data_9B4T
# 
_entry.id   9B4T 
# 
_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   9B4T         pdb_00009b4t 10.2210/pdb9b4t/pdb 
WWPDB D_1000282624 ?            ?                   
# 
_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                        9B4T 
_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 M-Ras' 20384.250  1  3.6.5.2                      Q35A                     ? ? 
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  ?                            ?                        ? ? 
6 water       nat water 18.015     27 ?                            ?                        ? ? 
# 
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-related protein R-Ras3' 
# 
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 
;GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFAKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMRE
QYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKD
PPLNVDKAFHDLVRVIRQQ
;
;GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFAKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMRE
QYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKD
PPLNVDKAFHDLVRVIRQQ
;
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  
6 water                                                                                                                HOH 
# 
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   THR n 
2 5   SER n 
2 6   ALA n 
2 7   VAL n 
2 8   PRO n 
2 9   SER n 
2 10  ASP n 
2 11  ASN n 
2 12  LEU n 
2 13  PRO n 
2 14  THR n 
2 15  TYR n 
2 16  LYS n 
2 17  LEU n 
2 18  VAL n 
2 19  VAL n 
2 20  VAL n 
2 21  GLY n 
2 22  ASP n 
2 23  GLY n 
2 24  GLY n 
2 25  VAL n 
2 26  GLY n 
2 27  LYS n 
2 28  SER n 
2 29  ALA n 
2 30  LEU n 
2 31  THR n 
2 32  ILE n 
2 33  GLN n 
2 34  PHE n 
2 35  PHE n 
2 36  ALA n 
2 37  LYS n 
2 38  ILE n 
2 39  PHE n 
2 40  VAL n 
2 41  PRO n 
2 42  ASP n 
2 43  TYR n 
2 44  ASP n 
2 45  PRO n 
2 46  THR n 
2 47  ILE n 
2 48  GLU n 
2 49  ASP n 
2 50  SER n 
2 51  TYR n 
2 52  LEU n 
2 53  LYS n 
2 54  HIS n 
2 55  THR n 
2 56  GLU n 
2 57  ILE n 
2 58  ASP n 
2 59  ASN n 
2 60  GLN n 
2 61  TRP n 
2 62  ALA n 
2 63  ILE n 
2 64  LEU n 
2 65  ASP n 
2 66  VAL n 
2 67  LEU n 
2 68  ASP n 
2 69  THR n 
2 70  ALA n 
2 71  GLY n 
2 72  GLN n 
2 73  GLU n 
2 74  GLU n 
2 75  PHE n 
2 76  SER n 
2 77  ALA n 
2 78  MET n 
2 79  ARG n 
2 80  GLU n 
2 81  GLN n 
2 82  TYR n 
2 83  MET n 
2 84  ARG n 
2 85  THR n 
2 86  GLY n 
2 87  ASP n 
2 88  GLY n 
2 89  PHE n 
2 90  LEU n 
2 91  ILE n 
2 92  VAL n 
2 93  TYR n 
2 94  SER n 
2 95  VAL n 
2 96  THR n 
2 97  ASP n 
2 98  LYS n 
2 99  ALA n 
2 100 SER n 
2 101 PHE n 
2 102 GLU n 
2 103 HIS n 
2 104 VAL n 
2 105 ASP n 
2 106 ARG n 
2 107 PHE n 
2 108 HIS n 
2 109 GLN n 
2 110 LEU n 
2 111 ILE n 
2 112 LEU n 
2 113 ARG n 
2 114 VAL n 
2 115 LYS n 
2 116 ASP n 
2 117 ARG n 
2 118 GLU n 
2 119 SER n 
2 120 PHE n 
2 121 PRO n 
2 122 MET n 
2 123 ILE n 
2 124 LEU n 
2 125 VAL n 
2 126 ALA n 
2 127 ASN n 
2 128 LYS n 
2 129 VAL n 
2 130 ASP n 
2 131 LEU n 
2 132 MET n 
2 133 HIS n 
2 134 LEU n 
2 135 ARG n 
2 136 LYS n 
2 137 ILE n 
2 138 THR n 
2 139 ARG n 
2 140 GLU n 
2 141 GLN n 
2 142 GLY n 
2 143 LYS n 
2 144 GLU n 
2 145 MET n 
2 146 ALA n 
2 147 THR n 
2 148 LYS n 
2 149 HIS n 
2 150 ASN n 
2 151 ILE n 
2 152 PRO n 
2 153 TYR n 
2 154 ILE n 
2 155 GLU n 
2 156 THR n 
2 157 SER n 
2 158 ALA n 
2 159 LYS n 
2 160 ASP n 
2 161 PRO n 
2 162 PRO n 
2 163 LEU n 
2 164 ASN n 
2 165 VAL n 
2 166 ASP n 
2 167 LYS n 
2 168 ALA n 
2 169 PHE n 
2 170 HIS n 
2 171 ASP 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 GLN n 
2 179 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 ? ? ? ? ? ? ? ? Trichoplusia       
7110 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 179 human ? 'MRAS, RRAS3' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
HOH non-polymer         . WATER ?        'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?        'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?        'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?        'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?        'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?        'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?        'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?        'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?        'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?        'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?        'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?        'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?        'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   104  ?    ?   ?   A . n 
A 1 2   VAL 2   105  ?    ?   ?   A . n 
A 1 3   GLY 3   106  106  GLY GLY 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  ?    ?   ?   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  344  VAL VAL A . n 
A 1 242 ASN 242 345  345  ASN ASN 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  ?    ?   ?   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  ?    ?   ?   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  863  LYS LYS A . n 
A 1 761 GLY 761 864  864  GLY GLY 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  ?    ?   ?   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  ?    ?   ?   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  949  ARG ARG A . n 
A 1 847 GLU 847 950  950  GLU GLU A . n 
A 1 848 ARG 848 951  951  ARG ARG 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 1054 LYS LYS 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   THR 4   3    3    THR THR B . n 
B 2 5   SER 5   4    4    SER SER B . n 
B 2 6   ALA 6   5    5    ALA ALA B . n 
B 2 7   VAL 7   6    6    VAL VAL B . n 
B 2 8   PRO 8   7    7    PRO PRO B . n 
B 2 9   SER 9   8    8    SER SER B . n 
B 2 10  ASP 10  9    9    ASP ASP B . n 
B 2 11  ASN 11  10   10   ASN ASN B . n 
B 2 12  LEU 12  11   11   LEU LEU B . n 
B 2 13  PRO 13  12   12   PRO PRO B . n 
B 2 14  THR 14  13   13   THR THR B . n 
B 2 15  TYR 15  14   14   TYR TYR B . n 
B 2 16  LYS 16  15   15   LYS LYS B . n 
B 2 17  LEU 17  16   16   LEU LEU B . n 
B 2 18  VAL 18  17   17   VAL VAL 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  GLY 21  20   20   GLY GLY B . n 
B 2 22  ASP 22  21   21   ASP ASP 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  VAL 25  24   24   VAL VAL B . n 
B 2 26  GLY 26  25   25   GLY GLY B . n 
B 2 27  LYS 27  26   26   LYS LYS B . n 
B 2 28  SER 28  27   27   SER SER B . n 
B 2 29  ALA 29  28   28   ALA ALA B . n 
B 2 30  LEU 30  29   29   LEU LEU B . n 
B 2 31  THR 31  30   30   THR THR B . n 
B 2 32  ILE 32  31   31   ILE ILE B . n 
B 2 33  GLN 33  32   32   GLN GLN B . n 
B 2 34  PHE 34  33   33   PHE PHE B . n 
B 2 35  PHE 35  34   34   PHE PHE B . n 
B 2 36  ALA 36  35   35   ALA ALA B . n 
B 2 37  LYS 37  36   36   LYS LYS B . n 
B 2 38  ILE 38  37   37   ILE ILE B . n 
B 2 39  PHE 39  38   38   PHE PHE B . n 
B 2 40  VAL 40  39   39   VAL VAL B . n 
B 2 41  PRO 41  40   40   PRO PRO B . n 
B 2 42  ASP 42  41   41   ASP ASP B . n 
B 2 43  TYR 43  42   42   TYR TYR B . n 
B 2 44  ASP 44  43   43   ASP ASP B . n 
B 2 45  PRO 45  44   44   PRO PRO B . n 
B 2 46  THR 46  45   45   THR THR B . n 
B 2 47  ILE 47  46   46   ILE ILE B . n 
B 2 48  GLU 48  47   47   GLU GLU B . n 
B 2 49  ASP 49  48   48   ASP ASP B . n 
B 2 50  SER 50  49   49   SER SER B . n 
B 2 51  TYR 51  50   50   TYR TYR B . n 
B 2 52  LEU 52  51   51   LEU LEU B . n 
B 2 53  LYS 53  52   52   LYS LYS B . n 
B 2 54  HIS 54  53   53   HIS HIS B . n 
B 2 55  THR 55  54   54   THR THR B . n 
B 2 56  GLU 56  55   55   GLU GLU B . n 
B 2 57  ILE 57  56   56   ILE ILE B . n 
B 2 58  ASP 58  57   57   ASP ASP B . n 
B 2 59  ASN 59  58   58   ASN ASN B . n 
B 2 60  GLN 60  59   59   GLN GLN B . n 
B 2 61  TRP 61  60   60   TRP TRP B . n 
B 2 62  ALA 62  61   61   ALA ALA B . n 
B 2 63  ILE 63  62   62   ILE ILE B . n 
B 2 64  LEU 64  63   63   LEU LEU B . n 
B 2 65  ASP 65  64   64   ASP ASP B . n 
B 2 66  VAL 66  65   65   VAL VAL B . n 
B 2 67  LEU 67  66   66   LEU LEU B . n 
B 2 68  ASP 68  67   67   ASP ASP B . n 
B 2 69  THR 69  68   68   THR THR B . n 
B 2 70  ALA 70  69   69   ALA ALA B . n 
B 2 71  GLY 71  70   70   GLY GLY B . n 
B 2 72  GLN 72  71   71   GLN GLN B . n 
B 2 73  GLU 73  72   72   GLU GLU B . n 
B 2 74  GLU 74  73   73   GLU GLU B . n 
B 2 75  PHE 75  74   74   PHE PHE B . n 
B 2 76  SER 76  75   75   SER SER B . n 
B 2 77  ALA 77  76   76   ALA ALA B . n 
B 2 78  MET 78  77   77   MET MET B . n 
B 2 79  ARG 79  78   78   ARG ARG B . n 
B 2 80  GLU 80  79   79   GLU GLU B . n 
B 2 81  GLN 81  80   80   GLN GLN B . n 
B 2 82  TYR 82  81   81   TYR TYR B . n 
B 2 83  MET 83  82   82   MET MET B . n 
B 2 84  ARG 84  83   83   ARG ARG B . n 
B 2 85  THR 85  84   84   THR THR B . n 
B 2 86  GLY 86  85   85   GLY GLY B . n 
B 2 87  ASP 87  86   86   ASP ASP B . n 
B 2 88  GLY 88  87   87   GLY GLY B . n 
B 2 89  PHE 89  88   88   PHE PHE B . n 
B 2 90  LEU 90  89   89   LEU LEU B . n 
B 2 91  ILE 91  90   90   ILE ILE B . n 
B 2 92  VAL 92  91   91   VAL VAL B . n 
B 2 93  TYR 93  92   92   TYR TYR B . n 
B 2 94  SER 94  93   93   SER SER B . n 
B 2 95  VAL 95  94   94   VAL VAL B . n 
B 2 96  THR 96  95   95   THR THR B . n 
B 2 97  ASP 97  96   96   ASP ASP B . n 
B 2 98  LYS 98  97   97   LYS LYS B . n 
B 2 99  ALA 99  98   98   ALA ALA B . n 
B 2 100 SER 100 99   99   SER SER B . n 
B 2 101 PHE 101 100  100  PHE PHE B . n 
B 2 102 GLU 102 101  101  GLU GLU B . n 
B 2 103 HIS 103 102  102  HIS HIS B . n 
B 2 104 VAL 104 103  103  VAL VAL B . n 
B 2 105 ASP 105 104  104  ASP ASP B . n 
B 2 106 ARG 106 105  105  ARG ARG B . n 
B 2 107 PHE 107 106  106  PHE PHE B . n 
B 2 108 HIS 108 107  107  HIS HIS B . n 
B 2 109 GLN 109 108  108  GLN GLN B . n 
B 2 110 LEU 110 109  109  LEU LEU B . n 
B 2 111 ILE 111 110  110  ILE ILE B . n 
B 2 112 LEU 112 111  111  LEU LEU B . n 
B 2 113 ARG 113 112  112  ARG ARG B . n 
B 2 114 VAL 114 113  113  VAL VAL B . n 
B 2 115 LYS 115 114  114  LYS LYS B . n 
B 2 116 ASP 116 115  115  ASP ASP B . n 
B 2 117 ARG 117 116  116  ARG ARG B . n 
B 2 118 GLU 118 117  117  GLU GLU B . n 
B 2 119 SER 119 118  118  SER SER B . n 
B 2 120 PHE 120 119  119  PHE PHE B . n 
B 2 121 PRO 121 120  120  PRO PRO B . n 
B 2 122 MET 122 121  121  MET MET B . n 
B 2 123 ILE 123 122  122  ILE ILE B . n 
B 2 124 LEU 124 123  123  LEU LEU B . n 
B 2 125 VAL 125 124  124  VAL VAL B . n 
B 2 126 ALA 126 125  125  ALA ALA B . n 
B 2 127 ASN 127 126  126  ASN ASN B . n 
B 2 128 LYS 128 127  127  LYS LYS B . n 
B 2 129 VAL 129 128  128  VAL VAL B . n 
B 2 130 ASP 130 129  129  ASP ASP B . n 
B 2 131 LEU 131 130  130  LEU LEU B . n 
B 2 132 MET 132 131  131  MET MET B . n 
B 2 133 HIS 133 132  132  HIS HIS B . n 
B 2 134 LEU 134 133  133  LEU LEU B . n 
B 2 135 ARG 135 134  134  ARG ARG B . n 
B 2 136 LYS 136 135  135  LYS LYS B . n 
B 2 137 ILE 137 136  136  ILE ILE B . n 
B 2 138 THR 138 137  137  THR THR B . n 
B 2 139 ARG 139 138  138  ARG ARG B . n 
B 2 140 GLU 140 139  139  GLU GLU B . n 
B 2 141 GLN 141 140  140  GLN GLN B . n 
B 2 142 GLY 142 141  141  GLY GLY B . n 
B 2 143 LYS 143 142  142  LYS LYS B . n 
B 2 144 GLU 144 143  143  GLU GLU B . n 
B 2 145 MET 145 144  144  MET MET B . n 
B 2 146 ALA 146 145  145  ALA ALA B . n 
B 2 147 THR 147 146  146  THR THR B . n 
B 2 148 LYS 148 147  147  LYS LYS B . n 
B 2 149 HIS 149 148  148  HIS HIS B . n 
B 2 150 ASN 150 149  149  ASN ASN B . n 
B 2 151 ILE 151 150  150  ILE ILE B . n 
B 2 152 PRO 152 151  151  PRO PRO B . n 
B 2 153 TYR 153 152  152  TYR TYR B . n 
B 2 154 ILE 154 153  153  ILE ILE B . n 
B 2 155 GLU 155 154  154  GLU GLU B . n 
B 2 156 THR 156 155  155  THR THR B . n 
B 2 157 SER 157 156  156  SER SER B . n 
B 2 158 ALA 158 157  157  ALA ALA B . n 
B 2 159 LYS 159 158  158  LYS LYS B . n 
B 2 160 ASP 160 159  159  ASP ASP B . n 
B 2 161 PRO 161 160  160  PRO PRO B . n 
B 2 162 PRO 162 161  161  PRO PRO B . n 
B 2 163 LEU 163 162  162  LEU LEU 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 LYS 167 166  166  LYS LYS 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 ASP 171 170  170  ASP ASP 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 GLN 178 177  177  GLN GLN B . n 
B 2 179 GLN 179 178  178  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 . 
