN A CD    
5418 O  OE1   . GLN A 712 ? 1.2604 1.3109 1.2051 -0.0433 -0.1182 0.1871  815  GLN A OE1   
5419 N  NE2   . GLN A 712 ? 1.2914 1.3620 1.2833 -0.0435 -0.1382 0.1831  815  GLN A NE2   
5420 N  N     . ILE A 713 ? 1.5864 1.6236 1.5186 -0.0035 -0.0679 0.2038  816  ILE A N     
5421 C  CA    . ILE A 713 ? 1.5075 1.5892 1.4627 0.0123  -0.0497 0.2112  816  ILE A CA    
5422 C  C     . ILE A 713 ? 1.4489 1.5264 1.4119 0.0262  -0.0393 0.2172  816  ILE A C     
5423 O  O     . ILE A 713 ? 1.3751 1.4911 1.3658 0.0385  -0.0338 0.2237  816  ILE A O     
5424 C  CB    . ILE A 713 ? 1.5266 1.6141 1.4689 0.0134  -0.0317 0.2141  816  ILE A CB    
5425 C  CG1   . ILE A 713 ? 1.6184 1.7440 1.5748 0.0074  -0.0372 0.2125  816  ILE A CG1   
5426 C  CG2   . ILE A 713 ? 1.4974 1.6034 1.4520 0.0313  -0.0078 0.2245  816  ILE A CG2   
5427 C  CD1   . ILE A 713 ? 1.7182 1.8235 1.6622 -0.0102 -0.0578 0.2032  816  ILE A CD1   
5428 N  N     . ILE A 714 ? 1.4964 1.5259 1.4332 0.0229  -0.0369 0.2153  817  ILE A N     
5429 C  CA    . ILE A 714 ? 1.4674 1.4872 1.4096 0.0344  -0.0273 0.2200  817  ILE A CA    
5430 C  C     . ILE A 714 ? 1.4818 1.5208 1.4521 0.0369  -0.0423 0.2198  817  ILE A C     
5431 O  O     . ILE A 714 ? 1.5445 1.6051 1.5353 0.0507  -0.0330 0.2265  817  ILE A O     
5432 C  CB    . ILE A 714 ? 1.7073 1.6671 1.6116 0.0257  -0.0245 0.2158  817  ILE A CB    
5433 C  CG1   . ILE A 714 ? 1.3509 1.2926 1.2294 0.0272  -0.0007 0.2170  817  ILE A CG1   
5434 C  CG2   . ILE A 714 ? 1.6902 1.6355 1.6002 0.0334  -0.0207 0.2186  817  ILE A CG2   
5435 C  CD1   . ILE A 714 ? 1.4556 1.3344 1.2901 0.0162  0.0048  0.2118  817  ILE A CD1   
5436 N  N     . ARG A 715 ? 1.3412 1.3720 1.3140 0.0237  -0.0647 0.2129  818  ARG A N     
5437 C  CA    . ARG A 715 ? 1.4099 1.4600 1.4126 0.0256  -0.0768 0.2121  818  ARG A CA    
5438 C  C     . ARG A 715 ? 1.3532 1.4568 1.3834 0.0340  -0.0713 0.2152  818  ARG A C     
5439 O  O     . ARG A 715 ? 1.7243 1.8496 1.7766 0.0425  -0.0687 0.2185  818  ARG A O     
5440 C  CB    . ARG A 715 ? 1.3205 1.3499 1.3236 0.0100  -0.1005 0.2052  818  ARG A CB    
5441 C  CG    . ARG A 715 ? 1.5935 1.6463 1.6317 0.0112  -0.1108 0.2033  818  ARG A CG    
5442 C  CD    . ARG A 715 ? 1.3796 1.4062 1.4227 -0.0024 -0.1332 0.1990  818  ARG A CD    
5443 N  NE    . ARG A 715 ? 1.3543 1.3414 1.3839 -0.0068 -0.1403 0.2008  818  ARG A NE    
5444 C  CZ    . ARG A 715 ? 1.8075 1.7718 1.8458 -0.0175 -0.1606 0.2001  818  ARG A CZ    
5445 N  NH1   . ARG A 715 ? 1.7139 1.6894 1.7771 -0.0234 -0.1745 0.1979  818  ARG A NH1   
5446 N  NH2   . ARG A 715 ? 1.7750 1.7044 1.7982 -0.0229 -0.1667 0.2023  818  ARG A NH2   
5447 N  N     . ILE A 716 ? 1.3881 1.5127 1.4154 0.0302  -0.0694 0.2143  819  ILE A N     
5448 C  CA    . ILE A 716 ? 1.3951 1.5707 1.4450 0.0352  -0.0652 0.2175  819  ILE A CA    
5449 C  C     . ILE A 716 ? 1.1805 1.3812 1.2387 0.0514  -0.0467 0.2293  819  ILE A C     
5450 O  O     . ILE A 716 ? 1.1405 1.3772 1.2196 0.0581  -0.0445 0.2346  819  ILE A O     
5451 C  CB    . ILE A 716 ? 1.2239 1.4138 1.2679 0.0252  -0.0684 0.2136  819  ILE A CB    
5452 C  CG1   . ILE A 716 ? 1.4347 1.5989 1.4731 0.0100  -0.0869 0.2034  819  ILE A CG1   
5453 C  CG2   . ILE A 716 ? 1.0556 1.2983 1.1203 0.0277  -0.0649 0.2169  819  ILE A CG2   
5454 C  CD1   . ILE A 716 ? 1.1113 1.2853 1.1429 -0.0010 -0.0904 0.1990  819  ILE A CD1   
5455 N  N     . MET A 717 ? 1.2856 1.4666 1.3275 0.0574  -0.0325 0.2343  820  MET A N     
5456 C  CA    . MET A 717 ? 1.2842 1.4851 1.3372 0.0743  -0.0135 0.2472  820  MET A CA    
5457 C  C     . MET A 717 ? 1.3421 1.5361 1.4052 0.0831  -0.0125 0.2507  820  MET A C     
5458 O  O     . MET A 717 ? 1.4510 1.6764 1.5330 0.0960  -0.0031 0.2620  820  MET A O     
5459 C  CB    . MET A 717 ? 1.2499 1.4233 1.2829 0.0786  0.0043  0.2505  820  MET A CB    
5460 C  CG    . MET A 717 ? 1.4044 1.5960 1.4346 0.0748  0.0104  0.2516  820  MET A CG    
5461 S  SD    . MET A 717 ? 1.3929 1.5532 1.4034 0.0817  0.0374  0.2563  820  MET A SD    
5462 C  CE    . MET A 717 ? 1.2852 1.4828 1.3045 0.0776  0.0422  0.2592  820  MET A CE    
5463 N  N     . GLU A 718 ? 1.3370 1.4908 1.3883 0.0758  -0.0225 0.2423  821  GLU A N     
5464 C  CA    . GLU A 718 ? 1.3584 1.5041 1.4199 0.0828  -0.0215 0.2449  821  GLU A CA    
5465 C  C     . GLU A 718 ? 1.4024 1.5839 1.4894 0.0828  -0.0308 0.2448  821  GLU A C     
5466 O  O     . GLU A 718 ? 1.2865 1.4841 1.3879 0.0933  -0.0237 0.2523  821  GLU A O     
5467 C  CB    . GLU A 718 ? 1.3825 1.4765 1.4257 0.0729  -0.0312 0.2365  821  GLU A CB    
5468 C  CG    . GLU A 718 ? 1.3677 1.4472 1.4185 0.0797  -0.0276 0.2394  821  GLU A CG    
5469 C  CD    . GLU A 718 ? 1.5431 1.5731 1.5762 0.0676  -0.0392 0.2318  821  GLU A CD    
5470 O  OE1   . GLU A 718 ? 1.7479 1.7590 1.7671 0.0530  -0.0540 0.2245  821  GLU A OE1   
5471 O  OE2   . GLU A 718 ? 1.4620 1.4722 1.4953 0.0717  -0.0341 0.2338  821  GLU A OE2   
5472 N  N     . ASN A 719 ? 1.3362 1.5287 1.4277 0.0706  -0.0452 0.2361  822  ASN A N     
5473 C  CA    . ASN A 719 ? 1.3278 1.5511 1.4406 0.0686  -0.0515 0.2342  822  ASN A CA    
5474 C  C     . ASN A 719 ? 1.4370 1.7084 1.5605 0.0767  -0.0418 0.2445  822  ASN A C     
5475 O  O     . ASN A 719 ? 1.2583 1.5525 1.3958 0.0801  -0.0404 0.2480  822  ASN A O     
5476 C  CB    . ASN A 719 ? 1.3471 1.5682 1.4618 0.0535  -0.0666 0.2225  822  ASN A CB    
5477 C  CG    . ASN A 719 ? 1.6555 1.8351 1.7682 0.0453  -0.0795 0.2147  822  ASN A CG    
5478 O  OD1   . ASN A 719 ? 1.3306 1.4906 1.4473 0.0496  -0.0790 0.2164  822  ASN A OD1   
5479 N  ND2   . ASN A 719 ? 2.0226 2.1891 2.1301 0.0329  -0.0919 0.2071  822  ASN A ND2   
5480 N  N     . ILE A 720 ? 1.2651 1.5526 1.3823 0.0788  -0.0352 0.2503  823  ILE A N     
5481 C  CA    . ILE A 720 ? 1.3620 1.6974 1.4918 0.0860  -0.0275 0.2629  823  ILE A CA    
5482 C  C     . ILE A 720 ? 1.2569 1.5964 1.3949 0.1027  -0.0145 0.2772  823  ILE A C     
5483 O  O     . ILE A 720 ? 1.2927 1.6684 1.4445 0.1081  -0.0123 0.2876  823  ILE A O     
5484 C  CB    . ILE A 720 ? 1.3293 1.6804 1.4544 0.0844  -0.0231 0.2666  823  ILE A CB    
5485 C  CG1   . ILE A 720 ? 1.0848 1.4361 1.2029 0.0671  -0.0361 0.2531  823  ILE A CG1   
5486 C  CG2   . ILE A 720 ? 1.3987 1.8006 1.5405 0.0928  -0.0155 0.2831  823  ILE A CG2   
5487 C  CD1   . ILE A 720 ? 1.1931 1.5605 1.3069 0.0636  -0.0321 0.2558  823  ILE A CD1   
5488 N  N     . TRP A 721 ? 1.2534 1.5541 1.3815 0.1101  -0.0057 0.2781  824  TRP A N     
5489 C  CA    . TRP A 721 ? 1.4417 1.7412 1.5771 0.1263  0.0086  0.2915  824  TRP A CA    
5490 C  C     . TRP A 721 ? 1.3152 1.6089 1.4577 0.1269  0.0039  0.2894  824  TRP A C     
5491 O  O     . TRP A 721 ? 1.3731 1.6898 1.5284 0.1373  0.0109  0.3020  824  TRP A O     
5492 C  CB    . TRP A 721 ? 1.4216 1.6773 1.5410 0.1322  0.0217  0.2915  824  TRP A CB    
5493 C  CG    . TRP A 721 ? 1.2127 1.4753 1.3279 0.1350  0.0325  0.2964  824  TRP A CG    
5494 C  CD1   . TRP A 721 ? 1.4058 1.7156 1.5372 0.1380  0.0347  0.3066  824  TRP A CD1   
5495 C  CD2   . TRP A 721 ? 1.2282 1.4487 1.3214 0.1335  0.0432  0.2915  824  TRP A CD2   
5496 N  NE1   . TRP A 721 ? 1.3653 1.6661 1.4897 0.1399  0.0470  0.3086  824  TRP A NE1   
5497 C  CE2   . TRP A 721 ? 1.4545 1.6994 1.5538 0.1371  0.0534  0.2988  824  TRP A CE2   
5498 C  CE3   . TRP A 721 ? 1.2706 1.4345 1.3382 0.1281  0.0452  0.2816  824  TRP A CE3   
5499 C  CZ2   . TRP A 721 ? 1.3164 1.5293 1.3967 0.1361  0.0677  0.2958  824  TRP A CZ2   
5500 C  CZ3   . TRP A 721 ? 1.4898 1.6210 1.5347 0.1257  0.0582  0.2785  824  TRP A CZ3   
5501 C  CH2   . TRP A 721 ? 1.2645 1.4193 1.3157 0.1301  0.0704  0.2852  824  TRP A CH2   
5502 N  N     . GLN A 722 ? 1.1958 1.4593 1.3318 0.1155  -0.0080 0.2746  825  GLN A N     
5503 C  CA    . GLN A 722 ? 1.0944 1.3514 1.2400 0.1154  -0.0115 0.2719  825  GLN A CA    
5504 C  C     . GLN A 722 ? 1.2944 1.5931 1.4539 0.1123  -0.0156 0.2738  825  GLN A C     
5505 O  O     . GLN A 722 ? 1.4814 1.7859 1.6499 0.1166  -0.0121 0.2778  825  GLN A O     
5506 C  CB    . GLN A 722 ? 0.9875 1.2059 1.1278 0.1031  -0.0242 0.2570  825  GLN A CB    
5507 C  CG    . GLN A 722 ? 1.2444 1.4163 1.3666 0.1032  -0.0215 0.2549  825  GLN A CG    
5508 C  CD    . GLN A 722 ? 1.3227 1.4763 1.4456 0.1140  -0.0094 0.2620  825  GLN A CD    
5509 O  OE1   . GLN A 722 ? 1.5292 1.7005 1.6679 0.1202  -0.0060 0.2671  825  GLN A OE1   
5510 N  NE2   . GLN A 722 ? 1.4003 1.5158 1.5038 0.1154  -0.0019 0.2621  825  GLN A NE2   
5511 N  N     . ASN A 723 ? 1.2358 1.5618 1.3951 0.1035  -0.0221 0.2706  826  ASN A N     
5512 C  CA    . ASN A 723 ? 1.1181 1.4823 1.2855 0.0976  -0.0256 0.2713  826  ASN A CA    
5513 C  C     . ASN A 723 ? 1.4223 1.8270 1.5947 0.1072  -0.0177 0.2899  826  ASN A C     
5514 O  O     . ASN A 723 ? 1.6442 2.0816 1.8198 0.1012  -0.0205 0.2927  826  ASN A O     
5515 C  CB    . ASN A 723 ? 1.1378 1.5124 1.3017 0.0821  -0.0359 0.2593  826  ASN A CB    
5516 C  CG    . ASN A 723 ? 1.5449 1.8840 1.7089 0.0719  -0.0452 0.2427  826  ASN A CG    
5517 O  OD1   . ASN A 723 ? 1.2608 1.5787 1.4322 0.0730  -0.0455 0.2388  826  ASN A OD1   
5518 N  ND2   . ASN A 723 ? 1.7708 2.1038 1.9285 0.0618  -0.0530 0.2340  826  ASN A ND2   
5519 N  N     . GLN A 724 ? 1.3863 1.7891 1.5597 0.1211  -0.0075 0.3033  827  GLN A N     
5520 C  CA    . GLN A 724 ? 1.3508 1.7920 1.5345 0.1323  0.0001  0.3244  827  GLN A CA    
5521 C  C     . GLN A 724 ? 1.5233 1.9500 1.7128 0.1491  0.0128  0.3376  827  GLN A C     
5522 O  O     . GLN A 724 ? 1.8102 2.2673 2.0110 0.1601  0.0195  0.3576  827  GLN A O     
5523 C  CB    . GLN A 724 ? 1.4023 1.8622 1.5890 0.1355  0.0036  0.3326  827  GLN A CB    
5524 C  CG    . GLN A 724 ? 1.6792 2.1653 1.8627 0.1194  -0.0081 0.3244  827  GLN A CG    
5525 C  CD    . GLN A 724 ? 1.8485 2.3601 2.0393 0.1233  -0.0034 0.3357  827  GLN A CD    
5526 O  OE1   . GLN A 724 ? 1.7071 2.2172 1.9074 0.1390  0.0098  0.3502  827  GLN A OE1   
5527 N  NE2   . GLN A 724 ? 1.8247 2.3591 2.0127 0.1088  -0.0129 0.3290  827  GLN A NE2   
5528 N  N     . GLY A 725 ? 1.2034 1.5850 1.3864 0.1509  0.0160  0.3280  828  GLY A N     
5529 C  CA    . GLY A 725 ? 1.0747 1.4377 1.2615 0.1654  0.0288  0.3385  828  GLY A CA    
5530 C  C     . GLY A 725 ? 1.4269 1.7522 1.6067 0.1746  0.0414  0.3394  828  GLY A C     
5531 O  O     . GLY A 725 ? 1.8591 2.1585 2.0387 0.1843  0.0525  0.3442  828  GLY A O     
5532 N  N     . LEU A 726 ? 1.4368 1.7562 1.6090 0.1708  0.0413  0.3343  829  LEU A N     
5533 C  CA    . LEU A 726 ? 1.4809 1.7606 1.6414 0.1771  0.0550  0.3335  829  LEU A CA    
5534 C  C     . LEU A 726 ? 1.4298 1.6588 1.5713 0.1656  0.0476  0.3150  829  LEU A C     
5535 O  O     . LEU A 726 ? 1.6074 1.8264 1.7384 0.1509  0.0338  0.3007  829  LEU A O     
5536 C  CB    . LEU A 726 ? 1.2109 1.5024 1.3690 0.1758  0.0584  0.3347  829  LEU A CB    
5537 C  CG    . LEU A 726 ? 1.4361 1.7714 1.6156 0.1896  0.0699  0.3560  829  LEU A CG    
5538 C  CD1   . LEU A 726 ? 1.3720 1.6988 1.5629 0.2089  0.0894  0.3730  829  LEU A CD1   
5539 C  CD2   . LEU A 726 ? 1.5542 1.9457 1.7492 0.1844  0.0556  0.3631  829  LEU A CD2   
5540 N  N     . ASP A 727 ? 1.2496 1.4468 1.3876 0.1716  0.0563  0.3162  830  ASP A N     
5541 C  CA    . ASP A 727 ? 1.2953 1.4448 1.4169 0.1601  0.0487  0.3009  830  ASP A CA    
5542 C  C     . ASP A 727 ? 1.3640 1.4693 1.4612 0.1579  0.0586  0.2960  830  ASP A C     
5543 O  O     . ASP A 727 ? 1.5422 1.6074 1.6267 0.1601  0.0691  0.2950  830  ASP A O     
5544 C  CB    . ASP A 727 ? 1.4723 1.6089 1.6014 0.1651  0.0525  0.3038  830  ASP A CB    
5545 C  CG    . ASP A 727 ? 1.4217 1.5169 1.5401 0.1512  0.0406  0.2889  830  ASP A CG    
5546 O  OD1   . ASP A 727 ? 1.3300 1.4122 1.4380 0.1370  0.0261  0.2769  830  ASP A OD1   
5547 O  OD2   . ASP A 727 ? 1.6903 1.7665 1.8119 0.1540  0.0454  0.2902  830  ASP A OD2   
5548 N  N     . LEU A 728 ? 1.5066 1.6183 1.5950 0.1522  0.0560  0.2924  831  LEU A N     
5549 C  CA    . LEU A 728 ? 1.5001 1.5701 1.5612 0.1474  0.0654  0.2864  831  LEU A CA    
5550 C  C     . LEU A 728 ? 1.4231 1.4605 1.4635 0.1268  0.0447  0.2697  831  LEU A C     
5551 O  O     . LEU A 728 ? 1.4817 1.5345 1.5219 0.1165  0.0296  0.2635  831  LEU A O     
5552 C  CB    . LEU A 728 ? 1.2722 1.3668 1.3363 0.1526  0.0756  0.2929  831  LEU A CB    
5553 C  CG    . LEU A 728 ? 1.1671 1.3037 1.2589 0.1726  0.0925  0.3125  831  LEU A CG    
5554 C  CD1   . LEU A 728 ? 1.4123 1.5700 1.5083 0.1761  0.1026  0.3185  831  LEU A CD1   
5555 C  CD2   . LEU A 728 ? 1.5690 1.6795 1.6614 0.1869  0.1141  0.3215  831  LEU A CD2   
5556 N  N     . ARG A 729 ? 1.3935 1.3856 1.4171 0.1201  0.0434  0.2635  832  ARG A N     
5557 C  CA    . ARG A 729 ? 1.3385 1.3006 1.3462 0.1002  0.0212  0.2503  832  ARG A CA    
5558 C  C     . ARG A 729 ? 1.5453 1.4790 1.5210 0.0882  0.0207  0.2435  832  ARG A C     
5559 O  O     . ARG A 729 ? 1.4467 1.3391 1.3936 0.0861  0.0354  0.2418  832  ARG A O     
5560 C  CB    . ARG A 729 ? 1.4591 1.3822 1.4584 0.0953  0.0196  0.2471  832  ARG A CB    
5561 C  CG    . ARG A 729 ? 1.3880 1.2819 1.3749 0.0742  -0.0055 0.2362  832  ARG A CG    
5562 C  CD    . ARG A 729 ? 1.4946 1.3499 1.4728 0.0678  -0.0071 0.2338  832  ARG A CD    
5563 N  NE    . ARG A 729 ? 1.7231 1.6021 1.7332 0.0787  -0.0046 0.2392  832  ARG A NE    
5564 C  CZ    . ARG A 729 ? 1.7484 1.6029 1.7602 0.0746  -0.0065 0.2381  832  ARG A CZ    
5565 N  NH1   . ARG A 729 ? 1.8547 1.6607 1.8378 0.0589  -0.0123 0.2320  832  ARG A NH1   
5566 N  NH2   . ARG A 729 ? 1.6133 1.4921 1.6547 0.0851  -0.0025 0.2433  832  ARG A NH2   
5567 N  N     . MET A 730 ? 1.6592 1.6130 1.6383 0.0796  0.0050  0.2391  833  MET A N     
5568 C  CA    . MET A 730 ? 1.4051 1.3310 1.3531 0.0652  0.0004  0.2319  833  MET A CA    
5569 C  C     . MET A 730 ? 1.6081 1.5000 1.5413 0.0453  -0.0247 0.2229  833  MET A C     
5570 O  O     . MET A 730 ? 1.5174 1.4218 1.4743 0.0430  -0.0415 0.2220  833  MET A O     
5571 C  CB    . MET A 730 ? 1.3707 1.3353 1.3299 0.0658  -0.0030 0.2327  833  MET A CB    
5572 C  CG    . MET A 730 ? 1.4995 1.5080 1.4815 0.0845  0.0168  0.2439  833  MET A CG    
5573 S  SD    . MET A 730 ? 1.5495 1.5334 1.5121 0.0953  0.0496  0.2502  833  MET A SD    
5574 C  CE    . MET A 730 ? 1.6255 1.5862 1.5557 0.0788  0.0470  0.2411  833  MET A CE    
5575 N  N     . LEU A 731 ? 1.6540 1.5022 1.5482 0.0303  -0.0269 0.2170  834  LEU A N     
5576 C  CA    . LEU A 731 ? 1.5565 1.3698 1.4327 0.0091  -0.0524 0.2106  834  LEU A CA    
5577 C  C     . LEU A 731 ? 1.6722 1.4842 1.5335 -0.0039 -0.0658 0.2067  834  LEU A C     
5578 O  O     . LEU A 731 ? 1.7654 1.5412 1.5859 -0.0152 -0.0604 0.2032  834  LEU A O     
5579 C  CB    . LEU A 731 ? 1.7229 1.4796 1.5600 -0.0016 -0.0462 0.2075  834  LEU A CB    
5580 C  CG    . LEU A 731 ? 1.6880 1.4088 1.5076 -0.0249 -0.0749 0.2032  834  LEU A CG    
5581 C  CD1   . LEU A 731 ? 1.7563 1.5054 1.6203 -0.0230 -0.0963 0.2057  834  LEU A CD1   
5582 C  CD2   . LEU A 731 ? 1.9132 1.5787 1.6923 -0.0363 -0.0671 0.2000  834  LEU A CD2   
5583 N  N     . PRO A 732 ? 1.6544 1.5031 1.5459 -0.0035 -0.0819 0.2069  835  PRO A N     
5584 C  CA    . PRO A 732 ? 1.4730 1.3184 1.3513 -0.0167 -0.0958 0.2035  835  PRO A CA    
5585 C  C     . PRO A 732 ? 1.3497 1.1641 1.2188 -0.0364 -0.1247 0.2012  835  PRO A C     
5586 O  O     . PRO A 732 ? 1.4407 1.2755 1.3421 -0.0383 -0.1437 0.2018  835  PRO A O     
5587 C  CB    . PRO A 732 ? 1.4262 1.3262 1.3434 -0.0063 -0.0968 0.2049  835  PRO A CB    
5588 C  CG    . PRO A 732 ? 1.5084 1.4347 1.4609 0.0072  -0.0934 0.2084  835  PRO A CG    
5589 C  CD    . PRO A 732 ? 1.7903 1.6821 1.7275 0.0079  -0.0868 0.2098  835  PRO A CD    
5590 N  N     . TYR A 733 ? 1.5458 1.3102 1.3711 -0.0519 -0.1278 0.1992  836  TYR A N     
5591 C  CA    . TYR A 733 ? 1.7039 1.4369 1.5177 -0.0726 -0.1572 0.1994  836  TYR A CA    
5592 C  C     . TYR A 733 ? 1.7810 1.5220 1.5977 -0.0827 -0.1763 0.1996  836  TYR A C     
5593 O  O     . TYR A 733 ? 1.9994 1.7580 1.8117 -0.0780 -0.1648 0.1978  836  TYR A O     
5594 C  CB    . TYR A 733 ? 1.7156 1.3909 1.4745 -0.0894 -0.1550 0.1971  836  TYR A CB    
5595 C  CG    . TYR A 733 ? 1.7182 1.3721 1.4325 -0.0923 -0.1334 0.1932  836  TYR A CG    
5596 C  CD1   . TYR A 733 ? 1.8545 1.5091 1.5603 -0.0773 -0.0996 0.1917  836  TYR A CD1   
5597 C  CD2   . TYR A 733 ? 1.8244 1.4566 1.5066 -0.1099 -0.1456 0.1917  836  TYR A CD2   
5598 C  CE1   . TYR A 733 ? 1.8561 1.4911 1.5252 -0.0793 -0.0773 0.1884  836  TYR A CE1   
5599 C  CE2   . TYR A 733 ? 1.9303 1.5417 1.5719 -0.1131 -0.1238 0.1877  836  TYR A CE2   
5600 C  CZ    . TYR A 733 ? 1.8532 1.4664 1.4896 -0.0976 -0.0890 0.1858  836  TYR A CZ    
5601 O  OH    . TYR A 733 ? 2.0645 1.6572 1.6644 -0.1002 -0.0649 0.1821  836  TYR A OH    
5602 N  N     . GLY A 734 ? 1.8146 1.5427 1.6410 -0.0970 -0.2059 0.2028  837  GLY A N     
5603 C  CA    . GLY A 734 ? 1.9274 1.6623 1.7618 -0.1062 -0.2254 0.2045  837  GLY A CA    
5604 C  C     . GLY A 734 ? 1.7373 1.4363 1.5181 -0.1229 -0.2270 0.2031  837  GLY A C     
5605 O  O     . GLY A 734 ? 1.7314 1.3869 1.4656 -0.1360 -0.2253 0.2022  837  GLY A O     
5606 N  N     . CYS A 735 ? 1.8554 1.5710 1.6409 -0.1234 -0.2291 0.2025  838  CYS A N     
5607 C  CA    . CYS A 735 ? 2.0050 1.6892 1.7421 -0.1395 -0.2306 0.2015  838  CYS A CA    
5608 C  C     . CYS A 735 ? 1.9118 1.6155 1.6700 -0.1427 -0.2454 0.2035  838  CYS A C     
5609 O  O     . CYS A 735 ? 1.9534 1.7004 1.7498 -0.1276 -0.2356 0.2013  838  CYS A O     
5610 C  CB    . CYS A 735 ? 1.9789 1.6611 1.6856 -0.1316 -0.1972 0.1955  838  CYS A CB    
5611 S  SG    . CYS A 735 ? 1.8052 1.4436 1.4472 -0.1522 -0.1939 0.1930  838  CYS A SG    
5612 N  N     . LEU A 736 ? 1.7794 1.4501 1.5113 -0.1632 -0.2687 0.2082  839  LEU A N     
5613 C  CA    . LEU A 736 ? 1.7897 1.4729 1.5405 -0.1680 -0.2847 0.2116  839  LEU A CA    
5614 C  C     . LEU A 736 ? 1.7138 1.3567 1.4090 -0.1886 -0.2916 0.2131  839  LEU A C     
5615 O  O     . LEU A 736 ? 1.9342 1.5343 1.5924 -0.2076 -0.3091 0.2181  839  LEU A O     
5616 C  CB    . LEU A 736 ? 1.6237 1.3132 1.4186 -0.1711 -0.3141 0.2201  839  LEU A CB    
5617 C  CG    . LEU A 736 ? 1.8212 1.5283 1.6488 -0.1722 -0.3283 0.2240  839  LEU A CG    
5618 C  CD1   . LEU A 736 ? 1.8389 1.5941 1.7063 -0.1525 -0.3068 0.2162  839  LEU A CD1   
5619 C  CD2   . LEU A 736 ? 1.6847 1.3867 1.5494 -0.1788 -0.3591 0.2351  839  LEU A CD2   
5620 N  N     . SER A 737 ? 1.8604 1.5162 1.5482 -0.1863 -0.2780 0.2089  840  SER A N     
5621 C  CA    . SER A 737 ? 2.0653 1.6844 1.7013 -0.2056 -0.2825 0.2101  840  SER A CA    
5622 C  C     . SER A 737 ? 1.9111 1.5216 1.5602 -0.2188 -0.3148 0.2196  840  SER A C     
5623 O  O     . SER A 737 ? 1.6706 1.3153 1.3715 -0.2087 -0.3216 0.2214  840  SER A O     
5624 C  CB    . SER A 737 ? 1.9008 1.5382 1.5263 -0.1981 -0.2541 0.2023  840  SER A CB    
5625 O  OG    . SER A 737 ? 1.9340 1.5340 1.5072 -0.2173 -0.2560 0.2029  840  SER A OG    
5626 N  N     . ILE A 738 ? 2.0339 1.5971 1.6349 -0.2422 -0.3342 0.2263  841  ILE A N     
5627 C  CA    . ILE A 738 ? 2.1780 1.7273 1.7875 -0.2569 -0.3679 0.2387  841  ILE A CA    
5628 C  C     . ILE A 738 ? 2.1046 1.6218 1.6601 -0.2749 -0.3680 0.2395  841  ILE A C     
5629 O  O     . ILE A 738 ? 2.3875 1.8679 1.8811 -0.2881 -0.3567 0.2353  841  ILE A O     
5630 C  CB    . ILE A 738 ? 2.0870 1.6089 1.6922 -0.2714 -0.3988 0.2501  841  ILE A CB    
5631 C  CG1   . ILE A 738 ? 2.0478 1.5978 1.7000 -0.2542 -0.3944 0.2478  841  ILE A CG1   
5632 C  CG2   . ILE A 738 ? 2.3520 1.8672 1.9796 -0.2834 -0.4347 0.2658  841  ILE A CG2   
5633 C  CD1   . ILE A 738 ? 2.0907 1.6905 1.8174 -0.2334 -0.3926 0.2477  841  ILE A CD1   
5634 N  N     . GLY A 739 ? 1.6324 1.1618 1.2107 -0.2758 -0.3787 0.2445  842  GLY A N     
5635 C  CA    . GLY A 739 ? 2.4964 1.9928 2.0256 -0.2951 -0.3839 0.2480  842  GLY A CA    
5636 C  C     . GLY A 739 ? 2.5452 2.0332 2.0276 -0.2952 -0.3496 0.2351  842  GLY A C     
5637 O  O     . GLY A 739 ? 2.4651 1.9905 1.9730 -0.2760 -0.3213 0.2244  842  GLY A O     
5638 N  N     . ASP A 740 ? 2.4152 1.8529 1.8280 -0.3179 -0.3519 0.2367  843  ASP A N     
5639 C  CA    . ASP A 740 ? 2.4067 1.8295 1.7712 -0.3210 -0.3189 0.2255  843  ASP A CA    
5640 C  C     . ASP A 740 ? 2.3969 1.8249 1.7543 -0.3086 -0.2898 0.2148  843  ASP A C     
5641 O  O     . ASP A 740 ? 2.4469 1.9146 1.8357 -0.2875 -0.2616 0.2060  843  ASP A O     
5642 C  CB    . ASP A 740 ? 2.5816 1.9443 1.8703 -0.3511 -0.3298 0.2305  843  ASP A CB    
5643 C  CG    . ASP A 740 ? 2.6593 2.0097 1.9060 -0.3552 -0.2974 0.2205  843  ASP A CG    
5644 O  OD1   . ASP A 740 ? 2.6811 2.0544 1.9378 -0.3383 -0.2624 0.2087  843  ASP A OD1   
5645 O  OD2   . ASP A 740 ? 2.6442 1.9620 1.8492 -0.3754 -0.3069 0.2255  843  ASP A OD2   
5646 N  N     . CYS A 741 ? 2.3940 1.7815 1.7100 -0.3224 -0.2966 0.2161  844  CYS A N     
5647 C  CA    . CYS A 741 ? 2.3448 1.7288 1.6478 -0.3128 -0.2677 0.2062  844  CYS A CA    
5648 C  C     . CYS A 741 ? 2.3548 1.7298 1.6669 -0.3139 -0.2848 0.2100  844  CYS A C     
5649 O  O     . CYS A 741 ? 2.4288 1.8029 1.7362 -0.3042 -0.2614 0.2024  844  CYS A O     
5650 C  CB    . CYS A 741 ? 2.4171 1.7500 1.6431 -0.3304 -0.2436 0.1989  844  CYS A CB    
5651 S  SG    . CYS A 741 ? 3.2112 2.4733 2.3587 -0.3708 -0.2748 0.2077  844  CYS A SG    
5652 N  N     . VAL A 742 ? 2.1522 1.5214 1.4799 -0.3251 -0.3242 0.2223  845  VAL A N     
5653 C  CA    . VAL A 742 ? 2.5552 1.9192 1.8970 -0.3268 -0.3421 0.2269  845  VAL A CA    
5654 C  C     . VAL A 742 ? 2.1345 1.5558 1.5522 -0.2967 -0.3328 0.2242  845  VAL A C     
5655 O  O     . VAL A 742 ? 1.9765 1.4404 1.4365 -0.2781 -0.3202 0.2211  845  VAL A O     
5656 C  CB    . VAL A 742 ? 2.5660 1.9075 1.9043 -0.3490 -0.3883 0.2431  845  VAL A CB    
5657 C  CG1   . VAL A 742 ? 2.4558 1.7399 1.7147 -0.3805 -0.3983 0.2467  845  VAL A CG1   
5658 C  CG2   . VAL A 742 ? 1.9936 1.3769 1.3995 -0.3368 -0.4084 0.2526  845  VAL A CG2   
5659 N  N     . GLY A 743 ? 2.1272 1.5488 1.5604 -0.2932 -0.3385 0.2252  846  GLY A N     
5660 C  CA    . GLY A 743 ? 1.9132 1.3854 1.4142 -0.2664 -0.3295 0.2228  846  GLY A CA    
5661 C  C     . GLY A 743 ? 1.7215 1.1818 1.2248 -0.2678 -0.3352 0.2238  846  GLY A C     
5662 O  O     . GLY A 743 ? 2.1623 1.5750 1.6100 -0.2881 -0.3391 0.2235  846  GLY A O     
5663 N  N     . LEU A 744 ? 1.7142 1.2169 1.2808 -0.2472 -0.3347 0.2244  847  LEU A N     
5664 C  CA    . LEU A 744 ? 2.0612 1.5599 1.6416 -0.2459 -0.3403 0.2258  847  LEU A CA    
5665 C  C     . LEU A 744 ? 1.9419 1.4636 1.5363 -0.2227 -0.3044 0.2157  847  LEU A C     
5666 O  O     . LEU A 744 ? 1.8085 1.3688 1.4316 -0.2023 -0.2831 0.2109  847  LEU A O     
5667 C  CB    . LEU A 744 ? 1.8090 1.3359 1.4536 -0.2417 -0.3694 0.2362  847  LEU A CB    
5668 C  CG    . LEU A 744 ? 1.8321 1.3423 1.4764 -0.2620 -0.4076 0.2498  847  LEU A CG    
5669 C  CD1   . LEU A 744 ? 1.5823 1.1238 1.2991 -0.2543 -0.4311 0.2601  847  LEU A CD1   
5670 C  CD2   . LEU A 744 ? 1.7969 1.2508 1.3752 -0.2922 -0.4262 0.2548  847  LEU A CD2   
5671 N  N     . ILE A 745 ? 2.0659 1.5630 1.6393 -0.2269 -0.2985 0.2134  848  ILE A N     
5672 C  CA    . ILE A 745 ? 1.9929 1.5053 1.5760 -0.2065 -0.2652 0.2056  848  ILE A CA    
5673 C  C     . ILE A 745 ? 1.8943 1.4108 1.5070 -0.2039 -0.2763 0.2089  848  ILE A C     
5674 O  O     . ILE A 745 ? 1.9806 1.4581 1.5632 -0.2250 -0.2946 0.2120  848  ILE A O     
5675 C  CB    . ILE A 745 ? 1.7764 1.2467 1.2948 -0.2140 -0.2367 0.1973  848  ILE A CB    
5676 C  CG1   . ILE A 745 ? 1.8757 1.3443 1.3684 -0.2155 -0.2229 0.1939  848  ILE A CG1   
5677 C  CG2   . ILE A 745 ? 1.9942 1.4790 1.5274 -0.1923 -0.2036 0.1916  848  ILE A CG2   
5678 C  CD1   . ILE A 745 ? 1.8827 1.3066 1.3113 -0.2244 -0.1935 0.1857  848  ILE A CD1   
5679 N  N     . GLU A 746 ? 1.9479 1.5109 1.6177 -0.1796 -0.2655 0.2084  849  GLU A N     
5680 C  CA    . GLU A 746 ? 2.0598 1.6295 1.7607 -0.1751 -0.2721 0.2110  849  GLU A CA    
5681 C  C     . GLU A 746 ? 2.0003 1.5389 1.6630 -0.1756 -0.2483 0.2050  849  GLU A C     
5682 O  O     . GLU A 746 ? 2.0203 1.5624 1.6677 -0.1620 -0.2159 0.1988  849  GLU A O     
5683 C  CB    . GLU A 746 ? 1.9433 1.5696 1.7116 -0.1497 -0.2643 0.2116  849  GLU A CB    
5684 C  CG    . GLU A 746 ? 1.9992 1.6365 1.8077 -0.1453 -0.2739 0.2152  849  GLU A CG    
5685 C  CD    . GLU A 746 ? 2.3388 1.9733 2.1401 -0.1327 -0.2465 0.2104  849  GLU A CD    
5686 O  OE1   . GLU A 746 ? 2.4660 2.1012 2.2440 -0.1220 -0.2179 0.2050  849  GLU A OE1   
5687 O  OE2   . GLU A 746 ? 2.5176 2.1495 2.3388 -0.1334 -0.2532 0.2128  849  GLU A OE2   
5688 N  N     . VAL A 747 ? 2.0488 1.5569 1.6980 -0.1915 -0.2642 0.2075  850  VAL A N     
5689 C  CA    . VAL A 747 ? 1.9333 1.4042 1.5421 -0.1961 -0.2437 0.2015  850  VAL A CA    
5690 C  C     . VAL A 747 ? 2.0370 1.5330 1.6920 -0.1793 -0.2366 0.2025  850  VAL A C     
5691 O  O     . VAL A 747 ? 1.9952 1.5117 1.6944 -0.1805 -0.2613 0.2092  850  VAL A O     
5692 C  CB    . VAL A 747 ? 1.9114 1.3239 1.4625 -0.2300 -0.2653 0.2025  850  VAL A CB    
5693 C  CG1   . VAL A 747 ? 1.9945 1.3634 1.4970 -0.2358 -0.2389 0.1942  850  VAL A CG1   
5694 C  CG2   . VAL A 747 ? 2.2729 1.6624 1.7810 -0.2481 -0.2766 0.2033  850  VAL A CG2   
5695 N  N     . VAL A 748 ? 2.0047 1.4988 1.6510 -0.1635 -0.2019 0.1967  851  VAL A N     
5696 C  CA    . VAL A 748 ? 1.9957 1.5087 1.6788 -0.1475 -0.1909 0.1975  851  VAL A CA    
5697 C  C     . VAL A 748 ? 2.0477 1.5096 1.6908 -0.1660 -0.1907 0.1947  851  VAL A C     
5698 O  O     . VAL A 748 ? 1.9968 1.4131 1.5812 -0.1777 -0.1738 0.1884  851  VAL A O     
5699 C  CB    . VAL A 748 ? 2.0371 1.5809 1.7385 -0.1184 -0.1540 0.1952  851  VAL A CB    
5700 C  CG1   . VAL A 748 ? 1.8489 1.3615 1.4982 -0.1199 -0.1260 0.1893  851  VAL A CG1   
5701 C  CG2   . VAL A 748 ? 2.3419 1.8942 2.0690 -0.1046 -0.1398 0.1962  851  VAL A CG2   
5702 N  N     . ARG A 749 ? 2.1445 1.6125 1.8187 -0.1698 -0.2086 0.1990  852  ARG A N     
5703 C  CA    . ARG A 749 ? 2.3460 1.7676 1.9859 -0.1894 -0.2114 0.1967  852  ARG A CA    
5704 C  C     . ARG A 749 ? 2.4454 1.8530 2.0699 -0.1740 -0.1712 0.1903  852  ARG A C     
5705 O  O     . ARG A 749 ? 2.3504 1.7942 2.0064 -0.1458 -0.1460 0.1905  852  ARG A O     
5706 C  CB    . ARG A 749 ? 2.4170 1.8545 2.1022 -0.1965 -0.2413 0.2041  852  ARG A CB    
5707 C  CG    . ARG A 749 ? 2.8316 2.2204 2.4804 -0.2247 -0.2556 0.2036  852  ARG A CG    
5708 C  CD    . ARG A 749 ? 2.7714 2.1103 2.3520 -0.2560 -0.2712 0.2019  852  ARG A CD    
5709 N  NE    . ARG A 749 ? 2.9039 2.1933 2.4431 -0.2856 -0.2838 0.2007  852  ARG A NE    
5710 C  CZ    . ARG A 749 ? 3.1733 2.4160 2.6587 -0.2932 -0.2564 0.1907  852  ARG A CZ    
5711 N  NH1   . ARG A 749 ? 3.1724 2.4117 2.6418 -0.2719 -0.2142 0.1822  852  ARG A NH1   
5712 N  NH2   . ARG A 749 ? 3.1548 2.3528 2.6027 -0.3233 -0.2714 0.1897  852  ARG A NH2   
5713 N  N     . ASN A 750 ? 2.3671 1.7207 1.9424 -0.1940 -0.1659 0.1852  853  ASN A N     
5714 C  CA    . ASN A 750 ? 2.4668 1.7942 2.0193 -0.1842 -0.1276 0.1788  853  ASN A CA    
5715 C  C     . ASN A 750 ? 2.3699 1.7136 1.9219 -0.1586 -0.0905 0.1763  853  ASN A C     
5716 O  O     . ASN A 750 ? 2.1938 1.5679 1.7816 -0.1311 -0.0659 0.1788  853  ASN A O     
5717 C  CB    . ASN A 750 ? 2.4113 1.7584 2.0085 -0.1719 -0.1251 0.1822  853  ASN A CB    
5718 C  CG    . ASN A 750 ? 2.4385 1.8530 2.1094 -0.1473 -0.1342 0.1900  853  ASN A CG    
5719 O  OD1   . ASN A 750 ? 2.6425 2.0910 2.3396 -0.1197 -0.1093 0.1912  853  ASN A OD1   
5720 N  ND2   . ASN A 750 ? 2.4199 1.8533 2.1248 -0.1582 -0.1696 0.1958  853  ASN A ND2   
5721 N  N     . SER A 751 ? 2.4117 1.7345 1.9221 -0.1690 -0.0874 0.1724  854  SER A N     
5722 C  CA    . SER A 751 ? 2.3983 1.7309 1.9027 -0.1492 -0.0529 0.1701  854  SER A CA    
5723 C  C     . SER A 751 ? 2.2217 1.4896 1.6516 -0.1693 -0.0331 0.1608  854  SER A C     
5724 O  O     . SER A 751 ? 2.1741 1.4047 1.5584 -0.1995 -0.0561 0.1577  854  SER A O     
5725 C  CB    . SER A 751 ? 2.3070 1.6892 1.8440 -0.1383 -0.0664 0.1750  854  SER A CB    
5726 O  OG    . SER A 751 ? 2.3213 1.6825 1.8275 -0.1647 -0.0964 0.1742  854  SER A OG    
5727 N  N     . HIS A 752 ? 2.1048 1.3587 1.5227 -0.1530 0.0101  0.1571  855  HIS A N     
5728 C  CA    . HIS A 752 ? 2.3926 1.5825 1.7414 -0.1696 0.0373  0.1472  855  HIS A CA    
5729 C  C     . HIS A 752 ? 2.3656 1.5729 1.7236 -0.1455 0.0751  0.1476  855  HIS A C     
5730 O  O     . HIS A 752 ? 2.4695 1.7262 1.8827 -0.1140 0.0912  0.1552  855  HIS A O     
5731 C  CB    . HIS A 752 ? 2.4286 1.5668 1.7464 -0.1783 0.0576  0.1410  855  HIS A CB    
5732 C  CG    . HIS A 752 ? 2.3151 1.4571 1.6513 -0.1897 0.0260  0.1441  855  HIS A CG    
5733 N  ND1   . HIS A 752 ? 2.4696 1.5910 1.7801 -0.2222 -0.0152 0.1436  855  HIS A ND1   
5734 C  CD2   . HIS A 752 ? 2.3016 1.4664 1.6815 -0.1733 0.0295  0.1487  855  HIS A CD2   
5735 C  CE1   . HIS A 752 ? 2.2701 1.4028 1.6102 -0.2249 -0.0353 0.1477  855  HIS A CE1   
5736 N  NE2   . HIS A 752 ? 2.1851 1.3431 1.5661 -0.1957 -0.0081 0.1501  855  HIS A NE2   
5737 N  N     . THR A 753 ? 2.1978 1.3646 1.5017 -0.1614 0.0891  0.1402  856  THR A N     
5738 C  CA    . THR A 753 ? 2.2102 1.3899 1.5213 -0.1408 0.1264  0.1405  856  THR A CA    
5739 C  C     . THR A 753 ? 2.5645 1.7147 1.8682 -0.1262 0.1743  0.1377  856  THR A C     
5740 O  O     . THR A 753 ? 2.8369 1.9502 2.1216 -0.1348 0.1792  0.1337  856  THR A O     
5741 C  CB    . THR A 753 ? 2.6047 1.7485 1.8599 -0.1634 0.1274  0.1332  856  THR A CB    
5742 O  OG1   . THR A 753 ? 2.8457 1.9122 2.0306 -0.1841 0.1557  0.1215  856  THR A OG1   
5743 C  CG2   . THR A 753 ? 2.4726 1.6190 1.7141 -0.1891 0.0769  0.1344  856  THR A CG2   
5744 N  N     . ILE A 754 ? 2.6194 1.7866 1.9406 -0.1036 0.2106  0.1406  857  ILE A N     
5745 C  CA    . ILE A 754 ? 2.7597 1.8997 2.0785 -0.0874 0.2597  0.1396  857  ILE A CA    
5746 C  C     . ILE A 754 ? 2.8629 1.9140 2.1003 -0.1165 0.2822  0.1245  857  ILE A C     
5747 O  O     . ILE A 754 ? 3.0290 2.0379 2.2486 -0.1165 0.3090  0.1201  857  ILE A O     
5748 C  CB    . ILE A 754 ? 2.5441 1.7275 1.9065 -0.0566 0.2914  0.1485  857  ILE A CB    
5749 C  CG1   . ILE A 754 ? 2.3577 1.6278 1.7958 -0.0311 0.2671  0.1632  857  ILE A CG1   
5750 C  CG2   . ILE A 754 ? 2.4919 1.6485 1.8581 -0.0379 0.3431  0.1499  857  ILE A CG2   
5751 C  CD1   . ILE A 754 ? 2.2577 1.5512 1.7356 -0.0160 0.2596  0.1707  857  ILE A CD1   
5752 N  N     . MET A 755 ? 2.7491 1.7681 1.9334 -0.1431 0.2724  0.1160  858  MET A N     
5753 C  CA    . MET A 755 ? 2.9178 1.8491 2.0167 -0.1761 0.2898  0.1008  858  MET A CA    
5754 C  C     . MET A 755 ? 3.0607 1.9541 2.1233 -0.2051 0.2585  0.0954  858  MET A C     
5755 O  O     . MET A 755 ? 3.0795 1.9000 2.0790 -0.2280 0.2790  0.0834  858  MET A O     
5756 C  CB    . MET A 755 ? 3.0650 1.9741 2.1158 -0.1983 0.2843  0.0944  858  MET A CB    
5757 C  CG    . MET A 755 ? 3.1397 1.9556 2.0969 -0.2326 0.3087  0.0781  858  MET A CG    
5758 S  SD    . MET A 755 ? 3.4661 2.2564 2.3660 -0.2586 0.3033  0.0715  858  MET A SD    
5759 C  CE    . MET A 755 ? 3.3356 2.1789 2.2976 -0.2173 0.3465  0.0789  858  MET A CE    
5760 N  N     . GLN A 756 ? 3.1813 2.1223 2.2834 -0.2051 0.2105  0.1040  859  GLN A N     
5761 C  CA    . GLN A 756 ? 3.1845 2.0966 2.2615 -0.2315 0.1786  0.1011  859  GLN A CA    
5762 C  C     . GLN A 756 ? 2.9785 1.8768 2.0711 -0.2193 0.2016  0.1005  859  GLN A C     
5763 O  O     . GLN A 756 ? 3.2126 2.0712 2.2720 -0.2444 0.1855  0.0952  859  GLN A O     
5764 C  CB    . GLN A 756 ? 3.1037 2.0741 2.2275 -0.2319 0.1238  0.1117  859  GLN A CB    
5765 C  CG    . GLN A 756 ? 2.8968 1.8726 1.9988 -0.2509 0.0932  0.1126  859  GLN A CG    
5766 C  CD    . GLN A 756 ? 3.1992 2.1078 2.2219 -0.2965 0.0704  0.1048  859  GLN A CD    
5767 O  OE1   . GLN A 756 ? 3.6354 2.4951 2.6204 -0.3158 0.0741  0.0984  859  GLN A OE1   
5768 N  NE2   . GLN A 756 ? 3.1258 2.0312 2.1217 -0.3152 0.0460  0.1059  859  GLN A NE2   
5769 N  N     . ILE A 757 ? 2.9096 1.8397 2.0520 -0.1823 0.2378  0.1066  860  ILE A N     
5770 C  CA    . ILE A 757 ? 3.1392 2.0603 2.3024 -0.1668 0.2620  0.1081  860  ILE A CA    
5771 C  C     . ILE A 757 ? 3.0378 1.9005 2.1619 -0.1636 0.3198  0.0993  860  ILE A C     
5772 O  O     . ILE A 757 ? 2.8120 1.6991 1.9670 -0.1357 0.3534  0.1049  860  ILE A O     
5773 C  CB    . ILE A 757 ? 3.0100 2.0113 2.2617 -0.1269 0.2590  0.1239  860  ILE A CB    
5774 C  CG1   . ILE A 757 ? 2.9613 2.0174 2.2510 -0.1309 0.2047  0.1313  860  ILE A CG1   
5775 C  CG2   . ILE A 757 ? 2.6711 1.6597 1.9415 -0.1116 0.2850  0.1262  860  ILE A CG2   
5776 C  CD1   . ILE A 757 ? 3.1254 2.1520 2.3911 -0.1593 0.1725  0.1268  860  ILE A CD1   
5777 N  N     . GLN A 758 ? 3.0150 1.8004 2.0724 -0.1929 0.3321  0.0859  861  GLN A N     
5778 C  CA    . GLN A 758 ? 3.1261 1.8451 2.1390 -0.1941 0.3891  0.0753  861  GLN A CA    
5779 C  C     . GLN A 758 ? 3.1644 1.8078 2.1143 -0.2267 0.3923  0.0620  861  GLN A C     
5780 O  O     . GLN A 758 ? 2.9425 1.5775 1.8681 -0.2561 0.3475  0.0595  861  GLN A O     
5781 C  CB    . GLN A 758 ? 2.8163 1.5041 1.7807 -0.2077 0.4074  0.0668  861  GLN A CB    
5782 C  CG    . GLN A 758 ? 2.8689 1.4878 1.7412 -0.2579 0.3863  0.0517  861  GLN A CG    
5783 C  CD    . GLN A 758 ? 2.9889 1.6400 1.8675 -0.2783 0.3198  0.0572  861  GLN A CD    
5784 O  OE1   . GLN A 758 ? 3.2050 1.9307 2.1459 -0.2583 0.2892  0.0702  861  GLN A OE1   
5785 N  NE2   . GLN A 758 ? 3.1326 1.7271 1.9477 -0.3188 0.2978  0.0478  861  GLN A NE2   
5786 N  N     . CYS A 759 ? 3.0018 1.5904 1.9273 -0.2215 0.4462  0.0542  862  CYS A N     
5787 C  CA    . CYS A 759 ? 3.0779 1.5864 1.9376 -0.2533 0.4574  0.0397  862  CYS A CA    
5788 C  C     . CYS A 759 ? 3.2967 1.7251 2.0971 -0.2608 0.5197  0.0251  862  CYS A C     
5789 O  O     . CYS A 759 ? 3.4169 1.8560 2.2566 -0.2261 0.5674  0.0305  862  CYS A O     
5790 C  CB    . CYS A 759 ? 3.1709 1.6998 2.0785 -0.2354 0.4561  0.0474  862  CYS A CB    
5791 S  SG    . CYS A 759 ? 3.3416 1.9421 2.3009 -0.2386 0.3839  0.0599  862  CYS A SG    
5792 N  N     . PHE A 769 ? 3.7017 1.9161 2.3255 -0.2902 0.6896  -0.0184 872  PHE A N     
5793 C  CA    . PHE A 769 ? 3.8126 2.0729 2.4943 -0.2516 0.7219  -0.0076 872  PHE A CA    
5794 C  C     . PHE A 769 ? 3.9837 2.3563 2.7648 -0.2149 0.6806  0.0157  872  PHE A C     
5795 O  O     . PHE A 769 ? 3.7743 2.1860 2.5702 -0.2241 0.6240  0.0215  872  PHE A O     
5796 C  CB    . PHE A 769 ? 3.6285 1.8548 2.3309 -0.2239 0.7945  -0.0083 872  PHE A CB    
5797 N  N     . ASN A 770 ? 4.2676 2.6911 3.1167 -0.1743 0.7100  0.0291  873  ASN A N     
5798 C  CA    . ASN A 770 ? 3.9527 2.4813 2.8950 -0.1387 0.6772  0.0512  873  ASN A CA    
5799 C  C     . ASN A 770 ? 3.7821 2.3475 2.8008 -0.0970 0.7027  0.0671  873  ASN A C     
5800 O  O     . ASN A 770 ? 4.0017 2.5265 3.0210 -0.0826 0.7602  0.0655  873  ASN A O     
5801 C  CB    . ASN A 770 ? 3.9178 2.4857 2.8842 -0.1248 0.6853  0.0571  873  ASN A CB    
5802 C  CG    . ASN A 770 ? 4.1925 2.7261 3.1622 -0.1067 0.7553  0.0552  873  ASN A CG    
5803 O  OD1   . ASN A 770 ? 4.3455 2.9258 3.3916 -0.0657 0.7824  0.0720  873  ASN A OD1   
5804 N  ND2   . ASN A 770 ? 4.0052 2.4562 2.8921 -0.1377 0.7854  0.0355  873  ASN A ND2   
5805 N  N     . SER A 771 ? 3.2484 1.8894 2.3311 -0.0781 0.6605  0.0830  874  SER A N     
5806 C  CA    . SER A 771 ? 2.9874 1.6698 2.1438 -0.0396 0.6773  0.1004  874  SER A CA    
5807 C  C     . SER A 771 ? 3.0123 1.7942 2.2423 -0.0179 0.6284  0.1191  874  SER A C     
5808 O  O     . SER A 771 ? 2.9362 1.7491 2.1583 -0.0335 0.5838  0.1173  874  SER A O     
5809 C  CB    . SER A 771 ? 2.7742 1.4010 1.9006 -0.0524 0.6864  0.0924  874  SER A CB    
5810 O  OG    . SER A 771 ? 3.0027 1.6702 2.2004 -0.0152 0.7011  0.1103  874  SER A OG    
5811 N  N     . HIS A 772 ? 3.1589 1.9888 2.4595 0.0177  0.6382  0.1374  875  HIS A N     
5812 C  CA    . HIS A 772 ? 2.8760 1.7982 2.2468 0.0394  0.5964  0.1555  875  HIS A CA    
5813 C  C     . HIS A 772 ? 2.9474 1.8724 2.3123 0.0242  0.5552  0.1529  875  HIS A C     