F 6 HOH 1  1201 23   HOH HOH A . 
F 6 HOH 2  1202 14   HOH HOH A . 
F 6 HOH 3  1203 4    HOH HOH A . 
F 6 HOH 4  1204 22   HOH HOH A . 
F 6 HOH 5  1205 17   HOH HOH A . 
F 6 HOH 6  1206 8    HOH HOH A . 
F 6 HOH 7  1207 15   HOH HOH A . 
F 6 HOH 8  1208 24   HOH HOH A . 
F 6 HOH 9  1209 5    HOH HOH A . 
F 6 HOH 10 1210 20   HOH HOH A . 
F 6 HOH 11 1211 25   HOH HOH A . 
F 6 HOH 12 1212 11   HOH HOH A . 
F 6 HOH 13 1213 19   HOH HOH A . 
F 6 HOH 14 1214 3    HOH HOH A . 
F 6 HOH 15 1215 10   HOH HOH A . 
F 6 HOH 16 1216 2    HOH HOH A . 
F 6 HOH 17 1217 16   HOH HOH A . 
F 6 HOH 18 1218 27   HOH HOH A . 
F 6 HOH 19 1219 13   HOH HOH A . 
F 6 HOH 20 1220 9    HOH HOH A . 
F 6 HOH 21 1221 6    HOH HOH A . 
F 6 HOH 22 1222 26   HOH HOH A . 
F 6 HOH 23 1223 18   HOH HOH A . 
G 6 HOH 1  301  7    HOH HOH B . 
G 6 HOH 2  302  1    HOH HOH B . 
G 6 HOH 3  303  21   HOH HOH B . 
G 6 HOH 4  304  12   HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ILE 181  ? CD1 ? A ILE 78  CD1 
2  1 Y 1 A ILE 354  ? CG1 ? A ILE 251 CG1 
3  1 Y 1 A ILE 354  ? CG2 ? A ILE 251 CG2 
4  1 Y 1 A ILE 354  ? CD1 ? A ILE 251 CD1 
5  1 Y 1 A ARG 382  ? CZ  ? A ARG 279 CZ  
6  1 Y 1 A ARG 382  ? NH1 ? A ARG 279 NH1 
7  1 Y 1 A ARG 382  ? NH2 ? A ARG 279 NH2 
8  1 Y 1 A ILE 391  ? CD1 ? A ILE 288 CD1 
9  1 Y 1 A PRO 449  ? CG  ? A PRO 346 CG  
10 1 Y 1 A PRO 449  ? CD  ? A PRO 346 CD  
11 1 Y 1 A HIS 450  ? CG  ? A HIS 347 CG  
12 1 Y 1 A HIS 450  ? ND1 ? A HIS 347 ND1 
13 1 Y 1 A HIS 450  ? CD2 ? A HIS 347 CD2 
14 1 Y 1 A HIS 450  ? CE1 ? A HIS 347 CE1 
15 1 Y 1 A HIS 450  ? NE2 ? A HIS 347 NE2 
16 1 Y 1 A LEU 452  ? CG  ? A LEU 349 CG  
17 1 Y 1 A LEU 452  ? CD1 ? A LEU 349 CD1 
18 1 Y 1 A LEU 452  ? CD2 ? A LEU 349 CD2 
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 ILE 543  ? CD1 ? A ILE 440 CD1 
26 1 Y 1 A TYR 557  ? CE1 ? A TYR 454 CE1 
27 1 Y 1 A TYR 557  ? CE2 ? A TYR 454 CE2 
28 1 Y 1 A TYR 557  ? CZ  ? A TYR 454 CZ  
29 1 Y 1 A TYR 557  ? OH  ? A TYR 454 OH  
30 1 Y 1 A ILE 561  ? CD1 ? A ILE 458 CD1 
31 1 Y 1 A LYS 594  ? CD  ? A LYS 491 CD  
32 1 Y 1 A LYS 594  ? CE  ? A LYS 491 CE  
33 1 Y 1 A LYS 594  ? NZ  ? A LYS 491 NZ  
34 1 Y 1 A ILE 788  ? CD1 ? A ILE 685 CD1 
35 1 Y 1 A ARG 818  ? CZ  ? A ARG 715 CZ  
36 1 Y 1 A ARG 818  ? NH1 ? A ARG 715 NH1 
37 1 Y 1 A ARG 818  ? NH2 ? A ARG 715 NH2 
38 1 Y 1 A ILE 860  ? CD1 ? A ILE 757 CD1 
39 1 Y 1 A ILE 913  ? CD1 ? A ILE 810 CD1 
40 1 Y 1 A LYS 924  ? NZ  ? A LYS 821 NZ  
41 1 Y 1 A ILE 999  ? CD1 ? A ILE 896 CD1 
42 1 Y 1 A ILE 1022 ? CD1 ? A ILE 919 CD1 
43 1 Y 1 A ARG 1023 ? CZ  ? A ARG 920 CZ  
44 1 Y 1 A ARG 1023 ? NH1 ? A ARG 920 NH1 
45 1 Y 1 A ARG 1023 ? NH2 ? A ARG 920 NH2 
# 
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                   97.50 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B4T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.935 
_cell.length_a_esd                 ? 
_cell.length_b                     105.936 
_cell.length_b_esd                 ? 
_cell.length_c                     114.493 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9B4T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B4T 
_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             2.67 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.89 
_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 (Tris/Bicine) 1.2%w/v cholic acid mix, 50%v/v (40%v/v ethylene glycol, 20%w/v PEG 8000)' 
_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 EIGER X 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         2022-12-17 
_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-E' 
_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-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B4T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.75 
_reflns.d_resolution_low                               50.03 
_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                                     35877 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.48 
_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                                0.084 
_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                              0.078 
_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 
2.75 2.92  ? ? ? ? ? ? 5713 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.205                ? ? 1 1 0.87               ? ? ? ? 1.119 ? ? ? ? ? 
? ? ? ? 
2.92 3.12  ? ? ? ? ? ? 5448 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.6579999999999999   ? ? 2 1 0.9590000000000001 ? ? ? ? 0.611 ? ? ? ? ? 
? ? ? ? 
3.12 3.37  ? ? ? ? ? ? 5055 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.368                ? ? 3 1 0.981              ? ? ? ? 0.34 ? ? ? ? ? ? 
? ? ? 
3.37 3.69  ? ? ? ? ? ? 4623 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.19399999999999998  ? ? 4 1 0.992              ? ? ? ? 0.18 ? ? ? ? ? ? 
? ? ? 
3.69 4.12  ? ? ? ? ? ? 4215 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.109                ? ? 5 1 0.997              ? ? ? ? 
0.10099999999999999  ? ? ? ? ? ? ? ? ? 
4.12 4.75  ? ? ? ? ? ? 3752 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.075                ? ? 6 1 0.998              ? ? ? ? 0.069 ? ? ? ? ? 
? ? ? ? 
4.75 5.81  ? ? ? ? ? ? 3167 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.064                ? ? 7 1 0.998              ? ? ? ? 
0.059000000000000004 ? ? ? ? ? ? ? ? ? 
5.81 8.16  ? ? ? ? ? ? 2500 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.055                ? ? 8 1 0.998              ? ? ? ? 0.051 ? ? ? ? ? 
? ? ? ? 
8.16 50.03 ? ? ? ? ? ? 1404 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.037000000000000005 ? ? 9 1 0.9990000000000001 ? ? ? ? 0.034 ? ? ? ? ? 
? ? ? ? 
# 
_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                                 9B4T 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.75 
_refine.ls_d_res_low                             50.03 
_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                     35732 
_refine.ls_number_reflns_R_free                  1787 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.31 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2158 
_refine.ls_R_factor_R_free                       0.2619 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2135 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 34.13 
_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                            0.50 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.75 
_refine_hist.d_res_low                        50.03 
_refine_hist.number_atoms_solvent             27 
_refine_hist.number_atoms_total               8714 
_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        8626 
_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' ? 0.002  ? 8878  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.406  ? 12014 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.681 ? 3366  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 1317  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 1533  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.75 2.83  . . 136 2582 96.00  . . . . 0.4547 . . . . . . . . . . . 0.4995 
'X-RAY DIFFRACTION' 2.83 2.91  . . 136 2554 98.00  . . . . 0.3757 . . . . . . . . . . . 0.3942 
'X-RAY DIFFRACTION' 2.91 3.00  . . 135 2604 98.00  . . . . 0.3211 . . . . . . . . . . . 0.3296 
'X-RAY DIFFRACTION' 3.00 3.11  . . 137 2619 98.00  . . . . 0.2846 . . . . . . . . . . . 0.3378 
'X-RAY DIFFRACTION' 3.11 3.23  . . 137 2586 98.00  . . . . 0.2777 . . . . . . . . . . . 0.3043 
'X-RAY DIFFRACTION' 3.23 3.38  . . 135 2580 98.00  . . . . 0.2856 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 3.38 3.56  . . 135 2557 97.00  . . . . 0.2577 . . . . . . . . . . . 0.3413 
'X-RAY DIFFRACTION' 3.56 3.78  . . 139 2625 99.00  . . . . 0.2250 . . . . . . . . . . . 0.3027 
'X-RAY DIFFRACTION' 3.78 4.08  . . 138 2635 99.00  . . . . 0.2098 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 4.08 4.49  . . 140 2641 99.00  . . . . 0.1982 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 4.49 5.13  . . 136 2595 98.00  . . . . 0.1767 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 5.13 6.46  . . 142 2682 100.00 . . . . 0.2081 . . . . . . . . . . . 0.2878 
'X-RAY DIFFRACTION' 6.47 50.03 . . 141 2685 99.00  . . . . 0.1681 . . . . . . . . . . . 0.1953 
# 
_struct.entry_id                     9B4T 
_struct.title                        'Crystal structure of the MRAS-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        9B4T 
_struct_keywords.text            'RAS, RRAS3, MRAS, 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 ? 
F N N 6 ? 
G N N 6 ? 
# 
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 RASM_HUMAN  O14807 ? 2 
;MATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQ
YMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDP
PLNVDKAFHDLVRVIRQQ
;
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 9B4T A 2 ? 965 ? P42336 105 ? 1068 ? 105 1068 
2 2 9B4T B 2 ? 179 ? O14807 1   ? 178  ? 1   178  
# 
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 9B4T GLY A 1   ? UNP P42336 ?   ?    'expression tag'      104  1 
1 9B4T ALA A 954 ? UNP P42336 TRP 1057 'engineered mutation' 1057 2 
1 9B4T ALA A 955 ? UNP P42336 ILE 1058 'engineered mutation' 1058 3 
1 9B4T ALA A 956 ? UNP P42336 PHE 1059 'engineered mutation' 1059 4 
2 9B4T GLY B 1   ? UNP O14807 ?   ?    'expression tag'      0    5 
2 9B4T ALA B 36  ? UNP O14807 GLN 35   'engineered mutation' 35   6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2800  ? 
1 MORE         -18   ? 
1 'SSA (A^2)'  47020 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 ASN A 4   ? GLY A 19  ? ASN A 107  GLY A 122  1 ? 16 
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  ? LEU A 53  ? ILE A 143  LEU A 156  1 ? 14 
HELX_P HELX_P5  AA5 ASN A 54  ? TYR A 64  ? ASN A 157  TYR A 167  1 ? 11 
HELX_P HELX_P6  AA6 PRO A 75  ? ASN A 80  ? PRO A 178  ASN A 183  1 ? 6  
HELX_P HELX_P7  AA7 VAL A 113 ? THR A 126 ? VAL A 216  THR A 229  1 ? 14 
HELX_P HELX_P8  AA8 SER A 132 ? GLN A 144 ? SER A 235  GLN A 247  1 ? 13 
HELX_P HELX_P9  AA9 PRO A 163 ? GLN A 166 ? PRO A 266  GLN A 269  5 ? 4  
HELX_P HELX_P10 AB1 TYR A 167 ? LEU A 176 ? TYR A 270  LEU A 279  1 ? 10 
HELX_P HELX_P11 AB2 LYS A 187 ? GLN A 193 ? LYS A 290  GLN A 296  1 ? 7  
HELX_P HELX_P12 AB3 PRO A 202 ? ARG A 206 ? PRO A 305  ARG A 309  5 ? 5  
HELX_P HELX_P13 AB4 TRP A 225 ? ILE A 227 ? TRP A 328  ILE A 330  5 ? 3  
HELX_P HELX_P14 AB5 PRO A 291 ? LEU A 293 ? PRO A 394  LEU A 396  5 ? 3  
HELX_P HELX_P15 AB6 ASP A 385 ? SER A 396 ? ASP A 488  SER A 499  1 ? 12 
HELX_P HELX_P16 AB7 ASN A 423 ? ARG A 434 ? ASN A 526  ARG A 537  1 ? 12 
HELX_P HELX_P17 AB8 THR A 441 ? HIS A 451 ? THR A 544  HIS A 554  1 ? 11 
HELX_P HELX_P18 AB9 HIS A 453 ? GLU A 460 ? HIS A 556  GLU A 563  5 ? 8  
HELX_P HELX_P19 AC1 ILE A 461 ? VAL A 469 ? ILE A 564  VAL A 572  1 ? 9  
HELX_P HELX_P20 AC2 ARG A 474 ? ASP A 486 ? ARG A 577  ASP A 589  1 ? 13 
HELX_P HELX_P21 AC3 LYS A 491 ? MET A 496 ? LYS A 594  MET A 599  1 ? 6  
HELX_P HELX_P22 AC4 GLU A 497 ? ASP A 500 ? GLU A 600  ASP A 603  5 ? 4  
HELX_P HELX_P23 AC5 ASP A 505 ? LEU A 520 ? ASP A 608  LEU A 623  1 ? 16 
HELX_P HELX_P24 AC6 THR A 521 ? TYR A 528 ? THR A 624  TYR A 631  1 ? 8  
HELX_P HELX_P25 AC7 TYR A 528 ? VAL A 535 ? TYR A 631  VAL A 638  1 ? 8  
HELX_P HELX_P26 AC8 ASN A 544 ? LEU A 555 ? ASN A 647  LEU A 658  1 ? 12 
HELX_P HELX_P27 AC9 ASN A 557 ? GLU A 571 ? ASN A 660  GLU A 674  1 ? 15 
HELX_P HELX_P28 AD1 MET A 572 ? ASN A 574 ? MET A 675  ASN A 677  5 ? 3  
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 ? LYS A 620 ? MET A 697  LYS A 723  1 ? 27 
HELX_P HELX_P31 AD4 THR A 624 ? ARG A 638 ? THR A 727  ARG A 741  1 ? 15 
HELX_P HELX_P32 AD5 ARG A 638 ? LEU A 645 ? ARG A 741  LEU A 748  1 ? 8  
HELX_P HELX_P33 AD6 ARG A 662 ? CYS A 666 ? ARG A 765  CYS A 769  5 ? 5  
HELX_P HELX_P34 AD7 MET A 686 ? LEU A 690 ? MET A 789  LEU A 793  5 ? 5  
HELX_P HELX_P35 AD8 LEU A 704 ? GLY A 725 ? LEU A 807  GLY A 828  1 ? 22 
HELX_P HELX_P36 AD9 ILE A 754 ? LYS A 760 ? ILE A 857  LYS A 863  1 ? 7  
HELX_P HELX_P37 AE1 HIS A 772 ? ASN A 782 ? HIS A 875  ASN A 885  1 ? 11 
HELX_P HELX_P38 AE2 ILE A 786 ? GLY A 809 ? ILE A 889  GLY A 912  1 ? 24 
HELX_P HELX_P39 AE3 THR A 854 ? SER A 862 ? THR A 957  SER A 965  1 ? 9  
HELX_P HELX_P40 AE4 THR A 871 ? GLN A 890 ? THR A 974  GLN A 993  1 ? 20 
HELX_P HELX_P41 AE5 HIS A 891 ? MET A 901 ? HIS A 994  MET A 1004 1 ? 11 
HELX_P HELX_P42 AE6 SER A 912 ? LEU A 923 ? SER A 1015 LEU A 1026 1 ? 12 
HELX_P HELX_P43 AE7 THR A 928 ? HIS A 945 ? THR A 1031 HIS A 1048 1 ? 18 
HELX_P HELX_P44 AE8 GLY B 26  ? LYS B 37  ? GLY B 25   LYS B 36   1 ? 12 
HELX_P HELX_P45 AE9 MET B 78  ? GLY B 86  ? MET B 77   GLY B 85   1 ? 9  
HELX_P HELX_P46 AF1 ASP B 97  ? HIS B 103 ? ASP B 96   HIS B 102  1 ? 7  
HELX_P HELX_P47 AF2 HIS B 103 ? ASP B 116 ? HIS B 102  ASP B 115  1 ? 14 
HELX_P HELX_P48 AF3 LEU B 131 ? ARG B 135 ? LEU B 130  ARG B 134  5 ? 5  
HELX_P HELX_P49 AF4 THR B 138 ? HIS B 149 ? THR B 137  HIS B 148  1 ? 12 
HELX_P HELX_P50 AF5 ASN B 164 ? GLN B 179 ? ASN B 163  GLN B 178  1 ? 16 
# 
_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 28 OG  ? ? ? 1_555 E MG . MG ? ? B SER 27  B MG 202 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
metalc2 metalc ? ? B THR 46 OG1 ? ? ? 1_555 E MG . MG ? ? B THR 45  B MG 202 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc3 metalc ? ? D GNP .  O2G ? ? ? 1_555 E MG . MG ? ? B GNP 201 B MG 202 1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc4 metalc ? ? D GNP .  O2B ? ? ? 1_555 E MG . MG ? ? B GNP 201 B MG 202 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
# 
_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 28 ? B SER 27  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 OG1 ? B THR 46 ? B THR 45  ? 1_555 68.6  ? 