5814 O  O     . HIS A 772 ? 2.8527 1.8111 2.2655 0.0455  0.5520  0.1657  875  HIS A O     
5815 C  CB    . HIS A 772 ? 2.8913 1.8661 2.3403 0.0839  0.6254  0.1783  875  HIS A CB    
5816 C  CG    . HIS A 772 ? 2.9943 1.9806 2.4627 0.1013  0.6610  0.1844  875  HIS A CG    
5817 N  ND1   . HIS A 772 ? 3.1514 2.1762 2.6865 0.1397  0.6943  0.2054  875  HIS A ND1   
5818 C  CD2   . HIS A 772 ? 2.9242 1.8895 2.3559 0.0850  0.6683  0.1734  875  HIS A CD2   
5819 C  CE1   . HIS A 772 ? 2.8829 1.9111 2.4243 0.1468  0.7209  0.2070  875  HIS A CE1   
5820 N  NE2   . HIS A 772 ? 2.8163 1.8079 2.2944 0.1140  0.7067  0.1871  875  HIS A NE2   
5821 N  N     . THR A 773 ? 2.8658 1.7548 2.1707 -0.0141 0.5231  0.1366  876  THR A N     
5822 C  CA    . THR A 773 ? 2.9179 1.8061 2.2139 -0.0331 0.4820  0.1331  876  THR A CA    
5823 C  C     . THR A 773 ? 2.9022 1.8721 2.2506 -0.0246 0.4306  0.1447  876  THR A C     
5824 O  O     . THR A 773 ? 3.0580 2.0337 2.4050 -0.0401 0.3935  0.1428  876  THR A O     
5825 C  CB    . THR A 773 ? 2.8944 1.7084 2.1044 -0.0797 0.4681  0.1124  876  THR A CB    
5826 O  OG1   . THR A 773 ? 2.8163 1.6394 2.0020 -0.0962 0.4455  0.1078  876  THR A OG1   
5827 C  CG2   . THR A 773 ? 2.9765 1.7030 2.1289 -0.0912 0.5207  0.0989  876  THR A CG2   
5828 N  N     . LEU A 774 ? 2.7571 1.7891 2.1517 -0.0013 0.4285  0.1564  877  LEU A N     
5829 C  CA    . LEU A 774 ? 2.5631 1.6716 2.0076 0.0073  0.3833  0.1669  877  LEU A CA    
5830 C  C     . LEU A 774 ? 2.5688 1.7181 2.0681 0.0294  0.3766  0.1799  877  LEU A C     
5831 O  O     . LEU A 774 ? 2.4545 1.6381 1.9743 0.0235  0.3363  0.1822  877  LEU A O     
5832 C  CB    . LEU A 774 ? 2.2831 1.4460 1.7630 0.0268  0.3867  0.1763  877  LEU A CB    
5833 C  CG    . LEU A 774 ? 2.2910 1.5346 1.8244 0.0378  0.3453  0.1873  877  LEU A CG    
5834 C  CD1   . LEU A 774 ? 1.9270 1.1632 1.4316 0.0070  0.2980  0.1772  877  LEU A CD1   
5835 C  CD2   . LEU A 774 ? 2.1492 1.4414 1.7142 0.0559  0.3537  0.1961  877  LEU A CD2   
5836 N  N     . HIS A 775 ? 2.6216 1.7667 2.1458 0.0550  0.4167  0.1892  878  HIS A N     
5837 C  CA    . HIS A 775 ? 2.2487 1.4275 1.8210 0.0753  0.4130  0.2022  878  HIS A CA    
5838 C  C     . HIS A 775 ? 2.3741 1.5060 1.9138 0.0523  0.4008  0.1915  878  HIS A C     
5839 O  O     . HIS A 775 ? 2.4037 1.5690 1.9768 0.0578  0.3776  0.1985  878  HIS A O     
5840 C  CB    . HIS A 775 ? 2.1864 1.3701 1.7931 0.1083  0.4599  0.2166  878  HIS A CB    
5841 C  CG    . HIS A 775 ? 2.1002 1.3324 1.7644 0.1337  0.4550  0.2344  878  HIS A CG    
5842 N  ND1   . HIS A 775 ? 2.4783 1.7080 2.1722 0.1610  0.4938  0.2486  878  HIS A ND1   
5843 C  CD2   . HIS A 775 ? 2.3691 1.6524 2.0659 0.1356  0.4170  0.2407  878  HIS A CD2   
5844 C  CE1   . HIS A 775 ? 2.5393 1.8165 2.2792 0.1778  0.4783  0.2633  878  HIS A CE1   
5845 N  NE2   . HIS A 775 ? 2.2919 1.6016 2.0335 0.1626  0.4328  0.2581  878  HIS A NE2   
5846 N  N     . GLN A 776 ? 2.7807 1.8348 2.2545 0.0250  0.4163  0.1746  879  GLN A N     
5847 C  CA    . GLN A 776 ? 2.9850 1.9923 2.4242 -0.0007 0.4032  0.1640  879  GLN A CA    
5848 C  C     . GLN A 776 ? 2.8995 1.9271 2.3314 -0.0264 0.3479  0.1588  879  GLN A C     
5849 O  O     . GLN A 776 ? 2.8618 1.8897 2.3012 -0.0364 0.3254  0.1584  879  GLN A O     
5850 C  CB    . GLN A 776 ? 2.9807 1.8966 2.3472 -0.0250 0.4363  0.1469  879  GLN A CB    
5851 C  CG    . GLN A 776 ? 3.0685 1.9302 2.3932 -0.0552 0.4245  0.1351  879  GLN A CG    
5852 C  CD    . GLN A 776 ? 2.8585 1.7330 2.2244 -0.0352 0.4356  0.1449  879  GLN A CD    
5853 O  OE1   . GLN A 776 ? 2.7568 1.6532 2.1649 -0.0009 0.4687  0.1579  879  GLN A OE1   
5854 N  NE2   . GLN A 776 ? 2.8566 1.7182 2.2118 -0.0571 0.4074  0.1398  879  GLN A NE2   
5855 N  N     . TRP A 777 ? 2.6893 1.7341 2.1092 -0.0371 0.3260  0.1557  880  TRP A N     
5856 C  CA    . TRP A 777 ? 2.7035 1.7695 2.1213 -0.0599 0.2737  0.1528  880  TRP A CA    
5857 C  C     . TRP A 777 ? 2.5546 1.6951 2.0426 -0.0389 0.2468  0.1665  880  TRP A C     
5858 O  O     . TRP A 777 ? 2.6451 1.7944 2.1408 -0.0545 0.2117  0.1654  880  TRP A O     
5859 C  CB    . TRP A 777 ? 2.6445 1.7138 2.0370 -0.0730 0.2594  0.1481  880  TRP A CB    
5860 C  CG    . TRP A 777 ? 2.5813 1.6908 1.9909 -0.0866 0.2070  0.1502  880  TRP A CG    
5861 C  CD1   . TRP A 777 ? 2.4721 1.6428 1.9211 -0.0729 0.1873  0.1581  880  TRP A CD1   
5862 C  CD2   . TRP A 777 ? 2.5947 1.6859 1.9855 -0.1164 0.1684  0.1453  880  TRP A CD2   
5863 N  NE1   . TRP A 777 ? 2.4761 1.6658 1.9320 -0.0914 0.1407  0.1580  880  TRP A NE1   
5864 C  CE2   . TRP A 777 ? 2.7407 1.8839 2.1635 -0.1178 0.1276  0.1511  880  TRP A CE2   
5865 C  CE3   . TRP A 777 ? 2.7057 1.7417 2.0568 -0.1428 0.1643  0.1370  880  TRP A CE3   
5866 C  CZ2   . TRP A 777 ? 2.7911 1.9343 2.2117 -0.1429 0.0837  0.1503  880  TRP A CZ2   
5867 C  CZ3   . TRP A 777 ? 2.9456 1.9833 2.2935 -0.1691 0.1187  0.1364  880  TRP A CZ3   
5868 C  CH2   . TRP A 777 ? 2.8209 1.9125 2.2053 -0.1681 0.0792  0.1437  880  TRP A CH2   
5869 N  N     . LEU A 778 ? 2.3357 1.5302 1.8756 -0.0045 0.2632  0.1798  881  LEU A N     
5870 C  CA    . LEU A 778 ? 2.3113 1.5731 1.9139 0.0151  0.2418  0.1926  881  LEU A CA    
5871 C  C     . LEU A 778 ? 2.3526 1.6036 1.9717 0.0231  0.2537  0.1967  881  LEU A C     
5872 O  O     . LEU A 778 ? 2.6389 1.9274 2.2952 0.0268  0.2294  0.2025  881  LEU A O     
5873 C  CB    . LEU A 778 ? 2.0819 1.4043 1.7309 0.0465  0.2538  0.2061  881  LEU A CB    
5874 C  CG    . LEU A 778 ? 2.1659 1.5079 1.8062 0.0405  0.2406  0.2033  881  LEU A CG    
5875 C  CD1   . LEU A 778 ? 2.1065 1.5140 1.7980 0.0709  0.2497  0.2180  881  LEU A CD1   
5876 C  CD2   . LEU A 778 ? 2.0663 1.4201 1.7008 0.0168  0.1940  0.1969  881  LEU A CD2   
5877 N  N     . LYS A 779 ? 2.3698 1.5683 1.9620 0.0255  0.2924  0.1937  882  LYS A N     
5878 C  CA    . LYS A 779 ? 2.3791 1.5583 1.9802 0.0295  0.3044  0.1962  882  LYS A CA    
5879 C  C     . LYS A 779 ? 2.6029 1.7430 2.1702 -0.0050 0.2770  0.1837  882  LYS A C     
5880 O  O     . LYS A 779 ? 2.7883 1.9416 2.3810 -0.0045 0.2638  0.1874  882  LYS A O     
5881 C  CB    . LYS A 779 ? 2.6479 1.7785 2.2294 0.0415  0.3558  0.1965  882  LYS A CB    
5882 C  CG    . LYS A 779 ? 2.5787 1.7534 2.2104 0.0810  0.3845  0.2148  882  LYS A CG    
5883 C  CD    . LYS A 779 ? 2.3783 1.5005 1.9942 0.0924  0.4360  0.2159  882  LYS A CD    
5884 C  CE    . LYS A 779 ? 2.2643 1.4334 1.9371 0.1327  0.4625  0.2379  882  LYS A CE    
5885 N  NZ    . LYS A 779 ? 2.3411 1.4587 2.0036 0.1456  0.5145  0.2406  882  LYS A NZ    
5886 N  N     . ASP A 780 ? 2.8149 1.9070 2.3250 -0.0361 0.2678  0.1694  883  ASP A N     
5887 C  CA    . ASP A 780 ? 3.0993 2.1493 2.5726 -0.0718 0.2424  0.1584  883  ASP A CA    
5888 C  C     . ASP A 780 ? 2.9958 2.0955 2.5040 -0.0807 0.1920  0.1626  883  ASP A C     
5889 O  O     . ASP A 780 ? 3.2067 2.2959 2.7169 -0.0980 0.1713  0.1606  883  ASP A O     
5890 C  CB    . ASP A 780 ? 3.2389 2.2224 2.6373 -0.1041 0.2467  0.1431  883  ASP A CB    
5891 C  CG    . ASP A 780 ? 3.4979 2.4158 2.8458 -0.1390 0.2416  0.1311  883  ASP A CG    
5892 O  OD1   . ASP A 780 ? 3.5989 2.5330 2.9720 -0.1460 0.2160  0.1343  883  ASP A OD1   
5893 O  OD2   . ASP A 780 ? 3.4699 2.3192 2.7520 -0.1605 0.2640  0.1183  883  ASP A OD2   
5894 N  N     . LYS A 781 ? 2.6401 1.7933 2.1777 -0.0694 0.1730  0.1687  884  LYS A N     
5895 C  CA    . LYS A 781 ? 2.5863 1.7845 2.1573 -0.0777 0.1274  0.1724  884  LYS A CA    
5896 C  C     . LYS A 781 ? 2.5234 1.7841 2.1629 -0.0505 0.1230  0.1847  884  LYS A C     
5897 O  O     . LYS A 781 ? 2.4432 1.7308 2.1121 -0.0589 0.0905  0.1870  884  LYS A O     
5898 C  CB    . LYS A 781 ? 2.6217 1.8423 2.1868 -0.0824 0.1078  0.1717  884  LYS A CB    
5899 C  CG    . LYS A 781 ? 2.6528 1.8994 2.2357 -0.1010 0.0595  0.1728  884  LYS A CG    
5900 C  CD    . LYS A 781 ? 2.6534 1.8487 2.1968 -0.1371 0.0386  0.1653  884  LYS A CD    
5901 C  CE    . LYS A 781 ? 2.3099 1.5346 1.8802 -0.1537 -0.0098 0.1693  884  LYS A CE    
5902 N  NZ    . LYS A 781 ? 2.7169 1.9578 2.2791 -0.1595 -0.0295 0.1698  884  LYS A NZ    
5903 N  N     . ASN A 782 ? 2.6965 1.9803 2.3621 -0.0191 0.1549  0.1934  885  ASN A N     
5904 C  CA    . ASN A 782 ? 2.5505 1.8917 2.2761 0.0066  0.1535  0.2058  885  ASN A CA    
5905 C  C     . ASN A 782 ? 2.4310 1.7497 2.1597 0.0216  0.1880  0.2105  885  ASN A C     
5906 O  O     . ASN A 782 ? 2.3387 1.6607 2.0726 0.0449  0.2209  0.2177  885  ASN A O     
5907 C  CB    . ASN A 782 ? 2.5235 1.9227 2.2822 0.0308  0.1552  0.2151  885  ASN A CB    
5908 C  CG    . ASN A 782 ? 2.4307 1.8517 2.1878 0.0165  0.1221  0.2107  885  ASN A CG    
5909 O  OD1   . ASN A 782 ? 2.3662 1.7846 2.1033 0.0164  0.1279  0.2084  885  ASN A OD1   
5910 N  ND2   . ASN A 782 ? 2.3432 1.7854 2.1232 0.0045  0.0883  0.2099  885  ASN A ND2   
5911 N  N     . LYS A 783 ? 2.6959 1.9923 2.4238 0.0083  0.1806  0.2074  886  LYS A N     
5912 C  CA    . LYS A 783 ? 2.7078 1.9796 2.4383 0.0199  0.2112  0.2114  886  LYS A CA    
5913 C  C     . LYS A 783 ? 2.5868 1.9120 2.3743 0.0414  0.2065  0.2243  886  LYS A C     
5914 O  O     . LYS A 783 ? 2.5223 1.8964 2.3438 0.0418  0.1774  0.2274  886  LYS A O     
5915 C  CB    . LYS A 783 ? 2.6787 1.8867 2.3678 -0.0104 0.2090  0.1992  886  LYS A CB    
5916 C  CG    . LYS A 783 ? 2.8570 2.0030 2.4814 -0.0340 0.2182  0.1858  886  LYS A CG    
5917 C  CD    . LYS A 783 ? 3.1040 2.1860 2.6858 -0.0651 0.2174  0.1742  886  LYS A CD    
5918 C  CE    . LYS A 783 ? 3.0699 2.0855 2.5807 -0.0908 0.2287  0.1601  886  LYS A CE    
5919 N  NZ    . LYS A 783 ? 3.2965 2.2469 2.7611 -0.1237 0.2285  0.1484  886  LYS A NZ    
5920 N  N     . GLY A 784 ? 2.4334 1.7465 2.2300 0.0588  0.2373  0.2319  887  GLY A N     
5921 C  CA    . GLY A 784 ? 2.3357 1.6938 2.1810 0.0793  0.2375  0.2450  887  GLY A CA    
5922 C  C     . GLY A 784 ? 2.2967 1.7169 2.1787 0.1069  0.2395  0.2590  887  GLY A C     
5923 O  O     . GLY A 784 ? 2.0160 1.4367 1.8896 0.1207  0.2594  0.2635  887  GLY A O     
5924 N  N     . GLU A 785 ? 2.3169 1.7896 2.2397 0.1139  0.2194  0.2658  888  GLU A N     
5925 C  CA    . GLU A 785 ? 2.2812 1.8147 2.2373 0.1367  0.2182  0.2786  888  GLU A CA    
5926 C  C     . GLU A 785 ? 2.5418 2.0991 2.4933 0.1292  0.1966  0.2727  888  GLU A C     
5927 O  O     . GLU A 785 ? 2.4737 2.0793 2.4485 0.1459  0.1955  0.2822  888  GLU A O     
5928 C  CB    . GLU A 785 ? 2.1927 1.7701 2.1892 0.1444  0.2058  0.2867  888  GLU A CB    
5929 C  CG    . GLU A 785 ? 2.4409 2.0053 2.4479 0.1570  0.2291  0.2966  888  GLU A CG    
5930 C  CD    . GLU A 785 ? 2.5194 2.0335 2.5084 0.1363  0.2279  0.2856  888  GLU A CD    
5931 O  OE1   . GLU A 785 ? 2.4246 1.9204 2.3978 0.1115  0.2048  0.2714  888  GLU A OE1   
5932 O  OE2   . GLU A 785 ? 2.4859 1.9791 2.4772 0.1442  0.2495  0.2920  888  GLU A OE2   
5933 N  N     . ILE A 786 ? 2.6686 2.1928 2.5898 0.1037  0.1790  0.2579  889  ILE A N     
5934 C  CA    . ILE A 786 ? 2.3375 1.8804 2.2521 0.0954  0.1585  0.2524  889  ILE A CA    
5935 C  C     . ILE A 786 ? 2.3119 1.8420 2.2029 0.1045  0.1811  0.2537  889  ILE A C     
5936 O  O     . ILE A 786 ? 2.4324 1.9911 2.3271 0.1062  0.1704  0.2537  889  ILE A O     
5937 C  CB    . ILE A 786 ? 2.5311 2.0430 2.4218 0.0640  0.1301  0.2382  889  ILE A CB    
5938 C  CG1   . ILE A 786 ? 2.5757 2.0894 2.4888 0.0543  0.1142  0.2373  889  ILE A CG1   
5939 C  CG2   . ILE A 786 ? 2.6850 2.2273 2.5811 0.0565  0.1032  0.2348  889  ILE A CG2   
5940 C  CD1   . ILE A 786 ? 2.6977 2.1847 2.5938 0.0232  0.0839  0.2263  889  ILE A CD1   
5941 N  N     . TYR A 787 ? 2.4345 1.9216 2.3029 0.1103  0.2136  0.2549  890  TYR A N     
5942 C  CA    . TYR A 787 ? 2.2596 1.7327 2.1090 0.1200  0.2393  0.2567  890  TYR A CA    
5943 C  C     . TYR A 787 ? 2.1402 1.6743 2.0291 0.1475  0.2461  0.2728  890  TYR A C     
5944 O  O     . TYR A 787 ? 2.0738 1.6216 1.9580 0.1506  0.2481  0.2730  890  TYR A O     
5945 C  CB    . TYR A 787 ? 2.3705 1.7865 2.1943 0.1235  0.2766  0.2562  890  TYR A CB    
5946 C  CG    . TYR A 787 ? 2.2886 1.6973 2.1073 0.1416  0.3110  0.2630  890  TYR A CG    
5947 C  CD1   . TYR A 787 ? 2.3131 1.6863 2.0916 0.1276  0.3182  0.2514  890  TYR A CD1   
5948 C  CD2   . TYR A 787 ? 2.2881 1.7256 2.1433 0.1724  0.3365  0.2819  890  TYR A CD2   
5949 C  CE1   . TYR A 787 ? 2.0811 1.4477 1.8583 0.1444  0.3519  0.2576  890  TYR A CE1   
5950 C  CE2   . TYR A 787 ? 2.1076 1.5408 1.9645 0.1898  0.3683  0.2898  890  TYR A CE2   
5951 C  CZ    . TYR A 787 ? 2.2403 1.6380 2.0593 0.1760  0.3769  0.2772  890  TYR A CZ    
5952 O  OH    . TYR A 787 ? 2.1914 1.5849 2.0152 0.1936  0.4108  0.2851  890  TYR A OH    
5953 N  N     . ASP A 788 ? 2.4346 2.0057 2.3617 0.1664  0.2493  0.2869  891  ASP A N     
5954 C  CA    . ASP A 788 ? 2.4084 2.0383 2.3721 0.1909  0.2545  0.3041  891  ASP A CA    
5955 C  C     . ASP A 788 ? 2.3661 2.0438 2.3431 0.1844  0.2240  0.3009  891  ASP A C     
5956 O  O     . ASP A 788 ? 2.2135 1.9319 2.2085 0.1983  0.2271  0.3108  891  ASP A O     
5957 C  CB    . ASP A 788 ? 2.5137 2.1701 2.5107 0.2088  0.2618  0.3198  891  ASP A CB    
5958 C  CG    . ASP A 788 ? 2.9271 2.6301 2.9558 0.2360  0.2773  0.3413  891  ASP A CG    
5959 O  OD1   . ASP A 788 ? 3.0357 2.7494 3.0628 0.2417  0.2847  0.3439  891  ASP A OD1   
5960 O  OD2   . ASP A 788 ? 3.0388 2.7680 3.0945 0.2509  0.2818  0.3564  891  ASP A OD2   
5961 N  N     . ALA A 789 ? 2.4029 2.0764 2.3731 0.1632  0.1947  0.2878  892  ALA A N     
5962 C  CA    . ALA A 789 ? 2.0838 1.7979 2.0661 0.1560  0.1667  0.2839  892  ALA A CA    
5963 C  C     . ALA A 789 ? 2.0240 1.7155 1.9750 0.1414  0.1608  0.2728  892  ALA A C     
5964 O  O     . ALA A 789 ? 2.1252 1.8521 2.0858 0.1429  0.1494  0.2737  892  ALA A O     
5965 C  CB    . ALA A 789 ? 2.1632 1.8861 2.1589 0.1416  0.1388  0.2768  892  ALA A CB    
5966 N  N     . ALA A 790 ? 2.0113 1.6429 1.9227 0.1258  0.1687  0.2622  893  ALA A N     
5967 C  CA    . ALA A 790 ? 1.9595 1.5646 1.8355 0.1099  0.1643  0.2515  893  ALA A CA    
5968 C  C     . ALA A 790 ? 1.6127 1.2261 1.4870 0.1266  0.1912  0.2586  893  ALA A C     
5969 O  O     . ALA A 790 ? 1.9677 1.5900 1.8316 0.1208  0.1840  0.2546  893  ALA A O     
5970 C  CB    . ALA A 790 ? 2.0761 1.6124 1.9059 0.0865  0.1662  0.2384  893  ALA A CB    
5971 N  N     . ILE A 791 ? 2.0645 1.6752 1.9512 0.1475  0.2227  0.2701  894  ILE A N     
5972 C  CA    . ILE A 791 ? 2.1991 1.8227 2.0933 0.1659  0.2495  0.2798  894  ILE A CA    
5973 C  C     . ILE A 791 ? 2.0140 1.7089 1.9476 0.1794  0.2352  0.2912  894  ILE A C     
5974 O  O     . ILE A 791 ? 1.7665 1.4778 1.7009 0.1835  0.2412  0.2934  894  ILE A O     
5975 C  CB    . ILE A 791 ? 1.8197 1.4245 1.7233 0.1861  0.2864  0.2917  894  ILE A CB    
5976 C  CG1   . ILE A 791 ? 1.8816 1.4105 1.7409 0.1700  0.3026  0.2783  894  ILE A CG1   
5977 C  CG2   . ILE A 791 ? 1.6574 1.2807 1.5777 0.2071  0.3144  0.3046  894  ILE A CG2   
5978 C  CD1   . ILE A 791 ? 2.0051 1.4862 1.8165 0.1507  0.3095  0.2630  894  ILE A CD1   
5979 N  N     . ASP A 792 ? 2.0527 1.7899 2.0180 0.1851  0.2166  0.2981  895  ASP A N     
5980 C  CA    . ASP A 792 ? 1.9096 1.7124 1.9079 0.1942  0.2012  0.3073  895  ASP A CA    
5981 C  C     . ASP A 792 ? 2.0057 1.8160 1.9903 0.1757  0.1758  0.2943  895  ASP A C     
5982 O  O     . ASP A 792 ? 2.0179 1.8646 2.0146 0.1809  0.1735  0.2990  895  ASP A O     
5983 C  CB    . ASP A 792 ? 2.0473 1.8860 2.0758 0.2004  0.1875  0.3150  895  ASP A CB    
5984 C  CG    . ASP A 792 ? 2.0060 1.9092 2.0635 0.2060  0.1705  0.3227  895  ASP A CG    
5985 O  OD1   . ASP A 792 ? 1.7732 1.7105 1.8498 0.2226  0.1833  0.3377  895  ASP A OD1   
5986 O  OD2   . ASP A 792 ? 2.1348 2.0544 2.1969 0.1932  0.1447  0.3140  895  ASP A OD2   
5987 N  N     . LEU A 793 ? 2.0983 1.8749 2.0588 0.1536  0.1561  0.2789  896  LEU A N     
5988 C  CA    . LEU A 793 ? 2.0160 1.7945 1.9620 0.1353  0.1320  0.2675  896  LEU A CA    
5989 C  C     . LEU A 793 ? 1.6658 1.4192 1.5825 0.1314  0.1470  0.2634  896  LEU A C     
5990 O  O     . LEU A 793 ? 1.7898 1.5623 1.7043 0.1248  0.1342  0.2598  896  LEU A O     
5991 C  CB    . LEU A 793 ? 1.6517 1.3963 1.5794 0.1125  0.1084  0.2545  896  LEU A CB    
5992 C  CG    . LEU A 793 ? 1.3898 1.1372 1.3072 0.0929  0.0793  0.2445  896  LEU A CG    
5993 C  CD1   . LEU A 793 ? 1.2174 1.0251 1.1724 0.1003  0.0629  0.2492  896  LEU A CD1   
5994 C  CD2   . LEU A 793 ? 1.7653 1.4756 1.6661 0.0706  0.0578  0.2346  896  LEU A CD2   
5995 N  N     . PHE A 794 ? 1.7283 1.4375 1.6220 0.1351  0.1759  0.2635  897  PHE A N     
5996 C  CA    . PHE A 794 ? 1.7557 1.4377 1.6210 0.1318  0.1952  0.2593  897  PHE A CA    
5997 C  C     . PHE A 794 ? 1.7338 1.4641 1.6309 0.1532  0.2110  0.2732  897  PHE A C     
5998 O  O     . PHE A 794 ? 1.8013 1.5293 1.6849 0.1491  0.2169  0.2699  897  PHE A O     
5999 C  CB    . PHE A 794 ? 2.0175 1.6352 1.8490 0.1291  0.2248  0.2548  897  PHE A CB    
6000 C  CG    . PHE A 794 ? 2.1474 1.7288 1.9448 0.1236  0.2483  0.2487  897  PHE A CG    
6001 C  CD1   . PHE A 794 ? 2.0467 1.5834 1.7951 0.0961  0.2358  0.2326  897  PHE A CD1   
6002 C  CD2   . PHE A 794 ? 2.2058 1.7972 2.0210 0.1455  0.2833  0.2600  897  PHE A CD2   
6003 C  CE1   . PHE A 794 ? 2.2191 1.7196 1.9327 0.0897  0.2590  0.2263  897  PHE A CE1   
6004 C  CE2   . PHE A 794 ? 2.2341 1.7908 2.0194 0.1404  0.3077  0.2539  897  PHE A CE2   
6005 C  CZ    . PHE A 794 ? 2.3840 1.8939 2.1163 0.1121  0.2963  0.2363  897  PHE A CZ    
6006 N  N     . THR A 795 ? 1.8170 1.5915 1.7560 0.1751  0.2175  0.2895  898  THR A N     
6007 C  CA    . THR A 795 ? 1.9267 1.7502 1.8994 0.1954  0.2313  0.3056  898  THR A CA    
6008 C  C     . THR A 795 ? 1.7992 1.6817 1.7949 0.1927  0.2036  0.3076  898  THR A C     
6009 O  O     . THR A 795 ? 1.8320 1.7427 1.8385 0.1974  0.2084  0.3128  898  THR A O     
6010 C  CB    . THR A 795 ? 1.7299 1.5736 1.7363 0.2196  0.2510  0.3248  898  THR A CB    
6011 O  OG1   . THR A 795 ? 2.1157 1.9804 2.1376 0.2188  0.2298  0.3266  898  THR A OG1   
6012 C  CG2   . THR A 795 ? 1.7364 1.5210 1.7221 0.2243  0.2842  0.3237  898  THR A CG2   
6013 N  N     . ARG A 796 ? 1.8096 1.7103 1.8136 0.1846  0.1760  0.3034  899  ARG A N     
6014 C  CA    . ARG A 796 ? 1.7691 1.7223 1.7933 0.1809  0.1515  0.3041  899  ARG A CA    
6015 C  C     . ARG A 796 ? 1.7537 1.6922 1.7526 0.1617  0.1367  0.2895  899  ARG A C     
6016 O  O     . ARG A 796 ? 1.5477 1.5240 1.5589 0.1616  0.1292  0.2918  899  ARG A O     
6017 C  CB    . ARG A 796 ? 1.7701 1.7421 1.8099 0.1773  0.1297  0.3028  899  ARG A CB    
6018 C  CG    . ARG A 796 ? 1.6999 1.6826 1.7613 0.1944  0.1433  0.3168  899  ARG A CG    
6019 C  CD    . ARG A 796 ? 1.7411 1.7443 1.8179 0.1898  0.1229  0.3150  899  ARG A CD    
6020 N  NE    . ARG A 796 ? 1.8684 1.9310 1.9710 0.1942  0.1111  0.3230  899  ARG A NE    
6021 C  CZ    . ARG A 796 ? 1.7212 1.8221 1.8486 0.2098  0.1189  0.3404  899  ARG A CZ    
6022 N  NH1   . ARG A 796 ? 1.5164 1.6042 1.6497 0.2247  0.1390  0.3528  899  ARG A NH1   
6023 N  NH2   . ARG A 796 ? 1.8201 1.9726 1.9654 0.2094  0.1060  0.3460  899  ARG A NH2   
6024 N  N     . SER A 797 ? 1.7116 1.5951 1.6741 0.1442  0.1317  0.2751  900  SER A N     
6025 C  CA    . SER A 797 ? 1.5524 1.4175 1.4873 0.1250  0.1178  0.2625  900  SER A CA    
6026 C  C     . SER A 797 ? 1.6386 1.4893 1.5567 0.1282  0.1420  0.2637  900  SER A C     
6027 O  O     . SER A 797 ? 1.8990 1.7563 1.8068 0.1183  0.1336  0.2584  900  SER A O     
6028 C  CB    . SER A 797 ? 1.6681 1.4794 1.5686 0.1036  0.1028  0.2488  900  SER A CB    
6029 O  OG    . SER A 797 ? 1.7294 1.4895 1.6031 0.1036  0.1257  0.2470  900  SER A OG    
6030 N  N     . CYS A 798 ? 1.6503 1.4805 1.5667 0.1419  0.1736  0.2707  901  CYS A N     
6031 C  CA    . CYS A 798 ? 1.6054 1.4226 1.5107 0.1467  0.2009  0.2726  901  CYS A CA    
6032 C  C     . CYS A 798 ? 1.6291 1.5103 1.5751 0.1623  0.2041  0.2866  901  CYS A C     
6033 O  O     . CYS A 798 ? 1.6708 1.5569 1.6097 0.1578  0.2090  0.2842  901  CYS A O     
6034 C  CB    . CYS A 798 ? 1.6148 1.3911 1.5106 0.1578  0.2364  0.2768  901  CYS A CB    
6035 S  SG    . CYS A 798 ? 2.4846 2.2353 2.3659 0.1635  0.2762  0.2780  901  CYS A SG    
6036 N  N     . ALA A 799 ? 1.9990 1.9296 1.9868 0.1795  0.2010  0.3016  902  ALA A N     
6037 C  CA    . ALA A 799 ? 2.0268 2.0215 2.0532 0.1921  0.2004  0.3162  902  ALA A CA    
6038 C  C     . ALA A 799 ? 1.9771 1.9995 2.0009 0.1763  0.1720  0.3073  902  ALA A C     
6039 O  O     . ALA A 799 ? 1.9130 1.9710 1.9528 0.1791  0.1742  0.3132  902  ALA A O     
6040 C  CB    . ALA A 799 ? 1.8930 1.9321 1.9590 0.2100  0.1989  0.3339  902  ALA A CB    
6041 N  N     . GLY A 800 ? 1.7227 1.7291 1.7286 0.1597  0.1458  0.2938  903  GLY A N     
6042 C  CA    . GLY A 800 ? 1.6797 1.7068 1.6826 0.1445  0.1203  0.2849  903  GLY A CA    
6043 C  C     . GLY A 800 ? 1.8097 1.8024 1.7790 0.1298  0.1234  0.2736  903  GLY A C     
6044 O  O     . GLY A 800 ? 1.8153 1.8351 1.7905 0.1259  0.1188  0.2736  903  GLY A O     
6045 N  N     . TYR A 801 ? 1.7892 1.7203 1.7204 0.1201  0.1315  0.2638  904  TYR A N     
6046 C  CA    . TYR A 801 ? 1.7256 1.6174 1.6179 0.1039  0.1351  0.2528  904  TYR A CA    
6047 C  C     . TYR A 801 ? 1.8140 1.7058 1.7076 0.1144  0.1676  0.2593  904  TYR A C     
6048 O  O     . TYR A 801 ? 1.9896 1.8539 1.8530 0.1016  0.1733  0.2510  904  TYR A O     
6049 C  CB    . TYR A 801 ? 1.5631 1.3874 1.4104 0.0872  0.1321  0.2406  904  TYR A CB    
6050 C  CG    . TYR A 801 ? 1.6174 1.4328 1.4522 0.0674  0.0962  0.2307  904  TYR A CG    
6051 C  CD1   . TYR A 801 ? 1.6889 1.4902 1.4982 0.0486  0.0806  0.2221  904  TYR A CD1   
6052 C  CD2   . TYR A 801 ? 1.6627 1.4839 1.5135 0.0678  0.0786  0.2312  904  TYR A CD2   
6053 C  CE1   . TYR A 801 ? 1.6976 1.4914 1.5000 0.0316  0.0479  0.2153  904  TYR A CE1   
6054 C  CE2   . TYR A 801 ? 1.8513 1.6658 1.6967 0.0508  0.0469  0.2237  904  TYR A CE2   
6055 C  CZ    . TYR A 801 ? 1.8011 1.6022 1.6234 0.0331  0.0314  0.2164  904  TYR A CZ    
6056 O  OH    . TYR A 801 ? 2.0111 1.8061 1.8321 0.0170  0.0000  0.2110  904  TYR A OH    
6057 N  N     . CYS A 802 ? 1.6753 1.5964 1.6039 0.1371  0.1895  0.2746  905  CYS A N     
6058 C  CA    . CYS A 802 ? 1.8029 1.7328 1.7438 0.1493  0.2205  0.2836  905  CYS A CA    
6059 C  C     . CYS A 802 ? 1.7730 1.7720 1.7544 0.1568  0.2125  0.2949  905  CYS A C     
6060 O  O     . CYS A 802 ? 1.6060 1.6108 1.5864 0.1546  0.2245  0.2950  905  CYS A O     
6061 C  CB    . CYS A 802 ? 1.7693 1.6898 1.7281 0.1704  0.2516  0.2962  905  CYS A CB    
6062 S  SG    . CYS A 802 ? 2.4120 2.3484 2.3983 0.1894  0.2928  0.3110  905  CYS A SG    
6063 N  N     . VAL A 803 ? 1.8125 1.8628 1.8277 0.1641  0.1925  0.3040  906  VAL A N     
6064 C  CA    . VAL A 803 ? 1.6805 1.7969 1.7318 0.1686  0.1829  0.3147  906  VAL A CA    
6065 C  C     . VAL A 803 ? 1.5539 1.6760 1.5876 0.1480  0.1579  0.3009  906  VAL A C     
6066 O  O     . VAL A 803 ? 1.4755 1.6431 1.5306 0.1475  0.1532  0.3065  906  VAL A O     
6067 C  CB    . VAL A 803 ? 1.4744 1.6410 1.5628 0.1812  0.1707  0.3289  906  VAL A CB    
6068 C  CG1   . VAL A 803 ? 1.6447 1.8132 1.7220 0.1668  0.1388  0.3170  906  VAL A CG1   
6069 C  CG2   . VAL A 803 ? 1.5252 1.7589 1.6554 0.1912  0.1721  0.3467  906  VAL A CG2   
6070 N  N     . ALA A 804 ? 1.6699 1.7471 1.6664 0.1303  0.1416  0.2839  907  ALA A N     
6071 C  CA    . ALA A 804 ? 1.4578 1.5359 1.4377 0.1109  0.1182  0.2716  907  ALA A CA    
6072 C  C     . ALA A 804 ? 1.5828 1.6261 1.5311 0.0996  0.1308  0.2635  907  ALA A C     
6073 O  O     . ALA A 804 ? 1.5711 1.6366 1.5218 0.0912  0.1233  0.2612  907  ALA A O     
6074 C  CB    . ALA A 804 ? 1.3889 1.4387 1.3489 0.0972  0.0925  0.2596  907  ALA A CB    
6075 N  N     . THR A 805 ? 1.7769 1.7641 1.6933 0.0980  0.1510  0.2587  908  THR A N     
6076 C  CA    . THR A 805 ? 1.5097 1.4590 1.3914 0.0863  0.1661  0.2507  908  THR A CA    
6077 C  C     . THR A 805 ? 1.6933 1.6776 1.6032 0.0991  0.1915  0.2618  908  THR A C     
6078 O  O     . THR A 805 ? 1.7740 1.7481 1.6666 0.0886  0.1982  0.2563  908  THR A O     
6079 C  CB    . THR A 805 ? 1.5298 1.4084 1.3681 0.0804  0.1840  0.2427  908  THR A CB    
6080 O  OG1   . THR A 805 ? 1.7107 1.5921 1.5714 0.1012  0.2100  0.2536  908  THR A OG1   
6081 C  CG2   . THR A 805 ? 1.4324 1.2751 1.2404 0.0634  0.1557  0.2316  908  THR A CG2   
6082 N  N     . PHE A 806 ? 1.7499 1.7760 1.7046 0.1214  0.2056  0.2784  909  PHE A N     
6083 C  CA    . PHE A 806 ? 1.5485 1.6161 1.5388 0.1342  0.2269  0.2920  909  PHE A CA    
6084 C  C     . PHE A 806 ? 1.7192 1.8426 1.7316 0.1272  0.2043  0.2940  909  PHE A C     
6085 O  O     . PHE A 806 ? 1.9073 2.0502 1.9313 0.1266  0.2169  0.2978  909  PHE A O     
6086 C  CB    . PHE A 806 ? 1.4629 1.5623 1.4978 0.1597  0.2450  0.3119  909  PHE A CB    
6087 C  CG    . PHE A 806 ? 1.6725 1.8130 1.7488 0.1745  0.2692  0.3288  909  PHE A CG    
6088 C  CD1   . PHE A 806 ? 2.0649 2.1699 2.1339 0.1807  0.3069  0.3297  909  PHE A CD1   
6089 C  CD2   . PHE A 806 ? 1.7574 1.9715 1.8802 0.1812  0.2550  0.3440  909  PHE A CD2   
6090 C  CE1   . PHE A 806 ? 2.1842 2.3285 2.2969 0.1950  0.3302  0.3465  909  PHE A CE1   
6091 C  CE2   . PHE A 806 ? 1.7527 2.0076 1.9175 0.1941  0.2755  0.3614  909  PHE A CE2   
6092 C  CZ    . PHE A 806 ? 2.0827 2.3038 2.2451 0.2019  0.3134  0.3631  909  PHE A CZ    
6093 N  N     . ILE A 807 ? 1.7040 1.8523 1.7225 0.1210  0.1726  0.2912  910  ILE A N     
6094 C  CA    . ILE A 807 ? 1.6245 1.8195 1.6584 0.1113  0.1510  0.2905  910  ILE A CA    
6095 C  C     . ILE A 807 ? 1.6660 1.8250 1.6600 0.0892  0.1407  0.2733  910  ILE A C     
6096 O  O     . ILE A 807 ? 1.6955 1.8800 1.6961 0.0814  0.1377  0.2727  910  ILE A O     
6097 C  CB    . ILE A 807 ? 1.3751 1.6051 1.4278 0.1118  0.1239  0.2926  910  ILE A CB    
6098 C  CG1   . ILE A 807 ? 1.3215 1.5871 1.4120 0.1331  0.1341  0.3114  910  ILE A CG1   
6099 C  CG2   . ILE A 807 ? 1.1583 1.4333 1.2240 0.1002  0.1032  0.2906  910  ILE A CG2   
6100 C  CD1   . ILE A 807 ? 1.2918 1.5840 1.3954 0.1334  0.1109  0.3130  910  ILE A CD1   
6101 N  N     . LEU A 808 ? 1.4303 1.5297 1.3821 0.0779  0.1345  0.2600  911  LEU A N     
6102 C  CA    . LEU A 808 ? 1.6379 1.6994 1.5493 0.0562  0.1235  0.2455  911  LEU A CA    
6103 C  C     . LEU A 808 ? 1.6722 1.7022 1.5602 0.0529  0.1517  0.2434  911  LEU A C     
6104 O  O     . LEU A 808 ? 1.7142 1.7460 1.5911 0.0407  0.1499  0.2386  911  LEU A O     
6105 C  CB    . LEU A 808 ? 1.8069 1.8175 1.6829 0.0439  0.1049  0.2342  911  LEU A CB    
6106 C  CG    . LEU A 808 ? 1.6356 1.6643 1.5205 0.0351  0.0706  0.2294  911  LEU A CG    
6107 C  CD1   . LEU A 808 ? 2.0497 2.0909 1.9290 0.0201  0.0567  0.2235  911  LEU A CD1   
6108 C  CD2   . LEU A 808 ? 1.2406 1.3231 1.1703 0.0506  0.0651  0.2392  911  LEU A CD2   
6109 N  N     . GLY A 809 ? 1.7946 1.7936 1.6745 0.0633  0.1798  0.2467  912  GLY A N     
6110 C  CA    . GLY A 809 ? 1.7697 1.7318 1.6244 0.0597  0.2105  0.2435  912  GLY A CA    
6111 C  C     . GLY A 809 ? 1.9285 1.8164 1.7185 0.0377  0.2067  0.2273  912  GLY A C     
6112 O  O     . GLY A 809 ? 2.3625 2.2237 2.1215 0.0232  0.2149  0.2200  912  GLY A O     
6113 N  N     . ILE A 810 ? 2.0108 1.8650 1.7795 0.0338  0.1933  0.2223  913  ILE A N     
6114 C  CA    . ILE A 810 ? 2.2358 2.0193 1.9423 0.0112  0.1865  0.2085  913  ILE A CA    
6115 C  C     . ILE A 810 ? 2.3248 2.0559 1.9960 0.0090  0.2256  0.2044  913  ILE A C     
6116 O  O     . ILE A 810 ? 2.4652 2.2113 2.1642 0.0282  0.2586  0.2130  913  ILE A O     
6117 C  CB    . ILE A 810 ? 2.0352 1.7988 1.7330 0.0084  0.1646  0.2058  913  ILE A CB    
6118 C  CG1   . ILE A 810 ? 1.7243 1.5494 1.4725 0.0197  0.1384  0.2132  913  ILE A CG1   
6119 C  CG2   . ILE A 810 ? 2.3865 2.0945 2.0290 -0.0189 0.1413  0.1936  913  ILE A CG2   
6120 N  N     . GLY A 811 ? 2.3892 2.0571 1.9982 -0.0155 0.2222  0.1918  914  GLY A N     
6121 C  CA    . GLY A 811 ? 2.6290 2.2378 2.1941 -0.0222 0.2592  0.1853  914  GLY A CA    
6122 C  C     . GLY A 811 ? 2.5734 2.1559 2.1387 -0.0095 0.2837  0.1871  914  GLY A C     
6123 O  O     . GLY A 811 ? 2.4766 2.0800 2.0691 0.0019  0.2691  0.1925  914  GLY A O     
6124 N  N     . ASP A 812 ? 2.8518 2.3847 2.3848 -0.0121 0.3242  0.1820  915  ASP A N     
6125 C  CA    . ASP A 812 ? 2.9536 2.4546 2.4841 -0.0003 0.3551  0.1830  915  ASP A CA    
6126 C  C     . ASP A 812 ? 2.9375 2.3966 2.4310 -0.0147 0.3314  0.1753  915  ASP A C     
6127 O  O     . ASP A 812 ? 3.0909 2.4891 2.5187 -0.0428 0.3219  0.1624  915  ASP A O     
6128 C  CB    . ASP A 812 ? 3.2574 2.7018 2.7494 -0.0060 0.4031  0.1757  915  ASP A CB    
6129 C  CG    . ASP A 812 ? 3.2619 2.7486 2.7958 0.0094  0.4298  0.1844  915  ASP A CG    
6130 O  OD1   . ASP A 812 ? 3.1991 2.7605 2.8023 0.0323  0.4214  0.1997  915  ASP A OD1   
6131 O  OD2   . ASP A 812 ? 3.2434 2.6883 2.7404 -0.0026 0.4592  0.1763  915  ASP A OD2   
6132 N  N     . ARG A 813 ? 2.7402 2.2320 2.2755 0.0033  0.3211  0.1841  916  ARG A N     
6133 C  CA    . ARG A 813 ? 2.5989 2.0588 2.1085 -0.0085 0.2978  0.1784  916  ARG A CA    
6134 C  C     . ARG A 813 ? 2.7059 2.0992 2.1769 -0.0116 0.3328  0.1717  916  ARG A C     
6135 O  O     . ARG A 813 ? 2.7517 2.1533 2.2533 0.0114  0.3694  0.1793  916  ARG A O     
6136 C  CB    . ARG A 813 ? 2.5081 2.0292 2.0779 0.0116  0.2746  0.1901  916  ARG A CB    
6137 C  CG    . ARG A 813 ? 2.3941 1.9867 2.0104 0.0192  0.2477  0.1981  916  ARG A CG    
6138 C  CD    . ARG A 813 ? 2.4096 2.0057 2.0147 0.0012  0.2009  0.1928  916  ARG A CD    
6139 N  NE    . ARG A 813 ? 2.3765 1.9273 1.9257 -0.0271 0.1882  0.1815  916  ARG A NE    
6140 C  CZ    . ARG A 813 ? 2.4624 2.0039 1.9932 -0.0466 0.1495  0.1768  916  ARG A CZ    
6141 N  NH1   . ARG A 813 ? 2.4690 2.0411 2.0325 -0.0414 0.1209  0.1810  916  ARG A NH1   
6142 N  NH2   . ARG A 813 ? 2.8188 2.3187 2.2981 -0.0721 0.1397  0.1685  916  ARG A NH2   
6143 N  N     . HIS A 814 ? 2.7892 2.1161 2.1931 -0.0408 0.3216  0.1582  917  HIS A N     
6144 C  CA    . HIS A 814 ? 2.8034 2.0604 2.1618 -0.0493 0.3510  0.1496  917  HIS A CA    
6145 C  C     . HIS A 814 ? 2.6546 1.9005 2.0083 -0.0561 0.3230  0.1485  917  HIS A C     
6146 O  O     . HIS A 814 ? 2.6112 1.9099 2.0080 -0.0478 0.2874  0.1564  917  HIS A O     
6147 C  CB    . HIS A 814 ? 2.8134 1.9960 2.0914 -0.0805 0.3650  0.1343  917  HIS A CB    
6148 C  CG    . HIS A 814 ? 2.7806 1.9665 2.0309 -0.1046 0.3261  0.1304  917  HIS A CG    
6149 N  ND1   . HIS A 814 ? 2.7833 1.9570 2.0083 -0.1270 0.2798  0.1273  917  HIS A ND1   
6150 C  CD2   . HIS A 814 ? 2.9762 2.1757 2.2218 -0.1096 0.3271  0.1299  917  HIS A CD2   
6151 C  CE1   . HIS A 814 ? 2.9996 2.1790 2.2060 -0.1442 0.2539  0.1258  917  HIS A CE1   
6152 N  NE2   . HIS A 814 ? 2.9970 2.1912 2.2138 -0.1344 0.2819  0.1268  917  HIS A NE2   
6153 N  N     . ASN A 815 ? 2.7885 1.9636 2.0888 -0.0723 0.3406  0.1382  918  ASN A N     
6154 C  CA    . ASN A 815 ? 2.6648 1.8257 1.9608 -0.0788 0.3189  0.1371  918  ASN A CA    
6155 C  C     . ASN A 815 ? 2.7419 1.9018 2.0151 -0.1054 0.2652  0.1336  918  ASN A C     
6156 O  O     . ASN A 815 ? 2.7174 1.8923 2.0108 -0.1051 0.2380  0.1371  918  ASN A O     
6157 C  CB    . ASN A 815 ? 2.7573 1.8390 1.9981 -0.0920 0.3531  0.1260  918  ASN A CB    
6158 C  CG    . ASN A 815 ? 2.9465 2.0305 2.2197 -0.0623 0.4062  0.1317  918  ASN A CG    
6159 O  OD1   . ASN A 815 ? 2.8317 1.9642 2.1535 -0.0374 0.4237  0.1419  918  ASN A OD1   
6160 N  ND2   . ASN A 815 ? 3.2697 2.3018 2.5181 -0.0651 0.4318  0.1261  918  ASN A ND2   
6161 N  N     . SER A 816 ? 2.8261 1.9686 2.0596 -0.1281 0.2498  0.1279  919  SER A N     
6162 C  CA    . SER A 816 ? 2.7635 1.9083 1.9807 -0.1520 0.1981  0.1273  919  SER A CA    
6163 C  C     . SER A 816 ? 2.6389 1.8614 1.9192 -0.1356 0.1676  0.1381  919  SER A C     
6164 O  O     . SER A 816 ? 2.4400 1.6750 1.7239 -0.1494 0.1243  0.1402  919  SER A O     
6165 C  CB    . SER A 816 ? 2.9282 2.0115 2.0670 -0.1875 0.1938  0.1168  919  SER A CB    
6166 O  OG    . SER A 816 ? 3.0562 2.1464 2.1920 -0.1809 0.2199  0.1157  919  SER A OG    
6167 N  N     . ASN A 817 ? 2.5313 1.8053 1.8618 -0.1074 0.1894  0.1453  920  ASN A N     
6168 C  CA    . ASN A 817 ? 2.4218 1.7705 1.8136 -0.0911 0.1632  0.1552  920  ASN A CA    
6169 C  C     . ASN A 817 ? 2.4615 1.8562 1.9111 -0.0696 0.1522  0.1639  920  ASN A C     
6170 O  O     . ASN A 817 ? 2.4832 1.9314 1.9763 -0.0623 0.1232  0.1703  920  ASN A O     
6171 C  CB    . ASN A 817 ? 2.4048 1.7919 1.8259 -0.0724 0.1887  0.1600  920  ASN A CB    
6172 C  CG    . ASN A 817 ? 2.6959 2.0517 2.0693 -0.0935 0.1916  0.1526  920  ASN A CG    
6173 O  OD1   . ASN A 817 ? 2.9109 2.2620 2.2802 -0.0862 0.2267  0.1519  920  ASN A OD1   
6174 N  ND2   . ASN A 817 ? 2.9315 2.2659 2.2703 -0.1198 0.1550  0.1482  920  ASN A ND2   
6175 N  N     . ILE A 818 ? 2.3211 1.6944 1.7709 -0.0600 0.1760  0.1641  921  ILE A N     
6176 C  CA    . ILE A 818 ? 2.1234 1.5366 1.6255 -0.0389 0.1706  0.1729  921  ILE A CA    
6177 C  C     . ILE A 818 ? 2.2164 1.5891 1.6915 -0.0573 0.1511  0.1674  921  ILE A C     
6178 O  O     . ILE A 818 ? 2.3497 1.6578 1.7714 -0.0743 0.1672  0.1585  921  ILE A O     
6179 C  CB    . ILE A 818 ? 2.1233 1.5488 1.6545 -0.0109 0.2136  0.1801  921  ILE A CB    
6180 C  CG1   . ILE A 818 ? 1.8687 1.3332 1.4264 0.0052  0.2331  0.1865  921  ILE A CG1   
6181 C  CG2   . ILE A 818 ? 2.2441 1.7124 1.8284 0.0103  0.2063  0.1904  921  ILE A CG2   
6182 C  CD1   . ILE A 818 ? 1.9291 1.4084 1.5201 0.0332  0.2753  0.1963  921  ILE A CD1   
6183 N  N     . MET A 819 ? 2.1015 1.5113 1.6133 -0.0548 0.1174  0.1724  922  MET A N     
6184 C  CA    . MET A 819 ? 2.0557 1.4368 1.5531 -0.0707 0.0959  0.1693  922  MET A CA    
6185 C  C     . MET A 819 ? 2.2419 1.6632 1.7939 -0.0477 0.0968  0.1776  922  MET A C     
6186 O  O     . MET A 819 ? 1.9069 1.3884 1.5116 -0.0246 0.0968  0.1865  922  MET A O     
6187 C  CB    . MET A 819 ? 1.9241 1.3058 1.4120 -0.0943 0.0504  0.1676  922  MET A CB    
6188 C  CG    . MET A 819 ? 1.9727 1.3124 1.4030 -0.1202 0.0448  0.1605  922  MET A CG    
6189 S  SD    . MET A 819 ? 2.1145 1.4461 1.5315 -0.1503 -0.0102 0.1611  922  MET A SD    
6190 C  CE    . MET A 819 ? 2.2180 1.5116 1.6201 -0.1648 -0.0208 0.1592  922  MET A CE    
6191 N  N     . VAL A 820 ? 2.3824 1.7684 1.9191 -0.0557 0.0977  0.1747  923  VAL A N     
6192 C  CA    . VAL A 820 ? 2.1076 1.5235 1.6899 -0.0373 0.0982  0.1819  923  VAL A CA    
6193 C  C     . VAL A 820 ? 2.0995 1.4989 1.6764 -0.0578 0.0647  0.1790  923  VAL A C     
6194 O  O     . VAL A 820 ? 2.3367 1.6862 1.8645 -0.0865 0.0507  0.1712  923  VAL A O     
6195 C  CB    . VAL A 820 ? 2.0572 1.4486 1.6347 -0.0215 0.1404  0.1832  923  VAL A CB    
6196 C  CG1   . VAL A 820 ? 2.2613 1.6776 1.8563 0.0018  0.1730  0.1894  923  VAL A CG1   
6197 C  CG2   . VAL A 820 ? 2.1487 1.4615 1.6610 -0.0465 0.1528  0.1715  923  VAL A CG2   
6198 N  N     . LYS A 821 ? 2.0198 1.4620 1.6478 -0.0438 0.0516  0.1861  924  LYS A N     
6199 C  CA    . LYS A 821 ? 2.0447 1.4786 1.6795 -0.0594 0.0224  0.1853  924  LYS A CA    
6200 C  C     . LYS A 821 ? 2.3962 1.8037 2.0280 -0.0550 0.0422  0.1850  924  LYS A C     
6201 O  O     . LYS A 821 ? 2.2541 1.6618 1.8914 -0.0346 0.0771  0.1879  924  LYS A O     
6202 C  CB    . LYS A 821 ? 1.9145 1.4101 1.6084 -0.0484 -0.0038 0.1924  924  LYS A CB    
6203 C  CG    . LYS A 821 ? 1.9302 1.4531 1.6309 -0.0525 -0.0240 0.1929  924  LYS A CG    
6204 C  CD    . LYS A 821 ? 1.7927 1.3777 1.5535 -0.0373 -0.0405 0.1995  924  LYS A CD    
6205 C  CE    . LYS A 821 ? 2.0443 1.6314 1.8302 -0.0459 -0.0647 0.2009  924  LYS A CE    
6206 N  NZ    . LYS A 821 ? 1.8928 1.5372 1.7362 -0.0313 -0.0766 0.2062  924  LYS A NZ    
6207 N  N     . ASP A 822 ? 2.5137 1.8984 2.1383 -0.0748 0.0193  0.1824  925  ASP A N     
6208 C  CA    . ASP A 822 ? 2.3930 1.7559 2.0194 -0.0717 0.0350  0.1823  925  ASP A CA    
6209 C  C     . ASP A 822 ? 2.3735 1.7907 2.0606 -0.0414 0.0446  0.1921  925  ASP A C     
6210 O  O     . ASP A 822 ? 2.5553 1.9611 2.2473 -0.0289 0.0700  0.1944  925  ASP A O     
6211 C  CB    . ASP A 822 ? 2.3610 1.6939 1.9721 -0.1006 0.0048  0.1785  925  ASP A CB    
6212 C  CG    . ASP A 822 ? 2.4365 1.8176 2.0988 -0.1010 -0.0325 0.1849  925  ASP A CG    
6213 O  OD1   . ASP A 822 ? 2.5899 2.0153 2.2809 -0.0890 -0.0418 0.1890  925  ASP A OD1   
6214 O  OD2   . ASP A 822 ? 2.4655 1.8394 2.1402 -0.1137 -0.0512 0.1857  925  ASP A OD2   
6215 N  N     . ASP A 823 ? 2.4611 1.9355 2.1928 -0.0303 0.0252  0.1981  926  ASP A N     
6216 C  CA    . ASP A 823 ? 2.2520 1.7794 2.0368 -0.0026 0.0351  0.2075  926  ASP A CA    
6217 C  C     . ASP A 823 ? 2.1461 1.6864 1.9332 0.0219  0.0704  0.2131  926  ASP A C     
6218 O  O     . ASP A 823 ? 2.0207 1.5903 1.8413 0.0441  0.0863  0.2220  926  ASP A O     
6219 C  CB    . ASP A 823 ? 2.2009 1.7816 2.0266 0.0002  0.0070  0.2109  926  ASP A CB    
6220 C  CG    . ASP A 823 ? 2.3646 1.9954 2.2422 0.0225  0.0118  0.2193  926  ASP A CG    
6221 O  OD1   . ASP A 823 ? 2.6132 2.2358 2.4972 0.0328  0.0307  0.2230  926  ASP A OD1   
6222 O  OD2   . ASP A 823 ? 2.2626 1.9393 2.1727 0.0288  -0.0028 0.2222  926  ASP A OD2   
6223 N  N     . GLY A 824 ? 2.0999 1.6194 1.8535 0.0179  0.0831  0.2092  927  GLY A N     
6224 C  CA    . GLY A 824 ? 1.9116 1.4429 1.6700 0.0402  0.1168  0.2154  927  GLY A CA    
6225 C  C     . GLY A 824 ? 1.9782 1.5584 1.7586 0.0511  0.1121  0.2202  927  GLY A C     
6226 O  O     . GLY A 824 ? 1.8065 1.4089 1.6029 0.0722  0.1376  0.2285  927  GLY A O     
6227 N  N     . GLN A 825 ? 2.0738 1.6715 1.8571 0.0372  0.0806  0.2161  928  GLN A N     
6228 C  CA    . GLN A 825 ? 1.6960 1.3401 1.5001 0.0455  0.0742  0.2198  928  GLN A CA    
6229 C  C     . GLN A 825 ? 1.7697 1.3847 1.5338 0.0352  0.0843  0.2137  928  GLN A C     
6230 O  O     . GLN A 825 ? 1.7519 1.3184 1.4724 0.0114  0.0743  0.2042  928  GLN A O     
6231 C  CB    . GLN A 825 ? 1.8641 1.5391 1.6920 0.0360  0.0379  0.2182  928  GLN A CB    
6232 C  CG    . GLN A 825 ? 1.9985 1.7202 1.8472 0.0425  0.0303  0.2209  928  GLN A CG    
6233 C  CD    . GLN A 825 ? 1.9316 1.6796 1.8044 0.0331  -0.0028 0.2189  928  GLN A CD    
6234 O  OE1   . GLN A 825 ? 1.7004 1.4344 1.5784 0.0226  -0.0207 0.2164  928  GLN A OE1   
6235 N  NE2   . GLN A 825 ? 1.8795 1.6656 1.7690 0.0367  -0.0102 0.2201  928  GLN A NE2   
6236 N  N     . LEU A 826 ? 1.7695 1.4143 1.5482 0.0520  0.1037  0.2199  929  LEU A N     
6237 C  CA    . LEU A 826 ? 1.7236 1.3463 1.4698 0.0450  0.1173  0.2153  929  LEU A CA    
6238 C  C     . LEU A 826 ? 1.9128 1.5720 1.6706 0.0395  0.0942  0.2145  929  LEU A C     
6239 O  O     . LEU A 826 ? 1.9461 1.6618 1.7474 0.0527  0.0838  0.2218  929  LEU A O     
6240 C  CB    . LEU A 826 ? 1.4674 1.0975 1.2246 0.0673  0.1569  0.2235  929  LEU A CB    
6241 C  CG    . LEU A 826 ? 1.6517 1.2538 1.3768 0.0628  0.1807  0.2192  929  LEU A CG    
6242 C  CD1   . LEU A 826 ? 1.7853 1.3620 1.5074 0.0785  0.2237  0.2239  929  LEU A CD1   
6243 C  CD2   . LEU A 826 ? 2.0523 1.7068 1.8043 0.0710  0.1761  0.2249  929  LEU A CD2   
6244 N  N     . PHE A 827 ? 1.8862 1.5109 1.6027 0.0188  0.0868  0.2056  930  PHE A N     
6245 C  CA    . PHE A 827 ? 1.9082 1.5608 1.6310 0.0118  0.0663  0.2044  930  PHE A CA    
6246 C  C     . PHE A 827 ? 1.8528 1.4622 1.5254 -0.0052 0.0755  0.1967  930  PHE A C     
6247 O  O     . PHE A 827 ? 2.0321 1.5827 1.6579 -0.0202 0.0851  0.1897  930  PHE A O     
6248 C  CB    . PHE A 827 ? 1.9087 1.5718 1.6435 -0.0019 0.0270  0.2021  930  PHE A CB    
6249 C  CG    . PHE A 827 ? 1.8226 1.4293 1.5157 -0.0273 0.0099  0.1946  930  PHE A CG    
6250 C  CD1   . PHE A 827 ? 2.0768 1.6587 1.7663 -0.0293 0.0112  0.1941  930  PHE A CD1   
6251 C  CD2   . PHE A 827 ? 1.7833 1.3625 1.4408 -0.0504 -0.0088 0.1890  930  PHE A CD2   
6252 C  CE1   . PHE A 827 ? 2.0844 1.6160 1.7357 -0.0547 -0.0065 0.1881  930  PHE A CE1   
6253 C  CE2   . PHE A 827 ? 1.7940 1.3227 1.4124 -0.0757 -0.0273 0.1840  930  PHE A CE2   
6254 C  CZ    . PHE A 827 ? 1.8747 1.3802 1.4903 -0.0783 -0.0266 0.1835  930  PHE A CZ    
6255 N  N     . HIS A 828 ? 1.9209 1.5586 1.6016 -0.0039 0.0732  0.1978  931  HIS A N     
6256 C  CA    . HIS A 828 ? 1.8474 1.4499 1.4836 -0.0193 0.0824  0.1911  931  HIS A CA    
6257 C  C     . HIS A 828 ? 2.0945 1.6852 1.7094 -0.0432 0.0468  0.1857  931  HIS A C     
6258 O  O     . HIS A 828 ? 1.9603 1.5832 1.6062 -0.0434 0.0175  0.1885  931  HIS A O     
6259 C  CB    . HIS A 828 ? 1.8732 1.5133 1.5322 -0.0027 0.1058  0.1966  931  HIS A CB    
6260 C  CG    . HIS A 828 ? 2.0548 1.7024 1.7332 0.0200  0.1432  0.2037  931  HIS A CG    
6261 N  ND1   . HIS A 828 ? 1.7573 1.4381 1.4606 0.0366  0.1678  0.2111  931  HIS A ND1   
6262 C  CD2   . HIS A 828 ? 2.1031 1.7295 1.7820 0.0291  0.1604  0.2058  931  HIS A CD2   
6263 C  CE1   . HIS A 828 ? 2.0372 1.7175 1.7574 0.0557  0.1983  0.2185  931  HIS A CE1   
6264 N  NE2   . HIS A 828 ? 1.8281 1.4745 1.5328 0.0517  0.1950  0.2151  931  HIS A NE2   
6265 N  N     . ILE A 829 ? 2.0191 1.5612 1.5801 -0.0638 0.0508  0.1785  932  ILE A N     
6266 C  CA    . ILE A 829 ? 2.0552 1.5770 1.5880 -0.0890 0.0183  0.1746  932  ILE A CA    
6267 C  C     . ILE A 829 ? 2.3301 1.8324 1.8269 -0.0993 0.0318  0.1704  932  ILE A C     
6268 O  O     . ILE A 829 ? 2.2684 1.7634 1.7561 -0.0896 0.0677  0.1691  932  ILE A O     
6269 C  CB    . ILE A 829 ? 2.1643 1.6303 1.6548 -0.1129 -0.0002 0.1701  932  ILE A CB    
6270 C  CG1   . ILE A 829 ? 2.0846 1.4917 1.5232 -0.1203 0.0321  0.1633  932  ILE A CG1   
6271 C  CG2   . ILE A 829 ? 2.0596 1.5494 1.5908 -0.1051 -0.0198 0.1747  932  ILE A CG2   
6272 C  CD1   . ILE A 829 ? 2.4148 1.7644 1.7844 -0.1482 0.0337  0.1556  932  ILE A CD1   
6273 N  N     . ASP A 830 ? 2.3598 1.8535 1.8379 -0.1191 0.0031  0.1689  933  ASP A N     
6274 C  CA    . ASP A 830 ? 2.3367 1.8059 1.7741 -0.1339 0.0104  0.1647  933  ASP A CA    
6275 C  C     . ASP A 830 ? 2.4626 1.9772 1.9332 -0.1134 0.0362  0.1673  933  ASP A C     
6276 O  O     . ASP A 830 ? 2.3564 1.8555 1.8104 -0.1077 0.0720  0.1649  933  ASP A O     
6277 C  CB    . ASP A 830 ? 2.3299 1.7260 1.6968 -0.1539 0.0300  0.1567  933  ASP A CB    
6278 C  CG    . ASP A 830 ? 2.5549 1.9177 1.8715 -0.1746 0.0328  0.1519  933  ASP A CG    
6279 O  OD1   . ASP A 830 ? 2.4496 1.8426 1.7841 -0.1763 0.0135  0.1553  933  ASP A OD1   
6280 O  OD2   . ASP A 830 ? 2.9426 2.2469 2.2002 -0.1901 0.0556  0.1444  933  ASP A OD2   
6281 N  N     . PHE A 831 ? 2.4925 2.0638 2.0118 -0.1031 0.0173  0.1726  934  PHE A N     
6282 C  CA    . PHE A 831 ? 2.2860 1.9065 1.8401 -0.0864 0.0351  0.1761  934  PHE A CA    
6283 C  C     . PHE A 831 ? 2.4722 2.0810 1.9988 -0.1035 0.0282  0.1727  934  PHE A C     
6284 O  O     . PHE A 831 ? 2.5898 2.2354 2.1430 -0.1034 0.0092  0.1750  934  PHE A O     
6285 C  CB    . PHE A 831 ? 2.0972 1.7837 1.7151 -0.0676 0.0208  0.1829  934  PHE A CB    
6286 C  CG    . PHE A 831 ? 1.9786 1.6772 1.6235 -0.0513 0.0265  0.1870  934  PHE A CG    
6287 C  CD1   . PHE A 831 ? 1.9498 1.6661 1.6145 -0.0307 0.0587  0.1919  934  PHE A CD1   
6288 C  CD2   . PHE A 831 ? 1.9398 1.6328 1.5926 -0.0564 0.0000  0.1870  934  PHE A CD2   
6289 C  CE1   . PHE A 831 ? 2.0420 1.7683 1.7307 -0.0158 0.0642  0.1966  934  PHE A CE1   
6290 C  CE2   . PHE A 831 ? 1.8752 1.5785 1.5521 -0.0421 0.0060  0.1906  934  PHE A CE2   
6291 C  CZ    . PHE A 831 ? 1.8768 1.5960 1.5701 -0.0219 0.0380  0.1953  934  PHE A CZ    
6292 N  N     . GLY A 832 ? 2.5053 2.0586 1.9751 -0.1195 0.0455  0.1667  935  GLY A N     
6293 C  CA    . GLY A 832 ? 2.4506 1.9840 1.8859 -0.1379 0.0417  0.1632  935  GLY A CA    
6294 C  C     . GLY A 832 ? 2.4088 1.9807 1.8697 -0.1248 0.0668  0.1650  935  GLY A C     
6295 O  O     . GLY A 832 ? 2.4115 1.9990 1.8746 -0.1327 0.0546  0.1650  935  GLY A O     
6296 N  N     . HIS A 833 ? 2.5978 2.1856 2.0804 -0.1050 0.1019  0.1673  936  HIS A N     
6297 C  CA    . HIS A 833 ? 2.6237 2.2498 2.1351 -0.0915 0.1285  0.1708  936  HIS A CA    
6298 C  C     . HIS A 833 ? 2.5519 2.2444 2.1316 -0.0635 0.1336  0.1806  936  HIS A C     
6299 O  O     . HIS A 833 ? 2.4297 2.1196 2.0218 -0.0488 0.1517  0.1841  936  HIS A O     
6300 C  CB    . HIS A 833 ? 2.6272 2.2090 2.1016 -0.0945 0.1700  0.1664  936  HIS A CB    
6301 C  CG    . HIS A 833 ? 2.7290 2.2462 2.1326 -0.1237 0.1678  0.1569  936  HIS A CG    
6302 N  ND1   . HIS A 833 ? 2.8133 2.2750 2.1648 -0.1456 0.1459  0.1511  936  HIS A ND1   
6303 C  CD2   . HIS A 833 ? 2.9306 2.4296 2.3058 -0.1358 0.1842  0.1528  936  HIS A CD2   
6304 C  CE1   . HIS A 833 ? 2.9870 2.3985 2.2789 -0.1705 0.1479  0.1444  936  HIS A CE1   
6305 N  NE2   . HIS A 833 ? 3.1524 2.5842 2.4565 -0.1649 0.1720  0.1448  936  HIS A NE2   
6306 N  N     . PHE A 834 ? 2.5291 2.2792 2.1508 -0.0574 0.1180  0.1854  937  PHE A N     
6307 C  CA    . PHE A 834 ? 2.2638 2.0804 1.9478 -0.0338 0.1215  0.1955  937  PHE A CA    
6308 C  C     . PHE A 834 ? 2.2787 2.1422 1.9914 -0.0297 0.1305  0.1998  937  PHE A C     
6309 O  O     . PHE A 834 ? 2.6874 2.5387 2.3771 -0.0461 0.1234  0.1942  937  PHE A O     
6310 C  CB    . PHE A 834 ? 2.4827 2.3270 2.1931 -0.0315 0.0876  0.1970  937  PHE A CB    
6311 C  CG    . PHE A 834 ? 2.4677 2.3276 2.1801 -0.0453 0.0584  0.1934  937  PHE A CG    
6312 C  CD1   . PHE A 834 ? 2.4235 2.2355 2.0912 -0.0678 0.0405  0.1858  937  PHE A CD1   
6313 C  CD2   . PHE A 834 ? 2.2524 2.1738 2.0108 -0.0368 0.0487  0.1981  937  PHE A CD2   
6314 C  CE1   . PHE A 834 ? 2.1150 1.9403 1.7873 -0.0795 0.0148  0.1836  937  PHE A CE1   
6315 C  CE2   . PHE A 834 ? 2.0114 1.9442 1.7717 -0.0496 0.0243  0.1941  937  PHE A CE2   
6316 C  CZ    . PHE A 834 ? 1.8294 1.7143 1.5484 -0.0700 0.0079  0.1872  937  PHE A CZ    
6317 N  N     . LEU A 835 ? 2.1832 2.1005 1.9464 -0.0084 0.1459  0.2108  938  LEU A N     
6318 C  CA    . LEU A 835 ? 2.2466 2.2124 2.0424 -0.0028 0.1586  0.2174  938  LEU A CA    
6319 C  C     . LEU A 835 ? 2.6913 2.6228 2.4584 -0.0100 0.1887  0.2138  938  LEU A C     
6320 O  O     . LEU A 835 ? 2.8297 2.7885 2.6106 -0.0133 0.1952  0.2157  938  LEU A O     
6321 C  CB    . LEU A 835 ? 2.1726 2.1739 1.9815 -0.0137 0.1291  0.2148  938  LEU A CB    
6322 C  CG    . LEU A 835 ? 2.0683 2.1324 1.9258 -0.0031 0.1096  0.2221  938  LEU A CG    
6323 C  CD1   . LEU A 835 ? 2.3923 2.4454 2.2514 0.0033  0.0948  0.2220  938  LEU A CD1   
6324 C  CD2   . LEU A 835 ? 1.8779 1.9639 1.7381 -0.0179 0.0851  0.2166  938  LEU A CD2   
6325 N  N     . ASP A 836 ? 2.6856 2.5562 2.4119 -0.0135 0.2085  0.2083  939  ASP A N     
6326 C  CA    . ASP A 836 ? 2.6883 2.5157 2.3781 -0.0234 0.2383  0.2026  939  ASP A CA    
6327 C  C     . ASP A 836 ? 2.8682 2.7214 2.5970 -0.0025 0.2788  0.2132  939  ASP A C     
6328 O  O     . ASP A 836 ? 2.6911 2.5770 2.4625 0.0190  0.2864  0.2244  939  ASP A O     
6329 C  CB    . ASP A 836 ? 2.7020 2.4483 2.3255 -0.0394 0.2423  0.1911  939  ASP A CB    
6330 C  CG    . ASP A 836 ? 2.9934 2.6873 2.5624 -0.0603 0.2594  0.1813  939  ASP A CG    
6331 O  OD1   . ASP A 836 ? 3.0063 2.7206 2.5932 -0.0559 0.2845  0.1846  939  ASP A OD1   
6332 O  OD2   . ASP A 836 ? 3.0569 2.6891 2.5649 -0.0821 0.2473  0.1711  939  ASP A OD2   
6333 N  N     . HIS A 837 ? 3.1577 2.9955 2.8726 -0.0093 0.3055  0.2107  940  HIS A N     
6334 C  CA    . HIS A 837 ? 3.1585 3.0199 2.9131 0.0095  0.3464  0.2214  940  HIS A CA    
6335 C  C     . HIS A 837 ? 3.1732 2.9762 2.8833 -0.0027 0.3829  0.2123  940  HIS A C     
6336 O  O     . HIS A 837 ? 3.0499 2.8558 2.7846 0.0116  0.4237  0.2193  940  HIS A O     
6337 C  CB    . HIS A 837 ? 3.1086 3.0521 2.9272 0.0200  0.3391  0.2345  940  HIS A CB    
6338 C  CG    . HIS A 837 ? 3.1672 3.1173 2.9685 -0.0003 0.3221  0.2271  940  HIS A CG    
6339 N  ND1   . HIS A 837 ? 2.9506 2.9199 2.7472 -0.0120 0.2804  0.2227  940  HIS A ND1   
6340 C  CD2   . HIS A 837 ? 3.0599 2.9987 2.8480 -0.0111 0.3427  0.2234  940  HIS A CD2   
6341 C  CE1   . HIS A 837 ? 3.0205 2.9895 2.8015 -0.0289 0.2755  0.2169  940  HIS A CE1   
6342 N  NE2   . HIS A 837 ? 2.9976 2.9486 2.7724 -0.0291 0.3122  0.2171  940  HIS A NE2   
6343 N  N     . LYS A 838 ? 3.0474 2.7968 2.6924 -0.0295 0.3691  0.1975  941  LYS A N     
6344 C  CA    . LYS A 838 ? 2.9195 2.6064 2.5107 -0.0461 0.4008  0.1869  941  LYS A CA    
6345 C  C     . LYS A 838 ? 2.7777 2.5003 2.4065 -0.0391 0.4310  0.1936  941  LYS A C     
6346 O  O     . LYS A 838 ? 2.5781 2.2768 2.2069 -0.0324 0.4761  0.1943  941  LYS A O     
6347 C  CB    . LYS A 838 ? 2.7262 2.3502 2.2831 -0.0435 0.4336  0.1817  941  LYS A CB    
6348 N  N     . VAL A 849 ? 2.0802 1.9830 2.0271 0.1637  0.3840  0.2957  952  VAL A N     
6349 C  CA    . VAL A 849 ? 2.3633 2.1988 2.2616 0.1508  0.4141  0.2815  952  VAL A CA    
6350 C  C     . VAL A 849 ? 2.4515 2.2154 2.2773 0.1250  0.3985  0.2596  952  VAL A C     
6351 O  O     . VAL A 849 ? 2.4576 2.1557 2.2437 0.1198  0.4261  0.2507  952  VAL A O     
6352 C  CB    . VAL A 849 ? 2.3318 2.1878 2.2349 0.1431  0.4200  0.2805  952  VAL A CB    
6353 C  CG1   . VAL A 849 ? 2.2314 2.0175 2.0867 0.1315  0.4576  0.2674  952  VAL A CG1   
6354 C  CG2   . VAL A 849 ? 2.1774 2.1100 2.1553 0.1666  0.4303  0.3036  952  VAL A CG2   
6355 N  N     . PRO A 850 ? 2.4047 2.1793 2.2130 0.1079  0.3553  0.2514  953  PRO A N     
6356 C  CA    . PRO A 850 ? 2.4211 2.1302 2.1651 0.0836  0.3387  0.2334  953  PRO A CA    
6357 C  C     . PRO A 850 ? 2.3321 2.0150 2.0709 0.0897  0.3397  0.2337  953  PRO A C     
6358 O  O     . PRO A 850 ? 2.3729 1.9867 2.0586 0.0747  0.3501  0.2212  953  PRO A O     
6359 C  CB    . PRO A 850 ? 2.2346 1.9736 1.9768 0.0685  0.2927  0.2288  953  PRO A CB    
6360 C  CG    . PRO A 850 ? 1.8497 1.6696 1.6578 0.0883  0.2822  0.2447  953  PRO A CG    
6361 C  CD    . PRO A 850 ? 2.0675 1.9085 1.9095 0.1073  0.3209  0.2570  953  PRO A CD    
6362 N  N     . PHE A 851 ? 2.2895 2.0244 2.0799 0.1098  0.3291  0.2477  954  PHE A N     
6363 C  CA    . PHE A 851 ? 2.1639 1.8791 1.9544 0.1170  0.3297  0.2494  954  PHE A CA    
6364 C  C     . PHE A 851 ? 2.3818 2.0995 2.2043 0.1423  0.3721  0.2631  954  PHE A C     
6365 O  O     . PHE A 851 ? 2.5240 2.3011 2.4045 0.1654  0.3739  0.2816  954  PHE A O     
6366 C  CB    . PHE A 851 ? 1.7796 1.5461 1.6035 0.1219  0.2921  0.2558  954  PHE A CB    
6367 N  N     . VAL A 852 ? 2.4171 2.0682 2.2007 0.1371  0.4067  0.2544  955  VAL A N     
6368 C  CA    . VAL A 852 ? 2.4058 2.0483 2.2161 0.1601  0.4519  0.2661  955  VAL A CA    
6369 C  C     . VAL A 852 ? 2.4030 2.0222 2.2119 0.1672  0.4536  0.2679  955  VAL A C     
6370 O  O     . VAL A 852 ? 2.3681 1.9345 2.1257 0.1465  0.4403  0.2521  955  VAL A O     
6371 C  CB    . VAL A 852 ? 2.3573 1.9360 2.1256 0.1505  0.4934  0.2548  955  VAL A CB    
6372 C  CG1   . VAL A 852 ? 2.2892 1.8564 2.0886 0.1755  0.5431  0.2672  955  VAL A CG1   
6373 C  CG2   . VAL A 852 ? 2.4055 2.0078 2.1758 0.1431  0.4920  0.2531  955  VAL A CG2   
6374 N  N     . LEU A 853 ? 2.3785 2.0375 2.2442 0.1957  0.4691  0.2883  956  LEU A N     
6375 C  CA    . LEU A 853 ? 2.4539 2.0926 2.3232 0.2052  0.4750  0.2923  956  LEU A CA    
6376 C  C     . LEU A 853 ? 2.5047 2.0616 2.3317 0.2004  0.5175  0.2815  956  LEU A C     
6377 O  O     . LEU A 853 ? 2.5146 2.0665 2.3697 0.2214  0.5595  0.2934  956  LEU A O     
6378 C  CB    . LEU A 853 ? 2.6524 2.3564 2.5943 0.2370  0.4810  0.3192  956  LEU A CB    
6379 C  CG    . LEU A 853 ? 2.5865 2.3562 2.5620 0.2412  0.4379  0.3290  956  LEU A CG    
6380 C  CD1   . LEU A 853 ? 2.5179 2.3303 2.4944 0.2275  0.4050  0.3241  956  LEU A CD1   
6381 C  CD2   . LEU A 853 ? 2.2730 2.0990 2.3146 0.2717  0.4492  0.3569  956  LEU A CD2   
6382 N  N     . THR A 854 ? 2.5193 2.0112 2.2792 0.1723  0.5074  0.2596  957  THR A N     
6383 C  CA    . THR A 854 ? 2.5162 1.9244 2.2265 0.1627  0.5460  0.2467  957  THR A CA    
6384 C  C     . THR A 854 ? 2.6612 2.0549 2.3901 0.1794  0.5636  0.2552  957  THR A C     
6385 O  O     . THR A 854 ? 2.5609 2.0061 2.3350 0.1954  0.5418  0.2696  957  THR A O     
6386 C  CB    . THR A 854 ? 2.4396 1.7845 2.0708 0.1248  0.5255  0.2221  957  THR A CB    
6387 O  OG1   . THR A 854 ? 2.2805 1.6343 1.9068 0.1152  0.4844  0.2195  957  THR A OG1   
6388 C  CG2   . THR A 854 ? 2.4925 1.8519 2.1054 0.1082  0.5067  0.2150  957  THR A CG2   
6389 N  N     . GLN A 855 ? 2.9366 2.2560 2.6275 0.1745  0.6051  0.2455  958  GLN A N     
6390 C  CA    . GLN A 855 ? 2.8182 2.1154 2.5231 0.1896  0.6270  0.2525  958  GLN A CA    
6391 C  C     . GLN A 855 ? 2.8677 2.1547 2.5489 0.1734  0.5887  0.2445  958  GLN A C     
6392 O  O     . GLN A 855 ? 2.7585 2.0677 2.4756 0.1910  0.5862  0.2573  958  GLN A O     
6393 C  CB    . GLN A 855 ? 2.7160 1.9293 2.3795 0.1846  0.6818  0.2413  958  GLN A CB    
6394 N  N     . ASP A 856 ? 2.8893 2.1438 2.5120 0.1399  0.5583  0.2246  959  ASP A N     
6395 C  CA    . ASP A 856 ? 2.6767 1.9201 2.2781 0.1228  0.5217  0.2170  959  ASP A CA    
6396 C  C     . ASP A 856 ? 2.5289 1.8538 2.1886 0.1383  0.4820  0.2323  959  ASP A C     
6397 O  O     . ASP A 856 ? 2.4020 1.7293 2.0671 0.1365  0.4623  0.2332  959  ASP A O     
6398 C  CB    . ASP A 856 ? 2.5813 1.7778 2.1125 0.0835  0.4954  0.1953  959  ASP A CB    
6399 C  CG    . ASP A 856 ? 2.6957 1.8031 2.1584 0.0628  0.5329  0.1780  959  ASP A CG    
6400 O  OD1   . ASP A 856 ? 2.7380 1.8339 2.1959 0.0681  0.5658  0.1774  959  ASP A OD1   
6401 O  OD2   . ASP A 856 ? 3.0029 2.0509 2.4158 0.0401  0.5301  0.1649  959  ASP A OD2   
6402 N  N     . PHE A 857 ? 2.5336 1.9243 2.2360 0.1524  0.4709  0.2441  960  PHE A N     
6403 C  CA    . PHE A 857 ? 2.3794 1.8461 2.1335 0.1652  0.4347  0.2577  960  PHE A CA    
6404 C  C     . PHE A 857 ? 2.4554 1.9546 2.2634 0.1958  0.4523  0.2783  960  PHE A C     
6405 O  O     . PHE A 857 ? 2.5651 2.0867 2.3914 0.1992  0.4298  0.2834  960  PHE A O     
6406 C  CB    . PHE A 857 ? 2.4422 1.9665 2.2222 0.1688  0.4188  0.2635  960  PHE A CB    
6407 C  CG    . PHE A 857 ? 2.7410 2.2397 2.4719 0.1392  0.3969  0.2452  960  PHE A CG    
6408 C  CD1   . PHE A 857 ? 2.6835 2.1353 2.3643 0.1117  0.3733  0.2286  960  PHE A CD1   
6409 C  CD2   . PHE A 857 ? 2.7490 2.2709 2.4846 0.1384  0.3991  0.2458  960  PHE A CD2   
6410 C  CE1   . PHE A 857 ? 2.4828 1.9113 2.1191 0.0842  0.3516  0.2142  960  PHE A CE1   
6411 C  CE2   . PHE A 857 ? 2.6404 2.1374 2.3299 0.1111  0.3790  0.2300  960  PHE A CE2   
6412 C  CZ    . PHE A 857 ? 2.5020 1.9522 2.1416 0.0842  0.3548  0.2148  960  PHE A CZ    
6413 N  N     . LEU A 858 ? 2.6519 2.1541 2.4873 0.2183  0.4931  0.2914  961  LEU A N     
6414 C  CA    . LEU A 858 ? 2.5300 2.0649 2.4198 0.2486  0.5102  0.3142  961  LEU A CA    
6415 C  C     . LEU A 858 ? 2.4060 1.8861 2.2740 0.2468  0.5256  0.3095  961  LEU A C     
6416 O  O     . LEU A 858 ? 2.5480 2.0560 2.4541 0.2657  0.5250  0.3258  961  LEU A O     
6417 C  CB    . LEU A 858 ? 2.5112 2.0615 2.4389 0.2730  0.5510  0.3308  961  LEU A CB    
6418 C  CG    . LEU A 858 ? 2.5100 2.1351 2.4828 0.2839  0.5369  0.3451  961  LEU A CG    
6419 C  CD1   . LEU A 858 ? 2.3328 2.0276 2.3382 0.2872  0.4919  0.3555  961  LEU A CD1   
6420 C  CD2   . LEU A 858 ? 2.3458 1.9527 2.2805 0.2621  0.5323  0.3272  961  LEU A CD2   
6421 N  N     . ILE A 859 ? 2.4745 1.8761 2.2800 0.2232  0.5395  0.2876  962  ILE A N     
6422 C  CA    . ILE A 859 ? 2.5142 1.8617 2.2930 0.2161  0.5491  0.2804  962  ILE A CA    
6423 C  C     . ILE A 859 ? 2.4404 1.8152 2.2233 0.2061  0.5032  0.2786  962  ILE A C     
6424 O  O     . ILE A 859 ? 2.4527 1.8173 2.2447 0.2122  0.5060  0.2833  962  ILE A O     
6425 C  CB    . ILE A 859 ? 2.4981 1.7552 2.2028 0.1879  0.5703  0.2559  962  ILE A CB    
6426 C  CG1   . ILE A 859 ? 2.2718 1.4955 1.9764 0.2013  0.6250  0.2588  962  ILE A CG1   
6427 C  CG2   . ILE A 859 ? 2.5932 1.7946 2.2633 0.1734  0.5711  0.2455  962  ILE A CG2   
6428 C  CD1   . ILE A 859 ? 2.4886 1.7132 2.2377 0.2325  0.6638  0.2776  962  ILE A CD1   
6429 N  N     . VAL A 860 ? 2.5000 1.9104 2.2793 0.1913  0.4620  0.2725  963  VAL A N     
6430 C  CA    . VAL A 860 ? 2.3222 1.7621 2.1105 0.1823  0.4190  0.2712  963  VAL A CA    
6431 C  C     . VAL A 860 ? 2.2020 1.7247 2.0541 0.2068  0.4030  0.2922  963  VAL A C     
6432 O  O     . VAL A 860 ? 1.9013 1.4456 1.7755 0.2127  0.3879  0.2991  963  VAL A O     
6433 C  CB    . VAL A 860 ? 2.1335 1.5614 1.8817 0.1512  0.3831  0.2528  963  VAL A CB    
6434 C  CG1   . VAL A 860 ? 2.2094 1.6647 1.9699 0.1419  0.3412  0.2514  963  VAL A CG1   
6435 C  CG2   . VAL A 860 ? 2.1057 1.4504 1.7863 0.1246  0.3982  0.2331  963  VAL A CG2   
6436 N  N     . ILE A 861 ? 2.3270 1.8962 2.2079 0.2198  0.4061  0.3027  964  ILE A N     
6437 C  CA    . ILE A 861 ? 2.0927 1.7414 2.0296 0.2393  0.3882  0.3222  964  ILE A CA    
6438 C  C     . ILE A 861 ? 2.1733 1.8379 2.1504 0.2668  0.4121  0.3438  964  ILE A C     
6439 O  O     . ILE A 861 ? 2.1970 1.8947 2.1992 0.2740  0.3944  0.3535  964  ILE A O     
6440 C  CB    . ILE A 861 ? 2.2169 1.9091 2.1732 0.2445  0.3869  0.3281  964  ILE A CB    
6441 C  CG1   . ILE A 861 ? 1.9932 1.6813 1.9162 0.2179  0.3552  0.3092  964  ILE A CG1   
6442 C  CG2   . ILE A 861 ? 1.9960 1.7673 2.0114 0.2669  0.3764  0.3517  964  ILE A CG2   
6443 C  CD1   . ILE A 861 ? 1.8285 1.5570 1.7674 0.2205  0.3526  0.3133  964  ILE A CD1   
6444 N  N     . SER A 862 ? 2.3758 2.0160 2.3600 0.2825  0.4537  0.3522  965  SER A N     
6445 C  CA    . SER A 862 ? 1.8847 1.5384 1.9101 0.3104  0.4796  0.3754  965  SER A CA    
6446 C  C     . SER A 862 ? 1.8610 1.4565 1.8607 0.3055  0.4923  0.3678  965  SER A C     
6447 O  O     . SER A 862 ? 2.0593 1.6069 2.0521 0.3145  0.5318  0.3699  965  SER A O     
6448 C  CB    . SER A 862 ? 2.1460 1.7967 2.1942 0.3300  0.5206  0.3884  965  SER A CB    
6449 O  OG    . SER A 862 ? 2.3584 2.0217 2.4497 0.3579  0.5461  0.4130  965  SER A OG    
6450 N  N     . LYS A 863 ? 2.4031 2.0034 2.3899 0.2906  0.4587  0.3589  966  LYS A N     
6451 C  CA    . LYS A 863 ? 2.4200 1.9710 2.3832 0.2824  0.4636  0.3508  966  LYS A CA    
6452 C  C     . LYS A 863 ? 2.4747 1.9418 2.3828 0.2641  0.4891  0.3301  966  LYS A C     
6453 O  O     . LYS A 863 ? 2.6596 2.1000 2.5250 0.2379  0.4725  0.3096  966  LYS A O     
6454 C  CB    . LYS A 863 ? 2.8292 2.3956 2.8332 0.3099  0.4853  0.3744  966  LYS A CB    
6455 N  N     . GLY A 864 ? 2.4177 1.8414 2.3249 0.2768  0.5298  0.3358  967  GLY A N     
6456 C  CA    . GLY A 864 ? 2.4478 1.7878 2.3009 0.2595  0.5594  0.3165  967  GLY A CA    
6457 C  C     . GLY A 864 ? 2.4545 1.7697 2.3224 0.2816  0.6120  0.3276  967  GLY A C     
6458 O  O     . GLY A 864 ? 2.8175 2.0595 2.6488 0.2739  0.6467  0.3162  967  GLY A O     
6459 N  N     . ALA A 865 ? 2.3360 1.7116 2.2586 0.3084  0.6190  0.3501  968  ALA A N     
6460 C  CA    . ALA A 865 ? 2.4538 1.8158 2.4030 0.3330  0.6687  0.3649  968  ALA A CA    
6461 C  C     . ALA A 865 ? 2.8425 2.1479 2.7457 0.3162  0.6948  0.3448  968  ALA A C     
6462 O  O     . ALA A 865 ? 2.8899 2.2224 2.7902 0.3086  0.6797  0.3401  968  ALA A O     
6463 C  CB    . ALA A 865 ? 2.2245 1.6716 2.2449 0.3626  0.6632  0.3948  968  ALA A CB    
6464 N  N     . GLN A 866 ? 3.1558 2.3799 3.0206 0.3094  0.7353  0.3324  969  GLN A N     
6465 C  CA    . GLN A 866 ? 3.1289 2.2890 2.9421 0.2908  0.7644  0.3116  969  GLN A CA    
6466 C  C     . GLN A 866 ? 3.2031 2.3799 3.0566 0.3156  0.8043  0.3268  969  GLN A C     
6467 O  O     . GLN A 866 ? 3.2279 2.3592 3.0430 0.3015  0.8288  0.3107  969  GLN A O     
6468 C  CB    . GLN A 866 ? 3.1222 2.1865 2.8781 0.2735  0.7967  0.2927  969  GLN A CB    
6469 C  CG    . GLN A 866 ? 3.1006 2.1454 2.8930 0.3021  0.8420  0.3103  969  GLN A CG    
6470 C  CD    . GLN A 866 ? 3.1009 2.1786 2.9241 0.3130  0.8172  0.3244  969  GLN A CD    
6471 O  OE1   . GLN A 866 ? 2.9212 1.9945 2.7124 0.2894  0.7787  0.3107  969  GLN A OE1   
6472 N  NE2   . GLN A 866 ? 3.1436 2.2551 3.0310 0.3487  0.8394  0.3531  969  GLN A NE2   
6473 N  N     . GLU A 867 ? 3.3477 2.5881 3.2773 0.3511  0.8114  0.3580  970  GLU A N     
6474 C  CA    . GLU A 867 ? 3.3703 2.6319 3.3475 0.3765  0.8491  0.3760  970  GLU A CA    
6475 C  C     . GLU A 867 ? 3.2619 2.6223 3.2979 0.3916  0.8153  0.3973  970  GLU A C     
6476 O  O     . GLU A 867 ? 3.1069 2.4855 3.1264 0.3765  0.7964  0.3864  970  GLU A O     
6477 C  CB    . GLU A 867 ? 3.4048 2.6488 3.4255 0.4073  0.8963  0.3976  970  GLU A CB    
6478 C  CG    . GLU A 867 ? 3.4326 2.5740 3.3970 0.3937  0.9385  0.3768  970  GLU A CG    
6479 C  CD    . GLU A 867 ? 3.5337 2.6582 3.5452 0.4258  0.9870  0.3995  970  GLU A CD    
6480 O  OE1   . GLU A 867 ? 3.6309 2.8269 3.7188 0.4580  0.9816  0.4330  970  GLU A OE1   
6481 O  OE2   . GLU A 867 ? 3.5719 2.6107 3.5433 0.4180  1.0304  0.3844  970  GLU A OE2   
6482 N  N     . CYS A 868 ? 3.1581 2.5810 3.2608 0.4202  0.8075  0.4281  971  CYS A N     
6483 C  CA    . CYS A 868 ? 3.0228 2.5404 3.1830 0.4347  0.7770  0.4508  971  CYS A CA    
6484 C  C     . CYS A 868 ? 2.8864 2.4389 3.0190 0.4106  0.7182  0.4366  971  CYS A C     
6485 O  O     . CYS A 868 ? 2.8923 2.4409 3.0081 0.4022  0.6925  0.4317  971  CYS A O     
6486 C  CB    . CYS A 868 ? 3.0893 2.6605 3.3220 0.4685  0.7819  0.4877  971  CYS A CB    
6487 S  SG    . CYS A 868 ? 3.1136 2.8031 3.4155 0.4841  0.7414  0.5178  971  CYS A SG    
6488 N  N     . THR A 869 ? 2.7347 2.3206 2.8646 0.3998  0.6985  0.4303  972  THR A N     
6489 C  CA    . THR A 869 ? 2.4007 2.0208 2.5082 0.3779  0.6450  0.4175  972  THR A CA    
6490 C  C     . THR A 869 ? 2.2826 1.9966 2.4486 0.3934  0.6119  0.4425  972  THR A C     
6491 O  O     . THR A 869 ? 2.3354 2.0785 2.4900 0.3796  0.5686  0.4359  972  THR A O     
6492 C  CB    . THR A 869 ? 2.4868 2.0874 2.5530 0.3543  0.6397  0.3950  972  THR A CB    
6493 O  OG1   . THR A 869 ? 2.5568 2.2055 2.6686 0.3701  0.6525  0.4115  972  THR A OG1   
6494 C  CG2   . THR A 869 ? 2.7601 2.2658 2.7646 0.3371  0.6747  0.3708  972  THR A CG2   
6495 N  N     . LYS A 870 ? 2.3258 2.0869 2.5539 0.4208  0.6312  0.4713  973  LYS A N     
6496 C  CA    . LYS A 870 ? 2.1795 2.0307 2.4631 0.4346  0.6008  0.4973  973  LYS A CA    
6497 C  C     . LYS A 870 ? 2.2355 2.1009 2.5433 0.4500  0.5953  0.5162  973  LYS A C     
6498 O  O     . LYS A 870 ? 1.9960 1.8769 2.3521 0.4767  0.6208  0.5439  973  LYS A O     
6499 C  CB    . LYS A 870 ? 2.1416 2.0388 2.4825 0.4555  0.6220  0.5216  973  LYS A CB    
6500 C  CG    . LYS A 870 ? 2.0013 1.8885 2.3210 0.4406  0.6277  0.5042  973  LYS A CG    
6501 C  CD    . LYS A 870 ? 2.2173 2.1526 2.6005 0.4626  0.6505  0.5304  973  LYS A CD    
6502 C  CE    . LYS A 870 ? 2.4985 2.4244 2.8604 0.4469  0.6565  0.5129  973  LYS A CE    
6503 N  NZ    . LYS A 870 ? 2.8476 2.8204 3.2745 0.4680  0.6804  0.5385  973  LYS A NZ    
6504 N  N     . THR A 871 ? 2.3510 2.2110 2.6262 0.4328  0.5619  0.5018  974  THR A N     
6505 C  CA    . THR A 871 ? 2.1366 2.0096 2.4293 0.4439  0.5532  0.5172  974  THR A CA    
6506 C  C     . THR A 871 ? 1.9401 1.8819 2.2468 0.4375  0.5058  0.5240  974  THR A C     
6507 O  O     . THR A 871 ? 1.9265 1.9160 2.2440 0.4312  0.4846  0.5245  974  THR A O     
6508 C  CB    . THR A 871 ? 2.1344 1.9324 2.3764 0.4297  0.5613  0.4946  974  THR A CB    
6509 O  OG1   . THR A 871 ? 2.1823 1.9623 2.3738 0.3993  0.5301  0.4647  974  THR A OG1   
6510 C  CG2   . THR A 871 ? 2.3504 2.0761 2.5751 0.4348  0.6109  0.4875  974  THR A CG2   
6511 N  N     . ARG A 872 ? 2.0683 2.0140 2.3738 0.4382  0.4905  0.5287  975  ARG A N     
6512 C  CA    . ARG A 872 ? 1.9546 1.9597 2.2689 0.4303  0.4479  0.5332  975  ARG A CA    
6513 C  C     . ARG A 872 ? 2.1218 2.1154 2.3919 0.4010  0.4177  0.5019  975  ARG A C     
6514 O  O     . ARG A 872 ? 2.2624 2.3085 2.5404 0.3924  0.3854  0.5026  975  ARG A O     
6515 C  CB    . ARG A 872 ? 1.8991 1.9063 2.2212 0.4379  0.4425  0.5455  975  ARG A CB    
6516 C  CG    . ARG A 872 ? 2.0517 2.0839 2.4237 0.4675  0.4650  0.5817  975  ARG A CG    
6517 C  CD    . ARG A 872 ? 2.1014 2.1358 2.4771 0.4726  0.4570  0.5931  975  ARG A CD    
6518 N  NE    . ARG A 872 ? 2.6258 2.6858 3.0502 0.5009  0.4765  0.6303  975  ARG A NE    
6519 C  CZ    . ARG A 872 ? 2.5694 2.6338 3.0046 0.5103  0.4751  0.6473  975  ARG A CZ    
6520 N  NH1   . ARG A 872 ? 2.4771 2.5224 2.8792 0.4941  0.4565  0.6301  975  ARG A NH1   
6521 N  NH2   . ARG A 872 ? 2.2803 2.3690 2.7623 0.5366  0.4930  0.6835  975  ARG A NH2   
6522 N  N     . GLU A 873 ? 2.0537 1.9789 2.2771 0.3846  0.4274  0.4751  976  GLU A N     
6523 C  CA    . GLU A 873 ? 1.8120 1.7240 1.9950 0.3568  0.3986  0.4471  976  GLU A CA    
6524 C  C     . GLU A 873 ? 1.9975 1.9336 2.1815 0.3503  0.3929  0.4423  976  GLU A C     
6525 O  O     . GLU A 873 ? 1.9867 1.9567 2.1657 0.3359  0.3605  0.4339  976  GLU A O     
6526 C  CB    . GLU A 873 ? 1.9619 1.7941 2.0946 0.3398  0.4101  0.4222  976  GLU A CB    
6527 C  CG    . GLU A 873 ? 1.8788 1.6866 2.0042 0.3394  0.4079  0.4217  976  GLU A CG    
6528 C  CD    . GLU A 873 ? 2.1042 1.8976 2.2544 0.3640  0.4432  0.4425  976  GLU A CD    
6529 O  OE1   . GLU A 873 ? 2.1209 1.9154 2.2918 0.3807  0.4724  0.4557  976  GLU A OE1   
6530 O  OE2   . GLU A 873 ? 1.8916 1.6722 2.0424 0.3667  0.4427  0.4463  976  GLU A OE2   
6531 N  N     . PHE A 874 ? 2.0242 1.9416 2.2151 0.3607  0.4258  0.4473  977  PHE A N     
6532 C  CA    . PHE A 874 ? 1.8760 1.8168 2.0706 0.3555  0.4234  0.4442  977  PHE A CA    
6533 C  C     . PHE A 874 ? 1.8911 1.9152 2.1381 0.3695  0.4082  0.4693  977  PHE A C     
6534 O  O     . PHE A 874 ? 2.1152 2.1731 2.3644 0.3598  0.3908  0.4649  977  PHE A O     
6535 C  CB    . PHE A 874 ? 1.8549 1.7493 2.0422 0.3622  0.4661  0.4420  977  PHE A CB    
6536 C  CG    . PHE A 874 ? 1.9962 1.9120 2.1884 0.3576  0.4678  0.4394  977  PHE A CG    
6537 C  CD1   . PHE A 874 ? 1.7434 1.6400 1.8917 0.3314  0.4473  0.4141  977  PHE A CD1   
6538 C  CD2   . PHE A 874 ? 1.9857 1.9412 2.2283 0.3792  0.4897  0.4632  977  PHE A CD2   
6539 C  CE1   . PHE A 874 ? 1.8047 1.7195 1.9564 0.3265  0.4495  0.4116  977  PHE A CE1   
6540 C  CE2   . PHE A 874 ? 1.9206 1.8962 2.1691 0.3744  0.4919  0.4607  977  PHE A CE2   
6541 C  CZ    . PHE A 874 ? 1.8564 1.8107 2.0579 0.3478  0.4723  0.4343  977  PHE A CZ    
6542 N  N     . GLU A 875 ? 2.0253 2.0829 2.3135 0.3909  0.4137  0.4961  978  GLU A N     
6543 C  CA    . GLU A 875 ? 2.1294 2.2675 2.4647 0.4015  0.3954  0.5214  978  GLU A CA    
6544 C  C     . GLU A 875 ? 1.9957 2.1703 2.3167 0.3822  0.3521  0.5107  978  GLU A C     
6545 O  O     . GLU A 875 ? 1.8444 2.0765 2.1864 0.3794  0.3329  0.5191  978  GLU A O     
6546 C  CB    . GLU A 875 ? 2.2220 2.3837 2.5998 0.4265  0.4084  0.5530  978  GLU A CB    
6547 C  CG    . GLU A 875 ? 2.2741 2.5186 2.7035 0.4385  0.3926  0.5838  978  GLU A CG    
6548 C  CD    . GLU A 875 ? 2.2595 2.5246 2.7307 0.4634  0.4058  0.6173  978  GLU A CD    
6549 O  OE1   . GLU A 875 ? 2.2083 2.4231 2.6666 0.4707  0.4258  0.6149  978  GLU A OE1   
6550 O  OE2   . GLU A 875 ? 2.2956 2.6270 2.8124 0.4749  0.3957  0.6469  978  GLU A OE2   
6551 N  N     . ARG A 876 ? 2.0910 2.2323 2.3773 0.3682  0.3373  0.4921  979  ARG A N     
6552 C  CA    . ARG A 876 ? 1.9765 2.1441 2.2474 0.3489  0.2994  0.4789  979  ARG A CA    
6553 C  C     . ARG A 876 ? 1.9626 2.1092 2.1996 0.3266  0.2869  0.4522  979  ARG A C     
6554 O  O     . ARG A 876 ? 1.8965 2.0746 2.1286 0.3121  0.2575  0.4439  979  ARG A O     
6555 C  CB    . ARG A 876 ? 2.1158 2.2584 2.3688 0.3435  0.2894  0.4713  979  ARG A CB    
6556 C  CG    . ARG A 876 ? 2.5393 2.7036 2.8229 0.3635  0.2984  0.4977  979  ARG A CG    
6557 C  CD    . ARG A 876 ? 2.6872 2.8208 2.9506 0.3569  0.2911  0.4880  979  ARG A CD    
6558 N  NE    . ARG A 876 ? 2.8208 2.9723 3.0680 0.3366  0.2580  0.4717  979  ARG A NE    
6559 C  CZ    . ARG A 876 ? 2.9026 3.0349 3.1342 0.3275  0.2467  0.4613  979  ARG A CZ    
6560 N  NH1   . ARG A 876 ? 2.9654 3.0601 3.1931 0.3355  0.2641  0.4648  979  ARG A NH1   
6561 N  NH2   . ARG A 876 ? 2.8084 2.9589 3.0296 0.3097  0.2187  0.4470  979  ARG A NH2   
6562 N  N     . PHE A 877 ? 1.8316 1.9239 2.0435 0.3230  0.3095  0.4387  980  PHE A N     
6563 C  CA    . PHE A 877 ? 1.5643 1.6354 1.7427 0.3018  0.2985  0.4154  980  PHE A CA    
6564 C  C     . PHE A 877 ? 1.7149 1.8394 1.9169 0.3024  0.2910  0.4235  980  PHE A C     
6565 O  O     . PHE A 877 ? 1.8079 1.9430 1.9930 0.2842  0.2674  0.4087  980  PHE A O     
6566 C  CB    . PHE A 877 ? 1.6770 1.6766 1.8210 0.2974  0.3270  0.4010  980  PHE A CB    
6567 C  CG    . PHE A 877 ? 1.8539 1.8251 1.9581 0.2741  0.3162  0.3774  980  PHE A CG    
6568 C  CD1   . PHE A 877 ? 1.8787 1.8156 1.9438 0.2519  0.2931  0.3560  980  PHE A CD1   
6569 C  CD2   . PHE A 877 ? 1.6991 1.6782 1.8064 0.2741  0.3290  0.3779  980  PHE A CD2   
6570 C  CE1   . PHE A 877 ? 1.8329 1.7437 1.8618 0.2303  0.2818  0.3365  980  PHE A CE1   
6571 C  CE2   . PHE A 877 ? 1.7293 1.6808 1.7980 0.2521  0.3190  0.3571  980  PHE A CE2   
6572 C  CZ    . PHE A 877 ? 1.9277 1.8448 1.9566 0.2301  0.2948  0.3368  980  PHE A CZ    
6573 N  N     . GLN A 878 ? 1.8810 2.0400 2.1243 0.3231  0.3108  0.4478  981  GLN A N     
6574 C  CA    . GLN A 878 ? 1.6965 1.9109 1.9672 0.3239  0.3037  0.4580  981  GLN A CA    
6575 C  C     . GLN A 878 ? 1.8067 2.0819 2.0919 0.3165  0.2678  0.4637  981  GLN A C     
6576 O  O     . GLN A 878 ? 1.6546 1.9597 1.9384 0.3035  0.2496  0.4571  981  GLN A O     
6577 C  CB    . GLN A 878 ? 1.9340 2.1732 2.2514 0.3486  0.3331  0.4857  981  GLN A CB    
6578 C  CG    . GLN A 878 ? 1.8714 2.0495 2.1771 0.3571  0.3739  0.4810  981  GLN A CG    
6579 C  CD    . GLN A 878 ? 1.9449 2.1450 2.3029 0.3852  0.4047  0.5115  981  GLN A CD    
6580 O  OE1   . GLN A 878 ? 1.7193 1.9681 2.1165 0.3997  0.3955  0.5366  981  GLN A OE1   
6581 N  NE2   . GLN A 878 ? 2.2305 2.3942 2.5898 0.3928  0.4421  0.5102  981  GLN A NE2   
6582 N  N     . GLU A 879 ? 1.7972 2.0892 2.0946 0.3237  0.2584  0.4753  982  GLU A N     
6583 C  CA    . GLU A 879 ? 1.6128 1.9596 1.9211 0.3158  0.2268  0.4807  982  GLU A CA    
6584 C  C     . GLU A 879 ? 1.6671 1.9975 1.9388 0.2912  0.2009  0.4528  982  GLU A C     
6585 O  O     . GLU A 879 ? 1.8051 2.1783 2.0814 0.2798  0.1770  0.4514  982  GLU A O     
6586 C  CB    . GLU A 879 ? 1.6061 1.9675 1.9311 0.3281  0.2252  0.4986  982  GLU A CB    
6587 C  CG    . GLU A 879 ? 1.9932 2.3718 2.3582 0.3538  0.2500  0.5293  982  GLU A CG    
6588 C  CD    . GLU A 879 ? 2.1971 2.6423 2.6025 0.3603  0.2452  0.5527  982  GLU A CD    
6589 O  OE1   . GLU A 879 ? 2.2087 2.6972 2.6128 0.3454  0.2176  0.5498  982  GLU A OE1   
6590 O  OE2   . GLU A 879 ? 2.0524 2.5062 2.4922 0.3799  0.2697  0.5742  982  GLU A OE2   
6591 N  N     . MET A 880 ? 1.4722 1.7409 1.7082 0.2821  0.2052  0.4311  983  MET A N     
6592 C  CA    . MET A 880 ? 1.4041 1.6555 1.6089 0.2592  0.1813  0.4060  983  MET A CA    
6593 C  C     . MET A 880 ? 1.6202 1.8796 1.8169 0.2476  0.1765  0.3965  983  MET A C     
6594 O  O     . MET A 880 ? 1.7529 2.0317 1.9419 0.2318  0.1524  0.3854  983  MET A O     
6595 C  CB    . MET A 880 ? 1.4409 1.6251 1.6113 0.2516  0.1863  0.3877  983  MET A CB    
6596 C  CG    . MET A 880 ? 1.6643 1.8373 1.8396 0.2597  0.1886  0.3939  983  MET A CG    
6597 S  SD    . MET A 880 ? 1.3813 1.4795 1.5159 0.2455  0.1884  0.3706  983  MET A SD    
6598 C  CE    . MET A 880 ? 1.7896 1.8355 1.9025 0.2482  0.2194  0.3661  983  MET A CE    
6599 N  N     . CYS A 881 ? 1.6332 1.8762 1.8318 0.2553  0.2008  0.4005  984  CYS A N     
6600 C  CA    . CYS A 881 ? 1.5148 1.7648 1.7063 0.2447  0.1990  0.3924  984  CYS A CA    
6601 C  C     . CYS A 881 ? 1.3383 1.6599 1.5646 0.2471  0.1865  0.4080  984  CYS A C     
6602 O  O     . CYS A 881 ? 1.4437 1.7827 1.6621 0.2318  0.1698  0.3978  984  CYS A O     
6603 C  CB    . CYS A 881 ? 1.5265 1.7388 1.7115 0.2524  0.2318  0.3931  984  CYS A CB    
6604 S  SG    . CYS A 881 ? 1.5912 1.7146 1.7286 0.2459  0.2479  0.3738  984  CYS A SG    
6605 N  N     . TYR A 882 ? 1.3396 1.7031 1.6044 0.2652  0.1938  0.4335  985  TYR A N     