2 OG  ? B SER 28 ? B SER 27  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2G ? D GNP .  ? B GNP 201 ? 1_555 117.9 ? 
3 OG1 ? B THR 46 ? B THR 45  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2G ? D GNP .  ? B GNP 201 ? 1_555 86.2  ? 
4 OG  ? B SER 28 ? B SER 27  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2B ? D GNP .  ? B GNP 201 ? 1_555 78.4  ? 
5 OG1 ? B THR 46 ? B THR 45  ? 1_555 MG ? E MG . ? B MG 202 ? 1_555 O2B ? D GNP .  ? B GNP 201 ? 1_555 133.4 ? 
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 81.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 3 ? 
AA9 ? 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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 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 
AA1 5 TYR A 157 ? PHE A 158 ? TYR A 260 PHE A 261 
AA2 1 LYS A 222 ? SER A 223 ? LYS A 325 SER A 326 
AA2 2 VAL A 381 ? LYS A 382 ? VAL A 484 LYS A 485 
AA3 1 ARG A 279 ? TYR A 289 ? ARG A 382 TYR A 392 
AA3 2 ALA A 230 ? CYS A 237 ? ALA A 333 CYS A 340 
AA3 3 GLU A 371 ? PHE A 374 ? GLU A 474 PHE A 477 
AA3 4 GLY A 336 ? ALA A 339 ? GLY A 439 ALA A 442 
AA4 1 ILE A 251 ? ARG A 254 ? ILE A 354 ARG A 357 
AA4 2 ARG A 298 ? VAL A 306 ? ARG A 401 VAL A 409 
AA4 3 ILE A 257 ? TYR A 258 ? ILE A 360 TYR A 361 
AA5 1 ILE A 251 ? ARG A 254 ? ILE A 354 ARG A 357 
AA5 2 ARG A 298 ? VAL A 306 ? ARG A 401 VAL A 409 
AA5 3 HIS A 316 ? ASN A 325 ? HIS A 419 ASN A 428 
AA5 4 TRP A 343 ? PRO A 344 ? TRP A 446 PRO A 447 
AA6 1 PHE A 648 ? SER A 650 ? PHE A 751 SER A 753 
AA6 2 ASN A 653 ? LEU A 658 ? ASN A 756 LEU A 761 
AA7 1 ARG A 667 ? ILE A 668 ? ARG A 770 ILE A 771 
AA7 2 LEU A 676 ? GLU A 681 ? LEU A 779 GLU A 784 
AA7 3 ASN A 693 ? ASN A 700 ? ASN A 796 ASN A 803 
AA7 4 VAL A 742 ? GLU A 746 ? VAL A 845 GLU A 849 
AA7 5 CYS A 735 ? SER A 737 ? CYS A 838 SER A 840 
AA8 1 SER A 751 ? THR A 753 ? SER A 854 THR A 856 
AA8 2 ILE A 818 ? LYS A 821 ? ILE A 921 LYS A 924 
AA8 3 LEU A 826 ? HIS A 828 ? LEU A 929 HIS A 931 
AA9 1 ASP B 49  ? ILE B 57  ? ASP B 48  ILE B 56  
AA9 2 GLN B 60  ? ASP B 68  ? GLN B 59  ASP B 67  
AA9 3 THR B 14  ? VAL B 20  ? THR B 13  VAL B 19  
AA9 4 GLY B 88  ? SER B 94  ? GLY B 87  SER B 93  
AA9 5 MET B 122 ? ASN B 127 ? MET B 121 ASN B 126 
AA9 6 TYR B 153 ? GLU B 155 ? TYR B 152 GLU B 154 
# 
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 LEU A 106 ? O LEU A 209 N VAL A 89  ? N VAL A 192 
AA1 2 3 N TRP A 92  ? N TRP A 195 O LEU A 182 ? O LEU A 285 
AA1 3 4 O MET A 185 ? O MET A 288 N ILE A 148 ? N ILE A 251 
AA1 4 5 N LEU A 149 ? N LEU A 252 O PHE A 158 ? O PHE A 261 
AA2 1 2 N LYS A 222 ? N LYS A 325 O LYS A 382 ? O LYS A 485 
AA3 1 2 O TRP A 280 ? O TRP A 383 N LEU A 236 ? N LEU A 339 
AA3 2 3 N LYS A 234 ? N LYS A 337 O GLU A 373 ? O GLU A 476 
AA3 3 4 O LEU A 372 ? O LEU A 475 N MET A 338 ? N MET A 441 
AA4 1 2 N TYR A 252 ? N TYR A 355 O CYS A 304 ? O CYS A 407 
AA4 2 3 O ARG A 298 ? O ARG A 401 N TYR A 258 ? N TYR A 361 
AA5 1 2 N TYR A 252 ? N TYR A 355 O CYS A 304 ? O CYS A 407 
AA5 2 3 N LEU A 299 ? N LEU A 402 O ILE A 324 ? O ILE A 427 
AA5 3 4 N TRP A 321 ? N TRP A 424 O TRP A 343 ? O TRP A 446 
AA6 1 2 N SER A 650 ? N SER A 753 O HIS A 656 ? O HIS A 759 
AA7 1 2 N ARG A 667 ? N ARG A 770 O TRP A 677 ? O TRP A 780 
AA7 2 3 N LEU A 676 ? N LEU A 779 O PHE A 698 ? O PHE A 801 
AA7 3 4 N ILE A 697 ? N ILE A 800 O ILE A 745 ? O ILE A 848 
AA7 4 5 O LEU A 744 ? O LEU A 847 N LEU A 736 ? N LEU A 839 
AA8 1 2 N HIS A 752 ? N HIS A 855 O VAL A 820 ? O VAL A 923 
AA8 2 3 N MET A 819 ? N MET A 922 O PHE A 827 ? O PHE A 930 
AA9 1 2 N ASP B 49  ? N ASP B 48  O ASP B 68  ? O ASP B 67  
AA9 2 3 O ILE B 63  ? O ILE B 62  N TYR B 15  ? N TYR B 14  
AA9 3 4 N VAL B 18  ? N VAL B 17  O GLY B 88  ? O GLY B 87  
AA9 4 5 N ILE B 91  ? N ILE B 90  O VAL B 125 ? O VAL B 124 
AA9 5 6 N ALA B 126 ? N ALA B 125 O ILE B 154 ? O ILE B 153 
# 
_pdbx_entry_details.entry_id                   9B4T 
_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 157  ? ? 61.02   70.02   
2  1 THR A 229  ? ? -82.86  36.56   
3  1 LYS A 264  ? ? -69.42  52.87   
4  1 LEU A 339  ? ? -99.36  -85.94  
5  1 HIS A 362  ? ? -113.00 64.73   
6  1 PRO A 381  ? ? -59.09  100.58  
7  1 TRP A 383  ? ? -125.41 -53.49  
8  1 GLU A 453  ? ? -94.23  -146.23 
9  1 PHE A 480  ? ? -115.11 -78.47  
10 1 SER A 481  ? ? -142.41 -62.37  
11 1 SER A 482  ? ? -129.78 -162.62 
12 1 SER A 501  ? ? -100.11 68.42   
13 1 ASN A 526  ? ? -145.52 -23.24  
14 1 HIS A 554  ? ? -99.59  30.56   
15 1 ASN A 660  ? ? -162.37 105.70  
16 1 SER A 773  ? ? -83.67  36.34   
17 1 SER A 774  ? ? -107.84 -161.35 
18 1 ARG A 777  ? ? 52.70   73.41   
19 1 LEU A 793  ? ? -114.65 -73.72  
20 1 LYS A 863  ? ? -87.00  47.11   
21 1 ILE A 932  ? ? -133.14 -36.50  
22 1 ASP A 933  ? ? -62.95  -70.60  
23 1 LEU A 938  ? ? 60.21   -145.30 
24 1 LEU A 956  ? ? 54.79   76.71   
25 1 LYS A 966  ? ? 57.02   -143.74 
26 1 CYS A 971  ? ? 63.89   -52.20  
27 1 LYS A 973  ? ? 37.97   47.57   
28 1 LEU A 1013 ? ? -144.62 54.60   
29 1 THR A 1052 ? ? -96.97  -79.04  
30 1 SER B 8    ? ? 57.32   -147.83 
31 1 GLU B 47   ? ? -167.94 104.08  
32 1 GLU B 72   ? ? 67.06   -13.15  
33 1 PHE B 74   ? ? -101.79 53.02   
34 1 MET B 77   ? ? 63.09   -12.59  
35 1 LEU B 130  ? ? -113.56 61.67   
36 1 LEU B 162  ? ? 62.50   80.74   
# 
_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         -1.6934 
_pdbx_refine_tls.origin_y         -12.2223 
_pdbx_refine_tls.origin_z         37.8298 
_pdbx_refine_tls.T[1][1]          0.6517 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0024 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0368 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.8096 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0261 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6542 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8789 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2281 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.2751 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.0712 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1974 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.7841 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0273 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0975 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0197 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0458 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0764 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0510 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.2040 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1330 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.1024 
_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 ILE 311  ? A ILE 208 
4  1 Y 1 A SER 312  ? A SER 209 
5  1 Y 1 A THR 313  ? A THR 210 
6  1 Y 1 A ALA 314  ? A ALA 211 
7  1 Y 1 A THR 315  ? A THR 212 
8  1 Y 1 A PRO 316  ? A PRO 213 
9  1 Y 1 A TYR 317  ? A TYR 214 
10 1 Y 1 A MET 318  ? A MET 215 
11 1 Y 1 A ASN 319  ? A ASN 216 
12 1 Y 1 A GLY 320  ? A GLY 217 
13 1 Y 1 A GLU 321  ? A GLU 218 
14 1 Y 1 A THR 322  ? A THR 219 
15 1 Y 1 A SER 323  ? A SER 220 
16 1 Y 1 A VAL 346  ? A VAL 243 
17 1 Y 1 A ASN 347  ? A ASN 244 
18 1 Y 1 A ILE 348  ? A ILE 245 
19 1 Y 1 A ARG 349  ? A ARG 246 
20 1 Y 1 A ASP 350  ? A ASP 247 
21 1 Y 1 A ILE 351  ? A ILE 248 
22 1 Y 1 A ASP 352  ? A ASP 249 
23 1 Y 1 A GLY 411  ? A GLY 308 
24 1 Y 1 A ARG 412  ? A ARG 309 
25 1 Y 1 A LYS 413  ? A LYS 310 
26 1 Y 1 A GLY 414  ? A GLY 311 
27 1 Y 1 A ALA 415  ? A ALA 312 
28 1 Y 1 A LYS 416  ? A LYS 313 
29 1 Y 1 A GLU 503  ? A GLU 400 
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 GLY 865  ? A GLY 762 
50 1 Y 1 A LEU 866  ? A LEU 763 
51 1 Y 1 A LYS 867  ? A LYS 764 
52 1 Y 1 A GLY 868  ? A GLY 765 
53 1 Y 1 A ALA 869  ? A ALA 766 
54 1 Y 1 A LEU 870  ? A LEU 767 
55 1 Y 1 A GLN 871  ? A GLN 768 
56 1 Y 1 A PHE 872  ? A PHE 769 
57 1 Y 1 A LYS 941  ? A LYS 838 
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 MET 1055 ? A MET 952 
66 1 Y 1 A ASP 1056 ? A ASP 953 
67 1 Y 1 A ALA 1057 ? A ALA 954 
68 1 Y 1 A ALA 1058 ? A ALA 955 
69 1 Y 1 A ALA 1059 ? A ALA 956 
70 1 Y 1 A HIS 1060 ? A HIS 957 
71 1 Y 1 A THR 1061 ? A THR 958 
72 1 Y 1 A ILE 1062 ? A ILE 959 
73 1 Y 1 A LYS 1063 ? A LYS 960 
74 1 Y 1 A GLN 1064 ? A GLN 961 
75 1 Y 1 A HIS 1065 ? A HIS 962 
76 1 Y 1 A ALA 1066 ? A ALA 963 
77 1 Y 1 A LEU 1067 ? A LEU 964 
78 1 Y 1 A ASN 1068 ? A ASN 965 
79 1 Y 1 B GLY 0    ? B GLY 1   
80 1 Y 1 B MET 1    ? B MET 2   
81 1 Y 1 B ALA 2    ? B ALA 3   
# 
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 
HOH O      O  N N 257 
HOH H1     H  N N 258 
HOH H2     H  N N 259 
ILE N      N  N N 260 
ILE CA     C  N S 261 
ILE C      C  N N 262 
ILE O      O  N N 263 
ILE CB     C  N S 264 
ILE CG1    C  N N 265 
ILE CG2    C  N N 266 
ILE CD1    C  N N 267 
ILE OXT    O  N N 268 
ILE H      H  N N 269 
ILE H2     H  N N 270 
ILE HA     H  N N 271 
ILE HB     H  N N 272 
ILE HG12   H  N N 273 
ILE HG13   H  N N 274 
ILE HG21   H  N N 275 
ILE HG22   H  N N 276 
ILE HG23   H  N N 277 
ILE HD11   H  N N 278 
ILE HD12   H  N N 279 
ILE HD13   H  N N 280 
ILE HXT    H  N N 281 
LEU N      N  N N 282 
LEU CA     C  N S 283 
LEU C      C  N N 284 
LEU O      O  N N 285 
LEU CB     C  N N 286 
LEU CG     C  N N 287 
LEU CD1    C  N N 288 
LEU CD2    C  N N 289 
LEU OXT    O  N N 290 
LEU H      H  N N 291 
LEU H2     H  N N 292 
LEU HA     H  N N 293 
LEU HB2    H  N N 294 
LEU HB3    H  N N 295 
LEU HG     H  N N 296 
LEU HD11   H  N N 297 
LEU HD12   H  N N 298 
LEU HD13   H  N N 299 
LEU HD21   H  N N 300 
LEU HD22   H  N N 301 
LEU HD23   H  N N 302 
LEU HXT    H  N N 303 
LYS N      N  N N 304 
LYS CA     C  N S 305 
LYS C      C  N N 306 
LYS O      O  N N 307 
LYS CB     C  N N 308 
LYS CG     C  N N 309 
LYS CD     C  N N 310 
LYS CE     C  N N 311 
LYS NZ     N  N N 312 
LYS OXT    O  N N 313 
LYS H      H  N N 314 
LYS H2     H  N N 315 
LYS HA     H  N N 316 
LYS HB2    H  N N 317 
LYS HB3    H  N N 318 
LYS HG2    H  N N 319 
LYS HG3    H  N N 320 
LYS HD2    H  N N 321 
LYS HD3    H  N N 322 
LYS HE2    H  N N 323 
LYS HE3    H  N N 324 
LYS HZ1    H  N N 325 
LYS HZ2    H  N N 326 
LYS HZ3    H  N N 327 
LYS HXT    H  N N 328 
MET N      N  N N 329 
MET CA     C  N S 330 
MET C      C  N N 331 
MET O      O  N N 332 
MET CB     C  N N 333 
MET CG     C  N N 334 
MET SD     S  N N 335 
MET CE     C  N N 336 
MET OXT    O  N N 337 
MET H      H  N N 338 
MET H2     H  N N 339 
MET HA     H  N N 340 
MET HB2    H  N N 341 
MET HB3    H  N N 342 
MET HG2    H  N N 343 
MET HG3    H  N N 344 
MET HE1    H  N N 345 
MET HE2    H  N N 346 
MET HE3    H  N N 347 
MET HXT    H  N N 348 
MG  MG     MG N N 349 
PHE N      N  N N 350 
PHE CA     C  N S 351 
PHE C      C  N N 352 
PHE O      O  N N 353 
PHE CB     C  N N 354 
PHE CG     C  Y N 355 
PHE CD1    C  Y N 356 
PHE CD2    C  Y N 357 
PHE CE1    C  Y N 358 
PHE CE2    C  Y N 359 
PHE CZ     C  Y N 360 
PHE OXT    O  N N 361 
PHE H      H  N N 362 
PHE H2     H  N N 363 
PHE HA     H  N N 364 
PHE HB2    H  N N 365 
PHE HB3    H  N N 366 
PHE HD1    H  N N 367 
PHE HD2    H  N N 368 
PHE HE1    H  N N 369 
PHE HE2    H  N N 370 
PHE HZ     H  N N 371 
PHE HXT    H  N N 372 
PRO N      N  N N 373 
PRO CA     C  N S 374 
PRO C      C  N N 375 
PRO O      O  N N 376 
PRO CB     C  N N 377 
PRO CG     C  N N 378 
PRO CD     C  N N 379 
PRO OXT    O  N N 380 
PRO H      H  N N 381 
PRO HA     H  N N 382 
PRO HB2    H  N N 383 
PRO HB3    H  N N 384 
PRO HG2    H  N N 385 
PRO HG3    H  N N 386 
PRO HD2    H  N N 387 
PRO HD3    H  N N 388 
PRO HXT    H  N N 389 
SER N      N  N N 390 
SER CA     C  N S 391 
SER C      C  N N 392 
SER O      O  N N 393 
SER CB     C  N N 394 
SER OG     O  N N 395 
SER OXT    O  N N 396 
SER H      H  N N 397 
SER H2     H  N N 398 
SER HA     H  N N 399 
SER HB2    H  N N 400 
SER HB3    H  N N 401 
SER HG     H  N N 402 
SER HXT    H  N N 403 
THR N      N  N N 404 
THR CA     C  N S 405 
THR C      C  N N 406 
THR O      O  N N 407 
THR CB     C  N R 408 
THR OG1    O  N N 409 
THR CG2    C  N N 410 
THR OXT    O  N N 411 
THR H      H  N N 412 
THR H2     H  N N 413 
THR HA     H  N N 414 
THR HB     H  N N 415 
THR HG1    H  N N 416 
THR HG21   H  N N 417 
THR HG22   H  N N 418 
THR HG23   H  N N 419 
THR HXT    H  N N 420 
TRP N      N  N N 421 
TRP CA     C  N S 422 
TRP C      C  N N 423 
TRP O      O  N N 424 
TRP CB     C  N N 425 
TRP CG     C  Y N 426 
TRP CD1    C  Y N 427 
TRP CD2    C  Y N 428 
TRP NE1    N  Y N 429 
TRP CE2    C  Y N 430 
TRP CE3    C  Y N 431 
TRP CZ2    C  Y N 432 
TRP CZ3    C  Y N 433 
TRP CH2    C  Y N 434 
TRP OXT    O  N N 435 
TRP H      H  N N 436 
TRP H2     H  N N 437 
TRP HA     H  N N 438 
TRP HB2    H  N N 439 
TRP HB3    H  N N 440 
TRP HD1    H  N N 441 
TRP HE1    H  N N 442 
TRP HE3    H  N N 443 
TRP HZ2    H  N N 444 
TRP HZ3    H  N N 445 
TRP HH2    H  N N 446 
TRP HXT    H  N N 447 
TYR N      N  N N 448 
TYR CA     C  N S 449 
TYR C      C  N N 450 
TYR O      O  N N 451 
TYR CB     C  N N 452 
TYR CG     C  Y N 453 
TYR CD1    C  Y N 454 
TYR CD2    C  Y N 455 
TYR CE1    C  Y N 456 
TYR CE2    C  Y N 457 
TYR CZ     C  Y N 458 
TYR OH     O  N N 459 
TYR OXT    O  N N 460 
TYR H      H  N N 461 
TYR H2     H  N N 462 
TYR HA     H  N N 463 
TYR HB2    H  N N 464 
TYR HB3    H  N N 465 
TYR HD1    H  N N 466 
TYR HD2    H  N N 467 
TYR HE1    H  N N 468 
TYR HE2    H  N N 469 
TYR HH     H  N N 470 
TYR HXT    H  N N 471 
VAL N      N  N N 472 
VAL CA     C  N S 473 
VAL C      C  N N 474 
VAL O      O  N N 475 
VAL CB     C  N N 476 
VAL CG1    C  N N 477 
VAL CG2    C  N N 478 
VAL OXT    O  N N 479 
VAL H      H  N N 480 
VAL H2     H  N N 481 
VAL HA     H  N N 482 
VAL HB     H  N N 483 
VAL HG11   H  N N 484 
VAL HG12   H  N N 485 
VAL HG13   H  N N 486 
VAL HG21   H  N N 487 
VAL HG22   H  N N 488 
VAL HG23   H  N N 489 
VAL HXT    H  N N 490 
# 
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 
HOH O     H1     sing N N 254 
HOH O     H2     sing N N 255 
ILE N     CA     sing N N 256 
ILE N     H      sing N N 257 
ILE N     H2     sing N N 258 
ILE CA    C      sing N N 259 
ILE CA    CB     sing N N 260 
ILE CA    HA     sing N N 261 
ILE C     O      doub N N 262 
ILE C     OXT    sing N N 263 
ILE CB    CG1    sing N N 264 
ILE CB    CG2    sing N N 265 
ILE CB    HB     sing N N 266 
ILE CG1   CD1    sing N N 267 
ILE CG1   HG12   sing N N 268 
ILE CG1   HG13   sing N N 269 
ILE CG2   HG21   sing N N 270 
ILE CG2   HG22   sing N N 271 
ILE CG2   HG23   sing N N 272 
ILE CD1   HD11   sing N N 273 
ILE CD1   HD12   sing N N 274 
ILE CD1   HD13   sing N N 275 
ILE OXT   HXT    sing N N 276 
LEU N     CA     sing N N 277 
LEU N     H      sing N N 278 
LEU N     H2     sing N N 279 
LEU CA    C      sing N N 280 
LEU CA    CB     sing N N 281 
LEU CA    HA     sing N N 282 
LEU C     O      doub N N 283 
LEU C     OXT    sing N N 284 
LEU CB    CG     sing N N 285 
LEU CB    HB2    sing N N 286 
LEU CB    HB3    sing N N 287 
LEU CG    CD1    sing N N 288 
LEU CG    CD2    sing N N 289 
LEU CG    HG     sing N N 290 
LEU CD1   HD11   sing N N 291 
LEU CD1   HD12   sing N N 292 
LEU CD1   HD13   sing N N 293 
LEU CD2   HD21   sing N N 294 
LEU CD2   HD22   sing N N 295 
LEU CD2   HD23   sing N N 296 
LEU OXT   HXT    sing N N 297 
LYS N     CA     sing N N 298 
LYS N     H      sing N N 299 
LYS N     H2     sing N N 300 
LYS CA    C      sing N N 301 
LYS CA    CB     sing N N 302 
LYS CA    HA     sing N N 303 
LYS C     O      doub N N 304 
LYS C     OXT    sing N N 305 
LYS CB    CG     sing N N 306 
LYS CB    HB2    sing N N 307 
LYS CB    HB3    sing N N 308 
LYS CG    CD     sing N N 309 
LYS CG    HG2    sing N N 310 
LYS CG    HG3    sing N N 311 
LYS CD    CE     sing N N 312 
LYS CD    HD2    sing N N 313 
LYS CD    HD3    sing N N 314 
LYS CE    NZ     sing N N 315 
LYS CE    HE2    sing N N 316 
LYS CE    HE3    sing N N 317 
LYS NZ    HZ1    sing N N 318 
LYS NZ    HZ2    sing N N 319 
LYS NZ    HZ3    sing N N 320 
LYS OXT   HXT    sing N N 321 
MET N     CA     sing N N 322 
MET N     H      sing N N 323 
MET N     H2     sing N N 324 
MET CA    C      sing N N 325 
MET CA    CB     sing N N 326 
MET CA    HA     sing N N 327 
MET C     O      doub N N 328 
MET C     OXT    sing N N 329 
MET CB    CG     sing N N 330 
MET CB    HB2    sing N N 331 
MET CB    HB3    sing N N 332 
MET CG    SD     sing N N 333 
MET CG    HG2    sing N N 334 
MET CG    HG3    sing N N 335 
MET SD    CE     sing N N 336 
MET CE    HE1    sing N N 337 
MET CE    HE2    sing N N 338 
MET CE    HE3    sing N N 339 
MET OXT   HXT    sing N N 340 
PHE N     CA     sing N N 341 
PHE N     H      sing N N 342 
PHE N     H2     sing N N 343 
PHE CA    C      sing N N 344 
PHE CA    CB     sing N N 345 
PHE CA    HA     sing N N 346 
PHE C     O      doub N N 347 
PHE C     OXT    sing N N 348 
PHE CB    CG     sing N N 349 
PHE CB    HB2    sing N N 350 
PHE CB    HB3    sing N N 351 
PHE CG    CD1    doub Y N 352 
PHE CG    CD2    sing Y N 353 
PHE CD1   CE1    sing Y N 354 
PHE CD1   HD1    sing N N 355 
PHE CD2   CE2    doub Y N 356 
PHE CD2   HD2    sing N N 357 
PHE CE1   CZ     doub Y N 358 
PHE CE1   HE1    sing N N 359 
PHE CE2   CZ     sing Y N 360 
PHE CE2   HE2    sing N N 361 
PHE CZ    HZ     sing N N 362 
PHE OXT   HXT    sing N N 363 
PRO N     CA     sing N N 364 
PRO N     CD     sing N N 365 
PRO N     H      sing N N 366 
PRO CA    C      sing N N 367 
PRO CA    CB     sing N N 368 
PRO CA    HA     sing N N 369 
PRO C     O      doub N N 370 
PRO C     OXT    sing N N 371 
PRO CB    CG     sing N N 372 
PRO CB    HB2    sing N N 373 
PRO CB    HB3    sing N N 374 
PRO CG    CD     sing N N 375 
PRO CG    HG2    sing N N 376 
PRO CG    HG3    sing N N 377 
PRO CD    HD2    sing N N 378 
PRO CD    HD3    sing N N 379 
PRO OXT   HXT    sing N N 380 
SER N     CA     sing N N 381 
SER N     H      sing N N 382 
SER N     H2     sing N N 383 
SER CA    C      sing N N 384 
SER CA    CB     sing N N 385 
SER CA    HA     sing N N 386 
SER C     O      doub N N 387 
SER C     OXT    sing N N 388 
SER CB    OG     sing N N 389 
SER CB    HB2    sing N N 390 
SER CB    HB3    sing N N 391 
SER OG    HG     sing N N 392 
SER OXT   HXT    sing N N 393 
THR N     CA     sing N N 394 
THR N     H      sing N N 395 
THR N     H2     sing N N 396 
THR CA    C      sing N N 397 
THR CA    CB     sing N N 398 
THR CA    HA     sing N N 399 
THR C     O      doub N N 400 
THR C     OXT    sing N N 401 
THR CB    OG1    sing N N 402 
THR CB    CG2    sing N N 403 
THR CB    HB     sing N N 404 
THR OG1   HG1    sing N N 405 
THR CG2   HG21   sing N N 406 
THR CG2   HG22   sing N N 407 
THR CG2   HG23   sing N N 408 
THR OXT   HXT    sing N N 409 
TRP N     CA     sing N N 410 
TRP N     H      sing N N 411 
TRP N     H2     sing N N 412 
TRP CA    C      sing N N 413 
TRP CA    CB     sing N N 414 
TRP CA    HA     sing N N 415 
TRP C     O      doub N N 416 
TRP C     OXT    sing N N 417 
TRP CB    CG     sing N N 418 
TRP CB    HB2    sing N N 419 
TRP CB    HB3    sing N N 420 
TRP CG    CD1    doub Y N 421 
TRP CG    CD2    sing Y N 422 
TRP CD1   NE1    sing Y N 423 
TRP CD1   HD1    sing N N 424 
TRP CD2   CE2    doub Y N 425 
TRP CD2   CE3    sing Y N 426 
TRP NE1   CE2    sing Y N 427 
TRP NE1   HE1    sing N N 428 
TRP CE2   CZ2    sing Y N 429 
TRP CE3   CZ3    doub Y N 430 
TRP CE3   HE3    sing N N 431 
TRP CZ2   CH2    doub Y N 432 
TRP CZ2   HZ2    sing N N 433 
TRP CZ3   CH2    sing Y N 434 
TRP CZ3   HZ3    sing N N 435 
TRP CH2   HH2    sing N N 436 
TRP OXT   HXT    sing N N 437 
TYR N     CA     sing N N 438 
TYR N     H      sing N N 439 
TYR N     H2     sing N N 440 
TYR CA    C      sing N N 441 
TYR CA    CB     sing N N 442 
TYR CA    HA     sing N N 443 
TYR C     O      doub N N 444 
TYR C     OXT    sing N N 445 
TYR CB    CG     sing N N 446 
TYR CB    HB2    sing N N 447 
TYR CB    HB3    sing N N 448 
TYR CG    CD1    doub Y N 449 
TYR CG    CD2    sing Y N 450 
TYR CD1   CE1    sing Y N 451 
TYR CD1   HD1    sing N N 452 
TYR CD2   CE2    doub Y N 453 
TYR CD2   HD2    sing N N 454 
TYR CE1   CZ     doub Y N 455 
TYR CE1   HE1    sing N N 456 
TYR CE2   CZ     sing Y N 457 
TYR CE2   HE2    sing N N 458 
TYR CZ    OH     sing N N 459 
TYR OH    HH     sing N N 460 
TYR OXT   HXT    sing N N 461 
VAL N     CA     sing N N 462 
VAL N     H      sing N N 463 
VAL N     H2     sing N N 464 
VAL CA    C      sing N N 465 
VAL CA    CB     sing N N 466 
VAL CA    HA     sing N N 467 
VAL C     O      doub N N 468 
VAL C     OXT    sing N N 469 
VAL CB    CG1    sing N N 470 
VAL CB    CG2    sing N N 471 
VAL CB    HB     sing N N 472 
VAL CG1   HG11   sing N N 473 
VAL CG1   HG12   sing N N 474 
VAL CG1   HG13   sing N N 475 
VAL CG2   HG21   sing N N 476 
VAL CG2   HG22   sing N N 477 
VAL CG2   HG23   sing N N 478 
VAL OXT   HXT    sing N N 479 
# 
_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 7TVF ? 