6606 C  CA    . TYR A 882 ? 1.3444 1.7782 1.6423 0.2660  0.1802  0.4505  985  TYR A CA    
6607 C  C     . TYR A 882 ? 1.3833 1.8428 1.6692 0.2483  0.1478  0.4403  985  TYR A C     
6608 O  O     . TYR A 882 ? 1.1673 1.6625 1.4570 0.2359  0.1323  0.4377  985  TYR A O     
6609 C  CB    . TYR A 882 ? 1.5908 2.0623 1.9314 0.2883  0.1923  0.4819  985  TYR A CB    
6610 C  CG    . TYR A 882 ? 1.6849 2.1353 2.0450 0.3078  0.2274  0.4947  985  TYR A CG    
6611 C  CD1   . TYR A 882 ? 1.7084 2.1325 2.0581 0.3040  0.2446  0.4835  985  TYR A CD1   
6612 C  CD2   . TYR A 882 ? 1.7792 2.2340 2.1678 0.3299  0.2450  0.5181  985  TYR A CD2   
6613 C  CE1   . TYR A 882 ? 1.6896 2.0915 2.0569 0.3214  0.2801  0.4942  985  TYR A CE1   
6614 C  CE2   . TYR A 882 ? 1.7624 2.1956 2.1711 0.3484  0.2800  0.5298  985  TYR A CE2   
6615 C  CZ    . TYR A 882 ? 1.6466 2.0529 2.0445 0.3440  0.2982  0.5172  985  TYR A CZ    
6616 O  OH    . TYR A 882 ? 1.7576 2.1397 2.1751 0.3619  0.3363  0.5279  985  TYR A OH    
6617 N  N     . LYS A 883 ? 1.3420 1.7824 1.6137 0.2464  0.1387  0.4342  986  LYS A N     
6618 C  CA    . LYS A 883 ? 1.1316 1.5913 1.3919 0.2298  0.1113  0.4233  986  LYS A CA    
6619 C  C     . LYS A 883 ? 1.2369 1.6671 1.4666 0.2096  0.0990  0.3964  986  LYS A C     
6620 O  O     . LYS A 883 ? 1.1536 1.6085 1.3791 0.1944  0.0784  0.3881  986  LYS A O     
6621 C  CB    . LYS A 883 ? 1.1471 1.5912 1.4019 0.2336  0.1078  0.4238  986  LYS A CB    
6622 C  CG    . LYS A 883 ? 1.4383 1.9141 1.7223 0.2522  0.1169  0.4518  986  LYS A CG    
6623 C  CD    . LYS A 883 ? 1.4935 1.9464 1.7689 0.2556  0.1161  0.4508  986  LYS A CD    
6624 C  CE    . LYS A 883 ? 1.6692 2.1512 1.9728 0.2745  0.1256  0.4802  986  LYS A CE    
6625 N  NZ    . LYS A 883 ? 1.8232 2.2809 2.1177 0.2779  0.1266  0.4794  986  LYS A NZ    
6626 N  N     . ALA A 884 ? 1.2534 1.6299 1.4608 0.2083  0.1115  0.3831  987  ALA A N     
6627 C  CA    . ALA A 884 ? 1.3856 1.7327 1.5639 0.1891  0.0993  0.3599  987  ALA A CA    
6628 C  C     . ALA A 884 ? 1.5398 1.9074 1.7217 0.1832  0.1011  0.3598  987  ALA A C     
6629 O  O     . ALA A 884 ? 1.4885 1.8583 1.6566 0.1661  0.0843  0.3455  987  ALA A O     
6630 C  CB    . ALA A 884 ? 1.2482 1.5277 1.3964 0.1869  0.1095  0.3460  987  ALA A CB    
6631 N  N     . TYR A 885 ? 1.4202 1.8022 1.6223 0.1972  0.1223  0.3757  988  TYR A N     
6632 C  CA    . TYR A 885 ? 1.1749 1.5802 1.3851 0.1923  0.1257  0.3774  988  TYR A CA    
6633 C  C     . TYR A 885 ? 1.5244 1.9934 1.7560 0.1849  0.1053  0.3849  988  TYR A C     
6634 O  O     . TYR A 885 ? 1.3092 1.7880 1.5312 0.1689  0.0932  0.3737  988  TYR A O     
6635 C  CB    . TYR A 885 ? 1.4568 1.8645 1.6899 0.2107  0.1554  0.3947  988  TYR A CB    
6636 C  CG    . TYR A 885 ? 1.5134 1.9446 1.7587 0.2070  0.1628  0.3977  988  TYR A CG    
6637 C  CD1   . TYR A 885 ? 1.4593 1.8459 1.6751 0.1971  0.1735  0.3810  988  TYR A CD1   
6638 C  CD2   . TYR A 885 ? 1.4249 1.9227 1.7106 0.2123  0.1588  0.4180  988  TYR A CD2   
6639 C  CE1   . TYR A 885 ? 1.4625 1.8696 1.6896 0.1934  0.1817  0.3836  988  TYR A CE1   
6640 C  CE2   . TYR A 885 ? 1.4825 2.0031 1.7821 0.2084  0.1657  0.4212  988  TYR A CE2   
6641 C  CZ    . TYR A 885 ? 1.6158 2.0905 1.8864 0.1994  0.1781  0.4036  988  TYR A CZ    
6642 O  OH    . TYR A 885 ? 1.7679 2.2646 2.0523 0.1951  0.1865  0.4065  988  TYR A OH    
6643 N  N     . LEU A 886 ? 1.4352 1.9466 1.6939 0.1950  0.1013  0.4040  989  LEU A N     
6644 C  CA    . LEU A 886 ? 1.2718 1.8437 1.5480 0.1861  0.0819  0.4124  989  LEU A CA    
6645 C  C     . LEU A 886 ? 1.3293 1.8949 1.5805 0.1661  0.0583  0.3921  989  LEU A C     
6646 O  O     . LEU A 886 ? 1.3251 1.9269 1.5788 0.1518  0.0428  0.3899  989  LEU A O     
6647 C  CB    . LEU A 886 ? 1.2943 1.9098 1.6023 0.2009  0.0831  0.4393  989  LEU A CB    
6648 C  CG    . LEU A 886 ? 1.7321 2.4146 2.0598 0.1920  0.0642  0.4531  989  LEU A CG    
6649 C  CD1   . LEU A 886 ? 1.5786 2.2930 1.9234 0.1868  0.0662  0.4583  989  LEU A CD1   
6650 C  CD2   . LEU A 886 ? 1.6286 2.3476 1.9849 0.2072  0.0656  0.4814  989  LEU A CD2   
6651 N  N     . ALA A 887 ? 1.2688 1.7882 1.4970 0.1644  0.0560  0.3775  990  ALA A N     
6652 C  CA    . ALA A 887 ? 1.2516 1.7622 1.4602 0.1466  0.0358  0.3585  990  ALA A CA    
6653 C  C     . ALA A 887 ? 1.4495 1.9431 1.6397 0.1301  0.0288  0.3402  990  ALA A C     
6654 O  O     . ALA A 887 ? 1.6037 2.1172 1.7898 0.1144  0.0128  0.3312  990  ALA A O     
6655 C  CB    . ALA A 887 ? 1.3874 1.8533 1.5809 0.1495  0.0360  0.3491  990  ALA A CB    
6656 N  N     . ILE A 888 ? 1.3921 1.8468 1.5690 0.1325  0.0413  0.3343  991  ILE A N     
6657 C  CA    . ILE A 888 ? 1.1649 1.6017 1.3227 0.1168  0.0354  0.3185  991  ILE A CA    
6658 C  C     . ILE A 888 ? 1.3331 1.8183 1.5078 0.1119  0.0343  0.3263  991  ILE A C     
6659 O  O     . ILE A 888 ? 1.3189 1.8100 1.4839 0.0952  0.0218  0.3144  991  ILE A O     
6660 C  CB    . ILE A 888 ? 1.1870 1.5685 1.3226 0.1195  0.0504  0.3114  991  ILE A CB    
6661 C  CG1   . ILE A 888 ? 1.5479 1.8826 1.6665 0.1222  0.0496  0.3040  991  ILE A CG1   
6662 C  CG2   . ILE A 888 ? 1.1072 1.4682 1.2204 0.1024  0.0435  0.2960  991  ILE A CG2   
6663 C  CD1   . ILE A 888 ? 1.2775 1.6001 1.3845 0.1079  0.0272  0.2890  991  ILE A CD1   
6664 N  N     . ARG A 889 ? 1.3626 1.8839 1.5650 0.1260  0.0473  0.3472  992  ARG A N     
6665 C  CA    . ARG A 889 ? 1.2023 1.7754 1.4260 0.1213  0.0453  0.3575  992  ARG A CA    
6666 C  C     . ARG A 889 ? 1.4248 2.0392 1.6519 0.1065  0.0232  0.3557  992  ARG A C     
6667 O  O     . ARG A 889 ? 1.3077 1.9488 1.5367 0.0924  0.0151  0.3523  992  ARG A O     
6668 C  CB    . ARG A 889 ? 1.5899 2.1959 1.8486 0.1408  0.0626  0.3835  992  ARG A CB    
6669 C  CG    . ARG A 889 ? 1.5378 2.2083 1.8268 0.1370  0.0576  0.3996  992  ARG A CG    
6670 C  CD    . ARG A 889 ? 1.2141 1.9139 1.5425 0.1582  0.0762  0.4272  992  ARG A CD    
6671 N  NE    . ARG A 889 ? 1.4721 2.2427 1.8342 0.1553  0.0650  0.4480  992  ARG A NE    
6672 C  CZ    . ARG A 889 ? 1.3650 2.1701 1.7446 0.1474  0.0647  0.4530  992  ARG A CZ    
6673 N  NH1   . ARG A 889 ? 1.3252 2.1004 1.6913 0.1419  0.0763  0.4385  992  ARG A NH1   
6674 N  NH2   . ARG A 889 ? 1.5393 2.4104 1.9498 0.1436  0.0522  0.4737  992  ARG A NH2   
6675 N  N     . GLN A 890 ? 1.3795 1.9973 1.6055 0.1083  0.0144  0.3570  993  GLN A N     
6676 C  CA    . GLN A 890 ? 1.3164 1.9665 1.5401 0.0925  -0.0045 0.3529  993  GLN A CA    
6677 C  C     . GLN A 890 ? 1.2566 1.8776 1.4546 0.0733  -0.0160 0.3275  993  GLN A C     
6678 O  O     . GLN A 890 ? 1.3141 1.9608 1.5089 0.0569  -0.0291 0.3216  993  GLN A O     
6679 C  CB    . GLN A 890 ? 1.3684 2.0248 1.5954 0.0993  -0.0082 0.3604  993  GLN A CB    
6680 C  CG    . GLN A 890 ? 1.6128 2.3093 1.8680 0.1155  -0.0011 0.3886  993  GLN A CG    
6681 C  CD    . GLN A 890 ? 1.8860 2.5826 2.1414 0.1226  -0.0035 0.3959  993  GLN A CD    
6682 O  OE1   . GLN A 890 ? 1.7926 2.4503 2.0290 0.1201  -0.0054 0.3800  993  GLN A OE1   
6683 N  NE2   . GLN A 890 ? 2.0803 2.8216 2.3584 0.1310  -0.0038 0.4211  993  GLN A NE2   
6684 N  N     . HIS A 891 ? 1.3880 1.9556 1.5674 0.0742  -0.0114 0.3132  994  HIS A N     
6685 C  CA    . HIS A 891 ? 1.3407 1.8784 1.4987 0.0572  -0.0220 0.2915  994  HIS A CA    
6686 C  C     . HIS A 891 ? 1.3463 1.8651 1.4941 0.0523  -0.0163 0.2857  994  HIS A C     
6687 O  O     . HIS A 891 ? 1.5984 2.0740 1.7251 0.0443  -0.0205 0.2703  994  HIS A O     
6688 C  CB    . HIS A 891 ? 1.2385 1.7289 1.3822 0.0589  -0.0256 0.2797  994  HIS A CB    
6689 C  CG    . HIS A 891 ? 1.3023 1.8070 1.4528 0.0592  -0.0323 0.2808  994  HIS A CG    
6690 N  ND1   . HIS A 891 ? 1.2799 1.7929 1.4415 0.0744  -0.0250 0.2947  994  HIS A ND1   
6691 C  CD2   . HIS A 891 ? 1.2063 1.7164 1.3532 0.0457  -0.0438 0.2695  994  HIS A CD2   
6692 C  CE1   . HIS A 891 ? 1.3782 1.9016 1.5413 0.0697  -0.0325 0.2920  994  HIS A CE1   
6693 N  NE2   . HIS A 891 ? 1.2569 1.7783 1.4112 0.0523  -0.0431 0.2763  994  HIS A NE2   
6694 N  N     . ALA A 892 ? 1.5170 2.0680 1.6804 0.0567  -0.0068 0.2990  995  ALA A N     
6695 C  CA    . ALA A 892 ? 1.2893 1.8225 1.4434 0.0525  0.0017  0.2943  995  ALA A CA    
6696 C  C     . ALA A 892 ? 1.4303 1.9601 1.5693 0.0314  -0.0115 0.2782  995  ALA A C     
6697 O  O     . ALA A 892 ? 1.4416 1.9346 1.5606 0.0246  -0.0090 0.2675  995  ALA A O     
6698 C  CB    . ALA A 892 ? 1.1901 1.7641 1.3707 0.0619  0.0157  0.3133  995  ALA A CB    
6699 N  N     . ASN A 893 ? 1.3936 1.9590 1.5398 0.0198  -0.0249 0.2763  996  ASN A N     
6700 C  CA    . ASN A 893 ? 1.3225 1.8835 1.4551 -0.0006 -0.0359 0.2607  996  ASN A CA    
6701 C  C     . ASN A 893 ? 1.4092 1.9163 1.5194 -0.0063 -0.0434 0.2431  996  ASN A C     
6702 O  O     . ASN A 893 ? 1.3808 1.8663 1.4761 -0.0196 -0.0483 0.2310  996  ASN A O     
6703 C  CB    . ASN A 893 ? 1.3512 1.9586 1.4937 -0.0128 -0.0470 0.2617  996  ASN A CB    
6704 C  CG    . ASN A 893 ? 1.6063 2.2711 1.7724 -0.0101 -0.0432 0.2808  996  ASN A CG    
6705 O  OD1   . ASN A 893 ? 1.8058 2.4783 1.9872 0.0058  -0.0308 0.2960  996  ASN A OD1   
6706 N  ND2   . ASN A 893 ? 1.8261 2.5311 1.9961 -0.0262 -0.0535 0.2807  996  ASN A ND2   
6707 N  N     . LEU A 894 ? 1.6346 2.1200 1.7437 0.0032  -0.0448 0.2428  997  LEU A N     
6708 C  CA    . LEU A 894 ? 1.5114 1.9488 1.6045 -0.0021 -0.0533 0.2283  997  LEU A CA    
6709 C  C     . LEU A 894 ? 1.3697 1.7607 1.4433 -0.0006 -0.0485 0.2249  997  LEU A C     
6710 O  O     . LEU A 894 ? 1.4166 1.7757 1.4745 -0.0123 -0.0571 0.2133  997  LEU A O     
6711 C  CB    . LEU A 894 ? 1.7173 2.1468 1.8171 0.0072  -0.0555 0.2299  997  LEU A CB    
6712 C  CG    . LEU A 894 ? 1.4558 1.8445 1.5477 0.0017  -0.0658 0.2167  997  LEU A CG    
6713 C  CD1   . LEU A 894 ? 1.8770 2.2802 1.9820 0.0044  -0.0688 0.2167  997  LEU A CD1   
6714 C  CD2   . LEU A 894 ? 1.1707 1.5118 1.2491 0.0088  -0.0636 0.2164  997  LEU A CD2   
6715 N  N     . PHE A 895 ? 1.3357 1.7207 1.4092 0.0130  -0.0343 0.2353  998  PHE A N     
6716 C  CA    . PHE A 895 ? 1.5046 1.8408 1.5543 0.0130  -0.0279 0.2314  998  PHE A CA    
6717 C  C     . PHE A 895 ? 1.4024 1.7377 1.4409 0.0022  -0.0242 0.2280  998  PHE A C     
6718 O  O     . PHE A 895 ? 1.4834 1.7759 1.4964 -0.0075 -0.0280 0.2190  998  PHE A O     
6719 C  CB    . PHE A 895 ? 1.3481 1.6750 1.4000 0.0303  -0.0104 0.2425  998  PHE A CB    
6720 C  CG    . PHE A 895 ? 1.3631 1.6781 1.4199 0.0398  -0.0134 0.2443  998  PHE A CG    
6721 C  CD1   . PHE A 895 ? 1.3689 1.6338 1.4054 0.0358  -0.0208 0.2352  998  PHE A CD1   
6722 C  CD2   . PHE A 895 ? 1.3479 1.7021 1.4298 0.0517  -0.0097 0.2559  998  PHE A CD2   
6723 C  CE1   . PHE A 895 ? 1.3234 1.5779 1.3659 0.0437  -0.0232 0.2368  998  PHE A CE1   
6724 C  CE2   . PHE A 895 ? 1.6280 1.9703 1.7139 0.0600  -0.0115 0.2575  998  PHE A CE2   
6725 C  CZ    . PHE A 895 ? 1.4373 1.7298 1.5042 0.0561  -0.0177 0.2475  998  PHE A CZ    
6726 N  N     . ILE A 896 ? 1.5486 1.9308 1.6057 0.0027  -0.0173 0.2360  999  ILE A N     
6727 C  CA    . ILE A 896 ? 1.5835 1.9679 1.6325 -0.0079 -0.0125 0.2332  999  ILE A CA    
6728 C  C     . ILE A 896 ? 1.3913 1.7621 1.4264 -0.0267 -0.0292 0.2190  999  ILE A C     
6729 O  O     . ILE A 896 ? 1.5678 1.9104 1.5820 -0.0372 -0.0287 0.2122  999  ILE A O     
6730 C  CB    . ILE A 896 ? 1.3422 1.7852 1.4195 -0.0040 -0.0033 0.2464  999  ILE A CB    
6731 C  CG1   . ILE A 896 ? 1.1898 1.6402 1.2823 0.0157  0.0163  0.2619  999  ILE A CG1   
6732 C  CG2   . ILE A 896 ? 1.3615 1.8112 1.4331 -0.0174 -0.0001 0.2425  999  ILE A CG2   
6733 C  CD1   . ILE A 896 ? 1.4740 1.9832 1.5998 0.0210  0.0254  0.2781  999  ILE A CD1   
6734 N  N     . ASN A 897 ? 1.2796 1.6677 1.3254 -0.0314 -0.0430 0.2144  1000 ASN A N     
6735 C  CA    . ASN A 897 ? 1.1498 1.5211 1.1851 -0.0479 -0.0572 0.2009  1000 ASN A CA    
6736 C  C     . ASN A 897 ? 1.1862 1.4991 1.1991 -0.0505 -0.0646 0.1933  1000 ASN A C     
6737 O  O     . ASN A 897 ? 1.4064 1.6954 1.4053 -0.0640 -0.0729 0.1847  1000 ASN A O     
6738 C  CB    . ASN A 897 ? 1.1809 1.5792 1.2325 -0.0518 -0.0671 0.1973  1000 ASN A CB    
6739 C  CG    . ASN A 897 ? 1.4743 1.9284 1.5419 -0.0572 -0.0645 0.2024  1000 ASN A CG    
6740 O  OD1   . ASN A 897 ? 1.6474 2.1176 1.7142 -0.0638 -0.0594 0.2046  1000 ASN A OD1   
6741 N  ND2   . ASN A 897 ? 1.5376 2.0214 1.6191 -0.0558 -0.0682 0.2048  1000 ASN A ND2   
6742 N  N     . LEU A 898 ? 1.1652 1.4545 1.1745 -0.0387 -0.0624 0.1971  1001 LEU A N     
6743 C  CA    . LEU A 898 ? 1.3831 1.6179 1.3707 -0.0427 -0.0712 0.1914  1001 LEU A CA    
6744 C  C     . LEU A 898 ? 1.4355 1.6368 1.3940 -0.0489 -0.0645 0.1908  1001 LEU A C     
6745 O  O     . LEU A 898 ? 1.4961 1.6543 1.4324 -0.0590 -0.0754 0.1852  1001 LEU A O     
6746 C  CB    . LEU A 898 ? 1.4143 1.6339 1.4053 -0.0300 -0.0702 0.1956  1001 LEU A CB    
6747 C  CG    . LEU A 898 ? 1.0799 1.3231 1.0959 -0.0252 -0.0775 0.1952  1001 LEU A CG    
6748 C  CD1   . LEU A 898 ? 1.2385 1.4674 1.2570 -0.0120 -0.0737 0.2006  1001 LEU A CD1   
6749 C  CD2   . LEU A 898 ? 1.0454 1.2729 1.0644 -0.0373 -0.0945 0.1853  1001 LEU A CD2   
6750 N  N     . PHE A 899 ? 1.4712 1.6910 1.4300 -0.0434 -0.0464 0.1973  1002 PHE A N     
6751 C  CA    . PHE A 899 ? 1.6773 1.8655 1.6075 -0.0502 -0.0366 0.1960  1002 PHE A CA    
6752 C  C     . PHE A 899 ? 1.6830 1.8801 1.6085 -0.0654 -0.0409 0.1906  1002 PHE A C     
6753 O  O     . PHE A 899 ? 1.6337 1.7918 1.5295 -0.0770 -0.0422 0.1860  1002 PHE A O     
6754 C  CB    . PHE A 899 ? 1.6343 1.8357 1.5695 -0.0372 -0.0121 0.2054  1002 PHE A CB    
6755 C  CG    . PHE A 899 ? 1.6021 1.7745 1.5282 -0.0253 -0.0039 0.2091  1002 PHE A CG    
6756 C  CD1   . PHE A 899 ? 1.9422 2.0584 1.8308 -0.0308 0.0021  0.2051  1002 PHE A CD1   
6757 C  CD2   . PHE A 899 ? 1.5260 1.7255 1.4786 -0.0101 -0.0019 0.2164  1002 PHE A CD2   
6758 C  CE1   . PHE A 899 ? 1.7427 1.8299 1.6207 -0.0217 0.0105  0.2076  1002 PHE A CE1   
6759 C  CE2   . PHE A 899 ? 1.5830 1.7543 1.5272 0.0004  0.0066  0.2196  1002 PHE A CE2   
6760 C  CZ    . PHE A 899 ? 1.6419 1.7569 1.5489 -0.0056 0.0130  0.2147  1002 PHE A CZ    
6761 N  N     . SER A 900 ? 1.4620 1.7080 1.4139 -0.0671 -0.0432 0.1913  1003 SER A N     
6762 C  CA    . SER A 900 ? 1.4147 1.6696 1.3626 -0.0826 -0.0468 0.1856  1003 SER A CA    
6763 C  C     . SER A 900 ? 1.4457 1.6682 1.3809 -0.0957 -0.0659 0.1758  1003 SER A C     
6764 O  O     . SER A 900 ? 1.7910 1.9978 1.7107 -0.1096 -0.0689 0.1707  1003 SER A O     
6765 C  CB    . SER A 900 ? 1.5561 1.8719 1.5342 -0.0829 -0.0446 0.1889  1003 SER A CB    
6766 O  OG    . SER A 900 ? 1.8705 2.2045 1.8660 -0.0808 -0.0564 0.1867  1003 SER A OG    
6767 N  N     . MET A 901 ? 1.3602 1.5723 1.3037 -0.0913 -0.0784 0.1738  1004 MET A N     
6768 C  CA    . MET A 901 ? 1.6036 1.7836 1.5405 -0.1018 -0.0962 0.1667  1004 MET A CA    
6769 C  C     . MET A 901 ? 1.7585 1.8825 1.6639 -0.1068 -0.1025 0.1670  1004 MET A C     
6770 O  O     . MET A 901 ? 1.4474 1.5424 1.3454 -0.1173 -0.1180 0.1633  1004 MET A O     
6771 C  CB    . MET A 901 ? 1.2838 1.4734 1.2443 -0.0953 -0.1058 0.1651  1004 MET A CB    
6772 C  CG    . MET A 901 ? 1.2296 1.4694 1.2160 -0.0948 -0.1021 0.1633  1004 MET A CG    
6773 S  SD    . MET A 901 ? 1.3144 1.5640 1.3256 -0.0865 -0.1089 0.1618  1004 MET A SD    
6774 C  CE    . MET A 901 ? 1.2220 1.4331 1.2345 -0.0981 -0.1250 0.1529  1004 MET A CE    
6775 N  N     . MET A 902 ? 1.6730 1.7802 1.5597 -0.1003 -0.0908 0.1719  1005 MET A N     
6776 C  CA    . MET A 902 ? 1.8587 1.9107 1.7088 -0.1075 -0.0953 0.1721  1005 MET A CA    
6777 C  C     . MET A 902 ? 2.0425 2.0790 1.8635 -0.1165 -0.0820 0.1718  1005 MET A C     
6778 O  O     . MET A 902 ? 2.1470 2.1369 1.9316 -0.1233 -0.0814 0.1721  1005 MET A O     
6779 C  CB    . MET A 902 ? 1.7057 1.7400 1.5494 -0.0963 -0.0906 0.1763  1005 MET A CB    
6780 C  CG    . MET A 902 ? 1.5223 1.5664 1.3924 -0.0881 -0.1033 0.1768  1005 MET A CG    
6781 S  SD    . MET A 902 ? 1.4954 1.5075 1.3658 -0.1010 -0.1319 0.1736  1005 MET A SD    
6782 C  CE    . MET A 902 ? 1.7646 1.7131 1.5851 -0.1133 -0.1379 0.1758  1005 MET A CE    
6783 N  N     . LEU A 903 ? 1.8914 1.9650 1.7263 -0.1180 -0.0711 0.1711  1006 LEU A N     
6784 C  CA    . LEU A 903 ? 1.8753 1.9366 1.6857 -0.1264 -0.0564 0.1709  1006 LEU A CA    
6785 C  C     . LEU A 903 ? 2.3070 2.3265 2.0871 -0.1450 -0.0700 0.1665  1006 LEU A C     
6786 O  O     . LEU A 903 ? 2.3609 2.3475 2.1062 -0.1540 -0.0608 0.1662  1006 LEU A O     
6787 C  CB    . LEU A 903 ? 1.7754 1.8911 1.6131 -0.1240 -0.0426 0.1723  1006 LEU A CB    
6788 C  CG    . LEU A 903 ? 1.8931 2.0482 1.7564 -0.1066 -0.0243 0.1802  1006 LEU A CG    
6789 C  CD1   . LEU A 903 ? 1.7956 2.0071 1.6879 -0.1072 -0.0154 0.1831  1006 LEU A CD1   
6790 C  CD2   . LEU A 903 ? 1.9680 2.0909 1.8070 -0.1012 -0.0045 0.1837  1006 LEU A CD2   
6791 N  N     . GLY A 904 ? 2.5724 2.5913 2.3649 -0.1512 -0.0908 0.1634  1007 GLY A N     
6792 C  CA    . GLY A 904 ? 2.6761 2.6561 2.4443 -0.1679 -0.1057 0.1614  1007 GLY A CA    
6793 C  C     . GLY A 904 ? 2.5300 2.4556 2.2678 -0.1735 -0.1207 0.1645  1007 GLY A C     
6794 O  O     . GLY A 904 ? 2.5397 2.4316 2.2583 -0.1876 -0.1365 0.1652  1007 GLY A O     
6795 N  N     . SER A 905 ? 1.8834 1.7991 1.6160 -0.1638 -0.1169 0.1673  1008 SER A N     
6796 C  CA    . SER A 905 ? 2.0795 1.9445 1.7824 -0.1705 -0.1320 0.1705  1008 SER A CA    
6797 C  C     . SER A 905 ? 2.0393 1.8590 1.6890 -0.1826 -0.1218 0.1709  1008 SER A C     
6798 O  O     . SER A 905 ? 2.0164 1.7897 1.6335 -0.1920 -0.1348 0.1736  1008 SER A O     
6799 C  CB    . SER A 905 ? 2.0086 1.8810 1.7285 -0.1561 -0.1322 0.1725  1008 SER A CB    
6800 O  OG    . SER A 905 ? 1.8206 1.7178 1.5464 -0.1429 -0.1065 0.1723  1008 SER A OG    
6801 N  N     . GLY A 906 ? 2.0484 1.8795 1.6879 -0.1838 -0.0989 0.1683  1009 GLY A N     
6802 C  CA    . GLY A 906 ? 2.3483 2.1349 1.9361 -0.1962 -0.0857 0.1677  1009 GLY A CA    
6803 C  C     . GLY A 906 ? 2.2416 2.0016 1.8050 -0.1910 -0.0714 0.1681  1009 GLY A C     
6804 O  O     . GLY A 906 ? 2.7363 2.4449 2.2481 -0.2051 -0.0667 0.1673  1009 GLY A O     
6805 N  N     . MET A 907 ? 2.0869 1.8783 1.6838 -0.1722 -0.0636 0.1693  1010 MET A N     
6806 C  CA    . MET A 907 ? 2.1962 1.9627 1.7726 -0.1662 -0.0477 0.1696  1010 MET A CA    
6807 C  C     . MET A 907 ? 2.3267 2.0891 1.8852 -0.1645 -0.0126 0.1679  1010 MET A C     
6808 O  O     . MET A 907 ? 2.2788 2.0803 1.8624 -0.1594 0.0012  0.1682  1010 MET A O     
6809 C  CB    . MET A 907 ? 2.3219 2.1255 1.9421 -0.1458 -0.0476 0.1724  1010 MET A CB    
6810 C  CG    . MET A 907 ? 2.4102 2.2168 2.0506 -0.1466 -0.0791 0.1739  1010 MET A CG    
6811 S  SD    . MET A 907 ? 1.7050 1.5545 1.3950 -0.1236 -0.0772 0.1768  1010 MET A SD    
6812 C  CE    . MET A 907 ? 1.8668 1.6790 1.5246 -0.1188 -0.0552 0.1774  1010 MET A CE    
6813 N  N     . PRO A 908 ? 2.3667 2.0810 1.8822 -0.1696 0.0033  0.1660  1011 PRO A N     
6814 C  CA    . PRO A 908 ? 2.3966 2.1010 1.8934 -0.1691 0.0397  0.1639  1011 PRO A CA    
6815 C  C     . PRO A 908 ? 2.4693 2.2297 2.0179 -0.1452 0.0654  0.1681  1011 PRO A C     
6816 O  O     . PRO A 908 ? 2.3098 2.0928 1.8703 -0.1429 0.0872  0.1688  1011 PRO A O     
6817 C  CB    . PRO A 908 ? 2.2587 1.8967 1.6989 -0.1795 0.0494  0.1604  1011 PRO A CB    
6818 C  CG    . PRO A 908 ? 2.2955 1.9289 1.7449 -0.1758 0.0242  0.1625  1011 PRO A CG    
6819 C  CD    . PRO A 908 ? 2.3441 2.0095 1.8254 -0.1775 -0.0100 0.1654  1011 PRO A CD    
6820 N  N     . GLU A 909 ? 2.4360 2.2202 2.0168 -0.1278 0.0630  0.1720  1012 GLU A N     
6821 C  CA    . GLU A 909 ? 2.2810 2.1194 1.9125 -0.1049 0.0846  0.1785  1012 GLU A CA    
6822 C  C     . GLU A 909 ? 2.0210 1.9257 1.7058 -0.0964 0.0675  0.1828  1012 GLU A C     
6823 O  O     . GLU A 909 ? 1.9948 1.9497 1.7239 -0.0786 0.0806  0.1899  1012 GLU A O     
6824 C  CB    . GLU A 909 ? 2.3397 2.1680 1.9768 -0.0904 0.0938  0.1814  1012 GLU A CB    
6825 C  CG    . GLU A 909 ? 2.5124 2.2874 2.1082 -0.0932 0.1245  0.1783  1012 GLU A CG    
6826 C  CD    . GLU A 909 ? 2.6079 2.4060 2.2245 -0.0816 0.1623  0.1826  1012 GLU A CD    
6827 O  OE1   . GLU A 909 ? 2.4104 2.2728 2.0815 -0.0669 0.1642  0.1906  1012 GLU A OE1   
6828 O  OE2   . GLU A 909 ? 2.8369 2.5885 2.4157 -0.0881 0.1904  0.1783  1012 GLU A OE2   
6829 N  N     . LEU A 910 ? 1.9248 1.8298 1.6060 -0.1093 0.0391  0.1791  1013 LEU A N     
6830 C  CA    . LEU A 910 ? 1.9575 1.9190 1.6832 -0.1048 0.0235  0.1811  1013 LEU A CA    
6831 C  C     . LEU A 910 ? 2.2650 2.2267 1.9795 -0.1213 0.0176  0.1771  1013 LEU A C     
6832 O  O     . LEU A 910 ? 2.3466 2.3013 2.0576 -0.1323 -0.0074 0.1736  1013 LEU A O     
6833 C  CB    . LEU A 910 ? 2.2465 2.2100 1.9857 -0.1029 -0.0045 0.1804  1013 LEU A CB    
6834 C  CG    . LEU A 910 ? 1.9363 1.9398 1.7159 -0.0832 -0.0021 0.1860  1013 LEU A CG    
6835 C  CD1   . LEU A 910 ? 2.1133 2.0972 1.8828 -0.0715 0.0203  0.1898  1013 LEU A CD1   
6836 C  CD2   . LEU A 910 ? 1.6185 1.6205 1.4097 -0.0840 -0.0293 0.1841  1013 LEU A CD2   
6837 N  N     . GLN A 911 ? 2.3110 2.2803 2.0220 -0.1228 0.0418  0.1780  1014 GLN A N     
6838 C  CA    . GLN A 911 ? 2.2130 2.1829 1.9133 -0.1384 0.0404  0.1744  1014 GLN A CA    
6839 C  C     . GLN A 911 ? 2.1567 2.1927 1.9036 -0.1324 0.0470  0.1780  1014 GLN A C     
6840 O  O     . GLN A 911 ? 2.1478 2.2023 1.9044 -0.1423 0.0308  0.1748  1014 GLN A O     
6841 C  CB    . GLN A 911 ? 2.2957 2.2189 1.9513 -0.1490 0.0632  0.1718  1014 GLN A CB    
6842 C  CG    . GLN A 911 ? 2.3011 2.1532 1.9002 -0.1624 0.0532  0.1674  1014 GLN A CG    
6843 C  CD    . GLN A 911 ? 2.5013 2.3304 2.0800 -0.1802 0.0218  0.1643  1014 GLN A CD    
6844 O  OE1   . GLN A 911 ? 2.5473 2.4032 2.1436 -0.1859 0.0139  0.1635  1014 GLN A OE1   
6845 N  NE2   . GLN A 911 ? 2.7670 2.5461 2.3095 -0.1896 0.0035  0.1634  1014 GLN A NE2   
6846 N  N     . SER A 912 ? 2.1176 2.1898 1.8944 -0.1170 0.0702  0.1853  1015 SER A N     
6847 C  CA    . SER A 912 ? 2.2941 2.4317 2.1163 -0.1121 0.0765  0.1911  1015 SER A CA    
6848 C  C     . SER A 912 ? 2.1980 2.3827 2.0636 -0.0920 0.0777  0.2005  1015 SER A C     
6849 O  O     . SER A 912 ? 2.0447 2.2094 1.9049 -0.0812 0.0768  0.2021  1015 SER A O     
6850 C  CB    . SER A 912 ? 2.4837 2.6252 2.3051 -0.1146 0.1054  0.1939  1015 SER A CB    
6851 O  OG    . SER A 912 ? 2.6691 2.7830 2.4788 -0.1038 0.1312  0.1974  1015 SER A OG    
6852 N  N     . PHE A 913 ? 2.2335 2.4812 2.1417 -0.0882 0.0791  0.2074  1016 PHE A N     
6853 C  CA    . PHE A 913 ? 1.9591 2.2571 1.9095 -0.0713 0.0777  0.2181  1016 PHE A CA    
6854 C  C     . PHE A 913 ? 2.0297 2.3367 1.9990 -0.0528 0.1051  0.2302  1016 PHE A C     
6855 O  O     . PHE A 913 ? 2.1343 2.4791 2.1377 -0.0372 0.1052  0.2411  1016 PHE A O     
6856 C  CB    . PHE A 913 ? 1.8511 2.2133 1.8376 -0.0767 0.0677  0.2220  1016 PHE A CB    
6857 C  CG    . PHE A 913 ? 1.9005 2.2588 1.8753 -0.0922 0.0416  0.2108  1016 PHE A CG    
6858 C  CD1   . PHE A 913 ? 2.0946 2.4311 2.0461 -0.1109 0.0370  0.2011  1016 PHE A CD1   
6859 C  CD2   . PHE A 913 ? 1.8092 2.1840 1.7970 -0.0879 0.0233  0.2102  1016 PHE A CD2   
6860 C  CE1   . PHE A 913 ? 2.2141 2.5452 2.1575 -0.1243 0.0151  0.1913  1016 PHE A CE1   
6861 C  CE2   . PHE A 913 ? 1.9137 2.2829 1.8931 -0.1017 0.0025  0.1996  1016 PHE A CE2   
6862 C  CZ    . PHE A 913 ? 2.2997 2.6470 2.2580 -0.1195 -0.0014 0.1904  1016 PHE A CZ    
6863 N  N     . ASP A 914 ? 2.4252 2.6974 2.3734 -0.0544 0.1295  0.2289  1017 ASP A N     
6864 C  CA    . ASP A 914 ? 2.4284 2.7019 2.3937 -0.0363 0.1590  0.2397  1017 ASP A CA    
6865 C  C     . ASP A 914 ? 2.4461 2.6799 2.3927 -0.0253 0.1597  0.2385  1017 ASP A C     
6866 O  O     . ASP A 914 ? 2.4380 2.6803 2.4067 -0.0072 0.1806  0.2490  1017 ASP A O     
6867 C  CB    . ASP A 914 ? 2.7463 2.9887 2.6913 -0.0426 0.1880  0.2370  1017 ASP A CB    
6868 C  CG    . ASP A 914 ? 2.8755 3.0429 2.7560 -0.0602 0.1841  0.2214  1017 ASP A CG    
6869 O  OD1   . ASP A 914 ? 2.8183 2.9636 2.6747 -0.0686 0.1561  0.2133  1017 ASP A OD1   
6870 O  OD2   . ASP A 914 ? 2.8746 3.0051 2.7288 -0.0662 0.2092  0.2179  1017 ASP A OD2   
6871 N  N     . ASP A 915 ? 2.2475 2.4384 2.1561 -0.0360 0.1375  0.2267  1018 ASP A N     
6872 C  CA    . ASP A 915 ? 2.1098 2.2634 2.0006 -0.0278 0.1355  0.2252  1018 ASP A CA    
6873 C  C     . ASP A 915 ? 2.0315 2.2271 1.9576 -0.0153 0.1177  0.2320  1018 ASP A C     
6874 O  O     . ASP A 915 ? 1.9057 2.1000 1.8438 0.0008  0.1275  0.2391  1018 ASP A O     
6875 C  CB    . ASP A 915 ? 2.1940 2.2833 2.0301 -0.0457 0.1188  0.2113  1018 ASP A CB    
6876 C  CG    . ASP A 915 ? 2.3031 2.3453 2.0971 -0.0601 0.1361  0.2045  1018 ASP A CG    
6877 O  OD1   . ASP A 915 ? 2.5449 2.5775 2.3387 -0.0525 0.1680  0.2084  1018 ASP A OD1   
6878 O  OD2   . ASP A 915 ? 2.2733 2.2874 2.0347 -0.0792 0.1186  0.1956  1018 ASP A OD2   
6879 N  N     . ILE A 916 ? 1.7795 2.0100 1.7210 -0.0231 0.0929  0.2298  1019 ILE A N     
6880 C  CA    . ILE A 916 ? 1.5979 1.8682 1.5706 -0.0133 0.0770  0.2356  1019 ILE A CA    
6881 C  C     . ILE A 916 ? 1.6880 2.0165 1.7073 0.0032  0.0920  0.2525  1019 ILE A C     
6882 O  O     . ILE A 916 ? 1.9006 2.2538 1.9434 0.0164  0.0876  0.2610  1019 ILE A O     
6883 C  CB    . ILE A 916 ? 1.4248 1.7140 1.3996 -0.0278 0.0497  0.2278  1019 ILE A CB    
6884 C  CG1   . ILE A 916 ? 1.5722 1.8055 1.5044 -0.0450 0.0367  0.2137  1019 ILE A CG1   
6885 C  CG2   . ILE A 916 ? 1.8287 2.1431 1.8246 -0.0202 0.0334  0.2305  1019 ILE A CG2   
6886 C  CD1   . ILE A 916 ? 1.5917 1.8377 1.5269 -0.0585 0.0121  0.2058  1019 ILE A CD1   
6887 N  N     . ALA A 917 ? 1.7038 2.0555 1.7386 0.0027  0.1097  0.2587  1020 ALA A N     
6888 C  CA    . ALA A 917 ? 1.7127 2.1201 1.7957 0.0189  0.1247  0.2775  1020 ALA A CA    
6889 C  C     . ALA A 917 ? 1.8164 2.2038 1.9060 0.0392  0.1475  0.2869  1020 ALA A C     
6890 O  O     . ALA A 917 ? 1.6834 2.1159 1.8156 0.0558  0.1558  0.3046  1020 ALA A O     
6891 C  CB    . ALA A 917 ? 1.6479 2.0812 1.7474 0.0130  0.1400  0.2821  1020 ALA A CB    
6892 N  N     . TYR A 918 ? 1.7062 2.0266 1.7541 0.0374  0.1576  0.2760  1021 TYR A N     
6893 C  CA    . TYR A 918 ? 1.6242 1.9190 1.6735 0.0551  0.1793  0.2827  1021 TYR A CA    
6894 C  C     . TYR A 918 ? 1.7338 2.0485 1.8017 0.0671  0.1640  0.2895  1021 TYR A C     
6895 O  O     . TYR A 918 ? 1.7419 2.0626 1.8318 0.0859  0.1813  0.3021  1021 TYR A O     
6896 C  CB    . TYR A 918 ? 1.6681 1.8835 1.6614 0.0458  0.1895  0.2676  1021 TYR A CB    
6897 C  CG    . TYR A 918 ? 1.7350 1.9146 1.7216 0.0608  0.2121  0.2714  1021 TYR A CG    
6898 C  CD1   . TYR A 918 ? 2.0312 2.2148 2.0404 0.0760  0.2480  0.2826  1021 TYR A CD1   
6899 C  CD2   . TYR A 918 ? 1.7596 1.9002 1.7188 0.0594  0.1987  0.2639  1021 TYR A CD2   
6900 C  CE1   . TYR A 918 ? 2.0209 2.1684 2.0234 0.0894  0.2709  0.2855  1021 TYR A CE1   
6901 C  CE2   . TYR A 918 ? 1.8861 1.9918 1.8374 0.0718  0.2199  0.2666  1021 TYR A CE2   
6902 C  CZ    . TYR A 918 ? 1.9257 2.0337 1.8975 0.0867  0.2565  0.2770  1021 TYR A CZ    
6903 O  OH    . TYR A 918 ? 1.8459 1.9163 1.8094 0.0988  0.2799  0.2793  1021 TYR A OH    
6904 N  N     . ILE A 919 ? 1.7400 2.0638 1.8000 0.0565  0.1333  0.2816  1022 ILE A N     
6905 C  CA    . ILE A 919 ? 1.4055 1.7516 1.4840 0.0663  0.1188  0.2878  1022 ILE A CA    
6906 C  C     . ILE A 919 ? 1.5009 1.9186 1.6306 0.0783  0.1203  0.3074  1022 ILE A C     
6907 O  O     . ILE A 919 ? 1.3512 1.7874 1.5040 0.0943  0.1234  0.3202  1022 ILE A O     
6908 C  CB    . ILE A 919 ? 1.4290 1.7650 1.4873 0.0510  0.0881  0.2738  1022 ILE A CB    
6909 C  CG1   . ILE A 919 ? 1.6084 1.8741 1.6209 0.0422  0.0844  0.2587  1022 ILE A CG1   
6910 C  CG2   . ILE A 919 ? 1.4202 1.7915 1.5031 0.0591  0.0732  0.2809  1022 ILE A CG2   
6911 C  CD1   . ILE A 919 ? 1.8308 2.0624 1.8098 0.0241  0.0837  0.2466  1022 ILE A CD1   
6912 N  N     . ARG A 920 ? 1.5613 2.0204 1.7092 0.0699  0.1177  0.3110  1023 ARG A N     
6913 C  CA    . ARG A 920 ? 1.5449 2.0750 1.7412 0.0782  0.1164  0.3309  1023 ARG A CA    
6914 C  C     . ARG A 920 ? 1.4541 1.9967 1.6833 0.1003  0.1442  0.3508  1023 ARG A C     
6915 O  O     . ARG A 920 ? 1.3967 1.9869 1.6644 0.1134  0.1423  0.3703  1023 ARG A O     
6916 C  CB    . ARG A 920 ? 1.6351 2.2031 1.8422 0.0625  0.1092  0.3299  1023 ARG A CB    
6917 C  CG    . ARG A 920 ? 1.4199 1.9814 1.6003 0.0409  0.0827  0.3120  1023 ARG A CG    
6918 C  CD    . ARG A 920 ? 1.4697 2.0686 1.6617 0.0252  0.0779  0.3117  1023 ARG A CD    
6919 N  NE    . ARG A 920 ? 1.0874 1.7574 1.3254 0.0304  0.0762  0.3322  1023 ARG A NE    
6920 N  N     . LYS A 921 ? 1.5423 2.0415 1.7569 0.1045  0.1710  0.3468  1024 LYS A N     
6921 C  CA    . LYS A 921 ? 1.7265 2.2338 1.9742 0.1259  0.2017  0.3653  1024 LYS A CA    
6922 C  C     . LYS A 921 ? 1.7234 2.1978 1.9643 0.1419  0.2101  0.3683  1024 LYS A C     
6923 O  O     . LYS A 921 ? 1.4790 1.9828 1.7600 0.1619  0.2229  0.3892  1024 LYS A O     
6924 C  CB    . LYS A 921 ? 1.6698 2.1419 1.9041 0.1231  0.2309  0.3592  1024 LYS A CB    
6925 C  CG    . LYS A 921 ? 1.7716 2.2788 2.0184 0.1089  0.2270  0.3587  1024 LYS A CG    
6926 C  CD    . LYS A 921 ? 1.9118 2.3903 2.1548 0.1099  0.2616  0.3570  1024 LYS A CD    
6927 C  CE    . LYS A 921 ? 2.0580 2.5559 2.3490 0.1348  0.2937  0.3793  1024 LYS A CE    
6928 N  NZ    . LYS A 921 ? 2.2684 2.7383 2.5584 0.1360  0.3312  0.3776  1024 LYS A NZ    
6929 N  N     . THR A 922 ? 1.7719 2.1859 1.9637 0.1332  0.2028  0.3487  1025 THR A N     
6930 C  CA    . THR A 922 ? 1.7799 2.1608 1.9629 0.1462  0.2095  0.3502  1025 THR A CA    
6931 C  C     . THR A 922 ? 1.5775 1.9993 1.7833 0.1525  0.1865  0.3601  1025 THR A C     
6932 O  O     . THR A 922 ? 1.3246 1.7361 1.5386 0.1678  0.1947  0.3685  1025 THR A O     
6933 C  CB    . THR A 922 ? 1.5975 1.9036 1.7218 0.1326  0.2062  0.3272  1025 THR A CB    
6934 O  OG1   . THR A 922 ? 1.8662 2.1380 1.9824 0.1449  0.2163  0.3289  1025 THR A OG1   
6935 C  CG2   . THR A 922 ? 1.4393 1.7473 1.5415 0.1139  0.1707  0.3129  1025 THR A CG2   
6936 N  N     . LEU A 923 ? 1.3671 1.8325 1.5813 0.1402  0.1592  0.3588  1026 LEU A N     
6937 C  CA    . LEU A 923 ? 1.2604 1.7698 1.4969 0.1444  0.1388  0.3693  1026 LEU A CA    
6938 C  C     . LEU A 923 ? 1.5678 2.1485 1.8559 0.1544  0.1410  0.3946  1026 LEU A C     
6939 O  O     . LEU A 923 ? 1.6037 2.2226 1.9121 0.1595  0.1270  0.4074  1026 LEU A O     
6940 C  CB    . LEU A 923 ? 1.4476 1.9605 1.6612 0.1237  0.1082  0.3527  1026 LEU A CB    
6941 C  CG    . LEU A 923 ? 1.5678 2.0218 1.7398 0.1154  0.0981  0.3323  1026 LEU A CG    
6942 C  CD1   . LEU A 923 ? 1.0030 1.4670 1.1616 0.0964  0.0702  0.3185  1026 LEU A CD1   
6943 C  CD2   . LEU A 923 ? 1.6749 2.1144 1.8511 0.1306  0.1025  0.3391  1026 LEU A CD2   
6944 N  N     . ALA A 924 ? 1.4224 2.0218 1.7320 0.1564  0.1579  0.4029  1027 ALA A N     
6945 C  CA    . ALA A 924 ? 1.4899 2.1595 1.8528 0.1648  0.1598  0.4288  1027 ALA A CA    
6946 C  C     . ALA A 924 ? 1.6444 2.3685 2.0151 0.1494  0.1275  0.4311  1027 ALA A C     
6947 O  O     . ALA A 924 ? 1.8237 2.5954 2.2236 0.1563  0.1168  0.4507  1027 ALA A O     
6948 C  CB    . ALA A 924 ? 1.5745 2.2571 1.9737 0.1905  0.1773  0.4532  1027 ALA A CB    
6949 N  N     . LEU A 925 ? 1.4605 2.1745 1.8020 0.1273  0.1126  0.4106  1028 LEU A N     
6950 C  CA    . LEU A 925 ? 1.5008 2.2576 1.8422 0.1091  0.0840  0.4081  1028 LEU A CA    
6951 C  C     . LEU A 925 ? 1.6287 2.4551 2.0116 0.1052  0.0806  0.4277  1028 LEU A C     
6952 O  O     . LEU A 925 ? 1.6741 2.5403 2.0580 0.0887  0.0575  0.4276  1028 LEU A O     
6953 C  CB    . LEU A 925 ? 1.5478 2.2669 1.8455 0.0871  0.0712  0.3798  1028 LEU A CB    
6954 C  CG    . LEU A 925 ? 1.4009 2.0546 1.6582 0.0872  0.0691  0.3604  1028 LEU A CG    
6955 C  CD1   . LEU A 925 ? 1.4994 2.1237 1.7205 0.0652  0.0540  0.3361  1028 LEU A CD1   
6956 C  CD2   . LEU A 925 ? 1.4930 2.1558 1.7547 0.0951  0.0580  0.3666  1028 LEU A CD2   
6957 N  N     . ASP A 926 ? 1.6678 2.5093 2.0850 0.1189  0.1035  0.4445  1029 ASP A N     
6958 C  CA    . ASP A 926 ? 1.6041 2.5149 2.0682 0.1170  0.1012  0.4666  1029 ASP A CA    
6959 C  C     . ASP A 926 ? 1.4729 2.4323 1.9858 0.1366  0.1033  0.4992  1029 ASP A C     
6960 O  O     . ASP A 926 ? 1.5968 2.6184 2.1553 0.1368  0.1006  0.5223  1029 ASP A O     
6961 C  CB    . ASP A 926 ? 1.6493 2.5510 2.1265 0.1184  0.1259  0.4659  1029 ASP A CB    
6962 C  CG    . ASP A 926 ? 1.7098 2.5704 2.1412 0.0968  0.1219  0.4366  1029 ASP A CG    
6963 O  OD1   . ASP A 926 ? 1.6959 2.5638 2.1028 0.0768  0.0960  0.4229  1029 ASP A OD1   
6964 O  OD2   . ASP A 926 ? 1.7334 2.5530 2.1528 0.0995  0.1455  0.4276  1029 ASP A OD2   
6965 N  N     . LYS A 927 ? 1.2798 2.2129 1.7854 0.1526  0.1074  0.5027  1030 LYS A N     
6966 C  CA    . LYS A 927 ? 1.5611 2.5337 2.1101 0.1725  0.1099  0.5339  1030 LYS A CA    
6967 C  C     . LYS A 927 ? 1.2920 2.2748 1.8220 0.1662  0.0839  0.5336  1030 LYS A C     
6968 O  O     . LYS A 927 ? 1.2466 2.2029 1.7321 0.1482  0.0672  0.5086  1030 LYS A O     
6969 C  CB    . LYS A 927 ? 1.6195 2.5497 2.1801 0.1991  0.1431  0.5407  1030 LYS A CB    
6970 C  CG    . LYS A 927 ? 1.6940 2.6086 2.2711 0.2053  0.1731  0.5401  1030 LYS A CG    
6971 C  CD    . LYS A 927 ? 1.6657 2.5271 2.2441 0.2287  0.2079  0.5419  1030 LYS A CD    
6972 C  CE    . LYS A 927 ? 1.7366 2.5840 2.3337 0.2349  0.2410  0.5429  1030 LYS A CE    
6973 N  NZ    . LYS A 927 ? 1.5840 2.3779 2.1819 0.2570  0.2780  0.5447  1030 LYS A NZ    
6974 N  N     . THR A 928 ? 1.7037 2.7249 2.2690 0.1814  0.0815  0.5626  1031 THR A N     
6975 C  CA    . THR A 928 ? 1.9811 3.0141 2.5302 0.1762  0.0589  0.5655  1031 THR A CA    
6976 C  C     . THR A 928 ? 1.9067 2.8766 2.4276 0.1901  0.0712  0.5529  1031 THR A C     
6977 O  O     . THR A 928 ? 2.0391 2.9542 2.5459 0.1994  0.0939  0.5387  1031 THR A O     
6978 C  CB    . THR A 928 ? 1.9798 3.0830 2.5769 0.1840  0.0485  0.6035  1031 THR A CB    
6979 O  OG1   . THR A 928 ? 2.2256 3.3385 2.8012 0.1758  0.0261  0.6048  1031 THR A OG1   
6980 C  CG2   . THR A 928 ? 1.7182 2.8197 2.3594 0.2152  0.0752  0.6295  1031 THR A CG2   
6981 N  N     . GLU A 929 ? 1.7003 2.6766 2.2108 0.1901  0.0562  0.5582  1032 GLU A N     
6982 C  CA    . GLU A 929 ? 1.8588 2.7777 2.3422 0.2009  0.0655  0.5459  1032 GLU A CA    
6983 C  C     . GLU A 929 ? 1.7752 2.6769 2.2883 0.2297  0.0938  0.5649  1032 GLU A C     
6984 O  O     . GLU A 929 ? 1.5955 2.4358 2.0871 0.2385  0.1134  0.5489  1032 GLU A O     
6985 C  CB    . GLU A 929 ? 2.0569 2.9904 2.5244 0.1931  0.0436  0.5482  1032 GLU A CB    
6986 C  CG    . GLU A 929 ? 1.9839 2.8633 2.4273 0.2039  0.0520  0.5379  1032 GLU A CG    
6987 C  CD    . GLU A 929 ? 2.1878 3.0798 2.6126 0.1935  0.0311  0.5373  1032 GLU A CD    
6988 O  OE1   . GLU A 929 ? 2.3237 3.2488 2.7378 0.1718  0.0097  0.5324  1032 GLU A OE1   
6989 O  OE2   . GLU A 929 ? 2.1750 3.0424 2.5949 0.2061  0.0374  0.5413  1032 GLU A OE2   
6990 N  N     . GLN A 930 ? 1.6429 2.5975 2.2056 0.2440  0.0966  0.5996  1033 GLN A N     
6991 C  CA    . GLN A 930 ? 1.5001 2.4401 2.0960 0.2726  0.1253  0.6200  1033 GLN A CA    
6992 C  C     . GLN A 930 ? 1.5720 2.4913 2.1839 0.2810  0.1540  0.6161  1033 GLN A C     
6993 O  O     . GLN A 930 ? 1.6715 2.5416 2.2825 0.2985  0.1833  0.6134  1033 GLN A O     
6994 C  CB    . GLN A 930 ? 1.5776 2.5824 2.2251 0.2856  0.1183  0.6610  1033 GLN A CB    
6995 C  CG    . GLN A 930 ? 1.6782 2.6720 2.3670 0.3168  0.1490  0.6858  1033 GLN A CG    
6996 C  CD    . GLN A 930 ? 1.5324 2.4613 2.1903 0.3285  0.1636  0.6729  1033 GLN A CD    
6997 O  OE1   . GLN A 930 ? 1.8037 2.7151 2.4221 0.3164  0.1450  0.6574  1033 GLN A OE1   
6998 N  NE2   . GLN A 930 ? 1.5759 2.4677 2.2523 0.3513  0.1983  0.6790  1033 GLN A NE2   
6999 N  N     . GLU A 931 ? 1.6570 2.6113 2.2819 0.2675  0.1472  0.6153  1034 GLU A N     
7000 C  CA    . GLU A 931 ? 1.6677 2.6027 2.3068 0.2738  0.1753  0.6111  1034 GLU A CA    
7001 C  C     . GLU A 931 ? 1.6930 2.5494 2.2758 0.2654  0.1878  0.5742  1034 GLU A C     
7002 O  O     . GLU A 931 ? 1.5263 2.3418 2.1104 0.2766  0.2193  0.5695  1034 GLU A O     
7003 C  CB    . GLU A 931 ? 1.6819 2.6746 2.3472 0.2592  0.1632  0.6186  1034 GLU A CB    
7004 C  CG    . GLU A 931 ? 1.7571 2.7486 2.4567 0.2700  0.1943  0.6257  1034 GLU A CG    
7005 C  CD    . GLU A 931 ? 1.8947 2.9448 2.6208 0.2540  0.1810  0.6328  1034 GLU A CD    
7006 O  OE1   . GLU A 931 ? 1.9607 3.0522 2.6771 0.2339  0.1472  0.6325  1034 GLU A OE1   
7007 O  OE2   . GLU A 931 ? 1.9092 2.9627 2.6650 0.2605  0.2055  0.6383  1034 GLU A OE2   
7008 N  N     . ALA A 932 ? 1.8390 2.6726 2.3723 0.2453  0.1641  0.5485  1035 ALA A N     
7009 C  CA    . ALA A 932 ? 1.7685 2.5277 2.2487 0.2372  0.1723  0.5160  1035 ALA A CA    
7010 C  C     . ALA A 932 ? 1.7418 2.4477 2.2075 0.2537  0.1898  0.5140  1035 ALA A C     
7011 O  O     . ALA A 932 ? 1.7188 2.3606 2.1498 0.2522  0.2064  0.4932  1035 ALA A O     
7012 C  CB    . ALA A 932 ? 1.6242 2.3772 2.0621 0.2120  0.1417  0.4917  1035 ALA A CB    
7013 N  N     . LEU A 933 ? 1.4864 2.2167 1.9762 0.2680  0.1862  0.5354  1036 LEU A N     
7014 C  CA    . LEU A 933 ? 1.4594 2.1407 1.9385 0.2843  0.2042  0.5352  1036 LEU A CA    
7015 C  C     . LEU A 933 ? 1.7619 2.4179 2.2647 0.3046  0.2434  0.5457  1036 LEU A C     
7016 O  O     . LEU A 933 ? 1.8187 2.4083 2.2914 0.3085  0.2645  0.5297  1036 LEU A O     
7017 C  CB    . LEU A 933 ? 1.6550 2.3714 2.1551 0.2940  0.1905  0.5572  1036 LEU A CB    
7018 C  CG    . LEU A 933 ? 1.7434 2.4144 2.2359 0.3111  0.2076  0.5597  1036 LEU A CG    
7019 C  CD1   . LEU A 933 ? 1.2742 1.8825 1.7099 0.2970  0.2008  0.5270  1036 LEU A CD1   
7020 C  CD2   . LEU A 933 ? 1.6746 2.3898 2.1964 0.3223  0.1958  0.5875  1036 LEU A CD2   
7021 N  N     . GLU A 934 ? 1.7039 2.4114 2.2610 0.3169  0.2541  0.5728  1037 GLU A N     
7022 C  CA    . GLU A 934 ? 1.6819 2.3675 2.2673 0.3371  0.2945  0.5840  1037 GLU A CA    
7023 C  C     . GLU A 934 ? 1.6421 2.2784 2.1945 0.3256  0.3133  0.5579  1037 GLU A C     
7024 O  O     . GLU A 934 ? 1.7632 2.3516 2.3139 0.3377  0.3497  0.5552  1037 GLU A O     
7025 C  CB    . GLU A 934 ? 1.7137 2.4717 2.3710 0.3525  0.2997  0.6212  1037 GLU A CB    
7026 C  CG    . GLU A 934 ? 1.8224 2.6220 2.5164 0.3684  0.2888  0.6522  1037 GLU A CG    
7027 C  CD    . GLU A 934 ? 1.8203 2.7065 2.5529 0.3612  0.2577  0.6766  1037 GLU A CD    
7028 O  OE1   . GLU A 934 ? 1.9887 2.9016 2.7182 0.3429  0.2441  0.6675  1037 GLU A OE1   
7029 O  OE2   . GLU A 934 ? 1.7122 2.6387 2.4764 0.3724  0.2463  0.7051  1037 GLU A OE2   
7030 N  N     . TYR A 935 ? 1.4576 2.1027 1.9823 0.3017  0.2902  0.5387  1038 TYR A N     
7031 C  CA    . TYR A 935 ? 1.6070 2.2020 2.0941 0.2884  0.3051  0.5130  1038 TYR A CA    
7032 C  C     . TYR A 935 ? 1.5941 2.1061 2.0240 0.2846  0.3155  0.4879  1038 TYR A C     
7033 O  O     . TYR A 935 ? 1.9161 2.3740 2.3269 0.2870  0.3467  0.4775  1038 TYR A O     
7034 C  CB    . TYR A 935 ? 1.6607 2.2811 2.1279 0.2630  0.2752  0.4979  1038 TYR A CB    
7035 C  CG    . TYR A 935 ? 1.3638 1.9252 1.7797 0.2456  0.2833  0.4682  1038 TYR A CG    
7036 C  CD1   . TYR A 935 ? 1.6062 2.1571 2.0315 0.2466  0.3112  0.4678  1038 TYR A CD1   
7037 C  CD2   . TYR A 935 ? 1.6541 2.1705 2.0132 0.2277  0.2631  0.4416  1038 TYR A CD2   
7038 C  CE1   . TYR A 935 ? 1.4379 1.9332 1.8128 0.2293  0.3182  0.4414  1038 TYR A CE1   
7039 C  CE2   . TYR A 935 ? 1.8036 2.2666 2.1156 0.2110  0.2684  0.4167  1038 TYR A CE2   
7040 C  CZ    . TYR A 935 ? 1.4920 1.9439 1.8097 0.2113  0.2956  0.4165  1038 TYR A CZ    
7041 O  OH    . TYR A 935 ? 2.0051 2.4023 2.2725 0.1934  0.3005  0.3925  1038 TYR A OH    
7042 N  N     . PHE A 936 ? 1.5757 2.0759 1.9769 0.2772  0.2900  0.4780  1039 PHE A N     
7043 C  CA    . PHE A 936 ? 1.5553 1.9805 1.9051 0.2725  0.2967  0.4559  1039 PHE A CA    
7044 C  C     . PHE A 936 ? 1.9123 2.3040 2.2756 0.2947  0.3314  0.4675  1039 PHE A C     
7045 O  O     . PHE A 936 ? 2.0546 2.3786 2.3818 0.2923  0.3550  0.4512  1039 PHE A O     
7046 C  CB    . PHE A 936 ? 1.5204 1.9471 1.8456 0.2613  0.2623  0.4457  1039 PHE A CB    
7047 C  CG    . PHE A 936 ? 1.7478 2.1016 2.0207 0.2527  0.2637  0.4223  1039 PHE A CG    
7048 C  CD1   . PHE A 936 ? 1.9537 2.2616 2.1799 0.2326  0.2597  0.3970  1039 PHE A CD1   
7049 C  CD2   . PHE A 936 ? 1.6056 1.9374 1.8761 0.2637  0.2677  0.4266  1039 PHE A CD2   
7050 C  CE1   . PHE A 936 ? 1.7233 1.9662 1.9023 0.2230  0.2584  0.3773  1039 PHE A CE1   
7051 C  CE2   . PHE A 936 ? 1.7182 1.9846 1.9418 0.2542  0.2677  0.4057  1039 PHE A CE2   
7052 C  CZ    . PHE A 936 ? 1.6615 1.8843 1.8398 0.2335  0.2622  0.3814  1039 PHE A CZ    
7053 N  N     . MET A 937 ? 1.6875 2.1242 2.1013 0.3155  0.3353  0.4961  1040 MET A N     
7054 C  CA    . MET A 937 ? 1.6179 2.0255 2.0507 0.3385  0.3706  0.5098  1040 MET A CA    
7055 C  C     . MET A 937 ? 1.9422 2.3283 2.3898 0.3470  0.4109  0.5124  1040 MET A C     
7056 O  O     . MET A 937 ? 2.1416 2.4697 2.5761 0.3567  0.4453  0.5080  1040 MET A O     
7057 C  CB    . MET A 937 ? 1.6777 2.1446 2.1665 0.3590  0.3646  0.5434  1040 MET A CB    
7058 C  CG    . MET A 937 ? 1.6980 2.1857 2.1726 0.3511  0.3280  0.5422  1040 MET A CG    
7059 S  SD    . MET A 937 ? 1.7992 2.3575 2.3361 0.3728  0.3198  0.5835  1040 MET A SD    
7060 C  CE    . MET A 937 ? 1.9290 2.4383 2.4842 0.4009  0.3653  0.5970  1040 MET A CE    
7061 N  N     . LYS A 938 ? 2.2673 2.6975 2.7416 0.3427  0.4087  0.5189  1041 LYS A N     
7062 C  CA    . LYS A 938 ? 2.4063 2.8165 2.8948 0.3490  0.4479  0.5200  1041 LYS A CA    
7063 C  C     . LYS A 938 ? 2.4131 2.7427 2.8324 0.3300  0.4613  0.4860  1041 LYS A C     
7064 O  O     . LYS A 938 ? 2.5370 2.8092 2.9429 0.3372  0.5009  0.4804  1041 LYS A O     
7065 C  CB    . LYS A 938 ? 2.4589 2.9390 2.9927 0.3467  0.4390  0.5350  1041 LYS A CB    
7066 C  CG    . LYS A 938 ? 2.4504 2.9119 2.9961 0.3492  0.4771  0.5331  1041 LYS A CG    
7067 C  CD    . LYS A 938 ? 2.3566 2.8015 2.9445 0.3769  0.5234  0.5530  1041 LYS A CD    
7068 C  CE    . LYS A 938 ? 2.5585 3.0034 3.1750 0.3814  0.5607  0.5573  1041 LYS A CE    
7069 N  NZ    . LYS A 938 ? 2.5250 2.9082 3.0746 0.3573  0.5690  0.5230  1041 LYS A NZ    
7070 N  N     . GLN A 939 ? 2.1151 2.4379 2.4889 0.3047  0.4290  0.4634  1042 GLN A N     
7071 C  CA    . GLN A 939 ? 2.2030 2.4525 2.5102 0.2843  0.4373  0.4328  1042 GLN A CA    
7072 C  C     . GLN A 939 ? 2.1273 2.3058 2.3883 0.2830  0.4457  0.4183  1042 GLN A C     
7073 O  O     . GLN A 939 ? 2.1471 2.2556 2.3593 0.2721  0.4673  0.3985  1042 GLN A O     
7074 C  CB    . GLN A 939 ? 2.0086 2.2718 2.2837 0.2585  0.3985  0.4151  1042 GLN A CB    
7075 C  CG    . GLN A 939 ? 1.9249 2.2562 2.2405 0.2560  0.3883  0.4270  1042 GLN A CG    
7076 C  CD    . GLN A 939 ? 2.2483 2.5679 2.5766 0.2591  0.4253  0.4290  1042 GLN A CD    
7077 O  OE1   . GLN A 939 ? 2.5982 2.8488 2.8826 0.2520  0.4508  0.4112  1042 GLN A OE1   
7078 N  NE2   . GLN A 939 ? 2.1661 2.5530 2.5542 0.2686  0.4286  0.4509  1042 GLN A NE2   
7079 N  N     . MET A 940 ? 2.1106 2.3046 2.3840 0.2924  0.4289  0.4275  1043 MET A N     
7080 C  CA    . MET A 940 ? 2.0798 2.2090 2.3149 0.2925  0.4388  0.4160  1043 MET A CA    
7081 C  C     . MET A 940 ? 2.2819 2.3781 2.5360 0.3133  0.4872  0.4272  1043 MET A C     
7082 O  O     . MET A 940 ? 2.1909 2.2127 2.3995 0.3073  0.5101  0.4105  1043 MET A O     
7083 C  CB    . MET A 940 ? 1.9442 2.1003 2.1882 0.2961  0.4076  0.4227  1043 MET A CB    
7084 C  CG    . MET A 940 ? 2.0421 2.2057 2.2524 0.2728  0.3639  0.4047  1043 MET A CG    
7085 S  SD    . MET A 940 ? 2.1329 2.2085 2.2655 0.2490  0.3576  0.3723  1043 MET A SD    
7086 C  CE    . MET A 940 ? 2.2338 2.2836 2.3313 0.2283  0.3634  0.3543  1043 MET A CE    
7087 N  N     . ASN A 941 ? 2.3581 2.5081 2.6795 0.3373  0.5037  0.4561  1044 ASN A N     
7088 C  CA    . ASN A 941 ? 2.1740 2.2960 2.5217 0.3592  0.5526  0.4692  1044 ASN A CA    
7089 C  C     . ASN A 941 ? 2.2421 2.3244 2.5739 0.3534  0.5895  0.4575  1044 ASN A C     
7090 O  O     . ASN A 941 ? 2.4198 2.4565 2.7553 0.3661  0.6351  0.4599  1044 ASN A O     
7091 C  CB    . ASN A 941 ? 2.2497 2.4454 2.6797 0.3872  0.5568  0.5068  1044 ASN A CB    
7092 C  CG    . ASN A 941 ? 2.3507 2.5176 2.8130 0.4128  0.6060  0.5232  1044 ASN A CG    
7093 O  OD1   . ASN A 941 ? 2.3972 2.5360 2.8538 0.4229  0.6131  0.5267  1044 ASN A OD1   
7094 N  ND2   . ASN A 941 ? 2.2815 2.4547 2.7797 0.4237  0.6418  0.5334  1044 ASN A ND2   
7095 N  N     . ASP A 942 ? 2.4123 2.5089 2.7258 0.3341  0.5726  0.4449  1045 ASP A N     
7096 C  CA    . ASP A 942 ? 2.5815 2.6352 2.8707 0.3246  0.6057  0.4309  1045 ASP A CA    
7097 C  C     . ASP A 942 ? 2.7194 2.6839 2.9212 0.2994  0.6088  0.3976  1045 ASP A C     
7098 O  O     . ASP A 942 ? 2.8901 2.7907 3.0636 0.2973  0.6506  0.3868  1045 ASP A O     
7099 C  CB    . ASP A 942 ? 2.4926 2.6015 2.8023 0.3148  0.5876  0.4334  1045 ASP A CB    
7100 C  CG    . ASP A 942 ? 2.4492 2.6447 2.8463 0.3377  0.5885  0.4673  1045 ASP A CG    
7101 O  OD1   . ASP A 942 ? 2.6707 2.8730 3.1153 0.3633  0.6185  0.4891  1045 ASP A OD1   
7102 O  OD2   . ASP A 942 ? 2.4137 2.6704 2.8325 0.3295  0.5590  0.4729  1045 ASP A OD2   
7103 N  N     . ALA A 943 ? 2.4868 2.4454 2.6453 0.2794  0.5654  0.3817  1046 ALA A N     
7104 C  CA    . ALA A 943 ? 2.4105 2.2873 2.4883 0.2549  0.5635  0.3529  1046 ALA A CA    
7105 C  C     . ALA A 943 ? 2.4741 2.2928 2.5337 0.2635  0.5902  0.3508  1046 ALA A C     
7106 O  O     . ALA A 943 ? 2.4213 2.1627 2.4270 0.2508  0.6182  0.3326  1046 ALA A O     
7107 C  CB    . ALA A 943 ? 2.4083 2.2984 2.4546 0.2341  0.5102  0.3401  1046 ALA A CB    
7108 N  N     . HIS A 944 ? 2.5277 2.3808 2.6293 0.2837  0.5824  0.3691  1047 HIS A N     
7109 C  CA    . HIS A 944 ? 2.5341 2.3394 2.6288 0.2956  0.6097  0.3709  1047 HIS A CA    
7110 C  C     . HIS A 944 ? 2.6418 2.4742 2.8040 0.3268  0.6511  0.3974  1047 HIS A C     
7111 O  O     . HIS A 944 ? 2.5300 2.4307 2.7559 0.3483  0.6391  0.4237  1047 HIS A O     
7112 C  CB    . HIS A 944 ? 2.4641 2.2860 2.5595 0.2968  0.5744  0.3740  1047 HIS A CB    
7113 C  CG    . HIS A 944 ? 2.4581 2.2964 2.5217 0.2732  0.5237  0.3591  1047 HIS A CG    
7114 N  ND1   . HIS A 944 ? 2.4215 2.3351 2.5241 0.2778  0.4860  0.3721  1047 HIS A ND1   
7115 C  CD2   . HIS A 944 ? 2.6115 2.3997 2.6089 0.2445  0.5052  0.3332  1047 HIS A CD2   
7116 C  CE1   . HIS A 944 ? 2.5914 2.4995 2.6551 0.2541  0.4486  0.3541  1047 HIS A CE1   
7117 N  NE2   . HIS A 944 ? 2.7832 2.6174 2.7849 0.2342  0.4583  0.3314  1047 HIS A NE2   
7118 N  N     . HIS A 945 ? 2.7353 2.5134 2.8836 0.3287  0.7005  0.3910  1048 HIS A N     
7119 C  CA    . HIS A 945 ? 2.7116 2.5104 2.9258 0.3580  0.7453  0.4155  1048 HIS A CA    
7120 C  C     . HIS A 945 ? 2.7963 2.6131 3.0562 0.3844  0.7519  0.4385  1048 HIS A C     
7121 O  O     . HIS A 945 ? 2.7254 2.4778 2.9543 0.3854  0.7754  0.4297  1048 HIS A O     
7122 C  CB    . HIS A 945 ? 2.5255 2.2453 2.7044 0.3527  0.8008  0.3999  1048 HIS A CB    
7123 C  CG    . HIS A 945 ? 2.5079 2.2047 2.6387 0.3262  0.7979  0.3778  1048 HIS A CG    
7124 N  ND1   . HIS A 945 ? 2.8694 2.6087 3.0411 0.3319  0.8107  0.3880  1048 HIS A ND1   
7125 C  CD2   . HIS A 945 ? 2.4949 2.1311 2.5406 0.2933  0.7830  0.3472  1048 HIS A CD2   
7126 C  CE1   . HIS A 945 ? 2.7906 2.4947 2.9027 0.3039  0.8049  0.3639  1048 HIS A CE1   
7127 N  NE2   . HIS A 945 ? 2.7444 2.3859 2.7793 0.2801  0.7875  0.3395  1048 HIS A NE2   
7128 N  N     . GLY A 946 ? 3.0232 2.9263 3.3550 0.4046  0.7309  0.4682  1049 GLY A N     
7129 C  CA    . GLY A 946 ? 2.9252 2.8521 3.3017 0.4290  0.7320  0.4926  1049 GLY A CA    
7130 C  C     . GLY A 946 ? 2.8381 2.7528 3.1753 0.4172  0.6944  0.4817  1049 GLY A C     
7131 O  O     . GLY A 946 ? 3.0469 2.9383 3.3901 0.4306  0.7074  0.4896  1049 GLY A O     
7132 N  N     . GLY A 947 ? 2.6209 2.5502 2.9198 0.3927  0.6490  0.4640  1050 GLY A N     
7133 C  CA    . GLY A 947 ? 2.7000 2.6168 2.9619 0.3799  0.6134  0.4522  1050 GLY A CA    
7134 C  C     . GLY A 947 ? 2.8027 2.8007 3.1048 0.3860  0.5697  0.4708  1050 GLY A C     
7135 O  O     . GLY A 947 ? 2.6354 2.6367 2.9383 0.3905  0.5538  0.4761  1050 GLY A O     
7136 N  N     . TRP A 948 ? 2.8343 2.8968 3.1681 0.3847  0.5506  0.4805  1051 TRP A N     
7137 C  CA    . TRP A 948 ? 2.5756 2.7152 2.9431 0.3869  0.5088  0.4969  1051 TRP A CA    
7138 C  C     . TRP A 948 ? 2.4024 2.6138 2.8473 0.4112  0.5180  0.5327  1051 TRP A C     
7139 O  O     . TRP A 948 ? 2.2602 2.5324 2.7313 0.4067  0.4970  0.5412  1051 TRP A O     
7140 C  CB    . TRP A 948 ? 2.2685 2.4270 2.6044 0.3607  0.4708  0.4774  1051 TRP A CB    
7141 C  CG    . TRP A 948 ? 2.1496 2.2592 2.4222 0.3381  0.4475  0.4494  1051 TRP A CG    
7142 C  CD1   . TRP A 948 ? 2.1652 2.1948 2.3813 0.3248  0.4638  0.4252  1051 TRP A CD1   
7143 C  CD2   . TRP A 948 ? 2.1519 2.2898 2.4126 0.3253  0.4036  0.4435  1051 TRP A CD2   
7144 N  NE1   . TRP A 948 ? 2.1396 2.1489 2.3128 0.3050  0.4310  0.4062  1051 TRP A NE1   
7145 C  CE2   . TRP A 948 ? 2.1406 2.2150 2.3417 0.3058  0.3951  0.4166  1051 TRP A CE2   
7146 C  CE3   . TRP A 948 ? 2.0117 2.2214 2.3058 0.3273  0.3714  0.4583  1051 TRP A CE3   
7147 C  CZ2   . TRP A 948 ? 2.1216 2.2036 2.3011 0.2904  0.3569  0.4051  1051 TRP A CZ2   
7148 C  CZ3   . TRP A 948 ? 2.1294 2.3430 2.3974 0.3113  0.3354  0.4450  1051 TRP A CZ3   
7149 C  CH2   . TRP A 948 ? 2.2438 2.3947 2.4577 0.2940  0.3290  0.4190  1051 TRP A CH2   
7150 N  N     . THR A 949 ? 2.6303 2.8354 3.1131 0.4366  0.5490  0.5548  1052 THR A N     
7151 C  CA    . THR A 949 ? 2.7768 3.0507 3.3380 0.4613  0.5572  0.5927  1052 THR A CA    
7152 C  C     . THR A 949 ? 2.6879 3.0353 3.2751 0.4614  0.5122  0.6117  1052 THR A C     
7153 O  O     . THR A 949 ? 2.5895 2.9258 3.1406 0.4499  0.4847  0.5995  1052 THR A O     
7154 C  CB    . THR A 949 ? 2.8947 3.1387 3.4890 0.4887  0.6018  0.6120  1052 THR A CB    
7155 O  OG1   . THR A 949 ? 2.9252 3.0820 3.4731 0.4825  0.6406  0.5861  1052 THR A OG1   
7156 C  CG2   . THR A 949 ? 2.4437 2.7473 3.1206 0.5136  0.6218  0.6487  1052 THR A CG2   
7157 N  N     . THR A 950 ? 2.4529 2.8761 3.1034 0.4734  0.5053  0.6422  1053 THR A N     
7158 C  CA    . THR A 950 ? 2.2085 2.7058 2.8852 0.4721  0.4636  0.6627  1053 THR A CA    
7159 C  C     . THR A 950 ? 2.2602 2.7530 2.9433 0.4858  0.4598  0.6783  1053 THR A C     
7160 O  O     . THR A 950 ? 2.5135 3.0189 3.2468 0.5113  0.4830  0.7085  1053 THR A O     
7161 C  CB    . THR A 950 ? 1.9881 2.5660 2.7373 0.4845  0.4613  0.6974  1053 THR A CB    
7162 O  OG1   . THR A 950 ? 1.9325 2.5098 2.7381 0.5144  0.4996  0.7268  1053 THR A OG1   
7163 C  CG2   . THR A 950 ? 2.0180 2.6040 2.7626 0.4700  0.4641  0.6825  1053 THR A CG2   
7164 N  N     . GLN B 13  ? 2.4810 2.1520 3.1729 -0.5283 -0.8481 0.4774  12   GLN B N     
7165 C  CA    . GLN B 13  ? 2.6357 2.3285 3.3991 -0.5496 -0.8778 0.4968  12   GLN B CA    
7166 C  C     . GLN B 13  ? 2.6969 2.3655 3.4273 -0.5601 -0.8554 0.4805  12   GLN B C     
7167 O  O     . GLN B 13  ? 2.6864 2.3169 3.3527 -0.5980 -0.8779 0.4808  12   GLN B O     
7168 C  CB    . GLN B 13  ? 2.4667 2.2194 3.3594 -0.5211 -0.8734 0.5116  12   GLN B CB    
7169 C  CG    . GLN B 13  ? 2.3620 2.1431 3.3292 -0.5333 -0.9012 0.5350  12   GLN B CG    
7170 C  CD    . GLN B 13  ? 2.3643 2.2007 3.4547 -0.5007 -0.8895 0.5480  12   GLN B CD    
7171 O  OE1   . GLN B 13  ? 1.9818 1.8364 3.1137 -0.4746 -0.8540 0.5342  12   GLN B OE1   
7172 N  NE2   . GLN B 13  ? 2.4301 2.2905 3.5785 -0.5027 -0.9178 0.5751  12   GLN B NE2   
7173 N  N     . GLU B 14  ? 2.7167 2.4058 3.4893 -0.5274 -0.8104 0.4663  13   GLU B N     
7174 C  CA    . GLU B 14  ? 2.4468 2.1149 3.1936 -0.5315 -0.7826 0.4500  13   GLU B CA    
7175 C  C     . GLU B 14  ? 2.4666 2.1352 3.1963 -0.4903 -0.7240 0.4256  13   GLU B C     
7176 O  O     . GLU B 14  ? 2.2836 1.9900 3.0897 -0.4615 -0.6986 0.4248  13   GLU B O     
7177 C  CB    . GLU B 14  ? 2.3699 2.0714 3.2115 -0.5409 -0.7971 0.4656  13   GLU B CB    
7178 C  CG    . GLU B 14  ? 2.7402 2.4363 3.5885 -0.5869 -0.8545 0.4888  13   GLU B CG    
7179 C  CD    . GLU B 14  ? 2.7898 2.4299 3.5351 -0.6219 -0.8587 0.4762  13   GLU B CD    
7180 O  OE1   . GLU B 14  ? 2.7274 2.3378 3.4200 -0.6116 -0.8165 0.4518  13   GLU B OE1   
7181 O  OE2   . GLU B 14  ? 2.7850 2.4128 3.4908 -0.6495 -0.8954 0.4890  13   GLU B OE2   
7182 N  N     . LYS B 15  ? 2.5023 2.1283 3.1314 -0.4887 -0.7028 0.4064  14   LYS B N     
7183 C  CA    . LYS B 15  ? 2.3211 1.9463 2.9272 -0.4512 -0.6502 0.3850  14   LYS B CA    
7184 C  C     . LYS B 15  ? 2.1338 1.7564 2.7527 -0.4425 -0.6164 0.3735  14   LYS B C     
7185 O  O     . LYS B 15  ? 2.3362 1.9210 2.9035 -0.4671 -0.6173 0.3673  14   LYS B O     
7186 C  CB    . LYS B 15  ? 2.3948 1.9738 2.8918 -0.4544 -0.6377 0.3694  14   LYS B CB    
7187 C  CG    . LYS B 15  ? 2.3145 1.8894 2.7811 -0.4186 -0.5844 0.3483  14   LYS B CG    
7188 C  CD    . LYS B 15  ? 2.2481 1.8703 2.7784 -0.3823 -0.5692 0.3504  14   LYS B CD    
7189 C  CE    . LYS B 15  ? 2.5753 2.2020 3.0942 -0.3853 -0.5950 0.3589  14   LYS B CE    
7190 N  NZ    . LYS B 15  ? 2.7860 2.3684 3.2023 -0.3920 -0.5861 0.3459  14   LYS B NZ    
7191 N  N     . TYR B 16  ? 2.1761 1.8367 2.8615 -0.4086 -0.5857 0.3704  15   TYR B N     
7192 C  CA    . TYR B 16  ? 1.9118 1.5724 2.6114 -0.3959 -0.5494 0.3594  15   TYR B CA    
7193 C  C     . TYR B 16  ? 2.1230 1.8073 2.8399 -0.3536 -0.5058 0.3478  15   TYR B C     
7194 O  O     . TYR B 16  ? 2.0527 1.7801 2.8512 -0.3344 -0.5006 0.3548  15   TYR B O     
7195 C  CB    . TYR B 16  ? 1.9003 1.5889 2.6872 -0.4085 -0.5666 0.3740  15   TYR B CB    
7196 C  CG    . TYR B 16  ? 2.0957 1.7594 2.8624 -0.4524 -0.6067 0.3844  15   TYR B CG    
7197 C  CD1   . TYR B 16  ? 1.9180 1.5338 2.6084 -0.4725 -0.5964 0.3717  15   TYR B CD1   
7198 C  CD2   . TYR B 16  ? 2.2080 1.8956 3.0325 -0.4747 -0.6548 0.4077  15   TYR B CD2   
7199 C  CE1   . TYR B 16  ? 1.8865 1.4774 2.5541 -0.5154 -0.6329 0.3803  15   TYR B CE1   
7200 C  CE2   . TYR B 16  ? 2.1218 1.7877 2.9266 -0.5173 -0.6938 0.4184  15   TYR B CE2   
7201 C  CZ    . TYR B 16  ? 1.8666 1.4835 2.5908 -0.5385 -0.6827 0.4039  15   TYR B CZ    
7202 O  OH    . TYR B 16  ? 2.0533 1.6464 2.7535 -0.5836 -0.7215 0.4137  15   TYR B OH    
7203 N  N     . ARG B 17  ? 2.3393 1.9948 2.9798 -0.3402 -0.4743 0.3306  16   ARG B N     
7204 C  CA    . ARG B 17  ? 2.0993 1.7740 2.7459 -0.3023 -0.4329 0.3194  16   ARG B CA    
7205 C  C     . ARG B 17  ? 2.1332 1.8085 2.7963 -0.2909 -0.3989 0.3120  16   ARG B C     
7206 O  O     . ARG B 17  ? 2.0154 1.6548 2.6167 -0.2939 -0.3783 0.3011  16   ARG B O     
7207 C  CB    . ARG B 17  ? 2.1055 1.7523 2.6669 -0.2932 -0.4170 0.3071  16   ARG B CB    
7208 C  CG    . ARG B 17  ? 2.3981 2.0442 2.9406 -0.3023 -0.4470 0.3135  16   ARG B CG    
7209 C  CD    . ARG B 17  ? 2.4542 2.0747 2.9163 -0.2910 -0.4264 0.3005  16   ARG B CD    
7210 N  NE    . ARG B 17  ? 2.8041 2.4236 3.2473 -0.2990 -0.4531 0.3063  16   ARG B NE    
7211 C  CZ    . ARG B 17  ? 2.7760 2.3768 3.1558 -0.2915 -0.4412 0.2973  16   ARG B CZ    
7212 N  NH1   . ARG B 17  ? 2.5541 2.1367 2.8850 -0.2751 -0.4034 0.2830  16   ARG B NH1   
7213 N  NH2   . ARG B 17  ? 2.6320 2.2327 2.9993 -0.3007 -0.4675 0.3040  16   ARG B NH2   
7214 N  N     . LEU B 18  ? 1.9359 1.6506 2.6831 -0.2779 -0.3915 0.3181  17   LEU B N     
7215 C  CA    . LEU B 18  ? 1.3508 1.0692 2.1205 -0.2669 -0.3593 0.3123  17   LEU B CA    
7216 C  C     . LEU B 18  ? 1.5105 1.2398 2.2654 -0.2322 -0.3168 0.3006  17   LEU B C     
7217 O  O     . LEU B 18  ? 1.7633 1.5178 2.5355 -0.2140 -0.3135 0.3006  17   LEU B O     
7218 C  CB    . LEU B 18  ? 1.4968 1.2509 2.3647 -0.2710 -0.3699 0.3245  17   LEU B CB    
7219 C  CG    . LEU B 18  ? 1.4194 1.1725 2.3185 -0.3050 -0.4161 0.3402  17   LEU B CG    
7220 C  CD1   . LEU B 18  ? 1.3514 1.1398 2.3505 -0.3064 -0.4188 0.3514  17   LEU B CD1   
7221 C  CD2   . LEU B 18  ? 1.4386 1.1441 2.2646 -0.3340 -0.4276 0.3359  17   LEU B CD2   
7222 N  N     . VAL B 19  ? 1.3747 1.0844 2.0967 -0.2243 -0.2848 0.2912  18   VAL B N     
7223 C  CA    . VAL B 19  ? 1.4477 1.1650 2.1497 -0.1935 -0.2449 0.2816  18   VAL B CA    
7224 C  C     . VAL B 19  ? 1.3563 1.0844 2.0978 -0.1840 -0.2171 0.2805  18   VAL B C     
7225 O  O     . VAL B 19  ? 1.2808 0.9887 2.0220 -0.2008 -0.2185 0.2815  18   VAL B O     
7226 C  CB    . VAL B 19  ? 1.3976 1.0764 2.0093 -0.1902 -0.2296 0.2720  18   VAL B CB    
7227 C  CG1   . VAL B 19  ? 1.5499 1.2412 2.1461 -0.1584 -0.1914 0.2651  18   VAL B CG1   
7228 C  CG2   . VAL B 19  ? 1.2864 0.9506 1.8563 -0.2026 -0.2570 0.2729  18   VAL B CG2   
7229 N  N     . VAL B 20  ? 1.1499 0.9085 1.9234 -0.1586 -0.1916 0.2781  19   VAL B N     
7230 C  CA    . VAL B 20  ? 1.3145 1.0849 2.1241 -0.1478 -0.1622 0.2768  19   VAL B CA    
7231 C  C     . VAL B 20  ? 1.2722 1.0342 2.0299 -0.1242 -0.1259 0.2685  19   VAL B C     
7232 O  O     . VAL B 20  ? 1.1714 0.9560 1.9303 -0.1040 -0.1122 0.2658  19   VAL B O     
7233 C  CB    . VAL B 20  ? 1.3513 1.1635 2.2449 -0.1399 -0.1611 0.2817  19   VAL B CB    
7234 C  CG1   . VAL B 20  ? 1.0906 0.9113 2.0182 -0.1312 -0.1295 0.2799  19   VAL B CG1   
7235 C  CG2   . VAL B 20  ? 1.1037 0.9267 2.0521 -0.1621 -0.1996 0.2928  19   VAL B CG2   
7236 N  N     . VAL B 21  ? 1.4655 1.1949 2.1782 -0.1275 -0.1103 0.2652  20   VAL B N     
7237 C  CA    . VAL B 21  ? 1.3221 1.0417 1.9872 -0.1060 -0.0764 0.2600  20   VAL B CA    
7238 C  C     . VAL B 21  ? 1.2246 0.9506 1.9186 -0.0977 -0.0479 0.2605  20   VAL B C     
7239 O  O     . VAL B 21  ? 1.3555 1.0814 2.0921 -0.1123 -0.0535 0.2635  20   VAL B O     
7240 C  CB    . VAL B 21  ? 1.2237 0.8990 1.8139 -0.1126 -0.0747 0.2563  20   VAL B CB    
7241 C  CG1   . VAL B 21  ? 1.2136 0.8809 1.7729 -0.1222 -0.1019 0.2554  20   VAL B CG1   
7242 C  CG2   . VAL B 21  ? 1.2709 0.9141 1.8570 -0.1344 -0.0778 0.2567  20   VAL B CG2   
7243 N  N     . GLY B 22  ? 1.2150 0.9468 1.8857 -0.0748 -0.0174 0.2585  21   GLY B N     
7244 C  CA    . GLY B 22  ? 1.2668 1.0030 1.9573 -0.0659 0.0117  0.2595  21   GLY B CA    
7245 C  C     . GLY B 22  ? 1.1803 0.9349 1.8530 -0.0405 0.0388  0.2589  21   GLY B C     
7246 O  O     . GLY B 22  ? 1.1069 0.8724 1.7544 -0.0298 0.0348  0.2575  21   GLY B O     
7247 N  N     . GLY B 23  ? 1.1214 0.8793 1.8072 -0.0323 0.0660  0.2604  22   GLY B N     
7248 C  CA    . GLY B 23  ? 1.1060 0.8808 1.7751 -0.0106 0.0922  0.2614  22   GLY B CA    
7249 C  C     . GLY B 23  ? 1.3677 1.1803 2.0755 -0.0045 0.0908  0.2590  22   GLY B C     
7250 O  O     . GLY B 23  ? 1.1922 1.0188 1.9373 -0.0142 0.0685  0.2570  22   GLY B O     
7251 N  N     . GLY B 24  ? 1.5159 1.3442 2.2136 0.0115  0.1160  0.2597  23   GLY B N     
7252 C  CA    . GLY B 24  ? 1.4045 1.2653 2.1313 0.0174  0.1203  0.2562  23   GLY B CA    
7253 C  C     . GLY B 24  ? 1.5018 1.3736 2.2852 0.0116  0.1342  0.2547  23   GLY B C     
7254 O  O     . GLY B 24  ? 1.5380 1.3988 2.3205 0.0124  0.1555  0.2572  23   GLY B O     
7255 N  N     . GLY B 25  ? 1.6364 1.5291 2.4707 0.0059  0.1232  0.2511  24   GLY B N     
7256 C  CA    . GLY B 25  ? 1.4225 1.3277 2.3164 0.0011  0.1383  0.2493  24   GLY B CA    
7257 C  C     . GLY B 25  ? 1.4137 1.3052 2.3461 -0.0132 0.1332  0.2528  24   GLY B C     
7258 O  O     . GLY B 25  ? 1.4494 1.3475 2.4262 -0.0162 0.1518  0.2522  24   GLY B O     
7259 N  N     . VAL B 26  ? 1.2320 1.1033 2.1477 -0.0236 0.1091  0.2561  25   VAL B N     
7260 C  CA    . VAL B 26  ? 1.3696 1.2272 2.3199 -0.0400 0.1018  0.2596  25   VAL B CA    
7261 C  C     . VAL B 26  ? 1.0349 0.9113 2.0586 -0.0533 0.0795  0.2617  25   VAL B C     
7262 O  O     . VAL B 26  ? 1.0446 0.9185 2.1144 -0.0668 0.0768  0.2652  25   VAL B O     
7263 C  CB    . VAL B 26  ? 1.0764 0.9015 1.9770 -0.0487 0.0859  0.2619  25   VAL B CB    
7264 C  CG1   . VAL B 26  ? 1.1855 0.9924 2.0187 -0.0338 0.1091  0.2617  25   VAL B CG1   
7265 C  CG2   . VAL B 26  ? 1.1250 0.9495 2.0129 -0.0559 0.0516  0.2621  25   VAL B CG2   
7266 N  N     . GLY B 27  ? 1.0133 0.9090 2.0514 -0.0500 0.0636  0.2606  26   GLY B N     
7267 C  CA    . GLY B 27  ? 0.9997 0.9148 2.1096 -0.0607 0.0421  0.2646  26   GLY B CA    
7268 C  C     . GLY B 27  ? 1.0236 0.9351 2.1265 -0.0718 0.0017  0.2691  26   GLY B C     
7269 O  O     . GLY B 27  ? 1.0862 1.0090 2.2492 -0.0853 -0.0215 0.2760  26   GLY B O     
7270 N  N     . LYS B 28  ? 1.0078 0.9042 2.0408 -0.0671 -0.0073 0.2664  27   LYS B N     
7271 C  CA    . LYS B 28  ? 1.0124 0.9032 2.0333 -0.0784 -0.0445 0.2702  27   LYS B CA    
7272 C  C     . LYS B 28  ? 1.4955 1.4145 2.5667 -0.0759 -0.0583 0.2724  27   LYS B C     
7273 O  O     . LYS B 28  ? 1.1800 1.1029 2.2834 -0.0902 -0.0908 0.2799  27   LYS B O     
7274 C  CB    . LYS B 28  ? 1.2380 1.1076 2.1742 -0.0716 -0.0455 0.2659  27   LYS B CB    
7275 C  CG    . LYS B 28  ? 1.0511 0.8912 1.9357 -0.0713 -0.0282 0.2640  27   LYS B CG    
7276 C  CD    . LYS B 28  ? 1.0589 0.8827 1.8672 -0.0600 -0.0226 0.2603  27   LYS B CD    
7277 C  CE    . LYS B 28  ? 1.2936 1.1412 2.0938 -0.0385 -0.0016 0.2566  27   LYS B CE    
7278 N  NZ    . LYS B 28  ? 1.3286 1.1629 2.0588 -0.0265 0.0064  0.2547  27   LYS B NZ    
7279 N  N     . SER B 29  ? 1.4353 1.3732 2.5133 -0.0586 -0.0337 0.2664  28   SER B N     
7280 C  CA    . SER B 29  ? 1.2686 1.2306 2.3914 -0.0551 -0.0428 0.2673  28   SER B CA    
7281 C  C     . SER B 29  ? 1.3582 1.3388 2.5733 -0.0624 -0.0441 0.2736  28   SER B C     
7282 O  O     . SER B 29  ? 1.1600 1.1542 2.4235 -0.0688 -0.0685 0.2808  28   SER B O     
7283 C  CB    . SER B 29  ? 1.2339 1.2076 2.3313 -0.0365 -0.0147 0.2579  28   SER B CB    
7284 O  OG    . SER B 29  ? 0.9546 0.9143 1.9721 -0.0294 -0.0145 0.2539  28   SER B OG    
7285 N  N     . ALA B 30  ? 1.1546 1.1363 2.3973 -0.0615 -0.0176 0.2721  29   ALA B N     
7286 C  CA    . ALA B 30  ? 1.1456 1.1458 2.4804 -0.0677 -0.0149 0.2782  29   ALA B CA    
7287 C  C     . ALA B 30  ? 1.1299 1.1274 2.5020 -0.0881 -0.0520 0.2910  29   ALA B C     
7288 O  O     . ALA B 30  ? 1.1513 1.1685 2.6005 -0.0946 -0.0678 0.3005  29   ALA B O     
7289 C  CB    . ALA B 30  ? 0.9340 0.9337 2.2839 -0.0625 0.0243  0.2729  29   ALA B CB    
7290 N  N     . LEU B 31  ? 1.0682 1.0407 2.3866 -0.0992 -0.0662 0.2921  30   LEU B N     
7291 C  CA    . LEU B 31  ? 1.3101 1.2771 2.6549 -0.1220 -0.1029 0.3039  30   LEU B CA    
7292 C  C     . LEU B 31  ? 1.1334 1.1033 2.4731 -0.1300 -0.1427 0.3112  30   LEU B C     
7293 O  O     . LEU B 31  ? 1.0600 1.0394 2.4532 -0.1469 -0.1746 0.3243  30   LEU B O     
7294 C  CB    . LEU B 31  ? 1.3708 1.3057 2.6539 -0.1330 -0.1036 0.3013  30   LEU B CB    
7295 C  CG    . LEU B 31  ? 1.1206 1.0493 2.4160 -0.1318 -0.0718 0.2978  30   LEU B CG    
7296 C  CD1   . LEU B 31  ? 1.2605 1.1531 2.4833 -0.1407 -0.0720 0.2944  30   LEU B CD1   
7297 C  CD2   . LEU B 31  ? 1.0275 0.9760 2.4169 -0.1451 -0.0790 0.3078  30   LEU B CD2   
7298 N  N     . THR B 32  ? 0.9783 0.9405 2.2551 -0.1187 -0.1420 0.3039  31   THR B N     
7299 C  CA    . THR B 32  ? 1.2686 1.2300 2.5321 -0.1266 -0.1787 0.3103  31   THR B CA    
7300 C  C     . THR B 32  ? 1.1105 1.1026 2.4558 -0.1237 -0.1894 0.3191  31   THR B C     
7301 O  O     . THR B 32  ? 1.0432 1.0418 2.4281 -0.1396 -0.2258 0.3331  31   THR B O     
7302 C  CB    . THR B 32  ? 1.4624 1.4092 2.6410 -0.1142 -0.1714 0.2999  31   THR B CB    
7303 O  OG1   . THR B 32  ? 1.3615 1.2782 2.4679 -0.1174 -0.1627 0.2937  31   THR B OG1   
7304 C  CG2   . THR B 32  ? 1.0023 0.9474 2.1663 -0.1226 -0.2077 0.3062  31   THR B CG2   
7305 N  N     . ILE B 33  ? 1.1095 1.1196 2.4806 -0.1042 -0.1577 0.3117  32   ILE B N     
7306 C  CA    . ILE B 33  ? 1.0411 1.0779 2.4912 -0.0999 -0.1627 0.3190  32   ILE B CA    
7307 C  C     . ILE B 33  ? 1.0467 1.1011 2.5927 -0.1096 -0.1668 0.3313  32   ILE B C     
7308 O  O     . ILE B 33  ? 1.4389 1.5142 3.0594 -0.1115 -0.1826 0.3432  32   ILE B O     
7309 C  CB    . ILE B 33  ? 0.9363 0.9840 2.3842 -0.0782 -0.1246 0.3061  32   ILE B CB    
7310 C  CG1   . ILE B 33  ? 1.4178 1.4668 2.8782 -0.0702 -0.0826 0.2971  32   ILE B CG1   
7311 C  CG2   . ILE B 33  ? 0.8896 0.9231 2.2469 -0.0694 -0.1230 0.2956  32   ILE B CG2   
7312 C  CD1   . ILE B 33  ? 1.0095 1.0669 2.4634 -0.0520 -0.0444 0.2841  32   ILE B CD1   
7313 N  N     . GLN B 34  ? 1.2342 1.2810 2.7829 -0.1156 -0.1525 0.3296  33   GLN B N     
7314 C  CA    . GLN B 34  ? 1.1261 1.1895 2.7655 -0.1272 -0.1588 0.3423  33   GLN B CA    
7315 C  C     . GLN B 34  ? 1.1496 1.2141 2.8118 -0.1502 -0.2102 0.3604  33   GLN B C     
7316 O  O     . GLN B 34  ? 1.3095 1.3966 3.0627 -0.1591 -0.2255 0.3760  33   GLN B O     
7317 C  CB    . GLN B 34  ? 1.4000 1.4521 3.0289 -0.1297 -0.1319 0.3357  33   GLN B CB    
7318 C  CG    . GLN B 34  ? 1.5188 1.5911 3.2472 -0.1377 -0.1269 0.3461  33   GLN B CG    
7319 C  CD    . GLN B 34  ? 1.4534 1.5480 3.2491 -0.1202 -0.0898 0.3419  33   GLN B CD    
7320 O  OE1   . GLN B 34  ? 1.5669 1.6566 3.3215 -0.1026 -0.0583 0.3274  33   GLN B OE1   
7321 N  NE2   . GLN B 34  ? 0.9816 1.1003 2.8815 -0.1258 -0.0929 0.3550  33   GLN B NE2   
7322 N  N     . PHE B 35  ? 1.2729 1.3132 2.8542 -0.1610 -0.2370 0.3593  34   PHE B N     
7323 C  CA    . PHE B 35  ? 1.4523 1.4892 3.0429 -0.1860 -0.2869 0.3760  34   PHE B CA    
7324 C  C     . PHE B 35  ? 1.4893 1.5448 3.1204 -0.1855 -0.3156 0.3890  34   PHE B C     
7325 O  O     . PHE B 35  ? 1.7482 1.8145 3.4286 -0.2046 -0.3550 0.4083  34   PHE B O     
7326 C  CB    . PHE B 35  ? 1.1887 1.1885 2.6739 -0.1990 -0.3019 0.3688  34   PHE B CB    
7327 C  CG    . PHE B 35  ? 1.1560 1.1465 2.6387 -0.2287 -0.3518 0.3843  34   PHE B CG    
7328 C  CD1   . PHE B 35  ? 1.3534 1.3476 2.8826 -0.2501 -0.3673 0.3953  34   PHE B CD1   
7329 C  CD2   . PHE B 35  ? 1.2288 1.2060 2.6606 -0.2370 -0.3833 0.3879  34   PHE B CD2   
7330 C  CE1   . PHE B 35  ? 1.4673 1.4526 2.9913 -0.2802 -0.4148 0.4100  34   PHE B CE1   
7331 C  CE2   . PHE B 35  ? 1.4600 1.4266 2.8845 -0.2668 -0.4298 0.4023  34   PHE B CE2   
7332 C  CZ    . PHE B 35  ? 1.5702 1.5410 3.0401 -0.2891 -0.4463 0.4136  34   PHE B CZ    
7333 N  N     . ILE B 36  ? 1.5380 1.5978 3.1504 -0.1648 -0.2971 0.3796  35   ILE B N     
7334 C  CA    . ILE B 36  ? 1.6776 1.7531 3.3255 -0.1619 -0.3198 0.3906  35   ILE B CA    
7335 C  C     . ILE B 36  ? 1.4418 1.5469 3.1827 -0.1442 -0.2930 0.3927  35   ILE B C     
7336 O  O     . ILE B 36  ? 1.2006 1.3288 3.0328 -0.1503 -0.3122 0.4114  35   ILE B O     
7337 C  CB    . ILE B 36  ? 1.7483 1.8052 3.3063 -0.1540 -0.3221 0.3795  35   ILE B CB    
7338 C  CG1   . ILE B 36  ? 1.3680 1.3938 2.8384 -0.1733 -0.3503 0.3790  35   ILE B CG1   
7339 C  CG2   . ILE B 36  ? 2.0027 2.0759 3.6002 -0.1490 -0.3408 0.3900  35   ILE B CG2   
7340 C  CD1   . ILE B 36  ? 1.2083 1.2089 2.5974 -0.1676 -0.3207 0.3604  35   ILE B CD1   
7341 N  N     . ALA B 37  ? 1.5608 1.6650 3.2801 -0.1228 -0.2478 0.3741  36   ALA B N     
7342 C  CA    . ALA B 37  ? 1.4478 1.5749 3.2459 -0.1064 -0.2175 0.3730  36   ALA B CA    
7343 C  C     . ALA B 37  ? 1.1372 1.2805 3.0209 -0.1092 -0.2001 0.3792  36   ALA B C     
7344 O  O     . ALA B 37  ? 1.3318 1.4967 3.3039 -0.1005 -0.1843 0.3850  36   ALA B O     
7345 C  CB    . ALA B 37  ? 1.1212 1.2403 2.8646 -0.0860 -0.1741 0.3507  36   ALA B CB    
7346 N  N     . SER B 38  ? 1.3777 1.5098 3.2381 -0.1211 -0.2010 0.3780  37   SER B N     
7347 C  CA    . SER B 38  ? 1.2559 1.4019 3.1936 -0.1260 -0.1858 0.3840  37   SER B CA    
7348 C  C     . SER B 38  ? 1.1281 1.2826 3.1001 -0.1063 -0.1312 0.3703  37   SER B C     
7349 O  O     . SER B 38  ? 0.9415 1.1165 3.0092 -0.1048 -0.1161 0.3780  37   SER B O     
7350 C  CB    . SER B 38  ? 1.1781 1.3490 3.2173 -0.1399 -0.2220 0.4096  37   SER B CB    
7351 O  OG    . SER B 38  ? 1.1357 1.2966 3.1386 -0.1618 -0.2730 0.4224  37   SER B OG    
7352 N  N     . TYR B 39  ? 1.2392 1.3773 3.1320 -0.0921 -0.1008 0.3502  38   TYR B N     
7353 C  CA    . TYR B 39  ? 1.1314 1.2724 3.0388 -0.0760 -0.0481 0.3352  38   TYR B CA    
7354 C  C     . TYR B 39  ? 1.1683 1.2860 2.9763 -0.0708 -0.0232 0.3174  38   TYR B C     
7355 O  O     . TYR B 39  ? 1.2510 1.3528 2.9735 -0.0702 -0.0384 0.3120  38   TYR B O     
7356 C  CB    . TYR B 39  ? 0.8667 1.0176 2.7978 -0.0613 -0.0337 0.3308  38   TYR B CB    
7357 C  CG    . TYR B 39  ? 0.9449 1.0803 2.7838 -0.0488 -0.0123 0.3117  38   TYR B CG    
7358 C  CD1   . TYR B 39  ? 0.8392 0.9653 2.6105 -0.0494 -0.0412 0.3114  38   TYR B CD1   
7359 C  CD2   . TYR B 39  ? 0.8383 0.9687 2.6586 -0.0374 0.0366  0.2945  38   TYR B CD2   
7360 C  CE1   . TYR B 39  ? 1.3752 1.4898 3.0665 -0.0385 -0.0225 0.2951  38   TYR B CE1   
7361 C  CE2   . TYR B 39  ? 1.0257 1.1442 2.7634 -0.0276 0.0540  0.2786  38   TYR B CE2   
7362 C  CZ    . TYR B 39  ? 1.3965 1.5083 3.0721 -0.0278 0.0241  0.2793  38   TYR B CZ    
7363 O  OH    . TYR B 39  ? 1.0743 1.1766 2.6714 -0.0186 0.0406  0.2646  38   TYR B OH    
7364 N  N     . PHE B 40  ? 1.0614 1.1771 2.8826 -0.0675 0.0148  0.3095  39   PHE B N     
7365 C  CA    . PHE B 40  ? 1.3934 1.4881 3.1276 -0.0627 0.0398  0.2951  39   PHE B CA    
7366 C  C     . PHE B 40  ? 1.1274 1.2189 2.8159 -0.0464 0.0722  0.2793  39   PHE B C     
7367 O  O     . PHE B 40  ? 1.3246 1.4281 3.0644 -0.0386 0.0980  0.2751  39   PHE B O     
7368 C  CB    . PHE B 40  ? 1.2107 1.3034 2.9763 -0.0671 0.0667  0.2942  39   PHE B CB    
7369 C  CG    . PHE B 40  ? 0.9885 1.0600 2.6709 -0.0614 0.0956  0.2809  39   PHE B CG    
7370 C  CD1   . PHE B 40  ? 1.2334 1.2845 2.8371 -0.0667 0.0764  0.2809  39   PHE B CD1   
7371 C  CD2   . PHE B 40  ? 1.1895 1.2603 2.8729 -0.0515 0.1426  0.2693  39   PHE B CD2   
7372 C  CE1   . PHE B 40  ? 1.1611 1.1935 2.6927 -0.0604 0.1028  0.2710  39   PHE B CE1   
7373 C  CE2   . PHE B 40  ? 1.2677 1.3199 2.8753 -0.0468 0.1673  0.2596  39   PHE B CE2   
7374 C  CZ    . PHE B 40  ? 0.9285 0.9623 2.4623 -0.0505 0.1469  0.2612  39   PHE B CZ    
7375 N  N     . VAL B 41  ? 0.8771 0.9517 2.4690 -0.0420 0.0715  0.2707  40   VAL B N     
7376 C  CA    . VAL B 41  ? 1.3161 1.3878 2.8546 -0.0286 0.0974  0.2568  40   VAL B CA    
7377 C  C     . VAL B 41  ? 0.9829 1.0419 2.4722 -0.0240 0.1336  0.2467  40   VAL B C     
7378 O  O     . VAL B 41  ? 1.6469 1.6945 3.1182 -0.0301 0.1316  0.2502  40   VAL B O     
7379 C  CB    . VAL B 41  ? 1.3546 1.4196 2.8227 -0.0262 0.0696  0.2560  40   VAL B CB    
7380 C  CG1   . VAL B 41  ? 1.2145 1.2598 2.5960 -0.0269 0.0656  0.2534  40   VAL B CG1   
7381 C  CG2   . VAL B 41  ? 1.3732 1.4443 2.8224 -0.0149 0.0879  0.2453  40   VAL B CG2   
7382 N  N     . THR B 42  ? 0.9478 1.0078 2.4144 -0.0143 0.1671  0.2346  41   THR B N     
7383 C  CA    . THR B 42  ? 1.0529 1.1020 2.4735 -0.0104 0.2032  0.2257  41   THR B CA    
7384 C  C     . THR B 42  ? 1.4302 1.4723 2.7602 -0.0021 0.2100  0.2173  41   THR B C     
7385 O  O     . THR B 42  ? 1.4982 1.5310 2.7812 0.0010  0.2363  0.2120  41   THR B O     
7386 C  CB    . THR B 42  ? 1.5616 1.6165 3.0386 -0.0092 0.2441  0.2188  41   THR B CB    
7387 O  OG1   . THR B 42  ? 1.6467 1.6893 3.0730 -0.0069 0.2785  0.2108  41   THR B OG1   
7388 C  CG2   . THR B 42  ? 1.4407 1.5051 2.9361 -0.0037 0.2545  0.2111  41   THR B CG2   
7389 N  N     . ASP B 43  ? 1.7172 1.7640 3.0223 0.0012  0.1870  0.2170  42   ASP B N     
7390 C  CA    . ASP B 43  ? 1.4920 1.5347 2.7146 0.0085  0.1920  0.2102  42   ASP B CA    
7391 C  C     . ASP B 43  ? 1.4677 1.4975 2.6262 0.0089  0.1730  0.2162  42   ASP B C     
7392 O  O     . ASP B 43  ? 1.5106 1.5336 2.6845 0.0023  0.1492  0.2248  42   ASP B O     
7393 C  CB    . ASP B 43  ? 1.4195 1.4720 2.6400 0.0115  0.1770  0.2070  42   ASP B CB    
7394 C  CG    . ASP B 43  ? 1.6363 1.6899 2.8708 0.0073  0.1340  0.2170  42   ASP B CG    
7395 O  OD1   . ASP B 43  ? 1.5479 1.5958 2.8030 0.0003  0.1155  0.2262  42   ASP B OD1   
7396 O  OD2   . ASP B 43  ? 2.0209 2.0801 3.2434 0.0096  0.1185  0.2155  42   ASP B OD2   
7397 N  N     . TYR B 44  ? 1.6738 1.6997 2.7599 0.0160  0.1844  0.2119  43   TYR B N     