2 ? 'experimental model' PDB 5DXT ? 
# 
_atom_sites.entry_id                    9B4T 
_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]   0.016968 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002233 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009440 
_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]   0.008809 
_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     . GLY A 1 3   ? 16.177  -47.356 24.399  1.00 165.96 ? 106  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 3   ? 17.303  -46.982 25.235  1.00 168.80 ? 106  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 3   ? 17.073  -47.240 26.711  1.00 170.94 ? 106  GLY A C     1 
ATOM   4    O  O     . GLY A 1 3   ? 16.753  -48.358 27.115  1.00 171.34 ? 106  GLY A O     1 
ATOM   5    N  N     . ASN A 1 4   ? 17.237  -46.196 27.520  1.00 161.60 ? 107  ASN A N     1 
ATOM   6    C  CA    . ASN A 1 4   ? 17.062  -46.325 28.960  1.00 158.60 ? 107  ASN A CA    1 
ATOM   7    C  C     . ASN A 1 4   ? 15.585  -46.492 29.296  1.00 153.70 ? 107  ASN A C     1 
ATOM   8    O  O     . ASN A 1 4   ? 14.737  -45.740 28.805  1.00 145.33 ? 107  ASN A O     1 
ATOM   9    C  CB    . ASN A 1 4   ? 17.635  -45.099 29.671  1.00 153.38 ? 107  ASN A CB    1 
ATOM   10   C  CG    . ASN A 1 4   ? 17.827  -45.320 31.161  1.00 157.23 ? 107  ASN A CG    1 
ATOM   11   O  OD1   . ASN A 1 4   ? 17.154  -46.147 31.774  1.00 159.64 ? 107  ASN A OD1   1 
ATOM   12   N  ND2   . ASN A 1 4   ? 18.753  -44.573 31.751  1.00 158.37 ? 107  ASN A ND2   1 
ATOM   13   N  N     . ARG A 1 5   ? 15.279  -47.483 30.137  1.00 164.74 ? 108  ARG A N     1 
ATOM   14   C  CA    . ARG A 1 5   ? 13.903  -47.682 30.577  1.00 162.69 ? 108  ARG A CA    1 
ATOM   15   C  C     . ARG A 1 5   ? 13.403  -46.525 31.432  1.00 165.23 ? 108  ARG A C     1 
ATOM   16   O  O     . ARG A 1 5   ? 12.188  -46.344 31.559  1.00 164.58 ? 108  ARG A O     1 
ATOM   17   C  CB    . ARG A 1 5   ? 13.771  -49.003 31.345  1.00 162.31 ? 108  ARG A CB    1 
ATOM   18   C  CG    . ARG A 1 5   ? 14.083  -48.930 32.839  1.00 165.56 ? 108  ARG A CG    1 
ATOM   19   C  CD    . ARG A 1 5   ? 15.545  -48.607 33.111  1.00 169.72 ? 108  ARG A CD    1 
ATOM   20   N  NE    . ARG A 1 5   ? 16.448  -49.475 32.366  1.00 177.52 ? 108  ARG A NE    1 
ATOM   21   C  CZ    . ARG A 1 5   ? 17.767  -49.336 32.339  1.00 173.39 ? 108  ARG A CZ    1 
ATOM   22   N  NH1   . ARG A 1 5   ? 18.373  -48.368 33.007  1.00 169.84 ? 108  ARG A NH1   1 
ATOM   23   N  NH2   . ARG A 1 5   ? 18.495  -50.188 31.623  1.00 173.31 ? 108  ARG A NH2   1 
ATOM   24   N  N     . GLU A 1 6   ? 14.311  -45.740 32.018  1.00 153.41 ? 109  GLU A N     1 
ATOM   25   C  CA    . GLU A 1 6   ? 13.898  -44.538 32.732  1.00 146.54 ? 109  GLU A CA    1 
ATOM   26   C  C     . GLU A 1 6   ? 13.492  -43.434 31.766  1.00 137.71 ? 109  GLU A C     1 
ATOM   27   O  O     . GLU A 1 6   ? 12.594  -42.642 32.072  1.00 131.44 ? 109  GLU A O     1 
ATOM   28   C  CB    . GLU A 1 6   ? 15.024  -44.058 33.648  1.00 151.52 ? 109  GLU A CB    1 
ATOM   29   C  CG    . GLU A 1 6   ? 15.585  -45.137 34.560  1.00 156.92 ? 109  GLU A CG    1 
ATOM   30   C  CD    . GLU A 1 6   ? 14.556  -45.677 35.535  1.00 157.75 ? 109  GLU A CD    1 
ATOM   31   O  OE1   . GLU A 1 6   ? 13.642  -44.919 35.922  1.00 156.30 ? 109  GLU A OE1   1 
ATOM   32   O  OE2   . GLU A 1 6   ? 14.661  -46.863 35.912  1.00 161.68 ? 109  GLU A OE2   1 
ATOM   33   N  N     . GLU A 1 7   ? 14.141  -43.364 30.601  1.00 141.90 ? 110  GLU A N     1 
ATOM   34   C  CA    . GLU A 1 7   ? 13.729  -42.406 29.582  1.00 139.59 ? 110  GLU A CA    1 
ATOM   35   C  C     . GLU A 1 7   ? 12.389  -42.790 28.969  1.00 130.40 ? 110  GLU A C     1 
ATOM   36   O  O     . GLU A 1 7   ? 11.603  -41.910 28.598  1.00 125.90 ? 110  GLU A O     1 
ATOM   37   C  CB    . GLU A 1 7   ? 14.803  -42.295 28.500  1.00 136.79 ? 110  GLU A CB    1 
ATOM   38   C  CG    . GLU A 1 7   ? 14.514  -41.247 27.437  1.00 133.73 ? 110  GLU A CG    1 
ATOM   39   C  CD    . GLU A 1 7   ? 15.632  -41.122 26.422  1.00 134.47 ? 110  GLU A CD    1 
ATOM   40   O  OE1   . GLU A 1 7   ? 16.652  -41.830 26.568  1.00 134.08 ? 110  GLU A OE1   1 
ATOM   41   O  OE2   . GLU A 1 7   ? 15.493  -40.316 25.478  1.00 126.83 ? 110  GLU A OE2   1 
ATOM   42   N  N     . LYS A 1 8   ? 12.110  -44.091 28.856  1.00 128.73 ? 111  LYS A N     1 
ATOM   43   C  CA    . LYS A 1 8   ? 10.804  -44.525 28.371  1.00 122.81 ? 111  LYS A CA    1 
ATOM   44   C  C     . LYS A 1 8   ? 9.701   -44.133 29.346  1.00 122.32 ? 111  LYS A C     1 
ATOM   45   O  O     . LYS A 1 8   ? 8.595   -43.768 28.929  1.00 117.78 ? 111  LYS A O     1 
ATOM   46   C  CB    . LYS A 1 8   ? 10.803  -46.035 28.137  1.00 120.53 ? 111  LYS A CB    1 
ATOM   47   C  CG    . LYS A 1 8   ? 11.931  -46.529 27.247  1.00 122.72 ? 111  LYS A CG    1 
ATOM   48   C  CD    . LYS A 1 8   ? 11.936  -45.812 25.906  1.00 118.79 ? 111  LYS A CD    1 
ATOM   49   C  CE    . LYS A 1 8   ? 13.119  -46.247 25.057  1.00 129.70 ? 111  LYS A CE    1 
ATOM   50   N  NZ    . LYS A 1 8   ? 13.216  -45.470 23.791  1.00 130.68 ? 111  LYS A NZ    1 
ATOM   51   N  N     . ILE A 1 9   ? 9.982   -44.202 30.649  1.00 121.69 ? 112  ILE A N     1 
ATOM   52   C  CA    . ILE A 1 9   ? 9.011   -43.755 31.642  1.00 118.16 ? 112  ILE A CA    1 
ATOM   53   C  C     . ILE A 1 9   ? 8.819   -42.246 31.555  1.00 115.65 ? 112  ILE A C     1 
ATOM   54   O  O     . ILE A 1 9   ? 7.693   -41.744 31.645  1.00 117.10 ? 112  ILE A O     1 
ATOM   55   C  CB    . ILE A 1 9   ? 9.447   -44.195 33.051  1.00 116.70 ? 112  ILE A CB    1 
ATOM   56   C  CG1   . ILE A 1 9   ? 9.471   -45.722 33.148  1.00 119.15 ? 112  ILE A CG1   1 
ATOM   57   C  CG2   . ILE A 1 9   ? 8.524   -43.609 34.108  1.00 109.82 ? 112  ILE A CG2   1 
ATOM   58   C  CD1   . ILE A 1 9   ? 9.927   -46.244 34.492  1.00 120.12 ? 112  ILE A CD1   1 
ATOM   59   N  N     . LEU A 1 10  ? 9.911   -41.500 31.366  1.00 113.09 ? 113  LEU A N     1 
ATOM   60   C  CA    . LEU A 1 10  ? 9.799   -40.052 31.226  1.00 108.45 ? 113  LEU A CA    1 
ATOM   61   C  C     . LEU A 1 10  ? 9.066   -39.676 29.944  1.00 108.30 ? 113  LEU A C     1 
ATOM   62   O  O     . LEU A 1 10  ? 8.282   -38.720 29.930  1.00 104.95 ? 113  LEU A O     1 
ATOM   63   C  CB    . LEU A 1 10  ? 11.186  -39.411 31.254  1.00 105.84 ? 113  LEU A CB    1 
ATOM   64   C  CG    . LEU A 1 10  ? 11.219  -37.890 31.091  1.00 98.38  ? 113  LEU A CG    1 
ATOM   65   C  CD1   . LEU A 1 10  ? 10.566  -37.199 32.284  1.00 80.27  ? 113  LEU A CD1   1 
ATOM   66   C  CD2   . LEU A 1 10  ? 12.643  -37.395 30.884  1.00 90.75  ? 113  LEU A CD2   1 
ATOM   67   N  N     . ASN A 1 11  ? 9.307   -40.417 28.858  1.00 113.13 ? 114  ASN A N     1 
ATOM   68   C  CA    . ASN A 1 11  ? 8.658   -40.107 27.587  1.00 110.47 ? 114  ASN A CA    1 
ATOM   69   C  C     . ASN A 1 11  ? 7.147   -40.276 27.667  1.00 112.83 ? 114  ASN A C     1 
ATOM   70   O  O     . ASN A 1 11  ? 6.407   -39.545 26.999  1.00 109.47 ? 114  ASN A O     1 
ATOM   71   C  CB    . ASN A 1 11  ? 9.229   -40.988 26.475  1.00 111.51 ? 114  ASN A CB    1 
ATOM   72   C  CG    . ASN A 1 11  ? 10.560  -40.483 25.955  1.00 107.84 ? 114  ASN A CG    1 
ATOM   73   O  OD1   . ASN A 1 11  ? 11.123  -39.524 26.483  1.00 109.60 ? 114  ASN A OD1   1 
ATOM   74   N  ND2   . ASN A 1 11  ? 11.072  -41.131 24.917  1.00 101.79 ? 114  ASN A ND2   1 
ATOM   75   N  N     . ARG A 1 12  ? 6.669   -41.226 28.473  1.00 124.85 ? 115  ARG A N     1 
ATOM   76   C  CA    . ARG A 1 12  ? 5.229   -41.418 28.602  1.00 125.79 ? 115  ARG A CA    1 
ATOM   77   C  C     . ARG A 1 12  ? 4.586   -40.310 29.426  1.00 117.89 ? 115  ARG A C     1 
ATOM   78   O  O     . ARG A 1 12  ? 3.441   -39.927 29.160  1.00 119.36 ? 115  ARG A O     1 
ATOM   79   C  CB    . ARG A 1 12  ? 4.932   -42.784 29.219  1.00 128.89 ? 115  ARG A CB    1 
ATOM   80   C  CG    . ARG A 1 12  ? 5.386   -43.958 28.365  1.00 133.12 ? 115  ARG A CG    1 
ATOM   81   C  CD    . ARG A 1 12  ? 4.997   -45.293 28.986  1.00 154.11 ? 115  ARG A CD    1 
ATOM   82   N  NE    . ARG A 1 12  ? 3.551   -45.480 29.036  1.00 162.83 ? 115  ARG A NE    1 
ATOM   83   C  CZ    . ARG A 1 12  ? 2.804   -45.276 30.112  1.00 161.03 ? 115  ARG A CZ    1 
ATOM   84   N  NH1   . ARG A 1 12  ? 3.336   -44.883 31.259  1.00 156.81 ? 115  ARG A NH1   1 
ATOM   85   N  NH2   . ARG A 1 12  ? 1.491   -45.471 30.037  1.00 161.65 ? 115  ARG A NH2   1 
ATOM   86   N  N     . GLU A 1 13  ? 5.299   -39.782 30.423  1.00 108.41 ? 116  GLU A N     1 
ATOM   87   C  CA    . GLU A 1 13  ? 4.750   -38.687 31.215  1.00 108.40 ? 116  GLU A CA    1 
ATOM   88   C  C     . GLU A 1 13  ? 4.757   -37.382 30.428  1.00 104.84 ? 116  GLU A C     1 
ATOM   89   O  O     . GLU A 1 13  ? 3.833   -36.570 30.554  1.00 106.41 ? 116  GLU A O     1 
ATOM   90   C  CB    . GLU A 1 13  ? 5.533   -38.534 32.519  1.00 112.73 ? 116  GLU A CB    1 
ATOM   91   C  CG    . GLU A 1 13  ? 5.746   -39.837 33.276  1.00 119.34 ? 116  GLU A CG    1 
ATOM   92   C  CD    . GLU A 1 13  ? 4.453   -40.586 33.541  1.00 141.49 ? 116  GLU A CD    1 
ATOM   93   O  OE1   . GLU A 1 13  ? 3.448   -39.939 33.907  1.00 137.67 ? 116  GLU A OE1   1 
ATOM   94   O  OE2   . GLU A 1 13  ? 4.441   -41.825 33.378  1.00 146.17 ? 116  GLU A OE2   1 
ATOM   95   N  N     . ILE A 1 14  ? 5.791   -37.164 29.611  1.00 104.56 ? 117  ILE A N     1 
ATOM   96   C  CA    . ILE A 1 14  ? 5.847   -35.962 28.785  1.00 99.60  ? 117  ILE A CA    1 
ATOM   97   C  C     . ILE A 1 14  ? 4.737   -35.979 27.742  1.00 99.25  ? 117  ILE A C     1 
ATOM   98   O  O     . ILE A 1 14  ? 4.094   -34.955 27.482  1.00 95.11  ? 117  ILE A O     1 
ATOM   99   C  CB    . ILE A 1 14  ? 7.236   -35.826 28.135  1.00 101.64 ? 117  ILE A CB    1 
ATOM   100  C  CG1   . ILE A 1 14  ? 8.303   -35.571 29.201  1.00 96.57  ? 117  ILE A CG1   1 
ATOM   101  C  CG2   . ILE A 1 14  ? 7.240   -34.713 27.096  1.00 97.76  ? 117  ILE A CG2   1 
ATOM   102  C  CD1   . ILE A 1 14  ? 9.707   -35.460 28.646  1.00 95.14  ? 117  ILE A CD1   1 
ATOM   103  N  N     . GLY A 1 15  ? 4.490   -37.140 27.133  1.00 103.06 ? 118  GLY A N     1 
ATOM   104  C  CA    . GLY A 1 15  ? 3.417   -37.241 26.160  1.00 101.22 ? 118  GLY A CA    1 