7398 C  CA    . TYR B 44  ? 1.3844 1.3976 2.4062 0.0188  0.1711  0.2173  43   TYR B CA    
7399 C  C     . TYR B 44  ? 1.4846 1.5028 2.4607 0.0238  0.1520  0.2161  43   TYR B C     
7400 O  O     . TYR B 44  ? 1.3246 1.3457 2.2470 0.0309  0.1641  0.2127  43   TYR B O     
7401 C  CB    . TYR B 44  ? 1.4802 1.4855 2.4591 0.0234  0.2002  0.2164  43   TYR B CB    
7402 C  CG    . TYR B 44  ? 1.7585 1.7468 2.6905 0.0252  0.1918  0.2242  43   TYR B CG    
7403 C  CD1   . TYR B 44  ? 1.5321 1.5134 2.4340 0.0258  0.1627  0.2288  43   TYR B CD1   
7404 C  CD2   . TYR B 44  ? 1.4860 1.4629 2.4031 0.0262  0.2151  0.2268  43   TYR B CD2   
7405 C  CE1   . TYR B 44  ? 1.5024 1.4650 2.3619 0.0274  0.1585  0.2352  43   TYR B CE1   
7406 C  CE2   . TYR B 44  ? 1.1088 1.0680 1.9846 0.0284  0.2097  0.2341  43   TYR B CE2   
7407 C  CZ    . TYR B 44  ? 1.5130 1.4646 2.3607 0.0292  0.1821  0.2380  43   TYR B CZ    
7408 O  OH    . TYR B 44  ? 1.7236 1.6545 2.5305 0.0313  0.1798  0.2446  43   TYR B OH    
7409 N  N     . ASP B 45  ? 1.5585 1.5782 2.5576 0.0192  0.1211  0.2196  44   ASP B N     
7410 C  CA    . ASP B 45  ? 1.4887 1.5109 2.4467 0.0226  0.1004  0.2192  44   ASP B CA    
7411 C  C     . ASP B 45  ? 1.5066 1.5120 2.4138 0.0225  0.0829  0.2256  44   ASP B C     
7412 O  O     . ASP B 45  ? 1.2812 1.2756 2.2075 0.0137  0.0606  0.2315  44   ASP B O     
7413 C  CB    . ASP B 45  ? 1.2474 1.2778 2.2536 0.0171  0.0767  0.2205  44   ASP B CB    
7414 C  CG    . ASP B 45  ? 1.6408 1.6747 2.6068 0.0203  0.0587  0.2188  44   ASP B CG    
7415 O  OD1   . ASP B 45  ? 1.6668 1.7000 2.5714 0.0275  0.0671  0.2159  44   ASP B OD1   
7416 O  OD2   . ASP B 45  ? 1.4677 1.5056 2.4650 0.0156  0.0358  0.2215  44   ASP B OD2   
7417 N  N     . PRO B 46  ? 1.0211 1.0233 1.8646 0.0312  0.0926  0.2252  45   PRO B N     
7418 C  CA    . PRO B 46  ? 1.0294 1.0134 1.8258 0.0320  0.0790  0.2312  45   PRO B CA    
7419 C  C     . PRO B 46  ? 1.2603 1.2391 2.0508 0.0264  0.0468  0.2329  45   PRO B C     
7420 O  O     . PRO B 46  ? 1.3636 1.3515 2.1295 0.0309  0.0397  0.2304  45   PRO B O     
7421 C  CB    . PRO B 46  ? 1.5966 1.5849 2.3342 0.0441  0.0967  0.2311  45   PRO B CB    
7422 C  CG    . PRO B 46  ? 1.4586 1.4622 2.2130 0.0467  0.1236  0.2260  45   PRO B CG    
7423 C  CD    . PRO B 46  ? 1.5192 1.5336 2.3317 0.0398  0.1174  0.2202  45   PRO B CD    
7424 N  N     . THR B 47  ? 1.4444 1.4080 2.2563 0.0150  0.0271  0.2375  46   THR B N     
7425 C  CA    . THR B 47  ? 1.1225 1.0787 1.9299 0.0065  -0.0051 0.2400  46   THR B CA    
7426 C  C     . THR B 47  ? 0.9299 0.8710 1.6679 0.0112  -0.0103 0.2405  46   THR B C     
7427 O  O     . THR B 47  ? 1.1843 1.1124 1.8846 0.0171  0.0053  0.2419  46   THR B O     
7428 C  CB    . THR B 47  ? 0.9317 0.8742 1.7756 -0.0094 -0.0251 0.2458  46   THR B CB    
7429 O  OG1   . THR B 47  ? 1.2143 1.1714 2.1258 -0.0123 -0.0153 0.2463  46   THR B OG1   
7430 C  CG2   . THR B 47  ? 0.9334 0.8714 1.7811 -0.0208 -0.0603 0.2494  46   THR B CG2   
7431 N  N     . ILE B 48  ? 1.2014 1.1441 1.9242 0.0089  -0.0310 0.2399  47   ILE B N     
7432 C  CA    . ILE B 48  ? 1.2265 1.1529 1.8879 0.0113  -0.0380 0.2405  47   ILE B CA    
7433 C  C     . ILE B 48  ? 1.1504 1.0532 1.8083 -0.0053 -0.0670 0.2440  47   ILE B C     
7434 O  O     . ILE B 48  ? 1.3860 1.2623 2.0126 -0.0106 -0.0674 0.2458  47   ILE B O     
7435 C  CB    . ILE B 48  ? 1.0242 0.9680 1.6626 0.0204  -0.0380 0.2370  47   ILE B CB    
7436 C  CG1   . ILE B 48  ? 0.9072 0.8728 1.5426 0.0342  -0.0098 0.2340  47   ILE B CG1   
7437 C  CG2   . ILE B 48  ? 0.9872 0.9136 1.5669 0.0220  -0.0457 0.2381  47   ILE B CG2   
7438 C  CD1   . ILE B 48  ? 0.9444 0.9286 1.5577 0.0416  -0.0090 0.2304  47   ILE B CD1   
7439 N  N     . GLU B 49  ? 1.0095 0.9204 1.6985 -0.0145 -0.0911 0.2453  48   GLU B N     
7440 C  CA    . GLU B 49  ? 1.2502 1.1411 1.9434 -0.0335 -0.1217 0.2503  48   GLU B CA    
7441 C  C     . GLU B 49  ? 1.2303 1.1397 1.9789 -0.0406 -0.1433 0.2540  48   GLU B C     
7442 O  O     . GLU B 49  ? 1.2679 1.1877 2.0086 -0.0364 -0.1506 0.2524  48   GLU B O     
7443 C  CB    . GLU B 49  ? 1.5143 1.3805 2.1417 -0.0374 -0.1327 0.2493  48   GLU B CB    
7444 C  CG    . GLU B 49  ? 1.5983 1.4365 2.2168 -0.0598 -0.1612 0.2540  48   GLU B CG    
7445 C  CD    . GLU B 49  ? 1.9666 1.7764 2.5161 -0.0648 -0.1687 0.2517  48   GLU B CD    
7446 O  OE1   . GLU B 49  ? 2.4060 2.2240 2.9261 -0.0521 -0.1599 0.2480  48   GLU B OE1   
7447 O  OE2   . GLU B 49  ? 1.5399 1.3182 2.0642 -0.0826 -0.1827 0.2533  48   GLU B OE2   
7448 N  N     . ASP B 50  ? 1.3111 1.2247 2.1172 -0.0512 -0.1532 0.2598  49   ASP B N     
7449 C  CA    . ASP B 50  ? 1.0486 0.9793 1.9165 -0.0585 -0.1746 0.2663  49   ASP B CA    
7450 C  C     . ASP B 50  ? 1.1430 1.0572 2.0236 -0.0808 -0.2089 0.2764  49   ASP B C     
7451 O  O     . ASP B 50  ? 1.3230 1.2199 2.1942 -0.0905 -0.2091 0.2779  49   ASP B O     
7452 C  CB    . ASP B 50  ? 1.0378 0.9933 1.9753 -0.0508 -0.1543 0.2659  49   ASP B CB    
7453 C  CG    . ASP B 50  ? 1.2893 1.2588 2.2099 -0.0317 -0.1195 0.2557  49   ASP B CG    
7454 O  OD1   . ASP B 50  ? 1.3700 1.3395 2.2432 -0.0240 -0.1173 0.2507  49   ASP B OD1   
7455 O  OD2   . ASP B 50  ? 1.3205 1.3008 2.2744 -0.0256 -0.0946 0.2530  49   ASP B OD2   
7456 N  N     . SER B 51  ? 1.3130 1.2320 2.2138 -0.0900 -0.2384 0.2837  50   SER B N     
7457 C  CA    . SER B 51  ? 1.2845 1.1894 2.1956 -0.1135 -0.2757 0.2953  50   SER B CA    
7458 C  C     . SER B 51  ? 1.4499 1.3795 2.4520 -0.1191 -0.2918 0.3073  50   SER B C     
7459 O  O     . SER B 51  ? 1.4046 1.3576 2.4492 -0.1071 -0.2850 0.3077  50   SER B O     
7460 C  CB    . SER B 51  ? 1.2942 1.1813 2.1511 -0.1227 -0.3011 0.2969  50   SER B CB    
7461 O  OG    . SER B 51  ? 1.4298 1.3027 2.2943 -0.1478 -0.3391 0.3090  50   SER B OG    
7462 N  N     . TYR B 52  ? 1.5258 1.4498 2.5588 -0.1378 -0.3125 0.3176  51   TYR B N     
7463 C  CA    . TYR B 52  ? 1.2593 1.2065 2.3827 -0.1457 -0.3316 0.3323  51   TYR B CA    
7464 C  C     . TYR B 52  ? 1.4104 1.3429 2.5319 -0.1738 -0.3763 0.3469  51   TYR B C     
7465 O  O     . TYR B 52  ? 1.3083 1.2120 2.3707 -0.1888 -0.3844 0.3440  51   TYR B O     
7466 C  CB    . TYR B 52  ? 1.1904 1.1536 2.3744 -0.1395 -0.3062 0.3313  51   TYR B CB    
7467 C  CG    . TYR B 52  ? 1.2432 1.2222 2.4359 -0.1144 -0.2629 0.3183  51   TYR B CG    
7468 C  CD1   . TYR B 52  ? 1.2486 1.2542 2.5076 -0.1026 -0.2532 0.3205  51   TYR B CD1   
7469 C  CD2   . TYR B 52  ? 1.4267 1.3925 2.5608 -0.1033 -0.2313 0.3044  51   TYR B CD2   
7470 C  CE1   . TYR B 52  ? 1.3288 1.3459 2.5907 -0.0825 -0.2133 0.3078  51   TYR B CE1   
7471 C  CE2   . TYR B 52  ? 1.1472 1.1270 2.2857 -0.0829 -0.1937 0.2936  51   TYR B CE2   
7472 C  CZ    . TYR B 52  ? 1.1395 1.1441 2.3397 -0.0735 -0.1848 0.2946  51   TYR B CZ    
7473 O  OH    . TYR B 52  ? 1.4809 1.4968 2.6805 -0.0559 -0.1470 0.2829  51   TYR B OH    
7474 N  N     . THR B 53  ? 1.5067 1.4584 2.6928 -0.1815 -0.4052 0.3633  52   THR B N     
7475 C  CA    . THR B 53  ? 1.6921 1.6342 2.8839 -0.2097 -0.4520 0.3806  52   THR B CA    
7476 C  C     . THR B 53  ? 1.7249 1.6967 3.0237 -0.2164 -0.4679 0.3990  52   THR B C     
7477 O  O     . THR B 53  ? 1.4335 1.4341 2.8038 -0.1994 -0.4546 0.4027  52   THR B O     
7478 C  CB    . THR B 53  ? 1.4862 1.4195 2.6421 -0.2158 -0.4803 0.3865  52   THR B CB    
7479 O  OG1   . THR B 53  ? 1.4534 1.4133 2.6601 -0.1957 -0.4697 0.3882  52   THR B OG1   
7480 C  CG2   . THR B 53  ? 1.5863 1.4863 2.6337 -0.2148 -0.4694 0.3703  52   THR B CG2   
7481 N  N     . LYS B 54  ? 1.5086 1.4728 2.8190 -0.2418 -0.4955 0.4107  53   LYS B N     
7482 C  CA    . LYS B 54  ? 1.7677 1.7608 3.1816 -0.2512 -0.5147 0.4309  53   LYS B CA    
7483 C  C     . LYS B 54  ? 1.8641 1.8436 3.2670 -0.2865 -0.5640 0.4481  53   LYS B C     
7484 O  O     . LYS B 54  ? 1.3102 1.2601 2.6478 -0.3036 -0.5667 0.4404  53   LYS B O     
7485 C  CB    . LYS B 54  ? 1.7097 1.7168 3.1731 -0.2406 -0.4792 0.4239  53   LYS B CB    
7486 C  CG    . LYS B 54  ? 1.7717 1.8112 3.3496 -0.2487 -0.4950 0.4446  53   LYS B CG    
7487 C  CD    . LYS B 54  ? 1.3125 1.3654 2.9387 -0.2359 -0.4546 0.4360  53   LYS B CD    
7488 C  CE    . LYS B 54  ? 1.6697 1.7572 3.4172 -0.2422 -0.4677 0.4571  53   LYS B CE    
7489 N  NZ    . LYS B 54  ? 1.7185 1.8187 3.5155 -0.2297 -0.4258 0.4484  53   LYS B NZ    
7490 N  N     . GLN B 55  ? 1.8721 1.8723 3.3384 -0.2979 -0.6026 0.4720  54   GLN B N     
7491 C  CA    . GLN B 55  ? 1.7151 1.7072 3.1810 -0.3336 -0.6539 0.4922  54   GLN B CA    
7492 C  C     . GLN B 55  ? 1.4634 1.4760 3.0083 -0.3449 -0.6576 0.5034  54   GLN B C     
7493 O  O     . GLN B 55  ? 1.1743 1.2239 2.8228 -0.3302 -0.6467 0.5137  54   GLN B O     
7494 C  CB    . GLN B 55  ? 1.6528 1.6603 3.1568 -0.3412 -0.6952 0.5158  54   GLN B CB    
7495 C  CG    . GLN B 55  ? 1.9841 1.9860 3.4896 -0.3763 -0.7496 0.5398  54   GLN B CG    
7496 C  CD    . GLN B 55  ? 2.0029 1.9592 3.3944 -0.4068 -0.7709 0.5312  54   GLN B CD    
7497 O  OE1   . GLN B 55  ? 2.1827 2.1236 3.5471 -0.4327 -0.7953 0.5386  54   GLN B OE1   
7498 N  NE2   . GLN B 55  ? 2.0148 1.9442 3.3186 -0.3947 -0.7525 0.5124  54   GLN B NE2   
7499 N  N     . CYS B 56  ? 1.6420 1.6296 3.1387 -0.3716 -0.6712 0.5012  55   CYS B N     
7500 C  CA    . CYS B 56  ? 1.7735 1.7766 3.3350 -0.3857 -0.6751 0.5104  55   CYS B CA    
7501 C  C     . CYS B 56  ? 1.6295 1.6196 3.1618 -0.4179 -0.7240 0.5278  55   CYS B C     
7502 O  O     . CYS B 56  ? 1.5371 1.4929 2.9812 -0.4403 -0.7491 0.5255  55   CYS B O     
7503 C  CB    . CYS B 56  ? 1.5877 1.5691 3.1021 -0.3781 -0.6318 0.4861  55   CYS B CB    
7504 S  SG    . CYS B 56  ? 2.2191 2.2134 3.7461 -0.3318 -0.5660 0.4633  55   CYS B SG    
7505 N  N     . VAL B 57  ? 1.8624 1.8779 3.4644 -0.4188 -0.7349 0.5449  56   VAL B N     
7506 C  CA    . VAL B 57  ? 2.0384 2.0449 3.6185 -0.4477 -0.7794 0.5633  56   VAL B CA    
7507 C  C     . VAL B 57  ? 2.0165 2.0270 3.6225 -0.4591 -0.7705 0.5615  56   VAL B C     
7508 O  O     . VAL B 57  ? 2.3148 2.3279 3.9285 -0.4798 -0.8029 0.5789  56   VAL B O     
7509 C  CB    . VAL B 57  ? 2.1219 2.1541 3.7628 -0.4406 -0.8105 0.5928  56   VAL B CB    
7510 C  CG1   . VAL B 57  ? 2.2396 2.2624 3.8441 -0.4334 -0.8223 0.5950  56   VAL B CG1   
7511 C  CG2   . VAL B 57  ? 1.7293 1.8019 3.4867 -0.4116 -0.7846 0.6013  56   VAL B CG2   
7512 N  N     . ILE B 58  ? 1.8612 1.8715 3.4802 -0.4462 -0.7262 0.5411  57   ILE B N     
7513 C  CA    . ILE B 58  ? 2.1868 2.1974 3.8250 -0.4571 -0.7140 0.5372  57   ILE B CA    
7514 C  C     . ILE B 58  ? 2.3805 2.3486 3.9228 -0.4942 -0.7367 0.5309  57   ILE B C     
7515 O  O     . ILE B 58  ? 2.1977 2.1667 3.7501 -0.5139 -0.7508 0.5380  57   ILE B O     
7516 C  CB    . ILE B 58  ? 2.0902 2.1054 3.7566 -0.4347 -0.6590 0.5168  57   ILE B CB    
7517 C  CG1   . ILE B 58  ? 1.8271 1.8819 3.5839 -0.3993 -0.6349 0.5218  57   ILE B CG1   
7518 C  CG2   . ILE B 58  ? 2.0766 2.0918 3.7650 -0.4454 -0.6447 0.5132  57   ILE B CG2   
7519 C  CD1   . ILE B 58  ? 1.8266 1.9182 3.6786 -0.3920 -0.6488 0.5447  57   ILE B CD1   
7520 N  N     . ASP B 59  ? 2.2904 2.2190 3.7376 -0.5049 -0.7394 0.5172  58   ASP B N     
7521 C  CA    . ASP B 59  ? 2.4545 2.3370 3.8022 -0.5409 -0.7614 0.5110  58   ASP B CA    
7522 C  C     . ASP B 59  ? 2.6800 2.5688 4.0219 -0.5637 -0.8137 0.5348  58   ASP B C     
7523 O  O     . ASP B 59  ? 2.6935 2.6179 4.1017 -0.5501 -0.8332 0.5564  58   ASP B O     
7524 C  CB    . ASP B 59  ? 2.2465 2.0842 3.4970 -0.5440 -0.7501 0.4922  58   ASP B CB    
7525 C  CG    . ASP B 59  ? 2.3226 2.1039 3.4679 -0.5771 -0.7542 0.4782  58   ASP B CG    
7526 O  OD1   . ASP B 59  ? 2.3676 2.1367 3.5134 -0.5842 -0.7331 0.4687  58   ASP B OD1   
7527 O  OD2   . ASP B 59  ? 2.3832 2.1300 3.4433 -0.5958 -0.7764 0.4762  58   ASP B OD2   
7528 N  N     . ASP B 60  ? 3.1027 2.9532 4.3620 -0.5994 -0.8354 0.5313  59   ASP B N     
7529 C  CA    . ASP B 60  ? 2.9824 2.8347 4.2281 -0.6249 -0.8851 0.5541  59   ASP B CA    
7530 C  C     . ASP B 60  ? 3.0012 2.8505 4.2179 -0.6227 -0.9126 0.5664  59   ASP B C     
7531 O  O     . ASP B 60  ? 3.0731 2.9302 4.2945 -0.6382 -0.9538 0.5906  59   ASP B O     
7532 C  CB    . ASP B 60  ? 3.1177 2.9240 4.2702 -0.6653 -0.8985 0.5444  59   ASP B CB    
7533 C  CG    . ASP B 60  ? 3.4075 3.1572 4.4410 -0.6788 -0.8894 0.5223  59   ASP B CG    
7534 O  OD1   . ASP B 60  ? 3.2775 3.0207 4.3042 -0.6552 -0.8580 0.5070  59   ASP B OD1   
7535 O  OD2   . ASP B 60  ? 3.6963 3.4064 4.6419 -0.7134 -0.9126 0.5204  59   ASP B OD2   
7536 N  N     . ARG B 61  ? 2.6977 2.5349 3.8846 -0.6046 -0.8911 0.5516  60   ARG B N     
7537 C  CA    . ARG B 61  ? 2.5886 2.4236 3.7509 -0.5999 -0.9133 0.5619  60   ARG B CA    
7538 C  C     . ARG B 61  ? 2.0864 1.9458 3.3020 -0.5616 -0.8807 0.5541  60   ARG B C     
7539 O  O     . ARG B 61  ? 1.9782 1.8648 3.2668 -0.5382 -0.8475 0.5478  60   ARG B O     
7540 C  CB    . ARG B 61  ? 2.7208 2.4994 3.7532 -0.6290 -0.9264 0.5489  60   ARG B CB    
7541 C  CG    . ARG B 61  ? 2.8990 2.6520 3.8739 -0.6688 -0.9608 0.5578  60   ARG B CG    
7542 C  CD    . ARG B 61  ? 2.9649 2.6570 3.8070 -0.6966 -0.9655 0.5409  60   ARG B CD    
7543 N  NE    . ARG B 61  ? 3.1286 2.7939 3.9120 -0.7363 -0.9952 0.5475  60   ARG B NE    
7544 C  CZ    . ARG B 61  ? 3.1658 2.7749 3.8309 -0.7667 -1.0015 0.5342  60   ARG B CZ    
7545 N  NH1   . ARG B 61  ? 3.0516 2.6238 3.6432 -0.7622 -0.9804 0.5138  60   ARG B NH1   
7546 N  NH2   . ARG B 61  ? 3.1972 2.7854 3.8161 -0.8028 -1.0283 0.5416  60   ARG B NH2   
7547 N  N     . ALA B 62  ? 1.8417 1.6909 3.0196 -0.5557 -0.8891 0.5544  61   ALA B N     
7548 C  CA    . ALA B 62  ? 1.9324 1.8002 3.1489 -0.5223 -0.8588 0.5453  61   ALA B CA    
7549 C  C     . ALA B 62  ? 2.1619 1.9987 3.3222 -0.5192 -0.8193 0.5155  61   ALA B C     
7550 O  O     . ALA B 62  ? 2.1274 1.9235 3.2125 -0.5429 -0.8162 0.5020  61   ALA B O     
7551 C  CB    . ALA B 62  ? 1.7074 1.5738 2.9021 -0.5181 -0.8818 0.5564  61   ALA B CB    
7552 N  N     . ALA B 63  ? 1.7469 1.6004 2.9379 -0.4862 -0.7849 0.5048  62   ALA B N     
7553 C  CA    . ALA B 63  ? 1.8394 1.6664 2.9598 -0.4630 -0.7330 0.4747  62   ALA B CA    
7554 C  C     . ALA B 63  ? 1.9885 1.8311 3.1143 -0.4255 -0.7049 0.4659  62   ALA B C     
7555 O  O     . ALA B 63  ? 1.8998 1.7841 3.1173 -0.4030 -0.6957 0.4744  62   ALA B O     
7556 C  CB    . ALA B 63  ? 1.6704 1.5074 2.8314 -0.4533 -0.6994 0.4655  62   ALA B CB    
7557 N  N     . ARG B 64  ? 2.0284 1.8372 3.0574 -0.4197 -0.6904 0.4487  63   ARG B N     
7558 C  CA    . ARG B 64  ? 1.9870 1.8059 3.0069 -0.3849 -0.6592 0.4366  63   ARG B CA    
7559 C  C     . ARG B 64  ? 2.0648 1.8726 3.0504 -0.3612 -0.6064 0.4123  63   ARG B C     
7560 O  O     . ARG B 64  ? 2.2587 2.0301 3.1525 -0.3611 -0.5889 0.3954  63   ARG B O     
7561 C  CB    . ARG B 64  ? 2.1417 1.9331 3.0815 -0.3933 -0.6769 0.4348  63   ARG B CB    
7562 C  CG    . ARG B 64  ? 2.4749 2.2827 3.4549 -0.4091 -0.7248 0.4597  63   ARG B CG    
7563 C  CD    . ARG B 64  ? 2.2787 2.1289 3.3405 -0.3784 -0.7135 0.4664  63   ARG B CD    
7564 N  NE    . ARG B 64  ? 2.2438 2.0871 3.2581 -0.3494 -0.6752 0.4456  63   ARG B NE    
7565 C  CZ    . ARG B 64  ? 2.2662 2.0929 3.2231 -0.3493 -0.6837 0.4432  63   ARG B CZ    
7566 N  NH1   . ARG B 64  ? 2.2105 2.0234 3.1456 -0.3764 -0.7287 0.4599  63   ARG B NH1   
7567 N  NH2   . ARG B 64  ? 2.4583 2.2821 3.3780 -0.3225 -0.6468 0.4243  63   ARG B NH2   
7568 N  N     . LEU B 65  ? 1.9199 1.7593 2.9814 -0.3412 -0.5802 0.4114  64   LEU B N     
7569 C  CA    . LEU B 65  ? 2.0365 1.8683 3.0740 -0.3200 -0.5316 0.3913  64   LEU B CA    
7570 C  C     . LEU B 65  ? 1.9020 1.7404 2.9146 -0.2877 -0.4989 0.3774  64   LEU B C     
7571 O  O     . LEU B 65  ? 1.7659 1.6380 2.8421 -0.2681 -0.4914 0.3818  64   LEU B O     
7572 C  CB    . LEU B 65  ? 1.9773 1.8388 3.1035 -0.3133 -0.5164 0.3961  64   LEU B CB    
7573 C  CG    . LEU B 65  ? 1.5966 1.4563 2.7571 -0.3450 -0.5468 0.4103  64   LEU B CG    
7574 C  CD1   . LEU B 65  ? 1.2413 1.1278 2.4824 -0.3345 -0.5222 0.4113  64   LEU B CD1   
7575 C  CD2   . LEU B 65  ? 1.6379 1.4492 2.7030 -0.3704 -0.5542 0.4014  64   LEU B CD2   
7576 N  N     . ASP B 66  ? 1.8468 1.6525 2.7678 -0.2827 -0.4787 0.3607  65   ASP B N     
7577 C  CA    . ASP B 66  ? 1.9728 1.7830 2.8627 -0.2533 -0.4460 0.3469  65   ASP B CA    
7578 C  C     . ASP B 66  ? 1.8917 1.6996 2.7706 -0.2344 -0.4016 0.3324  65   ASP B C     
7579 O  O     . ASP B 66  ? 1.9952 1.7701 2.8044 -0.2383 -0.3873 0.3219  65   ASP B O     
7580 C  CB    . ASP B 66  ? 2.3450 2.1226 3.1442 -0.2601 -0.4548 0.3404  65   ASP B CB    
7581 C  CG    . ASP B 66  ? 2.1883 1.9662 2.9937 -0.2798 -0.4992 0.3554  65   ASP B CG    
7582 O  OD1   . ASP B 66  ? 2.3243 2.1363 3.2061 -0.2746 -0.5139 0.3684  65   ASP B OD1   
7583 O  OD2   . ASP B 66  ? 2.0799 1.8224 2.8133 -0.3010 -0.5185 0.3545  65   ASP B OD2   
7584 N  N     . ILE B 67  ? 1.5450 1.3864 2.4925 -0.2143 -0.3789 0.3324  66   ILE B N     
7585 C  CA    . ILE B 67  ? 1.6669 1.5094 2.6133 -0.1976 -0.3381 0.3211  66   ILE B CA    
7586 C  C     . ILE B 67  ? 1.6571 1.5014 2.5596 -0.1710 -0.3058 0.3078  66   ILE B C     
7587 O  O     . ILE B 67  ? 1.4155 1.2798 2.3342 -0.1585 -0.3066 0.3081  66   ILE B O     
7588 C  CB    . ILE B 67  ? 1.4999 1.3756 2.5414 -0.1917 -0.3288 0.3278  66   ILE B CB    
7589 C  CG1   . ILE B 67  ? 1.2427 1.1216 2.3353 -0.2190 -0.3655 0.3440  66   ILE B CG1   
7590 C  CG2   . ILE B 67  ? 1.5614 1.4343 2.5975 -0.1781 -0.2882 0.3172  66   ILE B CG2   
7591 C  CD1   . ILE B 67  ? 1.2363 1.1482 2.4284 -0.2145 -0.3571 0.3521  66   ILE B CD1   
7592 N  N     . LEU B 68  ? 1.3710 1.1945 2.2188 -0.1628 -0.2774 0.2967  67   LEU B N     
7593 C  CA    . LEU B 68  ? 1.5726 1.3979 2.3770 -0.1385 -0.2462 0.2855  67   LEU B CA    
7594 C  C     . LEU B 68  ? 1.1724 1.0062 1.9925 -0.1226 -0.2090 0.2798  67   LEU B C     
7595 O  O     . LEU B 68  ? 1.3740 1.1846 2.1665 -0.1280 -0.1977 0.2772  67   LEU B O     
7596 C  CB    . LEU B 68  ? 1.3205 1.1105 2.0364 -0.1427 -0.2469 0.2792  67   LEU B CB    
7597 C  CG    . LEU B 68  ? 1.4514 1.2307 2.1345 -0.1540 -0.2762 0.2820  67   LEU B CG    
7598 C  CD1   . LEU B 68  ? 1.5263 1.2874 2.2149 -0.1850 -0.3145 0.2917  67   LEU B CD1   
7599 C  CD2   . LEU B 68  ? 1.2182 0.9713 1.8186 -0.1467 -0.2610 0.2726  67   LEU B CD2   
7600 N  N     . ASP B 69  ? 1.0260 0.8906 1.8880 -0.1041 -0.1894 0.2777  68   ASP B N     
7601 C  CA    . ASP B 69  ? 1.0597 0.9332 1.9318 -0.0882 -0.1524 0.2720  68   ASP B CA    
7602 C  C     . ASP B 69  ? 1.4619 1.3252 2.2643 -0.0715 -0.1289 0.2637  68   ASP B C     
7603 O  O     . ASP B 69  ? 1.1779 1.0572 1.9698 -0.0579 -0.1223 0.2600  68   ASP B O     
7604 C  CB    . ASP B 69  ? 1.0019 0.9097 1.9444 -0.0777 -0.1402 0.2727  68   ASP B CB    
7605 C  CG    . ASP B 69  ? 1.3320 1.2474 2.2845 -0.0640 -0.1021 0.2671  68   ASP B CG    
7606 O  OD1   . ASP B 69  ? 1.1396 1.0349 2.0572 -0.0647 -0.0886 0.2652  68   ASP B OD1   
7607 O  OD2   . ASP B 69  ? 1.3176 1.2575 2.3115 -0.0529 -0.0848 0.2646  68   ASP B OD2   
7608 N  N     . THR B 70  ? 1.2995 1.1364 2.0561 -0.0726 -0.1160 0.2614  69   THR B N     
7609 C  CA    . THR B 70  ? 1.1822 1.0066 1.8729 -0.0580 -0.0961 0.2560  69   THR B CA    
7610 C  C     . THR B 70  ? 1.1511 0.9925 1.8474 -0.0379 -0.0609 0.2532  69   THR B C     
7611 O  O     . THR B 70  ? 1.3372 1.1944 2.0829 -0.0367 -0.0493 0.2541  69   THR B O     
7612 C  CB    . THR B 70  ? 1.1990 0.9834 1.8364 -0.0686 -0.0976 0.2556  69   THR B CB    
7613 O  OG1   . THR B 70  ? 1.2203 0.9947 1.8793 -0.0751 -0.0867 0.2572  69   THR B OG1   
7614 C  CG2   . THR B 70  ? 1.1693 0.9344 1.7916 -0.0905 -0.1324 0.2578  69   THR B CG2   
7615 N  N     . ALA B 71  ? 1.0606 0.8983 1.7051 -0.0229 -0.0438 0.2505  70   ALA B N     
7616 C  CA    . ALA B 71  ? 1.0151 0.8688 1.6551 -0.0043 -0.0127 0.2493  70   ALA B CA    
7617 C  C     . ALA B 71  ? 1.1096 0.9416 1.7296 -0.0021 0.0082  0.2515  70   ALA B C     
7618 O  O     . ALA B 71  ? 1.0642 0.8653 1.6586 -0.0122 0.0014  0.2526  70   ALA B O     
7619 C  CB    . ALA B 71  ? 1.2130 1.0767 1.8102 0.0105  -0.0060 0.2476  70   ALA B CB    
7620 N  N     . GLY B 72  ? 1.0242 0.8711 1.6544 0.0104  0.0347  0.2521  71   GLY B N     
7621 C  CA    . GLY B 72  ? 1.0449 0.8736 1.6570 0.0147  0.0573  0.2553  71   GLY B CA    
7622 C  C     . GLY B 72  ? 1.4599 1.3035 2.0496 0.0339  0.0842  0.2578  71   GLY B C     
7623 O  O     . GLY B 72  ? 1.7580 1.5981 2.3510 0.0384  0.1063  0.2609  71   GLY B O     
7624 N  N     . GLN B 73  ? 1.2602 1.1208 1.8264 0.0441  0.0819  0.2571  72   GLN B N     
7625 C  CA    . GLN B 73  ? 1.3980 1.2764 1.9413 0.0606  0.1034  0.2607  72   GLN B CA    
7626 C  C     . GLN B 73  ? 1.6754 1.5374 2.1671 0.0719  0.1129  0.2677  72   GLN B C     
7627 O  O     . GLN B 73  ? 2.0037 1.8804 2.4749 0.0858  0.1296  0.2736  72   GLN B O     
7628 C  CB    . GLN B 73  ? 1.6261 1.5349 2.1755 0.0645  0.0964  0.2565  72   GLN B CB    
7629 C  CG    . GLN B 73  ? 1.5273 1.4521 2.1301 0.0547  0.0886  0.2498  72   GLN B CG    
7630 C  CD    . GLN B 73  ? 2.0850 2.0195 2.7164 0.0556  0.1115  0.2492  72   GLN B CD    
7631 O  OE1   . GLN B 73  ? 2.1004 2.0387 2.7812 0.0464  0.1094  0.2455  72   GLN B OE1   
7632 N  NE2   . GLN B 73  ? 2.2262 2.1648 2.8276 0.0664  0.1338  0.2537  72   GLN B NE2   
7633 N  N     . GLU B 74  ? 1.6495 1.4813 2.1202 0.0657  0.1028  0.2677  73   GLU B N     
7634 C  CA    . GLU B 74  ? 1.8936 1.7049 2.3179 0.0758  0.1132  0.2739  73   GLU B CA    
7635 C  C     . GLU B 74  ? 1.7435 1.5738 2.1415 0.0878  0.1106  0.2761  73   GLU B C     
7636 O  O     . GLU B 74  ? 2.1154 1.9302 2.4778 0.0963  0.1174  0.2812  73   GLU B O     
7637 C  CB    . GLU B 74  ? 1.8218 1.6254 2.2372 0.0865  0.1400  0.2826  73   GLU B CB    
7638 C  CG    . GLU B 74  ? 2.1278 1.8996 2.5536 0.0752  0.1451  0.2817  73   GLU B CG    
7639 C  CD    . GLU B 74  ? 2.0879 1.8197 2.4823 0.0685  0.1402  0.2805  73   GLU B CD    
7640 O  OE1   . GLU B 74  ? 1.9022 1.6290 2.2630 0.0770  0.1400  0.2825  73   GLU B OE1   
7641 O  OE2   . GLU B 74  ? 2.2704 1.9747 2.6732 0.0538  0.1375  0.2772  73   GLU B OE2   
7642 N  N     . GLU B 75  ? 1.5636 1.4266 1.9799 0.0883  0.1021  0.2723  74   GLU B N     
7643 C  CA    . GLU B 75  ? 1.5657 1.4474 1.9600 0.0966  0.0963  0.2731  74   GLU B CA    
7644 C  C     . GLU B 75  ? 1.4748 1.3468 1.8654 0.0856  0.0723  0.2660  74   GLU B C     
7645 O  O     . GLU B 75  ? 1.7045 1.5839 2.0710 0.0914  0.0676  0.2667  74   GLU B O     
7646 C  CB    . GLU B 75  ? 1.4748 1.3949 1.8854 0.1015  0.1003  0.2722  74   GLU B CB    
7647 C  CG    . GLU B 75  ? 1.5571 1.4889 2.0094 0.0891  0.0881  0.2626  74   GLU B CG    
7648 C  CD    . GLU B 75  ? 1.9194 1.8854 2.3806 0.0927  0.0916  0.2597  74   GLU B CD    
7649 O  OE1   . GLU B 75  ? 2.0227 2.0044 2.4551 0.1022  0.0951  0.2639  74   GLU B OE1   
7650 O  OE2   . GLU B 75  ? 2.1404 2.1169 2.6381 0.0853  0.0916  0.2532  74   GLU B OE2   
7651 N  N     . PHE B 76  ? 1.5032 1.3596 1.9176 0.0693  0.0564  0.2601  75   PHE B N     
7652 C  CA    . PHE B 76  ? 1.5891 1.4316 1.9978 0.0562  0.0318  0.2549  75   PHE B CA    
7653 C  C     . PHE B 76  ? 1.6172 1.4176 2.0033 0.0452  0.0281  0.2548  75   PHE B C     
7654 O  O     . PHE B 76  ? 1.4024 1.1864 1.7927 0.0279  0.0058  0.2507  75   PHE B O     
7655 C  CB    . PHE B 76  ? 1.2291 1.0879 1.6838 0.0440  0.0126  0.2498  75   PHE B CB    
7656 C  CG    . PHE B 76  ? 1.1923 1.0881 1.6719 0.0527  0.0200  0.2484  75   PHE B CG    
7657 C  CD1   . PHE B 76  ? 1.2272 1.1428 1.6887 0.0604  0.0179  0.2473  75   PHE B CD1   
7658 C  CD2   . PHE B 76  ? 1.3271 1.2365 1.8471 0.0517  0.0301  0.2475  75   PHE B CD2   
7659 C  CE1   . PHE B 76  ? 1.4668 1.4139 1.9475 0.0661  0.0253  0.2449  75   PHE B CE1   
7660 C  CE2   . PHE B 76  ? 1.6410 1.5804 2.1799 0.0578  0.0391  0.2449  75   PHE B CE2   
7661 C  CZ    . PHE B 76  ? 1.7574 1.7152 2.2754 0.0645  0.0364  0.2433  75   PHE B CZ    
7662 N  N     . GLY B 77  ? 1.5202 1.3015 1.8813 0.0541  0.0498  0.2597  76   GLY B N     
7663 C  CA    . GLY B 77  ? 1.6656 1.4031 2.0016 0.0434  0.0506  0.2587  76   GLY B CA    
7664 C  C     . GLY B 77  ? 1.7662 1.4798 2.0636 0.0362  0.0387  0.2551  76   GLY B C     
7665 O  O     . GLY B 77  ? 1.5932 1.2693 1.8723 0.0195  0.0308  0.2514  76   GLY B O     
7666 N  N     . ALA B 78  ? 1.4835 1.2166 1.7661 0.0470  0.0378  0.2558  77   ALA B N     
7667 C  CA    . ALA B 78  ? 1.5378 1.2494 1.7848 0.0393  0.0265  0.2517  77   ALA B CA    
7668 C  C     . ALA B 78  ? 1.7556 1.4600 2.0148 0.0164  -0.0048 0.2456  77   ALA B C     
7669 O  O     . ALA B 78  ? 1.9997 1.6735 2.2258 0.0028  -0.0160 0.2417  77   ALA B O     
7670 C  CB    . ALA B 78  ? 1.5670 1.3059 1.8017 0.0555  0.0315  0.2543  77   ALA B CB    
7671 N  N     . MET B 79  ? 1.6467 1.3779 1.9532 0.0115  -0.0185 0.2453  78   MET B N     
7672 C  CA    . MET B 79  ? 1.4221 1.1492 1.7489 -0.0098 -0.0491 0.2424  78   MET B CA    
7673 C  C     . MET B 79  ? 1.5295 1.2239 1.8583 -0.0296 -0.0573 0.2419  78   MET B C     
7674 O  O     . MET B 79  ? 1.5979 1.2819 1.9346 -0.0505 -0.0849 0.2410  78   MET B O     
7675 C  CB    . MET B 79  ? 1.4461 1.2144 1.8279 -0.0066 -0.0582 0.2432  78   MET B CB    
7676 C  CG    . MET B 79  ? 1.5909 1.3928 1.9721 0.0117  -0.0485 0.2432  78   MET B CG    
7677 S  SD    . MET B 79  ? 1.1965 1.0407 1.6390 0.0135  -0.0562 0.2422  78   MET B SD    
7678 C  CE    . MET B 79  ? 1.2797 1.1155 1.7372 -0.0073 -0.0932 0.2413  78   MET B CE    
7679 N  N     . ARG B 80  ? 1.9164 1.5944 2.2382 -0.0246 -0.0350 0.2433  79   ARG B N     
7680 C  CA    . ARG B 80  ? 1.7496 1.3939 2.0694 -0.0447 -0.0412 0.2423  79   ARG B CA    
7681 C  C     . ARG B 80  ? 1.7426 1.3434 2.0106 -0.0631 -0.0531 0.2380  79   ARG B C     
7682 O  O     . ARG B 80  ? 1.5191 1.1014 1.7901 -0.0883 -0.0778 0.2368  79   ARG B O     
7683 C  CB    . ARG B 80  ? 1.4836 1.1160 1.8003 -0.0340 -0.0115 0.2445  79   ARG B CB    
7684 C  CG    . ARG B 80  ? 1.4896 1.1582 1.8561 -0.0211 0.0002  0.2484  79   ARG B CG    
7685 C  CD    . ARG B 80  ? 1.5396 1.1887 1.9025 -0.0171 0.0251  0.2510  79   ARG B CD    
7686 N  NE    . ARG B 80  ? 1.4686 1.1482 1.8778 -0.0081 0.0363  0.2543  79   ARG B NE    
7687 C  CZ    . ARG B 80  ? 1.6748 1.3743 2.0835 0.0134  0.0606  0.2589  79   ARG B CZ    
7688 N  NH1   . ARG B 80  ? 1.9430 1.6388 2.3126 0.0298  0.0758  0.2621  79   ARG B NH1   
7689 N  NH2   . ARG B 80  ? 1.4156 1.1393 1.8645 0.0179  0.0701  0.2609  79   ARG B NH2   
7690 N  N     . GLU B 81  ? 1.8754 1.4595 2.0956 -0.0520 -0.0360 0.2362  80   GLU B N     
7691 C  CA    . GLU B 81  ? 1.9001 1.4387 2.0650 -0.0687 -0.0415 0.2310  80   GLU B CA    
7692 C  C     . GLU B 81  ? 1.9182 1.4586 2.0794 -0.0875 -0.0755 0.2291  80   GLU B C     
7693 O  O     . GLU B 81  ? 2.1114 1.6123 2.2247 -0.1056 -0.0834 0.2245  80   GLU B O     
7694 C  CB    . GLU B 81  ? 2.0920 1.6183 2.2145 -0.0491 -0.0127 0.2305  80   GLU B CB    
7695 C  CG    . GLU B 81  ? 1.9705 1.4864 2.0892 -0.0321 0.0213  0.2340  80   GLU B CG    
7696 C  CD    . GLU B 81  ? 2.3570 1.8190 2.4448 -0.0505 0.0290  0.2296  80   GLU B CD    
7697 O  OE1   . GLU B 81  ? 2.4019 1.8254 2.4488 -0.0716 0.0180  0.2229  80   GLU B OE1   
7698 O  OE2   . GLU B 81  ? 2.2850 1.7413 2.3872 -0.0450 0.0465  0.2326  80   GLU B OE2   
7699 N  N     . GLN B 82  ? 1.9927 1.5754 2.2015 -0.0845 -0.0949 0.2326  81   GLN B N     
7700 C  CA    . GLN B 82  ? 1.8872 1.4733 2.0972 -0.1016 -0.1280 0.2327  81   GLN B CA    
7701 C  C     . GLN B 82  ? 1.7403 1.3223 1.9829 -0.1270 -0.1579 0.2361  81   GLN B C     
7702 O  O     . GLN B 82  ? 1.7930 1.3424 2.0050 -0.1529 -0.1798 0.2352  81   GLN B O     
7703 C  CB    . GLN B 82  ? 1.9509 1.5835 2.1930 -0.0839 -0.1315 0.2350  81   GLN B CB    
7704 C  CG    . GLN B 82  ? 2.1917 1.8306 2.4413 -0.0997 -0.1654 0.2366  81   GLN B CG    
7705 C  CD    . GLN B 82  ? 2.2631 1.8602 2.4503 -0.1176 -0.1757 0.2330  81   GLN B CD    
7706 O  OE1   . GLN B 82  ? 2.2965 1.8694 2.4740 -0.1441 -0.2020 0.2344  81   GLN B OE1   
7707 N  NE2   . GLN B 82  ? 2.4370 2.0250 2.5810 -0.1040 -0.1546 0.2287  81   GLN B NE2   
7708 N  N     . TYR B 83  ? 1.6423 1.2572 1.9471 -0.1210 -0.1592 0.2406  82   TYR B N     
7709 C  CA    . TYR B 83  ? 1.7388 1.3557 2.0843 -0.1439 -0.1880 0.2458  82   TYR B CA    
7710 C  C     . TYR B 83  ? 1.8804 1.4568 2.2019 -0.1646 -0.1876 0.2443  82   TYR B C     
7711 O  O     . TYR B 83  ? 2.1074 1.6767 2.4486 -0.1899 -0.2161 0.2488  82   TYR B O     
7712 C  CB    . TYR B 83  ? 1.7527 1.4146 2.1739 -0.1313 -0.1857 0.2507  82   TYR B CB    
7713 C  CG    . TYR B 83  ? 1.4738 1.1447 1.9088 -0.1121 -0.1513 0.2489  82   TYR B CG    
7714 C  CD1   . TYR B 83  ? 1.5202 1.1697 1.9580 -0.1221 -0.1434 0.2491  82   TYR B CD1   
7715 C  CD2   . TYR B 83  ? 1.5780 1.2789 2.0235 -0.0854 -0.1277 0.2477  82   TYR B CD2   
7716 C  CE1   . TYR B 83  ? 1.5184 1.1751 1.9680 -0.1050 -0.1122 0.2484  82   TYR B CE1   
7717 C  CE2   . TYR B 83  ? 1.4737 1.1824 1.9296 -0.0692 -0.0978 0.2474  82   TYR B CE2   
7718 C  CZ    . TYR B 83  ? 1.5342 1.2205 1.9925 -0.0785 -0.0898 0.2480  82   TYR B CZ    
7719 O  OH    . TYR B 83  ? 1.5564 1.2492 2.0239 -0.0628 -0.0599 0.2486  82   TYR B OH    
7720 N  N     . MET B 84  ? 1.7146 1.2644 1.9954 -0.1551 -0.1563 0.2388  83   MET B N     
7721 C  CA    . MET B 84  ? 1.7329 1.2376 1.9818 -0.1758 -0.1532 0.2357  83   MET B CA    
7722 C  C     . MET B 84  ? 1.8057 1.2645 1.9896 -0.2006 -0.1687 0.2310  83   MET B C     
7723 O  O     . MET B 84  ? 1.9164 1.3319 2.0652 -0.2216 -0.1669 0.2271  83   MET B O     
7724 C  CB    . MET B 84  ? 1.8524 1.3426 2.0816 -0.1561 -0.1122 0.2322  83   MET B CB    
7725 C  CG    . MET B 84  ? 1.6971 1.2233 1.9846 -0.1379 -0.0964 0.2367  83   MET B CG    
7726 S  SD    . MET B 84  ? 1.6599 1.1633 1.9232 -0.1196 -0.0516 0.2350  83   MET B SD    
7727 C  CE    . MET B 84  ? 1.9456 1.4422 2.1561 -0.0964 -0.0293 0.2327  83   MET B CE    
7728 N  N     . ARG B 85  ? 1.8941 1.3591 2.0587 -0.2000 -0.1827 0.2308  84   ARG B N     
7729 C  CA    . ARG B 85  ? 1.9658 1.3883 2.0688 -0.2257 -0.2000 0.2269  84   ARG B CA    
7730 C  C     . ARG B 85  ? 2.0406 1.4736 2.1658 -0.2515 -0.2457 0.2342  84   ARG B C     
7731 O  O     . ARG B 85  ? 2.1659 1.5598 2.2465 -0.2826 -0.2665 0.2329  84   ARG B O     
7732 C  CB    . ARG B 85  ? 2.0422 1.4580 2.0998 -0.2090 -0.1822 0.2217  84   ARG B CB    
7733 C  CG    . ARG B 85  ? 2.0187 1.4293 2.0588 -0.1809 -0.1380 0.2172  84   ARG B CG    
7734 C  CD    . ARG B 85  ? 2.1909 1.5987 2.1922 -0.1652 -0.1225 0.2137  84   ARG B CD    
7735 N  NE    . ARG B 85  ? 2.3145 1.6693 2.2468 -0.1882 -0.1260 0.2067  84   ARG B NE    
7736 C  CZ    . ARG B 85  ? 2.5192 1.8595 2.4081 -0.1798 -0.1105 0.2023  84   ARG B CZ    
7737 N  NH1   . ARG B 85  ? 2.5942 1.9704 2.5018 -0.1491 -0.0921 0.2048  84   ARG B NH1   
7738 N  NH2   . ARG B 85  ? 2.6061 1.8939 2.4305 -0.2041 -0.1132 0.1951  84   ARG B NH2   
7739 N  N     . THR B 86  ? 1.9106 1.3943 2.1031 -0.2399 -0.2613 0.2425  85   THR B N     
7740 C  CA    . THR B 86  ? 1.8930 1.3916 2.1149 -0.2606 -0.3042 0.2521  85   THR B CA    
7741 C  C     . THR B 86  ? 2.1334 1.6493 2.4178 -0.2758 -0.3258 0.2613  85   THR B C     
7742 O  O     . THR B 86  ? 2.2359 1.7525 2.5358 -0.3012 -0.3645 0.2707  85   THR B O     
7743 C  CB    . THR B 86  ? 2.1279 1.6701 2.3860 -0.2391 -0.3087 0.2561  85   THR B CB    
7744 O  OG1   . THR B 86  ? 1.7552 1.3391 2.0741 -0.2120 -0.2876 0.2572  85   THR B OG1   
7745 C  CG2   . THR B 86  ? 2.2999 1.8269 2.4982 -0.2265 -0.2910 0.2480  85   THR B CG2   
7746 N  N     . GLY B 87  ? 1.8750 1.4052 2.1967 -0.2616 -0.3022 0.2601  86   GLY B N     
7747 C  CA    . GLY B 87  ? 1.8385 1.3880 2.2254 -0.2745 -0.3198 0.2690  86   GLY B CA    
7748 C  C     . GLY B 87  ? 1.9261 1.4332 2.2800 -0.3066 -0.3307 0.2680  86   GLY B C     
7749 O  O     . GLY B 87  ? 2.1634 1.6285 2.4540 -0.3097 -0.3078 0.2577  86   GLY B O     
7750 N  N     . GLU B 88  ? 1.9394 1.4580 2.3389 -0.3315 -0.3660 0.2793  87   GLU B N     
7751 C  CA    . GLU B 88  ? 1.9952 1.4787 2.3725 -0.3658 -0.3814 0.2801  87   GLU B CA    
7752 C  C     . GLU B 88  ? 1.9454 1.4516 2.3917 -0.3659 -0.3767 0.2854  87   GLU B C     
7753 O  O     . GLU B 88  ? 1.9689 1.4553 2.4142 -0.3966 -0.3956 0.2891  87   GLU B O     
7754 C  CB    . GLU B 88  ? 2.1163 1.5888 2.4811 -0.4017 -0.4306 0.2904  87   GLU B CB    
7755 C  CG    . GLU B 88  ? 2.1212 1.6445 2.5655 -0.3986 -0.4629 0.3070  87   GLU B CG    
7756 C  CD    . GLU B 88  ? 2.3142 1.8498 2.7424 -0.3813 -0.4651 0.3067  87   GLU B CD    
7757 O  OE1   . GLU B 88  ? 2.6373 2.1482 3.0001 -0.3674 -0.4377 0.2934  87   GLU B OE1   
7758 O  OE2   . GLU B 88  ? 2.1525 1.7224 2.6353 -0.3818 -0.4938 0.3204  87   GLU B OE2   
7759 N  N     . GLY B 89  ? 1.8417 1.3878 2.3462 -0.3339 -0.3516 0.2858  88   GLY B N     
7760 C  CA    . GLY B 89  ? 1.5782 1.1459 2.1485 -0.3318 -0.3425 0.2900  88   GLY B CA    
7761 C  C     . GLY B 89  ? 1.5470 1.1438 2.1502 -0.2939 -0.3024 0.2851  88   GLY B C     
7762 O  O     . GLY B 89  ? 1.7169 1.3479 2.3508 -0.2719 -0.2997 0.2872  88   GLY B O     
7763 N  N     . PHE B 90  ? 1.3792 0.9614 1.9741 -0.2870 -0.2710 0.2787  89   PHE B N     
7764 C  CA    . PHE B 90  ? 1.5882 1.1923 2.2036 -0.2530 -0.2313 0.2741  89   PHE B CA    
7765 C  C     . PHE B 90  ? 1.5652 1.1900 2.2483 -0.2533 -0.2216 0.2786  89   PHE B C     
7766 O  O     . PHE B 90  ? 1.4615 1.0748 2.1628 -0.2796 -0.2394 0.2831  89   PHE B O     
7767 C  CB    . PHE B 90  ? 1.4977 1.0655 2.0384 -0.2394 -0.1965 0.2630  89   PHE B CB    
7768 C  CG    . PHE B 90  ? 1.5767 1.1240 2.0516 -0.2368 -0.2005 0.2579  89   PHE B CG    
7769 C  CD1   . PHE B 90  ? 1.3891 0.9611 1.8619 -0.2089 -0.1866 0.2563  89   PHE B CD1   
7770 C  CD2   . PHE B 90  ? 1.4293 0.9316 1.8434 -0.2638 -0.2174 0.2546  89   PHE B CD2   
7771 C  CE1   . PHE B 90  ? 1.6604 1.2146 2.0753 -0.2067 -0.1895 0.2519  89   PHE B CE1   
7772 C  CE2   . PHE B 90  ? 1.6598 1.1418 2.0134 -0.2619 -0.2190 0.2496  89   PHE B CE2   
7773 C  CZ    . PHE B 90  ? 1.8528 1.3617 2.2086 -0.2327 -0.2049 0.2485  89   PHE B CZ    
7774 N  N     . LEU B 91  ? 1.4311 1.0863 2.1505 -0.2248 -0.1927 0.2773  90   LEU B N     
7775 C  CA    . LEU B 91  ? 1.3927 1.0681 2.1748 -0.2210 -0.1764 0.2803  90   LEU B CA    
7776 C  C     . LEU B 91  ? 1.6475 1.3189 2.4048 -0.1940 -0.1316 0.2729  90   LEU B C     
7777 O  O     . LEU B 91  ? 1.4125 1.1110 2.1833 -0.1690 -0.1143 0.2715  90   LEU B O     
7778 C  CB    . LEU B 91  ? 1.2236 0.9468 2.0920 -0.2161 -0.1898 0.2889  90   LEU B CB    
7779 C  CG    . LEU B 91  ? 1.2338 0.9674 2.1462 -0.2432 -0.2345 0.3004  90   LEU B CG    
7780 C  CD1   . LEU B 91  ? 1.3258 1.1074 2.3297 -0.2335 -0.2400 0.3091  90   LEU B CD1   
7781 C  CD2   . LEU B 91  ? 1.2734 0.9849 2.1908 -0.2719 -0.2470 0.3039  90   LEU B CD2   
7782 N  N     . LEU B 92  ? 1.4349 1.0716 2.1549 -0.1999 -0.1134 0.2688  91   LEU B N     
7783 C  CA    . LEU B 92  ? 1.4567 1.0885 2.1578 -0.1762 -0.0717 0.2645  91   LEU B CA    
7784 C  C     . LEU B 92  ? 1.3195 0.9846 2.0930 -0.1685 -0.0571 0.2683  91   LEU B C     
7785 O  O     . LEU B 92  ? 1.4574 1.1151 2.2600 -0.1833 -0.0555 0.2706  91   LEU B O     
7786 C  CB    . LEU B 92  ? 1.7203 1.3035 2.3657 -0.1865 -0.0568 0.2601  91   LEU B CB    
7787 C  CG    . LEU B 92  ? 1.7619 1.3039 2.3330 -0.1984 -0.0681 0.2552  91   LEU B CG    
7788 C  CD1   . LEU B 92  ? 1.7955 1.2880 2.3199 -0.2098 -0.0499 0.2506  91   LEU B CD1   
7789 C  CD2   . LEU B 92  ? 1.7981 1.3458 2.3294 -0.1731 -0.0554 0.2523  91   LEU B CD2   
7790 N  N     . VAL B 93  ? 1.2647 0.9654 2.0671 -0.1465 -0.0456 0.2687  92   VAL B N     
7791 C  CA    . VAL B 93  ? 1.5329 1.2653 2.4044 -0.1392 -0.0304 0.2715  92   VAL B CA    
7792 C  C     . VAL B 93  ? 1.4034 1.1366 2.2520 -0.1148 0.0104  0.2679  92   VAL B C     
7793 O  O     . VAL B 93  ? 1.3574 1.0847 2.1534 -0.0978 0.0225  0.2649  92   VAL B O     