ATOM   105  C  C     . GLY A 1 15  ? 2.041   -37.064 26.767  1.00 96.90  ? 118  GLY A C     1 
ATOM   106  O  O     . GLY A 1 15  ? 1.130   -36.553 26.108  1.00 92.41  ? 118  GLY A O     1 
ATOM   107  N  N     . PHE A 1 16  ? 1.867   -37.479 28.024  1.00 99.63  ? 119  PHE A N     1 
ATOM   108  C  CA    . PHE A 1 16  ? 0.571   -37.328 28.677  1.00 97.61  ? 119  PHE A CA    1 
ATOM   109  C  C     . PHE A 1 16  ? 0.287   -35.870 29.013  1.00 93.40  ? 119  PHE A C     1 
ATOM   110  O  O     . PHE A 1 16  ? -0.864  -35.423 28.942  1.00 91.09  ? 119  PHE A O     1 
ATOM   111  C  CB    . PHE A 1 16  ? 0.514   -38.192 29.937  1.00 97.21  ? 119  PHE A CB    1 
ATOM   112  C  CG    . PHE A 1 16  ? -0.798  -38.119 30.663  1.00 97.09  ? 119  PHE A CG    1 
ATOM   113  C  CD1   . PHE A 1 16  ? -1.858  -38.928 30.286  1.00 97.59  ? 119  PHE A CD1   1 
ATOM   114  C  CD2   . PHE A 1 16  ? -0.973  -37.244 31.725  1.00 99.05  ? 119  PHE A CD2   1 
ATOM   115  C  CE1   . PHE A 1 16  ? -3.068  -38.864 30.951  1.00 103.08 ? 119  PHE A CE1   1 
ATOM   116  C  CE2   . PHE A 1 16  ? -2.180  -37.175 32.394  1.00 97.07  ? 119  PHE A CE2   1 
ATOM   117  C  CZ    . PHE A 1 16  ? -3.229  -37.986 32.007  1.00 101.91 ? 119  PHE A CZ    1 
ATOM   118  N  N     . ALA A 1 17  ? 1.322   -35.112 29.382  1.00 93.61  ? 120  ALA A N     1 
ATOM   119  C  CA    . ALA A 1 17  ? 1.120   -33.708 29.723  1.00 94.68  ? 120  ALA A CA    1 
ATOM   120  C  C     . ALA A 1 17  ? 0.819   -32.873 28.485  1.00 89.73  ? 120  ALA A C     1 
ATOM   121  O  O     . ALA A 1 17  ? -0.030  -31.976 28.526  1.00 87.67  ? 120  ALA A O     1 
ATOM   122  C  CB    . ALA A 1 17  ? 2.348   -33.162 30.453  1.00 91.03  ? 120  ALA A CB    1 
ATOM   123  N  N     . ILE A 1 18  ? 1.500   -33.157 27.370  1.00 94.47  ? 121  ILE A N     1 
ATOM   124  C  CA    . ILE A 1 18  ? 1.324   -32.365 26.155  1.00 90.04  ? 121  ILE A CA    1 
ATOM   125  C  C     . ILE A 1 18  ? 0.220   -32.898 25.253  1.00 91.09  ? 121  ILE A C     1 
ATOM   126  O  O     . ILE A 1 18  ? -0.165  -32.212 24.293  1.00 93.75  ? 121  ILE A O     1 
ATOM   127  C  CB    . ILE A 1 18  ? 2.642   -32.284 25.360  1.00 90.38  ? 121  ILE A CB    1 
ATOM   128  C  CG1   . ILE A 1 18  ? 2.964   -33.631 24.716  1.00 96.33  ? 121  ILE A CG1   1 
ATOM   129  C  CG2   . ILE A 1 18  ? 3.779   -31.856 26.272  1.00 92.79  ? 121  ILE A CG2   1 
ATOM   130  C  CD1   . ILE A 1 18  ? 4.244   -33.627 23.906  1.00 102.82 ? 121  ILE A CD1   1 
ATOM   131  N  N     . GLY A 1 19  ? -0.302  -34.093 25.523  1.00 92.78  ? 122  GLY A N     1 
ATOM   132  C  CA    . GLY A 1 19  ? -1.411  -34.635 24.769  1.00 96.39  ? 122  GLY A CA    1 
ATOM   133  C  C     . GLY A 1 19  ? -1.035  -35.480 23.571  1.00 96.00  ? 122  GLY A C     1 
ATOM   134  O  O     . GLY A 1 19  ? -1.908  -36.159 23.016  1.00 96.14  ? 122  GLY A O     1 
ATOM   135  N  N     . MET A 1 20  ? 0.228   -35.462 23.151  1.00 96.98  ? 123  MET A N     1 
ATOM   136  C  CA    . MET A 1 20  ? 0.671   -36.258 22.021  1.00 100.46 ? 123  MET A CA    1 
ATOM   137  C  C     . MET A 1 20  ? 1.944   -37.009 22.384  1.00 102.60 ? 123  MET A C     1 
ATOM   138  O  O     . MET A 1 20  ? 2.798   -36.475 23.102  1.00 103.10 ? 123  MET A O     1 
ATOM   139  C  CB    . MET A 1 20  ? 0.916   -35.379 20.785  1.00 108.37 ? 123  MET A CB    1 
ATOM   140  C  CG    . MET A 1 20  ? 1.879   -34.227 21.015  1.00 104.16 ? 123  MET A CG    1 
ATOM   141  S  SD    . MET A 1 20  ? 2.232   -33.325 19.495  1.00 123.13 ? 123  MET A SD    1 
ATOM   142  C  CE    . MET A 1 20  ? 2.877   -34.643 18.467  1.00 105.68 ? 123  MET A CE    1 
ATOM   143  N  N     . PRO A 1 21  ? 2.100   -38.243 21.909  1.00 105.61 ? 124  PRO A N     1 
ATOM   144  C  CA    . PRO A 1 21  ? 3.287   -39.023 22.272  1.00 108.20 ? 124  PRO A CA    1 
ATOM   145  C  C     . PRO A 1 21  ? 4.553   -38.439 21.667  1.00 111.69 ? 124  PRO A C     1 
ATOM   146  O  O     . PRO A 1 21  ? 4.534   -37.805 20.609  1.00 112.28 ? 124  PRO A O     1 
ATOM   147  C  CB    . PRO A 1 21  ? 2.987   -40.413 21.700  1.00 108.69 ? 124  PRO A CB    1 
ATOM   148  C  CG    . PRO A 1 21  ? 2.042   -40.152 20.576  1.00 111.54 ? 124  PRO A CG    1 
ATOM   149  C  CD    . PRO A 1 21  ? 1.200   -38.986 21.011  1.00 106.64 ? 124  PRO A CD    1 
ATOM   150  N  N     . VAL A 1 22  ? 5.670   -38.663 22.364  1.00 114.99 ? 125  VAL A N     1 
ATOM   151  C  CA    . VAL A 1 22  ? 6.956   -38.156 21.904  1.00 116.47 ? 125  VAL A CA    1 
ATOM   152  C  C     . VAL A 1 22  ? 7.423   -38.875 20.645  1.00 122.26 ? 125  VAL A C     1 
ATOM   153  O  O     . VAL A 1 22  ? 8.297   -38.367 19.931  1.00 119.70 ? 125  VAL A O     1 
ATOM   154  C  CB    . VAL A 1 22  ? 8.000   -38.277 23.032  1.00 107.44 ? 125  VAL A CB    1 
ATOM   155  C  CG1   . VAL A 1 22  ? 9.227   -37.429 22.731  1.00 104.59 ? 125  VAL A CG1   1 
ATOM   156  C  CG2   . VAL A 1 22  ? 7.386   -37.872 24.361  1.00 108.40 ? 125  VAL A CG2   1 
ATOM   157  N  N     . CYS A 1 23  ? 6.850   -40.044 20.344  1.00 136.06 ? 126  CYS A N     1 
ATOM   158  C  CA    . CYS A 1 23  ? 7.263   -40.793 19.161  1.00 130.10 ? 126  CYS A CA    1 
ATOM   159  C  C     . CYS A 1 23  ? 6.961   -40.035 17.875  1.00 124.78 ? 126  CYS A C     1 
ATOM   160  O  O     . CYS A 1 23  ? 7.660   -40.216 16.872  1.00 140.67 ? 126  CYS A O     1 
ATOM   161  C  CB    . CYS A 1 23  ? 6.578   -42.160 19.140  1.00 127.14 ? 126  CYS A CB    1 
ATOM   162  S  SG    . CYS A 1 23  ? 6.899   -43.182 20.594  1.00 182.81 ? 126  CYS A SG    1 
ATOM   163  N  N     . GLU A 1 24  ? 5.932   -39.184 17.882  1.00 120.10 ? 127  GLU A N     1 
ATOM   164  C  CA    . GLU A 1 24  ? 5.579   -38.449 16.672  1.00 122.42 ? 127  GLU A CA    1 
ATOM   165  C  C     . GLU A 1 24  ? 6.641   -37.422 16.301  1.00 123.04 ? 127  GLU A C     1 
ATOM   166  O  O     . GLU A 1 24  ? 6.832   -37.132 15.115  1.00 124.11 ? 127  GLU A O     1 
ATOM   167  C  CB    . GLU A 1 24  ? 4.220   -37.770 16.843  1.00 120.81 ? 127  GLU A CB    1 
ATOM   168  C  CG    . GLU A 1 24  ? 3.070   -38.736 17.076  1.00 119.66 ? 127  GLU A CG    1 
ATOM   169  C  CD    . GLU A 1 24  ? 1.717   -38.052 17.035  1.00 122.80 ? 127  GLU A CD    1 
ATOM   170  O  OE1   . GLU A 1 24  ? 1.618   -36.961 16.435  1.00 121.21 ? 127  GLU A OE1   1 
ATOM   171  O  OE2   . GLU A 1 24  ? 0.752   -38.605 17.605  1.00 129.30 ? 127  GLU A OE2   1 
ATOM   172  N  N     . PHE A 1 25  ? 7.339   -36.863 17.293  1.00 120.11 ? 128  PHE A N     1 
ATOM   173  C  CA    . PHE A 1 25  ? 8.402   -35.909 16.995  1.00 117.10 ? 128  PHE A CA    1 
ATOM   174  C  C     . PHE A 1 25  ? 9.615   -36.594 16.379  1.00 120.98 ? 128  PHE A C     1 
ATOM   175  O  O     . PHE A 1 25  ? 10.309  -35.993 15.551  1.00 124.18 ? 128  PHE A O     1 
ATOM   176  C  CB    . PHE A 1 25  ? 8.803   -35.156 18.263  1.00 112.19 ? 128  PHE A CB    1 
ATOM   177  C  CG    . PHE A 1 25  ? 7.735   -34.238 18.786  1.00 115.48 ? 128  PHE A CG    1 
ATOM   178  C  CD1   . PHE A 1 25  ? 6.882   -33.580 17.915  1.00 111.09 ? 128  PHE A CD1   1 
ATOM   179  C  CD2   . PHE A 1 25  ? 7.581   -34.037 20.148  1.00 109.72 ? 128  PHE A CD2   1 
ATOM   180  C  CE1   . PHE A 1 25  ? 5.898   -32.733 18.393  1.00 114.27 ? 128  PHE A CE1   1 
ATOM   181  C  CE2   . PHE A 1 25  ? 6.598   -33.193 20.632  1.00 103.95 ? 128  PHE A CE2   1 
ATOM   182  C  CZ    . PHE A 1 25  ? 5.756   -32.541 19.754  1.00 103.53 ? 128  PHE A CZ    1 
ATOM   183  N  N     . ASP A 1 26  ? 9.886   -37.843 16.764  1.00 121.47 ? 129  ASP A N     1 
ATOM   184  C  CA    . ASP A 1 26  ? 11.005  -38.586 16.197  1.00 121.44 ? 129  ASP A CA    1 
ATOM   185  C  C     . ASP A 1 26  ? 10.796  -38.936 14.730  1.00 127.78 ? 129  ASP A C     1 
ATOM   186  O  O     . ASP A 1 26  ? 11.761  -39.319 14.060  1.00 125.43 ? 129  ASP A O     1 
ATOM   187  C  CB    . ASP A 1 26  ? 11.246  -39.865 17.001  1.00 123.90 ? 129  ASP A CB    1 
ATOM   188  C  CG    . ASP A 1 26  ? 11.580  -39.588 18.454  1.00 124.96 ? 129  ASP A CG    1 
ATOM   189  O  OD1   . ASP A 1 26  ? 12.306  -38.607 18.723  1.00 121.10 ? 129  ASP A OD1   1 
ATOM   190  O  OD2   . ASP A 1 26  ? 11.115  -40.349 19.328  1.00 125.96 ? 129  ASP A OD2   1 
ATOM   191  N  N     . MET A 1 27  ? 9.571   -38.816 14.220  1.00 135.63 ? 130  MET A N     1 
ATOM   192  C  CA    . MET A 1 27  ? 9.264   -39.147 12.836  1.00 124.36 ? 130  MET A CA    1 
ATOM   193  C  C     . MET A 1 27  ? 9.234   -37.931 11.920  1.00 119.55 ? 130  MET A C     1 
ATOM   194  O  O     . MET A 1 27  ? 9.123   -38.099 10.701  1.00 125.35 ? 130  MET A O     1 
ATOM   195  C  CB    . MET A 1 27  ? 7.916   -39.876 12.755  1.00 130.74 ? 130  MET A CB    1 
ATOM   196  C  CG    . MET A 1 27  ? 7.804   -41.071 13.687  1.00 135.19 ? 130  MET A CG    1 
ATOM   197  S  SD    . MET A 1 27  ? 9.075   -42.315 13.385  1.00 167.80 ? 130  MET A SD    1 
ATOM   198  C  CE    . MET A 1 27  ? 8.746   -43.466 14.718  1.00 159.95 ? 130  MET A CE    1 
ATOM   199  N  N     . VAL A 1 28  ? 9.326   -36.722 12.469  1.00 120.10 ? 131  VAL A N     1 
ATOM   200  C  CA    . VAL A 1 28  ? 9.315   -35.511 11.654  1.00 114.49 ? 131  VAL A CA    1 
ATOM   201  C  C     . VAL A 1 28  ? 10.655  -35.415 10.930  1.00 113.08 ? 131  VAL A C     1 
ATOM   202  O  O     . VAL A 1 28  ? 11.698  -35.221 11.559  1.00 114.55 ? 131  VAL A O     1 
ATOM   203  C  CB    . VAL A 1 28  ? 9.049   -34.263 12.503  1.00 105.62 ? 131  VAL A CB    1 
ATOM   204  C  CG1   . VAL A 1 28  ? 8.949   -33.035 11.615  1.00 98.97  ? 131  VAL A CG1   1 
ATOM   205  C  CG2   . VAL A 1 28  ? 7.781   -34.441 13.327  1.00 104.63 ? 131  VAL A CG2   1 
ATOM   206  N  N     . LYS A 1 29  ? 10.629  -35.551 9.606   1.00 120.94 ? 132  LYS A N     1 
ATOM   207  C  CA    . LYS A 1 29  ? 11.845  -35.519 8.804   1.00 114.95 ? 132  LYS A CA    1 
ATOM   208  C  C     . LYS A 1 29  ? 12.368  -34.109 8.563   1.00 107.85 ? 132  LYS A C     1 
ATOM   209  O  O     . LYS A 1 29  ? 13.440  -33.962 7.967   1.00 102.26 ? 132  LYS A O     1 
ATOM   210  C  CB    . LYS A 1 29  ? 11.608  -36.211 7.460   1.00 115.34 ? 132  LYS A CB    1 
ATOM   211  C  CG    . LYS A 1 29  ? 11.249  -37.683 7.571   1.00 125.28 ? 132  LYS A CG    1 