7794 C  CB    . VAL B 93  ? 1.2500 1.0224 2.1798 -0.1356 -0.0476 0.2749  92   VAL B CB    
7795 C  CG1   . VAL B 93  ? 1.2842 1.0548 2.2281 -0.1586 -0.0907 0.2805  92   VAL B CG1   
7796 C  CG2   . VAL B 93  ? 1.1797 0.9665 2.0804 -0.1119 -0.0350 0.2705  92   VAL B CG2   
7797 N  N     . PHE B 94  ? 1.1899 0.9306 2.0791 -0.1142 0.0314  0.2693  93   PHE B N     
7798 C  CA    . PHE B 94  ? 1.2115 0.9548 2.0852 -0.0934 0.0696  0.2675  93   PHE B CA    
7799 C  C     . PHE B 94  ? 1.2459 1.0152 2.1899 -0.0932 0.0846  0.2690  93   PHE B C     
7800 O  O     . PHE B 94  ? 1.1448 0.9252 2.1485 -0.1100 0.0674  0.2721  93   PHE B O     
7801 C  CB    . PHE B 94  ? 1.2807 0.9852 2.1005 -0.0934 0.0886  0.2672  93   PHE B CB    
7802 C  CG    . PHE B 94  ? 1.2272 0.9134 2.0736 -0.1143 0.0872  0.2688  93   PHE B CG    
7803 C  CD1   . PHE B 94  ? 1.3850 1.0492 2.2242 -0.1387 0.0586  0.2689  93   PHE B CD1   
7804 C  CD2   . PHE B 94  ? 1.3818 1.0720 2.2581 -0.1110 0.1145  0.2702  93   PHE B CD2   
7805 C  CE1   . PHE B 94  ? 1.2803 0.9281 2.1433 -0.1599 0.0564  0.2705  93   PHE B CE1   
7806 C  CE2   . PHE B 94  ? 1.3904 1.0643 2.2924 -0.1309 0.1136  0.2717  93   PHE B CE2   
7807 C  CZ    . PHE B 94  ? 1.2789 0.9322 2.1749 -0.1555 0.0840  0.2719  93   PHE B CZ    
7808 N  N     . SER B 95  ? 1.1880 0.9668 2.1249 -0.0748 0.1174  0.2674  94   SER B N     
7809 C  CA    . SER B 95  ? 1.1369 0.9366 2.1325 -0.0732 0.1385  0.2676  94   SER B CA    
7810 C  C     . SER B 95  ? 1.2458 1.0231 2.2349 -0.0773 0.1626  0.2692  94   SER B C     
7811 O  O     . SER B 95  ? 1.1684 0.9234 2.0990 -0.0671 0.1810  0.2696  94   SER B O     
7812 C  CB    . SER B 95  ? 1.1007 0.9234 2.0908 -0.0533 0.1605  0.2643  94   SER B CB    
7813 O  OG    . SER B 95  ? 1.1724 1.0092 2.2103 -0.0521 0.1866  0.2634  94   SER B OG    
7814 N  N     . VAL B 96  ? 1.2510 1.0343 2.3024 -0.0921 0.1627  0.2710  95   VAL B N     
7815 C  CA    . VAL B 96  ? 1.1789 0.9427 2.2313 -0.0970 0.1872  0.2724  95   VAL B CA    
7816 C  C     . VAL B 96  ? 1.2271 0.9970 2.2687 -0.0793 0.2266  0.2711  95   VAL B C     
7817 O  O     . VAL B 96  ? 1.4723 1.2225 2.4997 -0.0797 0.2506  0.2728  95   VAL B O     
7818 C  CB    . VAL B 96  ? 1.1823 0.9551 2.3106 -0.1179 0.1774  0.2753  95   VAL B CB    
7819 C  CG1   . VAL B 96  ? 1.2297 0.9945 2.3641 -0.1386 0.1363  0.2781  95   VAL B CG1   
7820 C  CG2   . VAL B 96  ? 1.1522 0.9624 2.3534 -0.1135 0.1851  0.2750  95   VAL B CG2   
7821 N  N     . THR B 97  ? 1.1489 0.9441 2.1950 -0.0652 0.2337  0.2683  96   THR B N     
7822 C  CA    . THR B 97  ? 1.1482 0.9484 2.1736 -0.0496 0.2689  0.2670  96   THR B CA    
7823 C  C     . THR B 97  ? 1.1540 0.9426 2.1007 -0.0331 0.2744  0.2686  96   THR B C     
7824 O  O     . THR B 97  ? 1.7897 1.5835 2.7117 -0.0203 0.3003  0.2691  96   THR B O     
7825 C  CB    . THR B 97  ? 1.3049 1.1374 2.3781 -0.0452 0.2766  0.2624  96   THR B CB    
7826 O  OG1   . THR B 97  ? 1.3720 1.2195 2.4345 -0.0399 0.2522  0.2603  96   THR B OG1   
7827 C  CG2   . THR B 97  ? 1.1159 0.9618 2.2745 -0.0600 0.2739  0.2625  96   THR B CG2   
7828 N  N     . ASP B 98  ? 1.1601 0.9331 2.0675 -0.0339 0.2511  0.2701  97   ASP B N     
7829 C  CA    . ASP B 98  ? 1.2675 1.0310 2.1053 -0.0180 0.2545  0.2727  97   ASP B CA    
7830 C  C     . ASP B 98  ? 1.6167 1.3444 2.4142 -0.0232 0.2467  0.2760  97   ASP B C     
7831 O  O     . ASP B 98  ? 1.4901 1.2093 2.2837 -0.0331 0.2193  0.2739  97   ASP B O     
7832 C  CB    . ASP B 98  ? 1.1380 0.9235 1.9683 -0.0113 0.2343  0.2695  97   ASP B CB    
7833 C  CG    . ASP B 98  ? 1.2157 0.9958 1.9794 0.0055  0.2385  0.2729  97   ASP B CG    
7834 O  OD1   . ASP B 98  ? 1.3822 1.1448 2.1084 0.0140  0.2597  0.2789  97   ASP B OD1   
7835 O  OD2   . ASP B 98  ? 1.4082 1.2020 2.1591 0.0101  0.2207  0.2706  97   ASP B OD2   
7836 N  N     . ARG B 99  ? 1.5321 1.2367 2.2981 -0.0172 0.2716  0.2811  98   ARG B N     
7837 C  CA    . ARG B 99  ? 1.3427 1.0095 2.0661 -0.0204 0.2694  0.2841  98   ARG B CA    
7838 C  C     . ARG B 99  ? 1.3885 1.0494 2.0583 -0.0079 0.2596  0.2857  98   ARG B C     
7839 O  O     . ARG B 99  ? 1.4867 1.1176 2.1261 -0.0140 0.2499  0.2853  98   ARG B O     
7840 C  CB    . ARG B 99  ? 1.3192 0.9628 2.0228 -0.0151 0.3009  0.2905  98   ARG B CB    
7841 C  CG    . ARG B 99  ? 1.7654 1.4082 2.5183 -0.0293 0.3127  0.2890  98   ARG B CG    
7842 C  CD    . ARG B 99  ? 1.5511 1.1607 2.2780 -0.0278 0.3391  0.2952  98   ARG B CD    
7843 N  NE    . ARG B 99  ? 1.5933 1.1649 2.2856 -0.0352 0.3302  0.2954  98   ARG B NE    
7844 C  CZ    . ARG B 99  ? 1.5688 1.1201 2.2818 -0.0574 0.3183  0.2910  98   ARG B CZ    
7845 N  NH1   . ARG B 99  ? 1.6149 1.1827 2.3879 -0.0737 0.3126  0.2875  98   ARG B NH1   
7846 N  NH2   . ARG B 99  ? 1.6299 1.1431 2.3030 -0.0641 0.3127  0.2903  98   ARG B NH2   
7847 N  N     . GLY B 100 ? 1.2902 0.9778 1.9471 0.0086  0.2630  0.2873  99   GLY B N     
7848 C  CA    . GLY B 100 ? 1.3802 1.0658 1.9912 0.0204  0.2532  0.2892  99   GLY B CA    
7849 C  C     . GLY B 100 ? 1.4660 1.1465 2.0804 0.0074  0.2218  0.2825  99   GLY B C     
7850 O  O     . GLY B 100 ? 1.8130 1.4691 2.3866 0.0083  0.2151  0.2831  99   GLY B O     
7851 N  N     . SER B 101 ? 1.7168 1.4192 2.3802 -0.0051 0.2028  0.2767  100  SER B N     
7852 C  CA    . SER B 101 ? 1.4868 1.1841 2.1565 -0.0201 0.1706  0.2719  100  SER B CA    
7853 C  C     . SER B 101 ? 1.5120 1.1724 2.1749 -0.0392 0.1633  0.2711  100  SER B C     
7854 O  O     . SER B 101 ? 1.3199 0.9604 1.9564 -0.0493 0.1429  0.2686  100  SER B O     
7855 C  CB    . SER B 101 ? 1.4502 1.1805 2.1800 -0.0286 0.1530  0.2683  100  SER B CB    
7856 O  OG    . SER B 101 ? 1.1680 0.9029 1.9494 -0.0389 0.1620  0.2686  100  SER B OG    
7857 N  N     . PHE B 102 ? 1.3424 0.9916 2.0264 -0.0456 0.1803  0.2729  101  PHE B N     
7858 C  CA    . PHE B 102 ? 1.3742 0.9875 2.0525 -0.0659 0.1744  0.2717  101  PHE B CA    
7859 C  C     . PHE B 102 ? 1.5339 1.1065 2.1450 -0.0605 0.1849  0.2726  101  PHE B C     
7860 O  O     . PHE B 102 ? 1.6447 1.1866 2.2332 -0.0778 0.1694  0.2690  101  PHE B O     
7861 C  CB    . PHE B 102 ? 1.2935 0.9051 2.0098 -0.0725 0.1935  0.2737  101  PHE B CB    
7862 C  CG    . PHE B 102 ? 1.3341 0.9073 2.0423 -0.0935 0.1911  0.2726  101  PHE B CG    
7863 C  CD1   . PHE B 102 ? 1.5054 1.0771 2.2455 -0.1197 0.1616  0.2698  101  PHE B CD1   
7864 C  CD2   . PHE B 102 ? 1.4374 0.9757 2.1065 -0.0881 0.2180  0.2752  101  PHE B CD2   
7865 C  CE1   . PHE B 102 ? 1.7149 1.2505 2.4451 -0.1417 0.1586  0.2684  101  PHE B CE1   
7866 C  CE2   . PHE B 102 ? 1.7632 1.2636 2.4229 -0.1087 0.2172  0.2732  101  PHE B CE2   
7867 C  CZ    . PHE B 102 ? 1.8599 1.3588 2.5489 -0.1364 0.1873  0.2692  101  PHE B CZ    
7868 N  N     . GLU B 103 ? 1.4458 1.0171 2.0246 -0.0374 0.2114  0.2780  102  GLU B N     
7869 C  CA    . GLU B 103 ? 1.5354 1.0700 2.0551 -0.0288 0.2250  0.2807  102  GLU B CA    
7870 C  C     . GLU B 103 ? 1.5370 1.0753 2.0220 -0.0199 0.2113  0.2793  102  GLU B C     
7871 O  O     . GLU B 103 ? 2.1020 1.6138 2.5399 -0.0093 0.2247  0.2824  102  GLU B O     
7872 C  CB    . GLU B 103 ? 1.6137 1.1454 2.1174 -0.0078 0.2593  0.2901  102  GLU B CB    
7873 C  CG    . GLU B 103 ? 1.8700 1.4423 2.3781 0.0139  0.2664  0.2956  102  GLU B CG    
7874 C  CD    . GLU B 103 ? 1.8586 1.4286 2.3526 0.0314  0.2981  0.3066  102  GLU B CD    
7875 O  OE1   . GLU B 103 ? 1.6902 1.2324 2.1843 0.0255  0.3151  0.3091  102  GLU B OE1   
7876 O  OE2   . GLU B 103 ? 1.9289 1.5246 2.4109 0.0500  0.3056  0.3133  102  GLU B OE2   
7877 N  N     . GLU B 104 ? 1.5022 1.0721 2.0110 -0.0236 0.1864  0.2753  103  GLU B N     
7878 C  CA    . GLU B 104 ? 1.6821 1.2560 2.1607 -0.0179 0.1712  0.2732  103  GLU B CA    
7879 C  C     . GLU B 104 ? 1.6279 1.1968 2.1165 -0.0413 0.1372  0.2660  103  GLU B C     
7880 O  O     . GLU B 104 ? 1.4052 0.9789 1.8728 -0.0395 0.1213  0.2636  103  GLU B O     
7881 C  CB    . GLU B 104 ? 1.6378 1.2555 2.1279 0.0020  0.1736  0.2763  103  GLU B CB    
7882 C  CG    . GLU B 104 ? 1.5837 1.2070 2.0543 0.0253  0.2039  0.2854  103  GLU B CG    
7883 C  CD    . GLU B 104 ? 2.0524 1.6525 2.4703 0.0389  0.2148  0.2904  103  GLU B CD    
7884 O  OE1   . GLU B 104 ? 2.2618 1.8662 2.6605 0.0407  0.1998  0.2874  103  GLU B OE1   
7885 O  OE2   . GLU B 104 ? 2.0643 1.6414 2.4615 0.0480  0.2393  0.2977  103  GLU B OE2   
7886 N  N     . ILE B 105 ? 1.7535 1.3137 2.2743 -0.0640 0.1250  0.2635  104  ILE B N     
7887 C  CA    . ILE B 105 ? 1.6699 1.2250 2.2005 -0.0886 0.0903  0.2589  104  ILE B CA    
7888 C  C     . ILE B 105 ? 1.8443 1.3531 2.3141 -0.0999 0.0853  0.2547  104  ILE B C     
7889 O  O     . ILE B 105 ? 1.8276 1.3333 2.2800 -0.1099 0.0608  0.2515  104  ILE B O     
7890 C  CB    . ILE B 105 ? 1.6560 1.2160 2.2405 -0.1105 0.0786  0.2593  104  ILE B CB    
7891 C  CG1   . ILE B 105 ? 1.6323 1.2416 2.2824 -0.1035 0.0740  0.2620  104  ILE B CG1   
7892 C  CG2   . ILE B 105 ? 1.7015 1.2401 2.2806 -0.1408 0.0454  0.2563  104  ILE B CG2   
7893 C  CD1   . ILE B 105 ? 1.6730 1.3098 2.3326 -0.1004 0.0497  0.2613  104  ILE B CD1   
7894 N  N     . TYR B 106 ? 1.9196 1.3894 2.3547 -0.0989 0.1101  0.2546  105  TYR B N     
7895 C  CA    . TYR B 106 ? 1.7157 1.1355 2.0922 -0.1116 0.1095  0.2494  105  TYR B CA    
7896 C  C     . TYR B 106 ? 1.7969 1.2162 2.1317 -0.0960 0.1103  0.2485  105  TYR B C     
7897 O  O     . TYR B 106 ? 1.7811 1.1696 2.0756 -0.1113 0.0974  0.2426  105  TYR B O     
7898 C  CB    . TYR B 106 ? 1.9406 1.3191 2.2899 -0.1093 0.1415  0.2502  105  TYR B CB    
7899 C  CG    . TYR B 106 ? 2.1290 1.5083 2.4545 -0.0770 0.1753  0.2567  105  TYR B CG    
7900 C  CD1   . TYR B 106 ? 2.2727 1.6884 2.6318 -0.0555 0.1915  0.2647  105  TYR B CD1   
7901 C  CD2   . TYR B 106 ? 2.1196 1.4625 2.3893 -0.0688 0.1913  0.2557  105  TYR B CD2   
7902 C  CE1   . TYR B 106 ? 2.3191 1.7371 2.6566 -0.0274 0.2197  0.2730  105  TYR B CE1   
7903 C  CE2   . TYR B 106 ? 2.2390 1.5849 2.4919 -0.0390 0.2209  0.2642  105  TYR B CE2   
7904 C  CZ    . TYR B 106 ? 2.2545 1.6390 2.5413 -0.0188 0.2335  0.2736  105  TYR B CZ    
7905 O  OH    . TYR B 106 ? 2.1994 1.5888 2.4698 0.0095  0.2603  0.2843  105  TYR B OH    
7906 N  N     . LYS B 107 ? 1.7796 1.2325 2.1227 -0.0673 0.1250  0.2543  106  LYS B N     
7907 C  CA    . LYS B 107 ? 1.8531 1.3106 2.1620 -0.0523 0.1252  0.2543  106  LYS B CA    
7908 C  C     . LYS B 107 ? 1.9371 1.4084 2.2514 -0.0676 0.0900  0.2492  106  LYS B C     
7909 O  O     . LYS B 107 ? 2.0600 1.5127 2.3330 -0.0696 0.0842  0.2456  106  LYS B O     
7910 C  CB    . LYS B 107 ? 1.8920 1.3886 2.2148 -0.0216 0.1436  0.2624  106  LYS B CB    
7911 C  CG    . LYS B 107 ? 1.9974 1.4789 2.3065 -0.0038 0.1787  0.2701  106  LYS B CG    
7912 C  CD    . LYS B 107 ? 2.2161 1.7321 2.5250 0.0253  0.1939  0.2793  106  LYS B CD    
7913 C  CE    . LYS B 107 ? 2.0870 1.5885 2.3825 0.0432  0.2274  0.2897  106  LYS B CE    
7914 N  NZ    . LYS B 107 ? 2.0437 1.5805 2.3383 0.0698  0.2396  0.3006  106  LYS B NZ    
7915 N  N     . PHE B 108 ? 1.9548 1.4581 2.3212 -0.0785 0.0672  0.2495  107  PHE B N     
7916 C  CA    . PHE B 108 ? 1.8451 1.3590 2.2203 -0.0956 0.0317  0.2464  107  PHE B CA    
7917 C  C     . PHE B 108 ? 1.6097 1.0789 1.9542 -0.1265 0.0137  0.2412  107  PHE B C     
7918 O  O     . PHE B 108 ? 1.7765 1.2345 2.0937 -0.1390 -0.0080 0.2379  107  PHE B O     
7919 C  CB    . PHE B 108 ? 1.8264 1.3848 2.2705 -0.0989 0.0141  0.2496  107  PHE B CB    
7920 C  CG    . PHE B 108 ? 1.3602 0.9626 1.8289 -0.0731 0.0250  0.2526  107  PHE B CG    
7921 C  CD1   . PHE B 108 ? 1.3502 0.9679 1.8365 -0.0549 0.0533  0.2562  107  PHE B CD1   
7922 C  CD2   . PHE B 108 ? 1.3214 0.9485 1.7934 -0.0686 0.0071  0.2519  107  PHE B CD2   
7923 C  CE1   . PHE B 108 ? 1.3169 0.9733 1.8213 -0.0341 0.0631  0.2586  107  PHE B CE1   
7924 C  CE2   . PHE B 108 ? 1.3607 1.0265 1.8527 -0.0471 0.0175  0.2538  107  PHE B CE2   
7925 C  CZ    . PHE B 108 ? 1.3338 1.0140 1.8409 -0.0305 0.0453  0.2569  107  PHE B CZ    
7926 N  N     . GLN B 109 ? 1.6014 1.0432 1.9473 -0.1405 0.0226  0.2404  108  GLN B N     
7927 C  CA    . GLN B 109 ? 1.7157 1.1134 2.0309 -0.1733 0.0053  0.2352  108  GLN B CA    
7928 C  C     . GLN B 109 ? 1.8322 1.1801 2.0722 -0.1736 0.0214  0.2288  108  GLN B C     
7929 O  O     . GLN B 109 ? 1.7916 1.1043 1.9937 -0.2004 0.0029  0.2231  108  GLN B O     
7930 C  CB    . GLN B 109 ? 1.7361 1.1193 2.0757 -0.1886 0.0118  0.2359  108  GLN B CB    
7931 C  CG    . GLN B 109 ? 1.6634 1.0111 1.9863 -0.2279 -0.0139 0.2319  108  GLN B CG    
7932 C  CD    . GLN B 109 ? 1.8941 1.1783 2.1478 -0.2388 0.0070  0.2242  108  GLN B CD    
7933 O  OE1   . GLN B 109 ? 2.0931 1.3600 2.3135 -0.2153 0.0412  0.2228  108  GLN B OE1   
7934 N  NE2   . GLN B 109 ? 2.0186 1.2671 2.2510 -0.2755 -0.0132 0.2197  108  GLN B NE2   
7935 N  N     . ARG B 110 ? 1.8282 1.1718 2.0461 -0.1451 0.0560  0.2304  109  ARG B N     
7936 C  CA    . ARG B 110 ? 1.8746 1.1718 2.0262 -0.1426 0.0752  0.2253  109  ARG B CA    
7937 C  C     . ARG B 110 ? 1.7095 1.0178 1.8379 -0.1369 0.0618  0.2235  109  ARG B C     
7938 O  O     . ARG B 110 ? 1.7254 0.9921 1.7998 -0.1505 0.0612  0.2166  109  ARG B O     
7939 C  CB    . ARG B 110 ? 1.8060 1.0948 1.9470 -0.1137 0.1173  0.2301  109  ARG B CB    
7940 C  CG    . ARG B 110 ? 1.9076 1.1826 2.0681 -0.1177 0.1343  0.2323  109  ARG B CG    
7941 C  CD    . ARG B 110 ? 1.9260 1.1459 2.0548 -0.1515 0.1289  0.2237  109  ARG B CD    
7942 N  NE    . ARG B 110 ? 1.7308 0.9466 1.8903 -0.1606 0.1360  0.2257  109  ARG B NE    
7943 C  CZ    . ARG B 110 ? 1.9710 1.1648 2.1225 -0.1470 0.1709  0.2288  109  ARG B CZ    
7944 N  NH1   . ARG B 110 ? 2.1010 1.2762 2.2180 -0.1226 0.2022  0.2317  109  ARG B NH1   
7945 N  NH2   . ARG B 110 ? 1.9699 1.1609 2.1510 -0.1581 0.1747  0.2302  109  ARG B NH2   
7946 N  N     . GLN B 111 ? 1.6714 1.0333 1.8381 -0.1181 0.0523  0.2290  110  GLN B N     
7947 C  CA    . GLN B 111 ? 1.6584 1.0332 1.8059 -0.1123 0.0398  0.2277  110  GLN B CA    
7948 C  C     . GLN B 111 ? 1.6480 1.0121 1.7866 -0.1435 0.0018  0.2229  110  GLN B C     
7949 O  O     . GLN B 111 ? 1.7713 1.1171 1.8677 -0.1491 -0.0051 0.2186  110  GLN B O     
7950 C  CB    . GLN B 111 ? 1.6639 1.0980 1.8551 -0.0862 0.0393  0.2344  110  GLN B CB    
7951 C  CG    . GLN B 111 ? 1.8392 1.2867 2.0330 -0.0550 0.0745  0.2408  110  GLN B CG    
7952 C  CD    . GLN B 111 ? 2.2103 1.7143 2.4408 -0.0330 0.0723  0.2465  110  GLN B CD    
7953 O  OE1   . GLN B 111 ? 1.8751 1.4042 2.1200 -0.0379 0.0480  0.2447  110  GLN B OE1   
7954 N  NE2   . GLN B 111 ? 2.3668 1.8895 2.6109 -0.0099 0.0979  0.2537  110  GLN B NE2   
7955 N  N     . ILE B 112 ? 1.9134 1.2889 2.0920 -0.1643 -0.0232 0.2247  111  ILE B N     
7956 C  CA    . ILE B 112 ? 1.9463 1.3147 2.1212 -0.1951 -0.0626 0.2232  111  ILE B CA    
7957 C  C     . ILE B 112 ? 2.1243 1.4294 2.2312 -0.2223 -0.0629 0.2151  111  ILE B C     
7958 O  O     . ILE B 112 ? 1.8509 1.1371 1.9178 -0.2374 -0.0805 0.2114  111  ILE B O     
7959 C  CB    . ILE B 112 ? 1.8114 1.2088 2.0515 -0.2104 -0.0880 0.2291  111  ILE B CB    
7960 C  CG1   . ILE B 112 ? 1.5041 0.9618 1.8087 -0.1854 -0.0880 0.2358  111  ILE B CG1   
7961 C  CG2   . ILE B 112 ? 1.8443 1.2303 2.0790 -0.2452 -0.1302 0.2299  111  ILE B CG2   
7962 C  CD1   . ILE B 112 ? 1.4155 0.9029 1.7907 -0.1957 -0.1049 0.2420  111  ILE B CD1   
7963 N  N     . LEU B 113 ? 2.0955 1.3646 2.1858 -0.2301 -0.0422 0.2117  112  LEU B N     
7964 C  CA    . LEU B 113 ? 1.8216 1.0259 1.8449 -0.2580 -0.0395 0.2027  112  LEU B CA    
7965 C  C     . LEU B 113 ? 1.9899 1.1613 1.9511 -0.2436 -0.0115 0.1963  112  LEU B C     
7966 O  O     . LEU B 113 ? 2.1864 1.3098 2.0874 -0.2674 -0.0165 0.1881  112  LEU B O     
7967 C  CB    . LEU B 113 ? 1.7310 0.9049 1.7545 -0.2689 -0.0216 0.2005  112  LEU B CB    
7968 C  CG    . LEU B 113 ? 1.7120 0.9149 1.7979 -0.2852 -0.0465 0.2067  112  LEU B CG    
7969 C  CD1   . LEU B 113 ? 2.0435 1.2104 2.1217 -0.2974 -0.0262 0.2035  112  LEU B CD1   
7970 C  CD2   . LEU B 113 ? 1.8048 1.0111 1.8948 -0.3199 -0.0941 0.2083  112  LEU B CD2   
7971 N  N     . ARG B 114 ? 1.9108 1.1068 1.8855 -0.2059 0.0181  0.2005  113  ARG B N     
7972 C  CA    . ARG B 114 ? 2.0498 1.2202 1.9739 -0.1897 0.0451  0.1965  113  ARG B CA    
7973 C  C     . ARG B 114 ? 2.1641 1.3479 2.0719 -0.1938 0.0219  0.1950  113  ARG B C     
7974 O  O     . ARG B 114 ? 2.1820 1.3264 2.0325 -0.1998 0.0324  0.1880  113  ARG B O     
7975 C  CB    . ARG B 114 ? 1.9785 1.1768 1.9270 -0.1489 0.0798  0.2041  113  ARG B CB    
7976 C  CG    . ARG B 114 ? 2.1508 1.3261 2.0557 -0.1288 0.1115  0.2027  113  ARG B CG    
7977 C  CD    . ARG B 114 ? 2.0475 1.2678 1.9659 -0.1090 0.1020  0.2071  113  ARG B CD    
7978 N  NE    . ARG B 114 ? 2.1561 1.4397 2.1362 -0.0879 0.0943  0.2168  113  ARG B NE    
7979 C  CZ    . ARG B 114 ? 2.5865 1.8965 2.5886 -0.0565 0.1203  0.2257  113  ARG B CZ    
7980 N  NH1   . ARG B 114 ? 2.7198 2.0020 2.6933 -0.0399 0.1555  0.2280  113  ARG B NH1   
7981 N  NH2   . ARG B 114 ? 2.4737 1.8386 2.5279 -0.0420 0.1111  0.2331  113  ARG B NH2   
7982 N  N     . VAL B 115 ? 2.1326 1.3699 2.0901 -0.1907 -0.0081 0.2014  114  VAL B N     
7983 C  CA    . VAL B 115 ? 2.1085 1.3611 2.0547 -0.1940 -0.0311 0.2009  114  VAL B CA    
7984 C  C     . VAL B 115 ? 2.2530 1.4631 2.1544 -0.2341 -0.0591 0.1946  114  VAL B C     
7985 O  O     . VAL B 115 ? 2.5505 1.7321 2.3991 -0.2418 -0.0585 0.1889  114  VAL B O     
7986 C  CB    . VAL B 115 ? 1.8376 1.1563 1.8512 -0.1810 -0.0545 0.2096  114  VAL B CB    
7987 C  CG1   . VAL B 115 ? 1.7669 1.0953 1.7724 -0.1958 -0.0884 0.2096  114  VAL B CG1   
7988 C  CG2   . VAL B 115 ? 1.9755 1.3332 2.0149 -0.1419 -0.0272 0.2145  114  VAL B CG2   
7989 N  N     . LYS B 116 ? 2.2503 1.4553 2.1714 -0.2613 -0.0841 0.1961  115  LYS B N     
7990 C  CA    . LYS B 116 ? 2.2468 1.4167 2.1300 -0.3026 -0.1168 0.1926  115  LYS B CA    
7991 C  C     . LYS B 116 ? 2.3994 1.4968 2.2107 -0.3263 -0.0977 0.1814  115  LYS B C     
7992 O  O     . LYS B 116 ? 2.7096 1.7692 2.4737 -0.3622 -0.1210 0.1768  115  LYS B O     
7993 C  CB    . LYS B 116 ? 2.2124 1.4120 2.1530 -0.3229 -0.1550 0.2011  115  LYS B CB    
7994 C  CG    . LYS B 116 ? 2.2859 1.5542 2.3002 -0.3012 -0.1725 0.2117  115  LYS B CG    
7995 C  CD    . LYS B 116 ? 2.1806 1.4777 2.2578 -0.3196 -0.2060 0.2210  115  LYS B CD    
7996 C  CE    . LYS B 116 ? 2.3650 1.7270 2.5156 -0.2975 -0.2196 0.2307  115  LYS B CE    
7997 N  NZ    . LYS B 116 ? 2.3387 1.7113 2.4722 -0.2962 -0.2386 0.2321  115  LYS B NZ    
7998 N  N     . ASP B 117 ? 2.3833 1.4592 2.1840 -0.3081 -0.0560 0.1774  116  ASP B N     
7999 C  CA    . ASP B 117 ? 2.4460 1.4502 2.1799 -0.3277 -0.0312 0.1662  116  ASP B CA    
8000 C  C     . ASP B 117 ? 2.5375 1.5124 2.2593 -0.3724 -0.0603 0.1636  116  ASP B C     
8001 O  O     . ASP B 117 ? 2.6812 1.6036 2.3388 -0.4072 -0.0708 0.1550  116  ASP B O     
8002 C  CB    . ASP B 117 ? 2.5025 1.4645 2.1651 -0.3309 -0.0162 0.1571  116  ASP B CB    
8003 C  CG    . ASP B 117 ? 2.9685 1.8582 2.5667 -0.3397 0.0235  0.1453  116  ASP B CG    
8004 O  OD1   . ASP B 117 ? 3.0027 1.8771 2.6128 -0.3397 0.0413  0.1447  116  ASP B OD1   
8005 O  OD2   . ASP B 117 ? 3.1256 1.9721 2.6612 -0.3466 0.0386  0.1364  116  ASP B OD2   
8006 N  N     . ARG B 118 ? 2.4772 1.4871 2.2620 -0.3720 -0.0734 0.1714  117  ARG B N     
8007 C  CA    . ARG B 118 ? 2.3577 1.3507 2.1462 -0.4122 -0.1028 0.1718  117  ARG B CA    
8008 C  C     . ARG B 118 ? 2.4412 1.4344 2.2639 -0.4047 -0.0805 0.1729  117  ARG B C     
8009 O  O     . ARG B 118 ? 2.2727 1.2985 2.1370 -0.3674 -0.0537 0.1776  117  ARG B O     
8010 C  CB    . ARG B 118 ? 2.4190 1.4637 2.2628 -0.4257 -0.1542 0.1835  117  ARG B CB    
8011 C  CG    . ARG B 118 ? 2.5969 1.6425 2.4095 -0.4356 -0.1805 0.1841  117  ARG B CG    
8012 C  CD    . ARG B 118 ? 2.6309 1.6150 2.3680 -0.4832 -0.2004 0.1766  117  ARG B CD    
8013 N  NE    . ARG B 118 ? 2.8329 1.8252 2.5988 -0.5199 -0.2429 0.1845  117  ARG B NE    
8014 C  CZ    . ARG B 118 ? 3.0074 1.9554 2.7190 -0.5669 -0.2707 0.1815  117  ARG B CZ    
8015 N  NH1   . ARG B 118 ? 3.0407 1.9289 2.6620 -0.5845 -0.2591 0.1692  117  ARG B NH1   
8016 N  NH2   . ARG B 118 ? 3.0560 2.0199 2.8047 -0.5979 -0.3109 0.1915  117  ARG B NH2   
8017 N  N     . ASP B 119 ? 2.5840 1.5394 2.3867 -0.4425 -0.0924 0.1688  118  ASP B N     
8018 C  CA    . ASP B 119 ? 2.4322 1.3847 2.2662 -0.4400 -0.0732 0.1696  118  ASP B CA    
8019 C  C     . ASP B 119 ? 2.2610 1.2827 2.1885 -0.4288 -0.0957 0.1831  118  ASP B C     
8020 O  O     . ASP B 119 ? 2.3471 1.3892 2.3172 -0.4049 -0.0707 0.1866  118  ASP B O     
8021 C  CB    . ASP B 119 ? 2.4153 1.3067 2.1998 -0.4864 -0.0805 0.1609  118  ASP B CB    
8022 C  CG    . ASP B 119 ? 2.7153 1.5314 2.4049 -0.4982 -0.0519 0.1458  118  ASP B CG    
8023 O  OD1   . ASP B 119 ? 2.7848 1.5926 2.4559 -0.4638 -0.0126 0.1424  118  ASP B OD1   
8024 O  OD2   . ASP B 119 ? 3.0440 1.8088 2.6777 -0.5427 -0.0682 0.1376  118  ASP B OD2   
8025 N  N     . GLU B 120 ? 2.4068 1.4642 2.3677 -0.4458 -0.1416 0.1913  119  GLU B N     
8026 C  CA    . GLU B 120 ? 2.5061 1.6285 2.5587 -0.4365 -0.1634 0.2043  119  GLU B CA    
8027 C  C     . GLU B 120 ? 2.3795 1.5450 2.4597 -0.4341 -0.1993 0.2128  119  GLU B C     
8028 O  O     . GLU B 120 ? 2.3666 1.5084 2.3931 -0.4471 -0.2133 0.2091  119  GLU B O     
8029 C  CB    . GLU B 120 ? 2.6050 1.7217 2.6857 -0.4720 -0.1865 0.2080  119  GLU B CB    
8030 C  CG    . GLU B 120 ? 2.6433 1.7310 2.6855 -0.5201 -0.2292 0.2081  119  GLU B CG    
8031 C  CD    . GLU B 120 ? 3.0648 2.1548 3.1437 -0.5552 -0.2553 0.2142  119  GLU B CD    
8032 O  OE1   . GLU B 120 ? 2.9754 2.0965 3.1192 -0.5401 -0.2423 0.2193  119  GLU B OE1   
8033 O  OE2   . GLU B 120 ? 3.1927 2.2534 3.2350 -0.5990 -0.2891 0.2142  119  GLU B OE2   
8034 N  N     . PHE B 121 ? 2.3747 1.6023 2.5397 -0.4174 -0.2127 0.2243  120  PHE B N     
8035 C  CA    . PHE B 121 ? 2.2445 1.5169 2.4474 -0.4136 -0.2460 0.2339  120  PHE B CA    
8036 C  C     . PHE B 121 ? 2.1306 1.4592 2.4307 -0.4096 -0.2634 0.2465  120  PHE B C     
8037 O  O     . PHE B 121 ? 2.2383 1.5821 2.5766 -0.3908 -0.2361 0.2463  120  PHE B O     
8038 C  CB    . PHE B 121 ? 2.2770 1.5675 2.4674 -0.3760 -0.2239 0.2310  120  PHE B CB    
8039 C  CG    . PHE B 121 ? 2.2187 1.5289 2.4087 -0.3807 -0.2566 0.2363  120  PHE B CG    
8040 C  CD1   . PHE B 121 ? 2.2151 1.4824 2.3337 -0.4070 -0.2736 0.2314  120  PHE B CD1   
8041 C  CD2   . PHE B 121 ? 2.1925 1.5616 2.4515 -0.3596 -0.2690 0.2459  120  PHE B CD2   
8042 C  CE1   . PHE B 121 ? 2.2068 1.4908 2.3235 -0.4118 -0.3037 0.2370  120  PHE B CE1   
8043 C  CE2   . PHE B 121 ? 2.1500 1.5356 2.4090 -0.3639 -0.2983 0.2512  120  PHE B CE2   
8044 C  CZ    . PHE B 121 ? 2.1811 1.5248 2.3692 -0.3898 -0.3164 0.2473  120  PHE B CZ    
8045 N  N     . PRO B 122 ? 2.0737 1.4328 2.4165 -0.4268 -0.3071 0.2582  121  PRO B N     
8046 C  CA    . PRO B 122 ? 2.1352 1.5466 2.5758 -0.4245 -0.3231 0.2711  121  PRO B CA    
8047 C  C     . PRO B 122 ? 2.1279 1.5849 2.6244 -0.3818 -0.2933 0.2720  121  PRO B C     
8048 O  O     . PRO B 122 ? 2.0125 1.4961 2.5184 -0.3599 -0.2942 0.2736  121  PRO B O     
8049 C  CB    . PRO B 122 ? 2.0825 1.5157 2.5488 -0.4463 -0.3737 0.2841  121  PRO B CB    
8050 C  CG    . PRO B 122 ? 2.1268 1.5303 2.5149 -0.4472 -0.3771 0.2772  121  PRO B CG    
8051 C  CD    . PRO B 122 ? 2.1398 1.4849 2.4437 -0.4508 -0.3440 0.2613  121  PRO B CD    
8052 N  N     . MET B 123 ? 2.0489 1.5134 2.5804 -0.3713 -0.2667 0.2707  122  MET B N     
8053 C  CA    . MET B 123 ? 1.6979 1.2036 2.2825 -0.3345 -0.2378 0.2718  122  MET B CA    
8054 C  C     . MET B 123 ? 1.6921 1.2133 2.3390 -0.3390 -0.2288 0.2761  122  MET B C     
8055 O  O     . MET B 123 ? 1.7320 1.2204 2.3584 -0.3620 -0.2280 0.2736  122  MET B O     
8056 C  CB    . MET B 123 ? 1.5676 1.0544 2.0964 -0.3044 -0.1955 0.2610  122  MET B CB    
8057 C  CG    . MET B 123 ? 1.9757 1.4110 2.4466 -0.3124 -0.1693 0.2523  122  MET B CG    
8058 S  SD    . MET B 123 ? 1.9344 1.3487 2.3429 -0.2768 -0.1223 0.2430  122  MET B SD    
8059 C  CE    . MET B 123 ? 1.6373 1.0378 1.9887 -0.2812 -0.1429 0.2397  122  MET B CE    
8060 N  N     . ILE B 124 ? 1.7297 1.2995 2.4519 -0.3178 -0.2210 0.2822  123  ILE B N     
8061 C  CA    . ILE B 124 ? 1.4850 1.0760 2.2768 -0.3203 -0.2122 0.2873  123  ILE B CA    
8062 C  C     . ILE B 124 ? 1.4208 1.0287 2.2271 -0.2850 -0.1677 0.2824  123  ILE B C     
8063 O  O     . ILE B 124 ? 1.5227 1.1575 2.3389 -0.2595 -0.1585 0.2819  123  ILE B O     
8064 C  CB    . ILE B 124 ? 1.5218 1.1570 2.4021 -0.3323 -0.2464 0.3012  123  ILE B CB    
8065 C  CG1   . ILE B 124 ? 1.5103 1.1305 2.3727 -0.3676 -0.2942 0.3083  123  ILE B CG1   
8066 C  CG2   . ILE B 124 ? 1.4957 1.1505 2.4487 -0.3372 -0.2363 0.3065  123  ILE B CG2   
8067 C  CD1   . ILE B 124 ? 2.0000 1.5776 2.8231 -0.4011 -0.3027 0.3057  123  ILE B CD1   
8068 N  N     . LEU B 125 ? 1.3847 0.9761 2.1903 -0.2850 -0.1407 0.2791  124  LEU B N     
8069 C  CA    . LEU B 125 ? 1.3558 0.9609 2.1741 -0.2547 -0.0988 0.2758  124  LEU B CA    
8070 C  C     . LEU B 125 ? 1.5338 1.1856 2.4453 -0.2492 -0.0980 0.2831  124  LEU B C     
8071 O  O     . LEU B 125 ? 1.3280 0.9850 2.2891 -0.2694 -0.1083 0.2885  124  LEU B O     
8072 C  CB    . LEU B 125 ? 1.5812 1.1466 2.3588 -0.2573 -0.0696 0.2702  124  LEU B CB    
8073 C  CG    . LEU B 125 ? 1.3758 0.9486 2.1559 -0.2278 -0.0254 0.2679  124  LEU B CG    
8074 C  CD1   . LEU B 125 ? 1.6142 1.1908 2.3495 -0.1990 -0.0092 0.2645  124  LEU B CD1   
8075 C  CD2   . LEU B 125 ? 1.4128 0.9447 2.1597 -0.2351 -0.0008 0.2644  124  LEU B CD2   
8076 N  N     . ILE B 126 ? 1.3271 1.0122 2.2631 -0.2229 -0.0847 0.2830  125  ILE B N     
8077 C  CA    . ILE B 126 ? 1.2353 0.9643 2.2586 -0.2159 -0.0816 0.2889  125  ILE B CA    
8078 C  C     . ILE B 126 ? 1.3796 1.1160 2.4068 -0.1911 -0.0368 0.2841  125  ILE B C     
8079 O  O     . ILE B 126 ? 1.2297 0.9586 2.2044 -0.1695 -0.0152 0.2784  125  ILE B O     
8080 C  CB    . ILE B 126 ? 1.2021 0.9634 2.2548 -0.2082 -0.1033 0.2928  125  ILE B CB    
8081 C  CG1   . ILE B 126 ? 1.2241 0.9751 2.2644 -0.2333 -0.1486 0.2985  125  ILE B CG1   
8082 C  CG2   . ILE B 126 ? 1.1676 0.9714 2.3143 -0.2020 -0.0980 0.2988  125  ILE B CG2   
8083 C  CD1   . ILE B 126 ? 1.2418 0.9991 2.3404 -0.2624 -0.1760 0.3087  125  ILE B CD1   
8084 N  N     . GLY B 127 ? 1.2121 0.9636 2.3017 -0.1951 -0.0233 0.2874  126  GLY B N     
8085 C  CA    . GLY B 127 ? 1.1958 0.9572 2.2969 -0.1739 0.0181  0.2839  126  GLY B CA    
8086 C  C     . GLY B 127 ? 1.1572 0.9614 2.3330 -0.1633 0.0237  0.2864  126  GLY B C     
8087 O  O     . GLY B 127 ? 1.4890 1.3126 2.7402 -0.1758 0.0163  0.2924  126  GLY B O     
8088 N  N     . ASN B 128 ? 1.1318 0.9503 2.2886 -0.1409 0.0377  0.2821  127  ASN B N     
8089 C  CA    . ASN B 128 ? 1.0978 0.9535 2.3184 -0.1312 0.0424  0.2831  127  ASN B CA    
8090 C  C     . ASN B 128 ? 1.2316 1.0967 2.4756 -0.1178 0.0848  0.2794  127  ASN B C     
8091 O  O     . ASN B 128 ? 1.3228 1.1666 2.5299 -0.1145 0.1097  0.2767  127  ASN B O     
8092 C  CB    . ASN B 128 ? 1.1295 0.9951 2.3170 -0.1168 0.0332  0.2799  127  ASN B CB    
8093 C  CG    . ASN B 128 ? 1.1501 1.0509 2.4079 -0.1131 0.0258  0.2826  127  ASN B CG    
8094 O  OD1   . ASN B 128 ? 1.3059 1.2236 2.6403 -0.1247 0.0167  0.2893  127  ASN B OD1   
8095 N  ND2   . ASN B 128 ? 1.1727 1.0847 2.4069 -0.0970 0.0302  0.2779  127  ASN B ND2   
8096 N  N     . LYS B 129 ? 1.0636 0.9594 2.3696 -0.1106 0.0939  0.2793  128  LYS B N     
8097 C  CA    . LYS B 129 ? 1.0569 0.9630 2.3897 -0.0995 0.1348  0.2750  128  LYS B CA    
8098 C  C     . LYS B 129 ? 1.0767 0.9736 2.4433 -0.1117 0.1495  0.2780  128  LYS B C     
8099 O  O     . LYS B 129 ? 1.0865 0.9741 2.4360 -0.1042 0.1850  0.2740  128  LYS B O     
8100 C  CB    . LYS B 129 ? 1.0624 0.9579 2.3209 -0.0801 0.1627  0.2676  128  LYS B CB    
8101 C  CG    . LYS B 129 ? 1.0371 0.9447 2.2665 -0.0676 0.1525  0.2640  128  LYS B CG    
8102 C  CD    . LYS B 129 ? 1.3281 1.2303 2.4946 -0.0497 0.1821  0.2580  128  LYS B CD    
8103 C  CE    . LYS B 129 ? 1.0330 0.9472 2.1686 -0.0388 0.1708  0.2546  128  LYS B CE    
8104 N  NZ    . LYS B 129 ? 1.1531 1.0632 2.2251 -0.0231 0.1962  0.2505  128  LYS B NZ    
8105 N  N     . ALA B 130 ? 1.0843 0.9840 2.4995 -0.1319 0.1213  0.2858  129  ALA B N     
8106 C  CA    . ALA B 130 ? 1.1037 0.9962 2.5563 -0.1461 0.1322  0.2892  129  ALA B CA    
8107 C  C     . ALA B 130 ? 1.0901 1.0073 2.6231 -0.1423 0.1610  0.2894  129  ALA B C     
8108 O  O     . ALA B 130 ? 1.1058 1.0163 2.6641 -0.1499 0.1811  0.2903  129  ALA B O     
8109 C  CB    . ALA B 130 ? 1.1212 1.0111 2.6029 -0.1712 0.0911  0.2983  129  ALA B CB    
8110 N  N     . ASP B 131 ? 1.0637 1.0072 2.6371 -0.1311 0.1652  0.2881  130  ASP B N     
8111 C  CA    . ASP B 131 ? 1.0538 1.0179 2.7013 -0.1267 0.1974  0.2869  130  ASP B CA    
8112 C  C     . ASP B 131 ? 1.0641 1.0135 2.6662 -0.1135 0.2445  0.2771  130  ASP B C     
8113 O  O     . ASP B 131 ? 1.4774 1.4316 3.1267 -0.1151 0.2758  0.2759  130  ASP B O     
8114 C  CB    . ASP B 131 ? 1.0264 1.0189 2.7259 -0.1183 0.1913  0.2875  130  ASP B CB    
8115 C  CG    . ASP B 131 ? 1.0790 1.0670 2.7090 -0.1003 0.1998  0.2782  130  ASP B CG    
8116 O  OD1   . ASP B 131 ? 1.0279 1.0020 2.5889 -0.0993 0.1753  0.2780  130  ASP B OD1   
8117 O  OD2   . ASP B 131 ? 1.1153 1.1128 2.7591 -0.0881 0.2322  0.2708  130  ASP B OD2   
8118 N  N     . LEU B 132 ? 1.0682 0.9999 2.5798 -0.1011 0.2501  0.2710  131  LEU B N     
8119 C  CA    . LEU B 132 ? 1.0809 0.9983 2.5414 -0.0892 0.2913  0.2639  131  LEU B CA    
8120 C  C     . LEU B 132 ? 1.3317 1.2224 2.7618 -0.0970 0.3018  0.2665  131  LEU B C     
8121 O  O     . LEU B 132 ? 1.5917 1.4588 2.9431 -0.0907 0.3058  0.2656  131  LEU B O     
8122 C  CB    . LEU B 132 ? 1.0986 1.0106 2.4794 -0.0734 0.2907  0.2588  131  LEU B CB    
8123 C  CG    . LEU B 132 ? 1.0483 0.9837 2.4494 -0.0651 0.2834  0.2549  131  LEU B CG    
8124 C  CD1   . LEU B 132 ? 1.0542 0.9827 2.3712 -0.0514 0.2809  0.2506  131  LEU B CD1   
8125 C  CD2   . LEU B 132 ? 1.4136 1.3647 2.8707 -0.0618 0.3183  0.2494  131  LEU B CD2   
8126 N  N     . ASP B 133 ? 1.5899 1.4847 3.0876 -0.1111 0.3069  0.2705  132  ASP B N     
8127 C  CA    . ASP B 133 ? 1.6332 1.5027 3.1104 -0.1207 0.3174  0.2730  132  ASP B CA    
8128 C  C     . ASP B 133 ? 1.4775 1.3305 2.9081 -0.1093 0.3615  0.2682  132  ASP B C     
8129 O  O     . ASP B 133 ? 1.7184 1.5436 3.0966 -0.1108 0.3699  0.2699  132  ASP B O     
8130 C  CB    . ASP B 133 ? 1.8937 1.7750 3.4603 -0.1394 0.3129  0.2788  132  ASP B CB    
8131 C  CG    . ASP B 133 ? 1.9640 1.8564 3.5672 -0.1549 0.2649  0.2865  132  ASP B CG    
8132 O  OD1   . ASP B 133 ? 1.6373 1.5099 3.1802 -0.1594 0.2380  0.2876  132  ASP B OD1   
8133 O  OD2   . ASP B 133 ? 1.9722 1.8925 3.6647 -0.1631 0.2545  0.2920  132  ASP B OD2   
8134 N  N     . HIS B 134 ? 1.3102 1.1782 2.7574 -0.0988 0.3903  0.2626  133  HIS B N     
8135 C  CA    . HIS B 134 ? 1.1728 1.0257 2.5730 -0.0896 0.4315  0.2586  133  HIS B CA    
8136 C  C     . HIS B 134 ? 1.1789 1.0155 2.4817 -0.0757 0.4294  0.2583  133  HIS B C     
8137 O  O     . HIS B 134 ? 1.1994 1.0204 2.4534 -0.0689 0.4592  0.2580  133  HIS B O     
8138 C  CB    . HIS B 134 ? 1.4669 1.3385 2.9095 -0.0847 0.4627  0.2518  133  HIS B CB    
8139 C  CG    . HIS B 134 ? 1.1383 1.0301 2.5815 -0.0753 0.4493  0.2472  133  HIS B CG    
8140 N  ND1   . HIS B 134 ? 1.1298 1.0440 2.6361 -0.0798 0.4195  0.2495  133  HIS B ND1   
8141 C  CD2   . HIS B 134 ? 1.1352 1.0280 2.5237 -0.0626 0.4613  0.2412  133  HIS B CD2   
8142 C  CE1   . HIS B 134 ? 1.4548 1.3815 2.9450 -0.0695 0.4151  0.2444  133  HIS B CE1   
8143 N  NE2   . HIS B 134 ? 1.6611 1.5753 3.0798 -0.0594 0.4400  0.2388  133  HIS B NE2   
8144 N  N     . GLN B 135 ? 1.3587 1.1989 2.6332 -0.0717 0.3952  0.2594  134  GLN B N     
8145 C  CA    . GLN B 135 ? 1.3464 1.1733 2.5339 -0.0585 0.3912  0.2603  134  GLN B CA    
8146 C  C     . GLN B 135 ? 1.1853 0.9944 2.3390 -0.0628 0.3590  0.2652  134  GLN B C     
8147 O  O     . GLN B 135 ? 1.1732 0.9748 2.2641 -0.0522 0.3484  0.2662  134  GLN B O     
8148 C  CB    . GLN B 135 ? 1.1715 1.0194 2.3458 -0.0469 0.3867  0.2552  134  GLN B CB    
8149 C  CG    . GLN B 135 ? 1.1454 1.0045 2.3330 -0.0421 0.4226  0.2490  134  GLN B CG    
8150 C  CD    . GLN B 135 ? 1.2862 1.1668 2.4742 -0.0343 0.4164  0.2428  134  GLN B CD    
8151 O  OE1   . GLN B 135 ? 1.6551 1.5451 2.8437 -0.0329 0.3841  0.2435  134  GLN B OE1   
8152 N  NE2   . GLN B 135 ? 1.6088 1.4955 2.7942 -0.0306 0.4484  0.2363  134  GLN B NE2   
8153 N  N     . ARG B 136 ? 1.1832 0.9847 2.3767 -0.0793 0.3441  0.2681  135  ARG B N     
8154 C  CA    . ARG B 136 ? 1.1952 0.9759 2.3553 -0.0869 0.3146  0.2715  135  ARG B CA    
8155 C  C     . ARG B 136 ? 1.5730 1.3200 2.6623 -0.0808 0.3323  0.2744  135  ARG B C     
8156 O  O     . ARG B 136 ? 1.3126 1.0463 2.4056 -0.0831 0.3598  0.2762  135  ARG B O     
8157 C  CB    . ARG B 136 ? 1.2008 0.9825 2.4231 -0.1092 0.2940  0.2742  135  ARG B CB    
8158 C  CG    . ARG B 136 ? 1.4106 1.1635 2.5934 -0.1214 0.2687  0.2769  135  ARG B CG    
8159 C  CD    . ARG B 136 ? 1.5119 1.2633 2.7530 -0.1462 0.2523  0.2802  135  ARG B CD    
8160 N  NE    . ARG B 136 ? 1.2396 1.0193 2.5412 -0.1568 0.2187  0.2826  135  ARG B NE    
8161 C  CZ    . ARG B 136 ? 1.2183 0.9923 2.5061 -0.1691 0.1801  0.2848  135  ARG B CZ    
8162 N  NH1   . ARG B 136 ? 1.2446 0.9840 2.4597 -0.1727 0.1713  0.2833  135  ARG B NH1   
8163 N  NH2   . ARG B 136 ? 1.5536 1.3557 2.9017 -0.1784 0.1505  0.2890  135  ARG B NH2   
8164 N  N     . GLN B 137 ? 1.4492 1.1816 2.4751 -0.0727 0.3175  0.2757  136  GLN B N     
8165 C  CA    . GLN B 137 ? 1.3727 1.0718 2.3325 -0.0660 0.3318  0.2799  136  GLN B CA    
8166 C  C     . GLN B 137 ? 1.4450 1.1147 2.3825 -0.0790 0.3094  0.2808  136  GLN B C     
8167 O  O     . GLN B 137 ? 1.6014 1.2385 2.4943 -0.0771 0.3237  0.2842  136  GLN B O     
8168 C  CB    . GLN B 137 ? 1.4031 1.1056 2.3022 -0.0443 0.3390  0.2818  136  GLN B CB    
8169 C  CG    . GLN B 137 ? 1.5826 1.3050 2.4849 -0.0322 0.3669  0.2818  136  GLN B CG    
8170 C  CD    . GLN B 137 ? 1.9755 1.7031 2.8180 -0.0131 0.3707  0.2850  136  GLN B CD    
8171 O  OE1   . GLN B 137 ? 1.7476 1.4731 2.5593 -0.0080 0.3489  0.2855  136  GLN B OE1   
8172 N  NE2   . GLN B 137 ? 1.8871 1.6214 2.7124 -0.0035 0.3983  0.2877  136  GLN B NE2   
8173 N  N     . VAL B 138 ? 1.3799 1.0585 2.3454 -0.0929 0.2756  0.2782  137  VAL B N     
8174 C  CA    . VAL B 138 ? 1.2957 0.9456 2.2409 -0.1100 0.2524  0.2781  137  VAL B CA    
8175 C  C     . VAL B 138 ? 1.4202 1.0787 2.4344 -0.1345 0.2367  0.2782  137  VAL B C     
8176 O  O     . VAL B 138 ? 1.6285 1.3164 2.6940 -0.1416 0.2132  0.2780  137  VAL B O     
8177 C  CB    . VAL B 138 ? 1.2945 0.9447 2.2052 -0.1077 0.2230  0.2761  137  VAL B CB    
8178 C  CG1   . VAL B 138 ? 1.3213 0.9343 2.1978 -0.1257 0.2044  0.2752  137  VAL B CG1   
8179 C  CG2   . VAL B 138 ? 1.2762 0.9285 2.1319 -0.0822 0.2380  0.2769  137  VAL B CG2   
8180 N  N     . THR B 139 ? 1.5361 1.1696 2.5538 -0.1478 0.2494  0.2794  138  THR B N     
8181 C  CA    . THR B 139 ? 1.6508 1.2928 2.7359 -0.1724 0.2355  0.2808  138  THR B CA    
8182 C  C     . THR B 139 ? 1.7300 1.3641 2.8135 -0.1942 0.1934  0.2807  138  THR B C     
8183 O  O     . THR B 139 ? 1.4670 1.0837 2.4924 -0.1908 0.1784  0.2786  138  THR B O     
8184 C  CB    . THR B 139 ? 1.3923 1.0079 2.4778 -0.1816 0.2613  0.2819  138  THR B CB    
8185 O  OG1   . THR B 139 ? 1.7512 1.3806 2.9101 -0.2055 0.2484  0.2840  138  THR B OG1   
8186 C  CG2   . THR B 139 ? 1.4086 0.9762 2.4224 -0.1877 0.2606  0.2807  138  THR B CG2   
8187 N  N     . GLN B 140 ? 1.7755 1.4229 2.9246 -0.2180 0.1742  0.2839  139  GLN B N     
8188 C  CA    . GLN B 140 ? 1.6074 1.2511 2.7611 -0.2420 0.1310  0.2856  139  GLN B CA    
8189 C  C     . GLN B 140 ? 1.9546 1.5480 3.0381 -0.2574 0.1263  0.2822  139  GLN B C     