ATOM   212  C  CD    . LYS A 1 29  ? 11.111  -38.316 6.195   1.00 142.33 ? 132  LYS A CD    1 
ATOM   213  C  CE    . LYS A 1 29  ? 10.820  -39.804 6.296   1.00 144.64 ? 132  LYS A CE    1 
ATOM   214  N  NZ    . LYS A 1 29  ? 10.786  -40.453 4.957   1.00 139.53 ? 132  LYS A NZ    1 
ATOM   215  N  N     . ASP A 1 30  ? 11.650  -33.083 9.003   1.00 99.51  ? 133  ASP A N     1 
ATOM   216  C  CA    . ASP A 1 30  ? 12.084  -31.707 8.802   1.00 95.47  ? 133  ASP A CA    1 
ATOM   217  C  C     . ASP A 1 30  ? 13.384  -31.457 9.558   1.00 97.99  ? 133  ASP A C     1 
ATOM   218  O  O     . ASP A 1 30  ? 13.407  -31.578 10.793  1.00 95.97  ? 133  ASP A O     1 
ATOM   219  C  CB    . ASP A 1 30  ? 11.000  -30.737 9.267   1.00 94.18  ? 133  ASP A CB    1 
ATOM   220  C  CG    . ASP A 1 30  ? 11.261  -29.305 8.827   1.00 93.80  ? 133  ASP A CG    1 
ATOM   221  O  OD1   . ASP A 1 30  ? 12.330  -29.036 8.240   1.00 95.84  ? 133  ASP A OD1   1 
ATOM   222  O  OD2   . ASP A 1 30  ? 10.387  -28.445 9.065   1.00 93.98  ? 133  ASP A OD2   1 
ATOM   223  N  N     . PRO A 1 31  ? 14.478  -31.115 8.873   1.00 98.19  ? 134  PRO A N     1 
ATOM   224  C  CA    . PRO A 1 31  ? 15.749  -30.891 9.580   1.00 97.07  ? 134  PRO A CA    1 
ATOM   225  C  C     . PRO A 1 31  ? 15.708  -29.742 10.570  1.00 88.78  ? 134  PRO A C     1 
ATOM   226  O  O     . PRO A 1 31  ? 16.558  -29.692 11.465  1.00 93.93  ? 134  PRO A O     1 
ATOM   227  C  CB    . PRO A 1 31  ? 16.740  -30.614 8.441   1.00 91.88  ? 134  PRO A CB    1 
ATOM   228  C  CG    . PRO A 1 31  ? 16.120  -31.245 7.242   1.00 83.07  ? 134  PRO A CG    1 
ATOM   229  C  CD    . PRO A 1 31  ? 14.645  -31.054 7.412   1.00 81.81  ? 134  PRO A CD    1 
ATOM   230  N  N     . GLU A 1 32  ? 14.757  -28.813 10.440  1.00 86.24  ? 135  GLU A N     1 
ATOM   231  C  CA    . GLU A 1 32  ? 14.629  -27.754 11.436  1.00 89.56  ? 135  GLU A CA    1 
ATOM   232  C  C     . GLU A 1 32  ? 14.027  -28.289 12.728  1.00 91.48  ? 135  GLU A C     1 
ATOM   233  O  O     . GLU A 1 32  ? 14.444  -27.898 13.825  1.00 86.12  ? 135  GLU A O     1 
ATOM   234  C  CB    . GLU A 1 32  ? 13.780  -26.608 10.887  1.00 88.72  ? 135  GLU A CB    1 
ATOM   235  C  CG    . GLU A 1 32  ? 13.646  -25.432 11.842  1.00 87.09  ? 135  GLU A CG    1 
ATOM   236  C  CD    . GLU A 1 32  ? 12.918  -24.255 11.226  1.00 90.98  ? 135  GLU A CD    1 
ATOM   237  O  OE1   . GLU A 1 32  ? 12.543  -24.339 10.038  1.00 113.60 ? 135  GLU A OE1   1 
ATOM   238  O  OE2   . GLU A 1 32  ? 12.721  -23.242 11.931  1.00 89.47  ? 135  GLU A OE2   1 
ATOM   239  N  N     . VAL A 1 33  ? 13.045  -29.185 12.614  1.00 96.07  ? 136  VAL A N     1 
ATOM   240  C  CA    . VAL A 1 33  ? 12.424  -29.775 13.796  1.00 87.19  ? 136  VAL A CA    1 
ATOM   241  C  C     . VAL A 1 33  ? 13.446  -30.579 14.589  1.00 87.71  ? 136  VAL A C     1 
ATOM   242  O  O     . VAL A 1 33  ? 13.506  -30.492 15.822  1.00 97.10  ? 136  VAL A O     1 
ATOM   243  C  CB    . VAL A 1 33  ? 11.216  -30.636 13.384  1.00 88.46  ? 136  VAL A CB    1 
ATOM   244  C  CG1   . VAL A 1 33  ? 10.741  -31.492 14.546  1.00 89.14  ? 136  VAL A CG1   1 
ATOM   245  C  CG2   . VAL A 1 33  ? 10.089  -29.750 12.873  1.00 86.84  ? 136  VAL A CG2   1 
ATOM   246  N  N     . GLN A 1 34  ? 14.273  -31.365 13.899  1.00 89.75  ? 137  GLN A N     1 
ATOM   247  C  CA    . GLN A 1 34  ? 15.265  -32.171 14.600  1.00 95.08  ? 137  GLN A CA    1 
ATOM   248  C  C     . GLN A 1 34  ? 16.411  -31.313 15.121  1.00 94.13  ? 137  GLN A C     1 
ATOM   249  O  O     . GLN A 1 34  ? 16.947  -31.577 16.204  1.00 89.29  ? 137  GLN A O     1 
ATOM   250  C  CB    . GLN A 1 34  ? 15.787  -33.278 13.684  1.00 97.13  ? 137  GLN A CB    1 
ATOM   251  C  CG    . GLN A 1 34  ? 14.716  -34.263 13.237  1.00 97.41  ? 137  GLN A CG    1 
ATOM   252  C  CD    . GLN A 1 34  ? 13.952  -34.873 14.401  1.00 105.82 ? 137  GLN A CD    1 
ATOM   253  O  OE1   . GLN A 1 34  ? 14.505  -35.093 15.480  1.00 109.63 ? 137  GLN A OE1   1 
ATOM   254  N  NE2   . GLN A 1 34  ? 12.670  -35.146 14.187  1.00 105.62 ? 137  GLN A NE2   1 
ATOM   255  N  N     . ASP A 1 35  ? 16.801  -30.280 14.370  1.00 92.84  ? 138  ASP A N     1 
ATOM   256  C  CA    . ASP A 1 35  ? 17.851  -29.387 14.846  1.00 92.50  ? 138  ASP A CA    1 
ATOM   257  C  C     . ASP A 1 35  ? 17.373  -28.489 15.976  1.00 88.43  ? 138  ASP A C     1 
ATOM   258  O  O     . ASP A 1 35  ? 18.204  -27.917 16.687  1.00 97.73  ? 138  ASP A O     1 
ATOM   259  C  CB    . ASP A 1 35  ? 18.396  -28.534 13.700  1.00 92.05  ? 138  ASP A CB    1 
ATOM   260  C  CG    . ASP A 1 35  ? 19.373  -29.293 12.823  1.00 97.52  ? 138  ASP A CG    1 
ATOM   261  O  OD1   . ASP A 1 35  ? 19.564  -30.506 13.054  1.00 105.65 ? 138  ASP A OD1   1 
ATOM   262  O  OD2   . ASP A 1 35  ? 19.955  -28.676 11.907  1.00 110.20 ? 138  ASP A OD2   1 
ATOM   263  N  N     . PHE A 1 36  ? 16.059  -28.343 16.155  1.00 88.12  ? 139  PHE A N     1 
ATOM   264  C  CA    . PHE A 1 36  ? 15.566  -27.622 17.322  1.00 88.89  ? 139  PHE A CA    1 
ATOM   265  C  C     . PHE A 1 36  ? 15.627  -28.488 18.572  1.00 85.17  ? 139  PHE A C     1 
ATOM   266  O  O     . PHE A 1 36  ? 16.040  -28.014 19.635  1.00 90.40  ? 139  PHE A O     1 
ATOM   267  C  CB    . PHE A 1 36  ? 14.135  -27.134 17.090  1.00 86.59  ? 139  PHE A CB    1 
ATOM   268  C  CG    . PHE A 1 36  ? 13.562  -26.370 18.254  1.00 82.54  ? 139  PHE A CG    1 
ATOM   269  C  CD1   . PHE A 1 36  ? 13.778  -25.007 18.378  1.00 81.34  ? 139  PHE A CD1   1 
ATOM   270  C  CD2   . PHE A 1 36  ? 12.812  -27.015 19.226  1.00 84.02  ? 139  PHE A CD2   1 
ATOM   271  C  CE1   . PHE A 1 36  ? 13.255  -24.301 19.447  1.00 83.86  ? 139  PHE A CE1   1 
ATOM   272  C  CE2   . PHE A 1 36  ? 12.289  -26.315 20.298  1.00 86.36  ? 139  PHE A CE2   1 
ATOM   273  C  CZ    . PHE A 1 36  ? 12.510  -24.956 20.408  1.00 82.92  ? 139  PHE A CZ    1 
ATOM   274  N  N     . ARG A 1 37  ? 15.225  -29.756 18.462  1.00 82.95  ? 140  ARG A N     1 
ATOM   275  C  CA    . ARG A 1 37  ? 15.183  -30.632 19.627  1.00 83.24  ? 140  ARG A CA    1 
ATOM   276  C  C     . ARG A 1 37  ? 16.564  -30.877 20.222  1.00 97.03  ? 140  ARG A C     1 
ATOM   277  O  O     . ARG A 1 37  ? 16.663  -31.198 21.411  1.00 96.25  ? 140  ARG A O     1 
ATOM   278  C  CB    . ARG A 1 37  ? 14.526  -31.962 19.258  1.00 75.32  ? 140  ARG A CB    1 
ATOM   279  C  CG    . ARG A 1 37  ? 13.093  -31.826 18.765  1.00 82.97  ? 140  ARG A CG    1 
ATOM   280  C  CD    . ARG A 1 37  ? 12.548  -33.163 18.300  1.00 91.98  ? 140  ARG A CD    1 
ATOM   281  N  NE    . ARG A 1 37  ? 12.428  -34.115 19.398  1.00 94.89  ? 140  ARG A NE    1 
ATOM   282  C  CZ    . ARG A 1 37  ? 12.279  -35.423 19.242  1.00 102.72 ? 140  ARG A CZ    1 
ATOM   283  N  NH1   . ARG A 1 37  ? 12.259  -35.977 18.041  1.00 109.07 ? 140  ARG A NH1   1 
ATOM   284  N  NH2   . ARG A 1 37  ? 12.152  -36.195 20.317  1.00 105.76 ? 140  ARG A NH2   1 
ATOM   285  N  N     . ARG A 1 38  ? 17.627  -30.730 19.432  1.00 86.21  ? 141  ARG A N     1 
ATOM   286  C  CA    . ARG A 1 38  ? 18.979  -30.886 19.956  1.00 89.42  ? 141  ARG A CA    1 
ATOM   287  C  C     . ARG A 1 38  ? 19.563  -29.558 20.425  1.00 89.44  ? 141  ARG A C     1 
ATOM   288  O  O     . ARG A 1 38  ? 20.120  -29.477 21.524  1.00 82.83  ? 141  ARG A O     1 
ATOM   289  C  CB    . ARG A 1 38  ? 19.890  -31.516 18.899  1.00 92.41  ? 141  ARG A CB    1 
ATOM   290  C  CG    . ARG A 1 38  ? 19.498  -32.925 18.497  1.00 108.17 ? 141  ARG A CG    1 
ATOM   291  C  CD    . ARG A 1 38  ? 20.554  -33.551 17.599  1.00 126.81 ? 141  ARG A CD    1 
ATOM   292  N  NE    . ARG A 1 38  ? 20.138  -34.852 17.090  1.00 134.87 ? 141  ARG A NE    1 
ATOM   293  C  CZ    . ARG A 1 38  ? 19.533  -35.040 15.925  1.00 134.95 ? 141  ARG A CZ    1 
ATOM   294  N  NH1   . ARG A 1 38  ? 19.262  -34.029 15.116  1.00 123.66 ? 141  ARG A NH1   1 
ATOM   295  N  NH2   . ARG A 1 38  ? 19.192  -36.274 15.562  1.00 144.79 ? 141  ARG A NH2   1 
ATOM   296  N  N     . ASN A 1 39  ? 19.440  -28.509 19.608  1.00 87.66  ? 142  ASN A N     1 
ATOM   297  C  CA    . ASN A 1 39  ? 20.028  -27.218 19.945  1.00 92.91  ? 142  ASN A CA    1 
ATOM   298  C  C     . ASN A 1 39  ? 19.301  -26.504 21.077  1.00 88.75  ? 142  ASN A C     1 
ATOM   299  O  O     . ASN A 1 39  ? 19.816  -25.501 21.580  1.00 86.41  ? 142  ASN A O     1 
ATOM   300  C  CB    . ASN A 1 39  ? 20.064  -26.316 18.710  1.00 90.65  ? 142  ASN A CB    1 
ATOM   301  C  CG    . ASN A 1 39  ? 21.038  -26.809 17.660  1.00 88.01  ? 142  ASN A CG    1 
ATOM   302  O  OD1   . ASN A 1 39  ? 22.057  -27.419 17.982  1.00 84.48  ? 142  ASN A OD1   1 
ATOM   303  N  ND2   . ASN A 1 39  ? 20.729  -26.546 16.396  1.00 92.48  ? 142  ASN A ND2   1 
ATOM   304  N  N     . ILE A 1 40  ? 18.122  -26.983 21.484  1.00 90.89  ? 143  ILE A N     1 
ATOM   305  C  CA    . ILE A 1 40  ? 17.407  -26.379 22.605  1.00 84.41  ? 143  ILE A CA    1 
ATOM   306  C  C     . ILE A 1 40  ? 17.818  -26.981 23.940  1.00 86.59  ? 143  ILE A C     1 
ATOM   307  O  O     . ILE A 1 40  ? 17.505  -26.405 24.994  1.00 87.35  ? 143  ILE A O     1 
ATOM   308  C  CB    . ILE A 1 40  ? 15.882  -26.517 22.411  1.00 79.33  ? 143  ILE A CB    1 
ATOM   309  C  CG1   . ILE A 1 40  ? 15.126  -25.494 23.263  1.00 81.26  ? 143  ILE A CG1   1 
ATOM   310  C  CG2   . ILE A 1 40  ? 15.428  -27.932 22.743  1.00 81.08  ? 143  ILE A CG2   1 
ATOM   311  C  CD1   . ILE A 1 40  ? 15.507  -24.060 22.976  1.00 81.82  ? 143  ILE A CD1   1 
ATOM   312  N  N     . LEU A 1 41  ? 18.532  -28.107 23.933  1.00 85.68  ? 144  LEU A N     1 
ATOM   313  C  CA    . LEU A 1 41  ? 18.829  -28.819 25.169  1.00 85.58  ? 144  LEU A CA    1 
ATOM   314  C  C     . LEU A 1 41  ? 19.860  -28.106 26.036  1.00 92.63  ? 144  LEU A C     1 
ATOM   315  O  O     . LEU A 1 41  ? 19.946  -28.401 27.233  1.00 94.57  ? 144  LEU A O     1 
ATOM   316  C  CB    . LEU A 1 41  ? 19.300  -30.237 24.849  1.00 85.49  ? 144  LEU A CB    1 
ATOM   317  C  CG    . LEU A 1 41  ? 18.210  -31.158 24.298  1.00 90.27  ? 144  LEU A CG    1 
ATOM   318  C  CD1   . LEU A 1 41  ? 18.804  -32.460 23.783  1.00 100.74 ? 144  LEU A CD1   1 
ATOM   319  C  CD2   . LEU A 1 41  ? 17.157  -31.429 25.363  1.00 86.25  ? 144  LEU A CD2   1 