8190 O  O     . GLN B 140 ? 1.7786 1.3568 2.8229 -0.2679 0.0978  0.2806  139  GLN B O     
8191 C  CB    . GLN B 140 ? 1.6481 1.3200 2.8932 -0.2645 0.1120  0.2921  139  GLN B CB    
8192 C  CG    . GLN B 140 ? 1.8333 1.5528 3.1551 -0.2503 0.1205  0.2955  139  GLN B CG    
8193 C  CD    . GLN B 140 ? 1.6708 1.4209 3.0872 -0.2723 0.0956  0.3042  139  GLN B CD    
8194 O  OE1   . GLN B 140 ? 1.6377 1.3761 3.0602 -0.2999 0.0662  0.3084  139  GLN B OE1   
8195 N  NE2   . GLN B 140 ? 1.6974 1.4865 3.1886 -0.2611 0.1077  0.3073  139  GLN B NE2   
8196 N  N     . GLU B 141 ? 2.0076 1.5724 3.0729 -0.2595 0.1555  0.2807  140  GLU B N     
8197 C  CA    . GLU B 141 ? 1.7131 1.2263 2.7138 -0.2752 0.1549  0.2769  140  GLU B CA    
8198 C  C     . GLU B 141 ? 1.7927 1.2795 2.7100 -0.2573 0.1599  0.2726  140  GLU B C     
8199 O  O     . GLU B 141 ? 2.0249 1.4758 2.8902 -0.2728 0.1443  0.2687  140  GLU B O     
8200 C  CB    . GLU B 141 ? 1.9161 1.4045 2.9153 -0.2775 0.1896  0.2767  140  GLU B CB    
8201 C  CG    . GLU B 141 ? 2.2951 1.7956 3.3654 -0.3047 0.1809  0.2800  140  GLU B CG    
8202 C  CD    . GLU B 141 ? 2.2187 1.7728 3.3765 -0.2968 0.1826  0.2852  140  GLU B CD    
8203 O  OE1   . GLU B 141 ? 2.1999 1.7753 3.3572 -0.2686 0.2018  0.2850  140  GLU B OE1   
8204 O  OE2   . GLU B 141 ? 2.3297 1.9042 3.5574 -0.3195 0.1652  0.2898  140  GLU B OE2   
8205 N  N     . GLU B 142 ? 1.4644 0.9680 2.3676 -0.2257 0.1821  0.2733  141  GLU B N     
8206 C  CA    . GLU B 142 ? 1.4671 0.9528 2.2995 -0.2074 0.1852  0.2708  141  GLU B CA    
8207 C  C     . GLU B 142 ? 1.7196 1.2207 2.5488 -0.2134 0.1478  0.2693  141  GLU B C     
8208 O  O     . GLU B 142 ? 1.9289 1.4063 2.6962 -0.2079 0.1434  0.2662  141  GLU B O     
8209 C  CB    . GLU B 142 ? 1.4398 0.9433 2.2615 -0.1739 0.2164  0.2736  141  GLU B CB    
8210 C  CG    . GLU B 142 ? 1.4567 0.9455 2.2783 -0.1664 0.2543  0.2765  141  GLU B CG    
8211 C  CD    . GLU B 142 ? 1.4319 0.9404 2.2424 -0.1359 0.2820  0.2805  141  GLU B CD    
8212 O  OE1   . GLU B 142 ? 1.6483 1.1637 2.4222 -0.1182 0.2779  0.2808  141  GLU B OE1   
8213 O  OE2   . GLU B 142 ? 1.9192 1.4361 2.7568 -0.1311 0.3077  0.2835  141  GLU B OE2   
8214 N  N     . GLY B 143 ? 1.5192 1.0588 2.4148 -0.2243 0.1220  0.2722  142  GLY B N     
8215 C  CA    . GLY B 143 ? 1.5296 1.0834 2.4245 -0.2315 0.0850  0.2722  142  GLY B CA    
8216 C  C     . GLY B 143 ? 1.5987 1.1172 2.4595 -0.2620 0.0566  0.2699  142  GLY B C     
8217 O  O     . GLY B 143 ? 1.4664 0.9647 2.2705 -0.2625 0.0433  0.2664  142  GLY B O     
8218 N  N     . GLN B 144 ? 1.5458 1.0555 2.4395 -0.2894 0.0474  0.2719  143  GLN B N     
8219 C  CA    . GLN B 144 ? 1.5860 1.0580 2.4428 -0.3223 0.0217  0.2693  143  GLN B CA    
8220 C  C     . GLN B 144 ? 1.9146 1.3294 2.6838 -0.3197 0.0460  0.2612  143  GLN B C     
8221 O  O     . GLN B 144 ? 1.9752 1.3524 2.6944 -0.3433 0.0277  0.2567  143  GLN B O     
8222 C  CB    . GLN B 144 ? 1.6141 1.0911 2.5281 -0.3529 0.0080  0.2739  143  GLN B CB    
8223 C  CG    . GLN B 144 ? 1.7822 1.3150 2.7903 -0.3577 -0.0169 0.2836  143  GLN B CG    
8224 C  CD    . GLN B 144 ? 1.7798 1.3426 2.8549 -0.3420 0.0131  0.2869  143  GLN B CD    
8225 O  OE1   . GLN B 144 ? 1.9926 1.5320 3.0508 -0.3378 0.0462  0.2834  143  GLN B OE1   
8226 N  NE2   . GLN B 144 ? 1.7490 1.3621 2.9003 -0.3335 0.0032  0.2939  143  GLN B NE2   
8227 N  N     . GLN B 145 ? 1.8578 1.2641 2.6074 -0.2924 0.0872  0.2600  144  GLN B N     
8228 C  CA    . GLN B 145 ? 1.7850 1.1395 2.4546 -0.2847 0.1126  0.2543  144  GLN B CA    
8229 C  C     . GLN B 145 ? 1.8947 1.2394 2.5089 -0.2749 0.1014  0.2508  144  GLN B C     
8230 O  O     . GLN B 145 ? 2.0736 1.3713 2.6249 -0.2882 0.0997  0.2446  144  GLN B O     
8231 C  CB    . GLN B 145 ? 1.8502 1.2049 2.5171 -0.2550 0.1567  0.2570  144  GLN B CB    
8232 C  CG    . GLN B 145 ? 2.2725 1.5838 2.8631 -0.2374 0.1849  0.2542  144  GLN B CG    
8233 C  CD    . GLN B 145 ? 2.1557 1.4070 2.7006 -0.2612 0.1924  0.2485  144  GLN B CD    
8234 O  OE1   . GLN B 145 ? 2.1296 1.3719 2.7016 -0.2891 0.1829  0.2471  144  GLN B OE1   
8235 N  NE2   . GLN B 145 ? 2.1820 1.3912 2.6582 -0.2507 0.2106  0.2451  144  GLN B NE2   
8236 N  N     . LEU B 146 ? 1.8265 1.2138 2.4626 -0.2523 0.0950  0.2541  145  LEU B N     
8237 C  CA    . LEU B 146 ? 1.7222 1.1053 2.3122 -0.2438 0.0820  0.2513  145  LEU B CA    
8238 C  C     . LEU B 146 ? 1.8014 1.1814 2.3911 -0.2743 0.0386  0.2496  145  LEU B C     
8239 O  O     . LEU B 146 ? 1.8099 1.1698 2.3468 -0.2760 0.0278  0.2454  145  LEU B O     
8240 C  CB    . LEU B 146 ? 1.6119 1.0418 2.2264 -0.2122 0.0880  0.2553  145  LEU B CB    
8241 C  CG    . LEU B 146 ? 1.9879 1.4080 2.5560 -0.1799 0.1219  0.2557  145  LEU B CG    
8242 C  CD1   . LEU B 146 ? 1.8357 1.2236 2.3358 -0.1795 0.1166  0.2510  145  LEU B CD1   
8243 C  CD2   . LEU B 146 ? 2.1736 1.5673 2.7304 -0.1735 0.1579  0.2573  145  LEU B CD2   
8244 N  N     . ALA B 147 ? 1.7558 1.1558 2.4039 -0.2989 0.0134  0.2538  146  ALA B N     
8245 C  CA    . ALA B 147 ? 1.7668 1.1630 2.4148 -0.3311 -0.0304 0.2545  146  ALA B CA    
8246 C  C     . ALA B 147 ? 2.0635 1.3980 2.6403 -0.3588 -0.0327 0.2468  146  ALA B C     
8247 O  O     . ALA B 147 ? 2.1687 1.4814 2.6976 -0.3735 -0.0549 0.2431  146  ALA B O     
8248 C  CB    . ALA B 147 ? 1.6873 1.1214 2.4207 -0.3505 -0.0556 0.2631  146  ALA B CB    
8249 N  N     . ARG B 148 ? 2.1506 1.4539 2.7177 -0.3671 -0.0086 0.2437  147  ARG B N     
8250 C  CA    . ARG B 148 ? 1.9623 1.2018 2.4585 -0.3931 -0.0053 0.2349  147  ARG B CA    
8251 C  C     . ARG B 148 ? 1.9385 1.1395 2.3570 -0.3712 0.0238  0.2274  147  ARG B C     
8252 O  O     . ARG B 148 ? 1.9287 1.0808 2.2804 -0.3911 0.0185  0.2194  147  ARG B O     
8253 C  CB    . ARG B 148 ? 2.0503 1.2671 2.5606 -0.4075 0.0144  0.2339  147  ARG B CB    
8254 C  CG    . ARG B 148 ? 2.0485 1.3067 2.6440 -0.4261 -0.0089 0.2424  147  ARG B CG    
8255 C  CD    . ARG B 148 ? 2.1610 1.3911 2.7633 -0.4442 0.0100  0.2404  147  ARG B CD    
8256 N  NE    . ARG B 148 ? 2.5198 1.7349 3.1057 -0.4132 0.0591  0.2382  147  ARG B NE    
8257 C  CZ    . ARG B 148 ? 2.3434 1.5949 2.9871 -0.3907 0.0803  0.2445  147  ARG B CZ    
8258 N  NH1   . ARG B 148 ? 2.0032 1.3082 2.7283 -0.3941 0.0600  0.2525  147  ARG B NH1   
8259 N  NH2   . ARG B 148 ? 2.2089 1.4417 2.8283 -0.3646 0.1237  0.2434  147  ARG B NH2   
8260 N  N     . GLN B 149 ? 1.9606 1.1824 2.3865 -0.3313 0.0547  0.2303  148  GLN B N     
8261 C  CA    . GLN B 149 ? 1.9597 1.1508 2.3200 -0.3078 0.0824  0.2258  148  GLN B CA    
8262 C  C     . GLN B 149 ? 2.0771 1.2738 2.4074 -0.3078 0.0583  0.2234  148  GLN B C     
8263 O  O     . GLN B 149 ? 2.1607 1.3116 2.4229 -0.3134 0.0653  0.2160  148  GLN B O     
8264 C  CB    . GLN B 149 ? 1.9551 1.1731 2.3362 -0.2668 0.1173  0.2320  148  GLN B CB    
8265 C  CG    . GLN B 149 ? 2.2641 1.4638 2.5902 -0.2385 0.1425  0.2309  148  GLN B CG    
8266 C  CD    . GLN B 149 ? 2.3529 1.5844 2.7021 -0.2001 0.1720  0.2393  148  GLN B CD    
8267 O  OE1   . GLN B 149 ? 2.3506 1.5903 2.7324 -0.1952 0.1898  0.2438  148  GLN B OE1   
8268 N  NE2   . GLN B 149 ? 2.0849 1.3345 2.4164 -0.1740 0.1769  0.2418  148  GLN B NE2   
8269 N  N     . LEU B 150 ? 2.0212 1.2718 2.4016 -0.3016 0.0316  0.2295  149  LEU B N     
8270 C  CA    . LEU B 150 ? 2.2861 1.5461 2.6443 -0.3022 0.0064  0.2283  149  LEU B CA    
8271 C  C     . LEU B 150 ? 2.1065 1.3522 2.4567 -0.3433 -0.0359 0.2267  149  LEU B C     
8272 O  O     . LEU B 150 ? 2.0933 1.3431 2.4222 -0.3483 -0.0599 0.2261  149  LEU B O     
8273 C  CB    . LEU B 150 ? 1.9483 1.2715 2.3625 -0.2758 -0.0015 0.2358  149  LEU B CB    
8274 C  CG    . LEU B 150 ? 1.8351 1.1780 2.2554 -0.2357 0.0360  0.2386  149  LEU B CG    
8275 C  CD1   . LEU B 150 ? 1.8373 1.2401 2.3113 -0.2156 0.0251  0.2446  149  LEU B CD1   
8276 C  CD2   . LEU B 150 ? 1.9515 1.2587 2.3007 -0.2189 0.0606  0.2339  149  LEU B CD2   
8277 N  N     . LYS B 151 ? 2.0176 1.2466 2.3836 -0.3738 -0.0463 0.2268  150  LYS B N     
8278 C  CA    . LYS B 151 ? 2.1705 1.3861 2.5303 -0.4169 -0.0887 0.2270  150  LYS B CA    
8279 C  C     . LYS B 151 ? 1.9258 1.1964 2.3430 -0.4189 -0.1292 0.2372  150  LYS B C     
8280 O  O     . LYS B 151 ? 2.0317 1.2940 2.4249 -0.4426 -0.1639 0.2379  150  LYS B O     
8281 C  CB    . LYS B 151 ? 2.2109 1.3647 2.4777 -0.4369 -0.0893 0.2162  150  LYS B CB    
8282 C  CG    . LYS B 151 ? 2.2029 1.2960 2.4125 -0.4395 -0.0501 0.2060  150  LYS B CG    
8283 C  CD    . LYS B 151 ? 2.1445 1.1744 2.2622 -0.4605 -0.0490 0.1944  150  LYS B CD    
8284 C  CE    . LYS B 151 ? 2.7617 1.7284 2.8245 -0.4624 -0.0068 0.1842  150  LYS B CE    
8285 N  NZ    . LYS B 151 ? 2.9619 1.8627 2.9336 -0.4833 -0.0016 0.1716  150  LYS B NZ    
8286 N  N     . VAL B 152 ? 1.6765 1.0021 2.1696 -0.3942 -0.1236 0.2453  151  VAL B N     
8287 C  CA    . VAL B 152 ? 1.6300 1.0096 2.1865 -0.3926 -0.1571 0.2557  151  VAL B CA    
8288 C  C     . VAL B 152 ? 1.6098 1.0258 2.2541 -0.4034 -0.1687 0.2653  151  VAL B C     
8289 O  O     . VAL B 152 ? 1.7100 1.1083 2.3614 -0.4130 -0.1515 0.2633  151  VAL B O     
8290 C  CB    . VAL B 152 ? 1.5727 0.9871 2.1411 -0.3517 -0.1394 0.2563  151  VAL B CB    
8291 C  CG1   . VAL B 152 ? 1.7282 1.1081 2.2134 -0.3410 -0.1271 0.2476  151  VAL B CG1   
8292 C  CG2   . VAL B 152 ? 1.9375 1.3722 2.5423 -0.3222 -0.1002 0.2566  151  VAL B CG2   
8293 N  N     . THR B 153 ? 1.8553 1.3217 2.5686 -0.4017 -0.1965 0.2761  152  THR B N     
8294 C  CA    . THR B 153 ? 1.8195 1.3263 2.6261 -0.4093 -0.2073 0.2867  152  THR B CA    
8295 C  C     . THR B 153 ? 1.6817 1.2304 2.5431 -0.3711 -0.1765 0.2881  152  THR B C     
8296 O  O     . THR B 153 ? 1.8667 1.4356 2.7236 -0.3459 -0.1719 0.2874  152  THR B O     
8297 C  CB    . THR B 153 ? 1.8005 1.3359 2.6548 -0.4339 -0.2586 0.2998  152  THR B CB    
8298 O  OG1   . THR B 153 ? 1.9845 1.4783 2.7797 -0.4719 -0.2882 0.2984  152  THR B OG1   
8299 C  CG2   . THR B 153 ? 1.5460 1.1235 2.5026 -0.4423 -0.2688 0.3121  152  THR B CG2   
8300 N  N     . TYR B 154 ? 1.5002 1.0601 2.4104 -0.3684 -0.1547 0.2898  153  TYR B N     
8301 C  CA    . TYR B 154 ? 1.4673 1.0636 2.4289 -0.3360 -0.1235 0.2907  153  TYR B CA    
8302 C  C     . TYR B 154 ? 1.6859 1.3338 2.7492 -0.3407 -0.1442 0.3027  153  TYR B C     
8303 O  O     . TYR B 154 ? 1.6075 1.2610 2.7131 -0.3701 -0.1726 0.3110  153  TYR B O     
8304 C  CB    . TYR B 154 ? 1.8045 1.3806 2.7568 -0.3282 -0.0826 0.2853  153  TYR B CB    
8305 C  CG    . TYR B 154 ? 1.5755 1.1834 2.5682 -0.2956 -0.0474 0.2854  153  TYR B CG    
8306 C  CD1   . TYR B 154 ? 1.5326 1.1436 2.4860 -0.2645 -0.0253 0.2805  153  TYR B CD1   
8307 C  CD2   . TYR B 154 ? 1.4603 1.0945 2.5291 -0.2974 -0.0358 0.2905  153  TYR B CD2   
8308 C  CE1   . TYR B 154 ? 1.4915 1.1296 2.4764 -0.2375 0.0061  0.2805  153  TYR B CE1   
8309 C  CE2   . TYR B 154 ? 1.3435 1.0033 2.4443 -0.2698 -0.0022 0.2897  153  TYR B CE2   
8310 C  CZ    . TYR B 154 ? 1.3226 0.9836 2.3790 -0.2406 0.0181  0.2846  153  TYR B CZ    
8311 O  OH    . TYR B 154 ? 1.3024 0.9871 2.3854 -0.2157 0.0507  0.2838  153  TYR B OH    
8312 N  N     . MET B 155 ? 1.5095 1.1946 2.6127 -0.3121 -0.1292 0.3040  154  MET B N     
8313 C  CA    . MET B 155 ? 1.3500 1.0842 2.5526 -0.3121 -0.1430 0.3149  154  MET B CA    
8314 C  C     . MET B 155 ? 1.2885 1.0502 2.5175 -0.2774 -0.1075 0.3111  154  MET B C     
8315 O  O     . MET B 155 ? 1.4760 1.2390 2.6648 -0.2569 -0.1012 0.3059  154  MET B O     
8316 C  CB    . MET B 155 ? 1.4605 1.2113 2.6805 -0.3262 -0.1895 0.3243  154  MET B CB    
8317 C  CG    . MET B 155 ? 1.7085 1.5102 3.0351 -0.3247 -0.2042 0.3374  154  MET B CG    
8318 S  SD    . MET B 155 ? 1.3030 1.1248 2.6441 -0.3332 -0.2538 0.3489  154  MET B SD    
8319 C  CE    . MET B 155 ? 1.3322 1.1137 2.6129 -0.3752 -0.2957 0.3522  154  MET B CE    
8320 N  N     . GLU B 156 ? 1.2470 1.0297 2.5415 -0.2722 -0.0838 0.3133  155  GLU B N     
8321 C  CA    . GLU B 156 ? 1.3651 1.1735 2.6877 -0.2428 -0.0498 0.3097  155  GLU B CA    
8322 C  C     . GLU B 156 ? 1.1735 1.0236 2.5662 -0.2375 -0.0687 0.3173  155  GLU B C     
8323 O  O     . GLU B 156 ? 1.4963 1.3627 2.9427 -0.2576 -0.1044 0.3286  155  GLU B O     
8324 C  CB    . GLU B 156 ? 1.2096 1.0222 2.5738 -0.2399 -0.0147 0.3087  155  GLU B CB    
8325 C  CG    . GLU B 156 ? 1.2394 1.0120 2.5321 -0.2371 0.0137  0.3005  155  GLU B CG    
8326 C  CD    . GLU B 156 ? 1.5074 1.2852 2.8350 -0.2289 0.0537  0.2989  155  GLU B CD    
8327 O  OE1   . GLU B 156 ? 1.6264 1.4360 3.0396 -0.2321 0.0561  0.3044  155  GLU B OE1   
8328 O  OE2   . GLU B 156 ? 1.4128 1.1625 2.6830 -0.2189 0.0836  0.2927  155  GLU B OE2   
8329 N  N     . ALA B 157 ? 1.1424 1.0090 2.5339 -0.2109 -0.0446 0.3117  156  ALA B N     
8330 C  CA    . ALA B 157 ? 1.2505 1.1530 2.7022 -0.2029 -0.0572 0.3173  156  ALA B CA    
8331 C  C     . ALA B 157 ? 1.3708 1.2914 2.8441 -0.1773 -0.0151 0.3102  156  ALA B C     
8332 O  O     . ALA B 157 ? 1.4004 1.3047 2.8298 -0.1651 0.0200  0.3013  156  ALA B O     
8333 C  CB    . ALA B 157 ? 1.2070 1.1044 2.6097 -0.2017 -0.0870 0.3174  156  ALA B CB    
8334 N  N     . SER B 158 ? 1.1456 1.0989 2.6866 -0.1701 -0.0187 0.3147  157  SER B N     
8335 C  CA    . SER B 158 ? 1.2654 1.2353 2.8280 -0.1480 0.0204  0.3072  157  SER B CA    
8336 C  C     . SER B 158 ? 1.0134 1.0104 2.6219 -0.1409 0.0052  0.3113  157  SER B C     
8337 O  O     . SER B 158 ? 1.1766 1.1973 2.8713 -0.1503 -0.0120 0.3227  157  SER B O     
8338 C  CB    . SER B 158 ? 1.2913 1.2713 2.9201 -0.1501 0.0504  0.3082  157  SER B CB    
8339 O  OG    . SER B 158 ? 1.0137 1.0079 2.6630 -0.1309 0.0887  0.3005  157  SER B OG    
8340 N  N     . ALA B 159 ? 1.1568 1.1508 2.7102 -0.1245 0.0115  0.3031  158  ALA B N     
8341 C  CA    . ALA B 159 ? 1.3300 1.3469 2.9208 -0.1169 -0.0002 0.3059  158  ALA B CA    
8342 C  C     . ALA B 159 ? 1.1919 1.2331 2.8624 -0.1069 0.0311  0.3046  158  ALA B C     
8343 O  O     . ALA B 159 ? 1.4493 1.5126 3.1816 -0.1050 0.0191  0.3110  158  ALA B O     
8344 C  CB    . ALA B 159 ? 1.1351 1.1417 2.6443 -0.1024 0.0018  0.2964  158  ALA B CB    
8345 N  N     . LYS B 160 ? 0.9868 1.0229 2.6571 -0.1007 0.0720  0.2966  159  LYS B N     
8346 C  CA    . LYS B 160 ? 1.0904 1.1454 2.8309 -0.0919 0.1067  0.2935  159  LYS B CA    
8347 C  C     . LYS B 160 ? 1.1809 1.2583 3.0317 -0.1041 0.0941  0.3073  159  LYS B C     
8348 O  O     . LYS B 160 ? 0.9639 1.0624 2.8889 -0.0975 0.1083  0.3091  159  LYS B O     
8349 C  CB    . LYS B 160 ? 0.9565 0.9973 2.6631 -0.0847 0.1529  0.2823  159  LYS B CB    
8350 C  CG    . LYS B 160 ? 0.9497 1.0045 2.7138 -0.0757 0.1948  0.2760  159  LYS B CG    
8351 C  CD    . LYS B 160 ? 0.9632 1.0005 2.6658 -0.0667 0.2384  0.2631  159  LYS B CD    
8352 C  CE    . LYS B 160 ? 1.0986 1.1458 2.8546 -0.0605 0.2825  0.2558  159  LYS B CE    
8353 N  NZ    . LYS B 160 ? 1.3811 1.4102 3.0713 -0.0535 0.3238  0.2438  159  LYS B NZ    
8354 N  N     . ILE B 161 ? 1.0383 1.1112 2.9026 -0.1222 0.0679  0.3175  160  ILE B N     
8355 C  CA    . ILE B 161 ? 0.9552 1.0510 2.9241 -0.1364 0.0503  0.3332  160  ILE B CA    
8356 C  C     . ILE B 161 ? 0.9591 1.0602 2.9371 -0.1532 -0.0063 0.3485  160  ILE B C     
8357 O  O     . ILE B 161 ? 1.4601 1.5811 3.5221 -0.1679 -0.0285 0.3645  160  ILE B O     
8358 C  CB    . ILE B 161 ? 1.0366 1.1265 3.0305 -0.1471 0.0699  0.3339  160  ILE B CB    
8359 C  CG1   . ILE B 161 ? 0.9967 1.0567 2.9059 -0.1596 0.0526  0.3317  160  ILE B CG1   
8360 C  CG2   . ILE B 161 ? 0.9711 1.0574 2.9656 -0.1319 0.1267  0.3204  160  ILE B CG2   
8361 C  CD1   . ILE B 161 ? 1.0165 1.0669 2.9424 -0.1708 0.0717  0.3319  160  ILE B CD1   
8362 N  N     . ARG B 162 ? 0.9623 1.0462 2.8566 -0.1524 -0.0302 0.3448  161  ARG B N     
8363 C  CA    . ARG B 162 ? 1.1376 1.2209 3.0240 -0.1695 -0.0836 0.3579  161  ARG B CA    
8364 C  C     . ARG B 162 ? 0.9968 1.0732 2.8983 -0.1950 -0.1075 0.3680  161  ARG B C     
8365 O  O     . ARG B 162 ? 1.5389 1.6363 3.5186 -0.2113 -0.1371 0.3853  161  ARG B O     
8366 C  CB    . ARG B 162 ? 0.9758 1.0894 2.9429 -0.1678 -0.1061 0.3717  161  ARG B CB    
8367 C  CG    . ARG B 162 ? 1.1710 1.2800 3.1050 -0.1800 -0.1573 0.3819  161  ARG B CG    
8368 C  CD    . ARG B 162 ? 1.3214 1.4603 3.3386 -0.1777 -0.1792 0.3975  161  ARG B CD    
8369 N  NE    . ARG B 162 ? 0.9563 1.0864 2.9177 -0.1782 -0.2111 0.3994  161  ARG B NE    
8370 C  CZ    . ARG B 162 ? 0.9646 1.0854 2.8975 -0.1996 -0.2590 0.4111  161  ARG B CZ    
8371 N  NH1   . ARG B 162 ? 0.9875 1.1067 2.9407 -0.2235 -0.2829 0.4222  161  ARG B NH1   
8372 N  NH2   . ARG B 162 ? 1.1314 1.2433 3.0120 -0.1984 -0.2831 0.4115  161  ARG B NH2   
8373 N  N     . MET B 163 ? 1.1893 1.2351 3.0134 -0.1986 -0.0937 0.3572  162  MET B N     
8374 C  CA    . MET B 163 ? 1.1427 1.1738 2.9622 -0.2232 -0.1119 0.3631  162  MET B CA    
8375 C  C     . MET B 163 ? 1.3297 1.3298 3.0550 -0.2361 -0.1439 0.3611  162  MET B C     
8376 O  O     . MET B 163 ? 1.3941 1.3689 3.0305 -0.2231 -0.1269 0.3475  162  MET B O     
8377 C  CB    . MET B 163 ? 1.0751 1.0915 2.8808 -0.2190 -0.0693 0.3527  162  MET B CB    
8378 C  CG    . MET B 163 ? 1.1078 1.1066 2.9073 -0.2448 -0.0846 0.3576  162  MET B CG    
8379 S  SD    . MET B 163 ? 1.3541 1.3327 3.1328 -0.2389 -0.0330 0.3456  162  MET B SD    
8380 C  CE    . MET B 163 ? 1.4602 1.4056 3.1150 -0.2163 -0.0084 0.3283  162  MET B CE    
8381 N  N     . ASN B 164 ? 1.1891 1.1911 2.9348 -0.2624 -0.1899 0.3753  163  ASN B N     
8382 C  CA    . ASN B 164 ? 1.3073 1.2773 2.9666 -0.2800 -0.2225 0.3742  163  ASN B CA    
8383 C  C     . ASN B 164 ? 1.3390 1.3007 2.9341 -0.2640 -0.2273 0.3673  163  ASN B C     
8384 O  O     . ASN B 164 ? 1.1439 1.0715 2.6442 -0.2663 -0.2302 0.3578  163  ASN B O     
8385 C  CB    . ASN B 164 ? 1.2284 1.1593 2.8142 -0.2879 -0.2039 0.3625  163  ASN B CB    
8386 C  CG    . ASN B 164 ? 1.3256 1.2614 2.9691 -0.3073 -0.2020 0.3693  163  ASN B CG    
8387 O  OD1   . ASN B 164 ? 1.6432 1.6037 3.3634 -0.3265 -0.2330 0.3856  163  ASN B OD1   
8388 N  ND2   . ASN B 164 ? 1.5404 1.4535 3.1491 -0.3025 -0.1660 0.3579  163  ASN B ND2   
8389 N  N     . VAL B 165 ? 1.5608 1.5527 3.2080 -0.2477 -0.2268 0.3718  164  VAL B N     
8390 C  CA    . VAL B 165 ? 1.0999 1.0864 2.6924 -0.2337 -0.2330 0.3663  164  VAL B CA    
8391 C  C     . VAL B 165 ? 1.3240 1.3048 2.8999 -0.2557 -0.2854 0.3786  164  VAL B C     
8392 O  O     . VAL B 165 ? 1.1011 1.0551 2.5903 -0.2576 -0.2966 0.3717  164  VAL B O     
8393 C  CB    . VAL B 165 ? 1.0714 1.0890 2.7221 -0.2089 -0.2105 0.3654  164  VAL B CB    
8394 C  CG1   . VAL B 165 ? 1.0966 1.1105 2.6969 -0.1973 -0.2214 0.3614  164  VAL B CG1   
8395 C  CG2   . VAL B 165 ? 1.0130 1.0303 2.6619 -0.1885 -0.1574 0.3513  164  VAL B CG2   
8396 N  N     . ASP B 166 ? 1.4603 1.4664 3.1198 -0.2731 -0.3182 0.3979  165  ASP B N     
8397 C  CA    . ASP B 166 ? 1.3649 1.3651 3.0091 -0.2981 -0.3711 0.4119  165  ASP B CA    
8398 C  C     . ASP B 166 ? 1.2574 1.2208 2.8318 -0.3260 -0.3887 0.4090  165  ASP B C     
8399 O  O     . ASP B 166 ? 1.2263 1.1643 2.7304 -0.3417 -0.4180 0.4093  165  ASP B O     
8400 C  CB    . ASP B 166 ? 1.4958 1.5352 3.2534 -0.3097 -0.4022 0.4359  165  ASP B CB    
8401 C  CG    . ASP B 166 ? 1.3461 1.4152 3.1590 -0.2867 -0.3971 0.4413  165  ASP B CG    
8402 O  OD1   . ASP B 166 ? 1.1247 1.2070 2.9678 -0.2607 -0.3536 0.4308  165  ASP B OD1   
8403 O  OD2   . ASP B 166 ? 1.4524 1.5299 3.2767 -0.2957 -0.4362 0.4559  165  ASP B OD2   
8404 N  N     . GLN B 167 ? 1.2674 1.2251 2.8581 -0.3334 -0.3697 0.4056  166  GLN B N     
8405 C  CA    . GLN B 167 ? 1.3534 1.2739 2.8805 -0.3614 -0.3839 0.4023  166  GLN B CA    
8406 C  C     . GLN B 167 ? 1.3666 1.2428 2.7751 -0.3524 -0.3628 0.3825  166  GLN B C     
8407 O  O     . GLN B 167 ? 1.5161 1.3556 2.8534 -0.3761 -0.3822 0.3797  166  GLN B O     
8408 C  CB    . GLN B 167 ? 1.3150 1.2405 2.8911 -0.3698 -0.3650 0.4030  166  GLN B CB    
8409 C  CG    . GLN B 167 ? 1.2220 1.1872 2.9130 -0.3869 -0.3923 0.4250  166  GLN B CG    
8410 C  CD    . GLN B 167 ? 1.3740 1.3840 3.1620 -0.3602 -0.3729 0.4314  166  GLN B CD    
8411 O  OE1   . GLN B 167 ? 1.4470 1.4580 3.2136 -0.3302 -0.3398 0.4187  166  GLN B OE1   
8412 N  NE2   . GLN B 167 ? 1.3972 1.4439 3.2897 -0.3704 -0.3922 0.4507  166  GLN B NE2   
8413 N  N     . ALA B 168 ? 1.2036 1.0819 2.5898 -0.3195 -0.3228 0.3691  167  ALA B N     
8414 C  CA    . ALA B 168 ? 1.2180 1.0578 2.4981 -0.3088 -0.3015 0.3521  167  ALA B CA    
8415 C  C     . ALA B 168 ? 1.4799 1.3024 2.6983 -0.3175 -0.3330 0.3531  167  ALA B C     
8416 O  O     . ALA B 168 ? 1.5893 1.3708 2.7231 -0.3312 -0.3383 0.3456  167  ALA B O     
8417 C  CB    . ALA B 168 ? 1.1805 1.0316 2.4570 -0.2726 -0.2551 0.3403  167  ALA B CB    
8418 N  N     . PHE B 169 ? 1.3778 1.2294 2.6372 -0.3102 -0.3525 0.3622  168  PHE B N     
8419 C  CA    . PHE B 169 ? 1.3828 1.2193 2.5866 -0.3186 -0.3827 0.3641  168  PHE B CA    
8420 C  C     . PHE B 169 ? 1.6545 1.4795 2.8580 -0.3570 -0.4323 0.3782  168  PHE B C     
8421 O  O     . PHE B 169 ? 1.9700 1.7639 3.0978 -0.3725 -0.4537 0.3758  168  PHE B O     
8422 C  CB    . PHE B 169 ? 1.4262 1.2962 2.6732 -0.2976 -0.3857 0.3693  168  PHE B CB    
8423 C  CG    . PHE B 169 ? 1.3586 1.2362 2.5910 -0.2626 -0.3404 0.3546  168  PHE B CG    
8424 C  CD1   . PHE B 169 ? 1.1487 1.0040 2.2968 -0.2497 -0.3282 0.3421  168  PHE B CD1   
8425 C  CD2   . PHE B 169 ? 1.1477 1.0543 2.4503 -0.2440 -0.3099 0.3538  168  PHE B CD2   
8426 C  CE1   . PHE B 169 ? 1.1177 0.9817 2.2523 -0.2195 -0.2889 0.3301  168  PHE B CE1   
8427 C  CE2   . PHE B 169 ? 1.1166 1.0288 2.4013 -0.2147 -0.2696 0.3406  168  PHE B CE2   
8428 C  CZ    . PHE B 169 ? 1.0873 0.9793 2.2882 -0.2028 -0.2604 0.3294  168  PHE B CZ    
8429 N  N     . HIS B 170 ? 1.4249 1.2743 2.7110 -0.3738 -0.4510 0.3932  169  HIS B N     
8430 C  CA    . HIS B 170 ? 1.5124 1.3537 2.8014 -0.4129 -0.5010 0.4087  169  HIS B CA    
8431 C  C     . HIS B 170 ? 1.5168 1.3110 2.7286 -0.4385 -0.5001 0.3987  169  HIS B C     
8432 O  O     . HIS B 170 ? 1.5227 1.2885 2.6792 -0.4692 -0.5350 0.4026  169  HIS B O     
8433 C  CB    . HIS B 170 ? 1.6837 1.5693 3.0919 -0.4225 -0.5220 0.4299  169  HIS B CB    
8434 C  CG    . HIS B 170 ? 1.7298 1.6578 3.2143 -0.4041 -0.5320 0.4433  169  HIS B CG    
8435 N  ND1   . HIS B 170 ? 1.5179 1.4887 3.1099 -0.3864 -0.5147 0.4514  169  HIS B ND1   
8436 C  CD2   . HIS B 170 ? 1.5703 1.5024 3.0391 -0.4008 -0.5558 0.4498  169  HIS B CD2   
8437 C  CE1   . HIS B 170 ? 1.5491 1.5478 3.1889 -0.3727 -0.5267 0.4622  169  HIS B CE1   
8438 N  NE2   . HIS B 170 ? 1.7134 1.6899 3.2801 -0.3810 -0.5525 0.4618  169  HIS B NE2   
8439 N  N     . GLU B 171 ? 1.6371 1.4202 2.8419 -0.4274 -0.4599 0.3859  170  GLU B N     
8440 C  CA    . GLU B 171 ? 1.7962 1.5299 2.9211 -0.4484 -0.4529 0.3743  170  GLU B CA    
8441 C  C     . GLU B 171 ? 1.8570 1.5472 2.8708 -0.4411 -0.4396 0.3582  170  GLU B C     
8442 O  O     . GLU B 171 ? 1.7732 1.4167 2.7108 -0.4645 -0.4436 0.3504  170  GLU B O     
8443 C  CB    . GLU B 171 ? 1.5798 1.3125 2.7273 -0.4368 -0.4114 0.3656  170  GLU B CB    
8444 C  CG    . GLU B 171 ? 1.7609 1.5229 3.0025 -0.4551 -0.4262 0.3801  170  GLU B CG    
8445 C  CD    . GLU B 171 ? 1.8483 1.5857 3.0676 -0.5008 -0.4658 0.3878  170  GLU B CD    
8446 O  OE1   . GLU B 171 ? 1.8583 1.5459 2.9790 -0.5171 -0.4683 0.3766  170  GLU B OE1   
8447 O  OE2   . GLU B 171 ? 2.1030 1.8706 3.4038 -0.5212 -0.4939 0.4053  170  GLU B OE2   
8448 N  N     . LEU B 172 ? 1.5963 1.3002 2.6001 -0.4099 -0.4230 0.3530  171  LEU B N     
8449 C  CA    . LEU B 172 ? 1.5553 1.2216 2.4595 -0.4028 -0.4121 0.3395  171  LEU B CA    
8450 C  C     . LEU B 172 ? 1.6743 1.3232 2.5376 -0.4309 -0.4572 0.3469  171  LEU B C     
8451 O  O     . LEU B 172 ? 1.8864 1.4880 2.6585 -0.4458 -0.4580 0.3370  171  LEU B O     
8452 C  CB    . LEU B 172 ? 1.5160 1.2045 2.4245 -0.3622 -0.3811 0.3324  171  LEU B CB    
8453 C  CG    . LEU B 172 ? 1.5285 1.1848 2.3432 -0.3507 -0.3676 0.3195  171  LEU B CG    
8454 C  CD1   . LEU B 172 ? 1.5729 1.1798 2.3103 -0.3572 -0.3425 0.3060  171  LEU B CD1   
8455 C  CD2   . LEU B 172 ? 1.3204 1.0044 2.1493 -0.3118 -0.3382 0.3141  171  LEU B CD2   
8456 N  N     . VAL B 173 ? 1.9199 1.6051 2.8497 -0.4389 -0.4943 0.3648  172  VAL B N     
8457 C  CA    . VAL B 173 ? 1.8291 1.4996 2.7233 -0.4672 -0.5401 0.3745  172  VAL B CA    
8458 C  C     . VAL B 173 ? 1.8667 1.5086 2.7374 -0.5121 -0.5715 0.3804  172  VAL B C     
8459 O  O     . VAL B 173 ? 2.1672 1.7807 2.9793 -0.5411 -0.6048 0.3840  172  VAL B O     
8460 C  CB    . VAL B 173 ? 1.7112 1.4300 2.6870 -0.4609 -0.5702 0.3939  172  VAL B CB    
8461 C  CG1   . VAL B 173 ? 1.7791 1.5310 2.8504 -0.4812 -0.5998 0.4144  172  VAL B CG1   
8462 C  CG2   . VAL B 173 ? 2.0000 1.7016 2.9210 -0.4764 -0.6047 0.3992  172  VAL B CG2   
8463 N  N     . ARG B 174 ? 1.7850 1.4322 2.6973 -0.5202 -0.5613 0.3813  173  ARG B N     
8464 C  CA    . ARG B 174 ? 1.8866 1.5040 2.7724 -0.5639 -0.5876 0.3851  173  ARG B CA    
8465 C  C     . ARG B 174 ? 2.1899 1.7432 2.9633 -0.5745 -0.5629 0.3639  173  ARG B C     
8466 O  O     . ARG B 174 ? 2.4171 1.9328 3.1380 -0.6148 -0.5884 0.3644  173  ARG B O     
8467 C  CB    . ARG B 174 ? 1.8339 1.4812 2.8090 -0.5696 -0.5854 0.3942  173  ARG B CB    
8468 C  CG    . ARG B 174 ? 1.7924 1.4998 2.8843 -0.5685 -0.6162 0.4184  173  ARG B CG    
8469 C  CD    . ARG B 174 ? 1.9166 1.6485 3.0913 -0.5797 -0.6154 0.4274  173  ARG B CD    
8470 N  NE    . ARG B 174 ? 2.0715 1.8642 3.3601 -0.5707 -0.6365 0.4492  173  ARG B NE    
8471 C  CZ    . ARG B 174 ? 1.8182 1.6507 3.1932 -0.5385 -0.6080 0.4514  173  ARG B CZ    
8472 N  NH1   . ARG B 174 ? 1.6738 1.4963 3.0247 -0.5065 -0.5555 0.4315  173  ARG B NH1   
8473 N  NH2   . ARG B 174 ? 1.8660 1.7509 3.3317 -0.5263 -0.6248 0.4697  173  ARG B NH2   
8474 N  N     . VAL B 175 ? 2.0363 1.5758 2.7725 -0.5401 -0.5136 0.3460  174  VAL B N     
8475 C  CA    . VAL B 175 ? 1.8813 1.3592 2.5124 -0.5473 -0.4878 0.3269  174  VAL B CA    
8476 C  C     . VAL B 175 ? 2.1344 1.5825 2.6837 -0.5514 -0.4987 0.3213  174  VAL B C     
8477 O  O     . VAL B 175 ? 2.2531 1.6447 2.7110 -0.5727 -0.4941 0.3094  174  VAL B O     
8478 C  CB    . VAL B 175 ? 1.7783 1.2535 2.4057 -0.5099 -0.4309 0.3123  174  VAL B CB    
8479 C  CG1   . VAL B 175 ? 2.0217 1.4324 2.5511 -0.5195 -0.4032 0.2946  174  VAL B CG1   
8480 C  CG2   . VAL B 175 ? 1.7212 1.2323 2.4382 -0.5030 -0.4202 0.3192  174  VAL B CG2   
8481 N  N     . ILE B 176 ? 1.9615 1.4446 2.5411 -0.5322 -0.5117 0.3293  175  ILE B N     
8482 C  CA    . ILE B 176 ? 2.0980 1.5552 2.6041 -0.5369 -0.5238 0.3253  175  ILE B CA    
8483 C  C     . ILE B 176 ? 2.3046 1.7349 2.7737 -0.5859 -0.5730 0.3346  175  ILE B C     
8484 O  O     . ILE B 176 ? 2.4480 1.8272 2.8221 -0.6050 -0.5750 0.3246  175  ILE B O     
8485 C  CB    . ILE B 176 ? 1.8677 1.3710 2.4212 -0.5053 -0.5265 0.3325  175  ILE B CB    
8486 C  CG1   . ILE B 176 ? 1.7533 1.2811 2.3379 -0.4597 -0.4778 0.3229  175  ILE B CG1   
8487 C  CG2   . ILE B 176 ? 1.9036 1.3799 2.3810 -0.5100 -0.5377 0.3283  175  ILE B CG2   
8488 C  CD1   . ILE B 176 ? 1.7636 1.3376 2.3993 -0.4293 -0.4778 0.3291  175  ILE B CD1   
8489 N  N     . ARG B 177 ? 2.4272 1.8910 2.9703 -0.6079 -0.6133 0.3545  176  ARG B N     
8490 C  CA    . ARG B 177 ? 2.3820 1.8228 2.8931 -0.6575 -0.6637 0.3659  176  ARG B CA    
8491 C  C     . ARG B 177 ? 2.5205 1.9059 2.9631 -0.6914 -0.6565 0.3537  176  ARG B C     
8492 O  O     . ARG B 177 ? 2.6742 2.0120 3.0342 -0.7289 -0.6790 0.3508  176  ARG B O     
8493 C  CB    . ARG B 177 ? 2.2920 1.7875 2.9089 -0.6707 -0.7088 0.3929  176  ARG B CB    
8494 C  CG    . ARG B 177 ? 2.5707 2.0988 3.2748 -0.6631 -0.6946 0.3973  176  ARG B CG    
8495 C  CD    . ARG B 177 ? 2.8179 2.3989 3.6242 -0.6774 -0.7389 0.4245  176  ARG B CD    
8496 N  NE    . ARG B 177 ? 2.9219 2.5297 3.8023 -0.6719 -0.7226 0.4268  176  ARG B NE    
8497 C  CZ    . ARG B 177 ? 2.8232 2.4836 3.7927 -0.6703 -0.7445 0.4459  176  ARG B CZ    
8498 N  NH1   . ARG B 177 ? 2.7802 2.4728 3.7796 -0.6725 -0.7844 0.4665  176  ARG B NH1   
8499 N  NH2   . ARG B 177 ? 2.4900 2.1692 3.5200 -0.6656 -0.7248 0.4454  176  ARG B NH2   
8500 N  N     . LYS B 178 ? 2.3394 1.7275 2.8122 -0.6798 -0.6241 0.3461  177  LYS B N     
8501 C  CA    . LYS B 178 ? 2.2635 1.5985 2.6753 -0.7089 -0.6115 0.3333  177  LYS B CA    
8502 C  C     . LYS B 178 ? 2.3896 1.6673 2.7009 -0.6945 -0.5645 0.3086  177  LYS B C     
8503 O  O     . LYS B 178 ? 2.4107 1.6409 2.6697 -0.7123 -0.5440 0.2954  177  LYS B O     
8504 C  CB    . LYS B 178 ? 2.1380 1.4998 2.6270 -0.7028 -0.5959 0.3365  177  LYS B CB    
8505 N  N     . PHE B 179 ? 2.4892 1.7705 2.7751 -0.6628 -0.5462 0.3025  178  PHE B N     
8506 C  CA    . PHE B 179 ? 2.6243 1.8540 2.8184 -0.6482 -0.5032 0.2811  178  PHE B CA    
8507 C  C     . PHE B 179 ? 2.7714 1.9447 2.8661 -0.6859 -0.5246 0.2755  178  PHE B C     
8508 O  O     . PHE B 179 ? 2.8736 1.9893 2.8989 -0.7172 -0.5178 0.2643  178  PHE B O     
8509 C  CB    . PHE B 179 ? 2.5051 1.7666 2.7199 -0.5974 -0.4733 0.2778  178  PHE B CB    
8510 C  CG    . PHE B 179 ? 2.6493 1.8650 2.7821 -0.5778 -0.4268 0.2582  178  PHE B CG    
8511 C  CD1   . PHE B 179 ? 2.6273 1.8278 2.7554 -0.5572 -0.3806 0.2470  178  PHE B CD1   
8512 C  CD2   . PHE B 179 ? 2.9370 2.1255 3.0002 -0.5794 -0.4287 0.2521  178  PHE B CD2   
8513 C  CE1   . PHE B 179 ? 2.7782 1.9384 2.8367 -0.5380 -0.3378 0.2313  178  PHE B CE1   
8514 C  CE2   . PHE B 179 ? 2.8617 2.0099 2.8553 -0.5606 -0.3848 0.2353  178  PHE B CE2   
8515 C  CZ    . PHE B 179 ? 2.6177 1.7524 2.6105 -0.5395 -0.3395 0.2254  178  PHE B CZ    
8516 N  N     . GLN B 180 ? 2.9659 2.1533 3.0520 -0.6842 -0.5496 0.2829  179  GLN B N     
8517 C  CA    . GLN B 180 ? 3.1328 2.2709 3.1280 -0.7210 -0.5743 0.2799  179  GLN B CA    
8518 C  C     . GLN B 180 ? 3.1507 2.2168 3.0387 -0.7242 -0.5318 0.2559  179  GLN B C     
8519 O  O     . GLN B 180 ? 3.0856 2.1487 2.9578 -0.6853 -0.4883 0.2441  179  GLN B O     
8520 C  CB    . GLN B 180 ? 3.2444 2.3745 3.2424 -0.7750 -0.6270 0.2937  179  GLN B CB    
8521 C  CG    . GLN B 180 ? 3.2567 2.3318 3.1553 -0.8195 -0.6553 0.2911  179  GLN B CG    
8522 C  CD    . GLN B 180 ? 3.1876 2.1868 2.9912 -0.8542 -0.6359 0.2722  179  GLN B CD    
8523 O  OE1   . GLN B 180 ? 3.1834 2.1750 3.0050 -0.8531 -0.6126 0.2653  179  GLN B OE1   
8524 N  NE2   . GLN B 180 ? 3.3913 2.3328 3.0916 -0.8849 -0.6435 0.2632  179  GLN B NE2   
8525 C  C2    . 5H5 C .   ? 2.3939 1.4995 1.5991 -0.2817 -0.0850 0.1451  1101 5H5 A C2    
8526 C  C4    . 5H5 C .   ? 2.2486 1.3965 1.4991 -0.2856 -0.1333 0.1564  1101 5H5 A C4    
8527 C  C6    . 5H5 C .   ? 2.2705 1.3979 1.5165 -0.3081 -0.1642 0.1599  1101 5H5 A C6    
8528 C  C8    . 5H5 C .   ? 2.2673 1.5245 1.6222 -0.2343 -0.1262 0.1655  1101 5H5 A C8    
8529 C  C12   . 5H5 C .   ? 2.1170 1.5850 1.6738 -0.1599 -0.1481 0.1847  1101 5H5 A C12   
8530 C  C15   . 5H5 C .   ? 2.1071 1.5584 1.5915 -0.1641 -0.1083 0.1761  1101 5H5 A C15   
8531 C  C16   . 5H5 C .   ? 2.2659 1.6607 1.6832 -0.1881 -0.1044 0.1709  1101 5H5 A C16   
8532 C  C18   . 5H5 C .   ? 2.0724 1.4461 1.4974 -0.1911 -0.1132 0.1717  1101 5H5 A C18   
8533 C  C19   . 5H5 C .   ? 2.0146 1.3504 1.4184 -0.2041 -0.1180 0.1700  1101 5H5 A C19   
8534 C  C21   . 5H5 C .   ? 2.4445 1.6729 1.7490 -0.2470 -0.1165 0.1608  1101 5H5 A C21   
8535 C  C24   . 5H5 C .   ? 2.4436 1.8584 1.8334 -0.1924 -0.0893 0.1685  1101 5H5 A C24   
8536 C  C27   . 5H5 C .   ? 2.1942 1.4544 1.4436 -0.2451 -0.0843 0.1568  1101 5H5 A C27   
8537 N  N1    . 5H5 C .   ? 2.3988 1.4448 1.5258 -0.3068 -0.0718 0.1365  1101 5H5 A N1    
8538 O  O3    . 5H5 C .   ? 2.4807 1.6026 1.7169 -0.2574 -0.0569 0.1438  1101 5H5 A O3    
8539 O  O7    . 5H5 C .   ? 2.2973 1.5151 1.6265 -0.2507 -0.1301 0.1629  1101 5H5 A O7    
8540 C  C9    . 5H5 C .   ? 2.1200 1.4442 1.5492 -0.2064 -0.1313 0.1723  1101 5H5 A C9    
8541 C  C10   . 5H5 C .   ? 2.1220 1.4863 1.5767 -0.1912 -0.1276 0.1745  1101 5H5 A C10   
8542 O  O11   . 5H5 C .   ? 2.1452 1.5715 1.6689 -0.1666 -0.1326 0.1804  1101 5H5 A O11   
8543 C  C13   . 5H5 C .   ? 2.0435 1.5263 1.5936 -0.1450 -0.1173 0.1814  1101 5H5 A C13   
8544 N  N14   . 5H5 C .   ? 1.9661 1.4030 1.4544 -0.1660 -0.1133 0.1766  1101 5H5 A N14   
8545 N  N17   . 5H5 C .   ? 2.3082 1.6546 1.6870 -0.2054 -0.1074 0.1680  1101 5H5 A N17   
8546 C  C20   . 5H5 C .   ? 2.2698 1.5372 1.5994 -0.2316 -0.1123 0.1632  1101 5H5 A C20   
8547 C  C22   . 5H5 C .   ? 2.2899 1.6777 1.6793 -0.1953 -0.0972 0.1686  1101 5H5 A C22   
8548 N  N23   . 5H5 C .   ? 2.2789 1.7172 1.7099 -0.1795 -0.0974 0.1718  1101 5H5 A N23   
8549 N  N25   . 5H5 C .   ? 2.3320 1.6814 1.6538 -0.2161 -0.0835 0.1631  1101 5H5 A N25   
8550 N  N26   . 5H5 C .   ? 2.2431 1.5755 1.5650 -0.2182 -0.0890 0.1631  1101 5H5 A N26   
8551 C  C28   . 5H5 C .   ? 2.5078 1.7375 1.7219 -0.2772 -0.1267 0.1611  1101 5H5 A C28   
8552 C  C29   . 5H5 C .   ? 2.3690 1.5904 1.5671 -0.2484 -0.0422 0.1475  1101 5H5 A C29   
8553 P  PG    . GNP D .   ? 1.1411 1.0647 1.9659 0.0072  0.0662  0.2455  201  GNP B PG    
8554 O  O1G   . GNP D .   ? 1.0685 1.0020 1.8705 0.0210  0.0986  0.2432  201  GNP B O1G   
8555 O  O2G   . GNP D .   ? 1.1670 1.1046 2.0006 0.0059  0.0437  0.2434  201  GNP B O2G   
8556 O  O3G   . GNP D .   ? 1.3865 1.2803 2.1718 0.0015  0.0560  0.2496  201  GNP B O3G   
8557 N  N3B   . GNP D .   ? 1.1437 1.0747 2.0513 -0.0047 0.0692  0.2465  201  GNP B N3B   
8558 P  PB    . GNP D .   ? 1.2249 1.1427 2.1699 -0.0239 0.0408  0.2524  201  GNP B PB    
8559 O  O1B   . GNP D .   ? 1.0086 0.9006 1.9304 -0.0298 0.0480  0.2552  201  GNP B O1B   
8560 O  O2B   . GNP D .   ? 1.1727 1.0907 2.1120 -0.0308 0.0068  0.2544  201  GNP B O2B   
8561 O  O3A   . GNP D .   ? 1.4038 1.3422 2.4380 -0.0300 0.0479  0.2535  201  GNP B O3A   
8562 P  PA    . GNP D .   ? 1.1290 1.0928 2.2084 -0.0208 0.0735  0.2482  201  GNP B PA    
8563 O  O1A   . GNP D .   ? 0.9332 0.9123 2.0980 -0.0304 0.0629  0.2524  201  GNP B O1A   
8564 O  O2A   . GNP D .   ? 1.5002 1.4728 2.5355 -0.0076 0.0823  0.2419  201  GNP B O2A   
8565 O  "O5'" . GNP D .   ? 1.1342 1.0892 2.2093 -0.0180 0.1084  0.2467  201  GNP B "O5'" 
8566 C  "C5'" . GNP D .   ? 1.3838 1.3456 2.4384 -0.0062 0.1417  0.2406  201  GNP B "C5'" 
8567 C  "C4'" . GNP D .   ? 1.4214 1.3912 2.5352 -0.0091 0.1681  0.2386  201  GNP B "C4'" 
8568 O  "O4'" . GNP D .   ? 1.3556 1.3157 2.5067 -0.0208 0.1614  0.2446  201  GNP B "O4'" 
8569 C  "C3'" . GNP D .   ? 1.2410 1.2323 2.4198 -0.0098 0.1709  0.2349  201  GNP B "C3'" 
8570 O  "O3'" . GNP D .   ? 1.1419 1.1379 2.3281 -0.0047 0.2093  0.2279  201  GNP B "O3'" 
8571 C  "C2'" . GNP D .   ? 1.2542 1.2488 2.5073 -0.0226 0.1531  0.2425  201  GNP B "C2'" 
8572 O  "O2'" . GNP D .   ? 0.9624 0.9739 2.2903 -0.0234 0.1687  0.2406  201  GNP B "O2'" 
8573 C  "C1'" . GNP D .   ? 1.1253 1.1013 2.3594 -0.0275 0.1636  0.2455  201  GNP B "C1'" 
8574 N  N9    . GNP D .   ? 0.9667 0.9382 2.2426 -0.0423 0.1386  0.2541  201  GNP B N9    
8575 C  C8    . GNP D .   ? 1.1821 1.1470 2.4465 -0.0515 0.0998  0.2604  201  GNP B C8    
8576 N  N7    . GNP D .   ? 1.0239 0.9859 2.3325 -0.0667 0.0836  0.2679  201  GNP B N7    
8577 C  C5    . GNP D .   ? 0.9806 0.9487 2.3356 -0.0666 0.1137  0.2666  201  GNP B C5    
8578 C  C6    . GNP D .   ? 1.1738 1.1436 2.5911 -0.0802 0.1139  0.2729  201  GNP B C6    
8579 O  O6    . GNP D .   ? 1.0321 0.9989 2.4753 -0.0964 0.0850  0.2814  201  GNP B O6    
8580 N  N1    . GNP D .   ? 0.9911 0.9667 2.4393 -0.0744 0.1539  0.2682  201  GNP B N1    
8581 C  C2    . GNP D .   ? 1.0740 1.0517 2.4939 -0.0593 0.1879  0.2588  201  GNP B C2    
8582 N  N2    . GNP D .   ? 0.9925 0.9730 2.4457 -0.0578 0.2249  0.2552  201  GNP B N2    
8583 N  N3    . GNP D .   ? 1.0195 0.9964 2.3813 -0.0480 0.1858  0.2535  201  GNP B N3    
8584 C  C4    . GNP D .   ? 0.9743 0.9470 2.3082 -0.0515 0.1488  0.2578  201  GNP B C4    
8585 MG MG    . MG  E .   ? 1.0521 0.9868 1.9593 -0.0182 0.0000  0.2496  202  MG  B MG    
# 