ATOM   320  N  N     . ASN A 1 42  ? 20.644  -27.182 25.474  1.00 87.86  ? 145  ASN A N     1 
ATOM   321  C  CA    . ASN A 1 42  ? 21.574  -26.432 26.313  1.00 87.97  ? 145  ASN A CA    1 
ATOM   322  C  C     . ASN A 1 42  ? 20.856  -25.383 27.153  1.00 90.97  ? 145  ASN A C     1 
ATOM   323  O  O     . ASN A 1 42  ? 21.353  -25.006 28.219  1.00 94.74  ? 145  ASN A O     1 
ATOM   324  C  CB    . ASN A 1 42  ? 22.669  -25.781 25.463  1.00 87.83  ? 145  ASN A CB    1 
ATOM   325  C  CG    . ASN A 1 42  ? 22.119  -24.832 24.420  1.00 89.33  ? 145  ASN A CG    1 
ATOM   326  O  OD1   . ASN A 1 42  ? 21.932  -25.210 23.265  1.00 106.17 ? 145  ASN A OD1   1 
ATOM   327  N  ND2   . ASN A 1 42  ? 21.869  -23.590 24.817  1.00 86.88  ? 145  ASN A ND2   1 
ATOM   328  N  N     . VAL A 1 43  ? 19.697  -24.902 26.695  1.00 90.39  ? 146  VAL A N     1 
ATOM   329  C  CA    . VAL A 1 43  ? 18.868  -24.044 27.538  1.00 90.30  ? 146  VAL A CA    1 
ATOM   330  C  C     . VAL A 1 43  ? 18.382  -24.817 28.755  1.00 90.48  ? 146  VAL A C     1 
ATOM   331  O  O     . VAL A 1 43  ? 18.259  -24.258 29.853  1.00 90.52  ? 146  VAL A O     1 
ATOM   332  C  CB    . VAL A 1 43  ? 17.693  -23.466 26.723  1.00 84.30  ? 146  VAL A CB    1 
ATOM   333  C  CG1   . VAL A 1 43  ? 16.792  -22.614 27.603  1.00 81.20  ? 146  VAL A CG1   1 
ATOM   334  C  CG2   . VAL A 1 43  ? 18.213  -22.650 25.555  1.00 85.19  ? 146  VAL A CG2   1 
ATOM   335  N  N     . CYS A 1 44  ? 18.111  -26.113 28.588  1.00 88.80  ? 147  CYS A N     1 
ATOM   336  C  CA    . CYS A 1 44  ? 17.743  -26.946 29.727  1.00 94.97  ? 147  CYS A CA    1 
ATOM   337  C  C     . CYS A 1 44  ? 18.929  -27.156 30.661  1.00 93.11  ? 147  CYS A C     1 
ATOM   338  O  O     . CYS A 1 44  ? 18.772  -27.135 31.887  1.00 90.97  ? 147  CYS A O     1 
ATOM   339  C  CB    . CYS A 1 44  ? 17.203  -28.290 29.240  1.00 93.09  ? 147  CYS A CB    1 
ATOM   340  S  SG    . CYS A 1 44  ? 15.827  -28.165 28.076  1.00 98.17  ? 147  CYS A SG    1 
ATOM   341  N  N     . LYS A 1 45  ? 20.123  -27.361 30.098  1.00 92.24  ? 148  LYS A N     1 
ATOM   342  C  CA    . LYS A 1 45  ? 21.310  -27.567 30.921  1.00 91.81  ? 148  LYS A CA    1 
ATOM   343  C  C     . LYS A 1 45  ? 21.631  -26.326 31.745  1.00 97.43  ? 148  LYS A C     1 
ATOM   344  O  O     . LYS A 1 45  ? 21.910  -26.418 32.946  1.00 95.93  ? 148  LYS A O     1 
ATOM   345  C  CB    . LYS A 1 45  ? 22.500  -27.946 30.040  1.00 87.63  ? 148  LYS A CB    1 
ATOM   346  C  CG    . LYS A 1 45  ? 23.825  -27.999 30.783  1.00 97.56  ? 148  LYS A CG    1 
ATOM   347  C  CD    . LYS A 1 45  ? 24.998  -27.797 29.837  1.00 104.34 ? 148  LYS A CD    1 
ATOM   348  C  CE    . LYS A 1 45  ? 26.321  -27.799 30.586  1.00 110.70 ? 148  LYS A CE    1 
ATOM   349  N  NZ    . LYS A 1 45  ? 26.329  -26.829 31.717  1.00 111.47 ? 148  LYS A NZ    1 
ATOM   350  N  N     . GLU A 1 46  ? 21.594  -25.151 31.112  1.00 92.62  ? 149  GLU A N     1 
ATOM   351  C  CA    . GLU A 1 46  ? 21.921  -23.917 31.820  1.00 93.50  ? 149  GLU A CA    1 
ATOM   352  C  C     . GLU A 1 46  ? 20.915  -23.612 32.923  1.00 89.36  ? 149  GLU A C     1 
ATOM   353  O  O     . GLU A 1 46  ? 21.286  -23.042 33.956  1.00 90.46  ? 149  GLU A O     1 
ATOM   354  C  CB    . GLU A 1 46  ? 21.997  -22.751 30.835  1.00 88.49  ? 149  GLU A CB    1 
ATOM   355  C  CG    . GLU A 1 46  ? 23.110  -22.879 29.808  1.00 98.65  ? 149  GLU A CG    1 
ATOM   356  C  CD    . GLU A 1 46  ? 23.060  -21.788 28.756  1.00 116.32 ? 149  GLU A CD    1 
ATOM   357  O  OE1   . GLU A 1 46  ? 22.358  -20.779 28.979  1.00 114.99 ? 149  GLU A OE1   1 
ATOM   358  O  OE2   . GLU A 1 46  ? 23.719  -21.942 27.706  1.00 110.00 ? 149  GLU A OE2   1 
ATOM   359  N  N     . ALA A 1 47  ? 19.648  -23.982 32.729  1.00 92.67  ? 150  ALA A N     1 
ATOM   360  C  CA    . ALA A 1 47  ? 18.632  -23.719 33.742  1.00 89.64  ? 150  ALA A CA    1 
ATOM   361  C  C     . ALA A 1 47  ? 18.756  -24.669 34.927  1.00 92.54  ? 150  ALA A C     1 
ATOM   362  O  O     . ALA A 1 47  ? 18.601  -24.251 36.079  1.00 91.82  ? 150  ALA A O     1 
ATOM   363  C  CB    . ALA A 1 47  ? 17.239  -23.817 33.123  1.00 86.08  ? 150  ALA A CB    1 
ATOM   364  N  N     . VAL A 1 48  ? 19.027  -25.950 34.663  1.00 92.27  ? 151  VAL A N     1 
ATOM   365  C  CA    . VAL A 1 48  ? 19.231  -26.907 35.747  1.00 91.93  ? 151  VAL A CA    1 
ATOM   366  C  C     . VAL A 1 48  ? 20.467  -26.535 36.558  1.00 98.55  ? 151  VAL A C     1 
ATOM   367  O  O     . VAL A 1 48  ? 20.490  -26.682 37.787  1.00 103.83 ? 151  VAL A O     1 
ATOM   368  C  CB    . VAL A 1 48  ? 19.324  -28.338 35.183  1.00 96.51  ? 151  VAL A CB    1 
ATOM   369  C  CG1   . VAL A 1 48  ? 19.745  -29.321 36.264  1.00 99.77  ? 151  VAL A CG1   1 
ATOM   370  C  CG2   . VAL A 1 48  ? 17.993  -28.753 34.576  1.00 90.32  ? 151  VAL A CG2   1 
ATOM   371  N  N     . ASP A 1 49  ? 21.508  -26.033 35.887  1.00 94.73  ? 152  ASP A N     1 
ATOM   372  C  CA    . ASP A 1 49  ? 22.713  -25.616 36.597  1.00 94.01  ? 152  ASP A CA    1 
ATOM   373  C  C     . ASP A 1 49  ? 22.438  -24.450 37.538  1.00 94.47  ? 152  ASP A C     1 
ATOM   374  O  O     . ASP A 1 49  ? 23.112  -24.311 38.565  1.00 102.09 ? 152  ASP A O     1 
ATOM   375  C  CB    . ASP A 1 49  ? 23.812  -25.246 35.600  1.00 92.17  ? 152  ASP A CB    1 
ATOM   376  C  CG    . ASP A 1 49  ? 24.444  -26.463 34.951  1.00 99.77  ? 152  ASP A CG    1 
ATOM   377  O  OD1   . ASP A 1 49  ? 24.358  -27.560 35.541  1.00 101.19 ? 152  ASP A OD1   1 
ATOM   378  O  OD2   . ASP A 1 49  ? 25.031  -26.321 33.856  1.00 97.79  ? 152  ASP A OD2   1 
ATOM   379  N  N     . LEU A 1 50  ? 21.462  -23.601 37.209  1.00 87.19  ? 153  LEU A N     1 
ATOM   380  C  CA    . LEU A 1 50  ? 21.102  -22.512 38.111  1.00 91.56  ? 153  LEU A CA    1 
ATOM   381  C  C     . LEU A 1 50  ? 20.332  -23.018 39.323  1.00 100.53 ? 153  LEU A C     1 
ATOM   382  O  O     . LEU A 1 50  ? 20.481  -22.473 40.423  1.00 97.34  ? 153  LEU A O     1 
ATOM   383  C  CB    . LEU A 1 50  ? 20.288  -21.455 37.365  1.00 86.81  ? 153  LEU A CB    1 
ATOM   384  C  CG    . LEU A 1 50  ? 21.036  -20.190 36.941  1.00 81.93  ? 153  LEU A CG    1 
ATOM   385  C  CD1   . LEU A 1 50  ? 22.232  -20.532 36.070  1.00 89.13  ? 153  LEU A CD1   1 
ATOM   386  C  CD2   . LEU A 1 50  ? 20.098  -19.234 36.221  1.00 87.24  ? 153  LEU A CD2   1 
ATOM   387  N  N     . ARG A 1 51  ? 19.509  -24.054 39.146  1.00 100.17 ? 154  ARG A N     1 
ATOM   388  C  CA    . ARG A 1 51  ? 18.787  -24.652 40.262  1.00 99.37  ? 154  ARG A CA    1 
ATOM   389  C  C     . ARG A 1 51  ? 19.684  -25.484 41.167  1.00 107.44 ? 154  ARG A C     1 
ATOM   390  O  O     . ARG A 1 51  ? 19.245  -25.876 42.253  1.00 115.35 ? 154  ARG A O     1 
ATOM   391  C  CB    . ARG A 1 51  ? 17.638  -25.515 39.737  1.00 100.12 ? 154  ARG A CB    1 
ATOM   392  C  CG    . ARG A 1 51  ? 16.447  -24.718 39.235  1.00 96.95  ? 154  ARG A CG    1 
ATOM   393  C  CD    . ARG A 1 51  ? 15.896  -25.294 37.942  1.00 90.08  ? 154  ARG A CD    1 
ATOM   394  N  NE    . ARG A 1 51  ? 15.574  -26.712 38.052  1.00 95.31  ? 154  ARG A NE    1 
ATOM   395  C  CZ    . ARG A 1 51  ? 15.045  -27.435 37.074  1.00 91.15  ? 154  ARG A CZ    1 
ATOM   396  N  NH1   . ARG A 1 51  ? 14.749  -26.900 35.901  1.00 91.93  ? 154  ARG A NH1   1 
ATOM   397  N  NH2   . ARG A 1 51  ? 14.808  -28.728 37.277  1.00 91.04  ? 154  ARG A NH2   1 
ATOM   398  N  N     . ASP A 1 52  ? 20.919  -25.764 40.750  1.00 111.57 ? 155  ASP A N     1 
ATOM   399  C  CA    . ASP A 1 52  ? 21.859  -26.523 41.559  1.00 118.68 ? 155  ASP A CA    1 
ATOM   400  C  C     . ASP A 1 52  ? 22.979  -25.670 42.136  1.00 124.48 ? 155  ASP A C     1 
ATOM   401  O  O     . ASP A 1 52  ? 23.668  -26.126 43.056  1.00 138.11 ? 155  ASP A O     1 
ATOM   402  C  CB    . ASP A 1 52  ? 22.460  -27.671 40.737  1.00 131.32 ? 155  ASP A CB    1 
ATOM   403  C  CG    . ASP A 1 52  ? 21.405  -28.641 40.239  1.00 140.49 ? 155  ASP A CG    1 
ATOM   404  O  OD1   . ASP A 1 52  ? 20.406  -28.853 40.958  1.00 142.96 ? 155  ASP A OD1   1 
ATOM   405  O  OD2   . ASP A 1 52  ? 21.572  -29.188 39.128  1.00 140.55 ? 155  ASP A OD2   1 
ATOM   406  N  N     . LEU A 1 53  ? 23.184  -24.459 41.624  1.00 115.15 ? 156  LEU A N     1 
ATOM   407  C  CA    . LEU A 1 53  ? 24.126  -23.521 42.227  1.00 120.05 ? 156  LEU A CA    1 
ATOM   408  C  C     . LEU A 1 53  ? 23.586  -23.098 43.587  1.00 124.64 ? 156  LEU A C     1 
ATOM   409  O  O     . LEU A 1 53  ? 22.563  -22.410 43.665  1.00 134.37 ? 156  LEU A O     1 
ATOM   410  C  CB    . LEU A 1 53  ? 24.329  -22.319 41.310  1.00 112.05 ? 156  LEU A CB    1 
ATOM   411  C  CG    . LEU A 1 53  ? 25.278  -21.223 41.794  1.00 129.89 ? 156  LEU A CG    1 
ATOM   412  C  CD1   . LEU A 1 53  ? 26.652  -21.796 42.105  1.00 135.08 ? 156  LEU A CD1   1 
ATOM   413  C  CD2   . LEU A 1 53  ? 25.380  -20.116 40.756  1.00 118.49 ? 156  LEU A CD2   1 
ATOM   414  N  N     . ASN A 1 54  ? 24.268  -23.512 44.658  1.00 126.71 ? 157  ASN A N     1 
ATOM   415  C  CA    . ASN A 1 54  ? 23.759  -23.412 46.028  1.00 133.17 ? 157  ASN A CA    1 
ATOM   416  C  C     . ASN A 1 54  ? 22.469  -24.229 46.164  1.00 133.70 ? 157  ASN A C     1 
ATOM   417  O  O     . ASN A 1 54  ? 21.366  -23.703 46.317  1.00 126.05 ? 157  ASN A O     1 
ATOM   418  C  CB    . ASN A 1 54  ? 23.552  -21.947 46.439  1.00 128.19 ? 157  ASN A CB    1 
ATOM   419  C  CG    . ASN A 1 54  ? 23.446  -21.766 47.941  1.00 131.26 ? 157  ASN A CG    1 
ATOM   420  O  OD1   . ASN A 1 54  ? 22.961  -22.643 48.656  1.00 136.28 ? 157  ASN A OD1   1 
ATOM   421  N  ND2   . ASN A 1 54  ? 23.903  -20.618 48.428  1.00 126.11 ? 157  ASN A ND2   1 
ATOM   422  N  N     . SER A 1 55  ? 22.662  -25.546 46.106  1.00 181.32 ? 158  SER A N     1 
ATOM   423  C  CA    . SER A 1 55  ? 21.548  -26.485 45.990  1.00 181.62 ? 158  SER A CA    1 
ATOM   424  C  C     . SER A 1 55  ? 20.449  -26.317 47.035  1.00 182.14 ? 158  SER A C     1 
ATOM   425  O  O     . SER A 1 55  ? 19.269  -26.393 46.654  1.00 186.83 ? 158  SER A O     1 
ATOM   426  C  CB    . SER A 1 55  ? 22.088  -27.923 46.018  1.00 183.23 ? 158  SER A CB    1 
ATOM   427  O  OG    . SER A 1 55  ? 22.874  -28.194 44.872  1.00 190.86 ? 158  SER A OG    1 
ATOM   428  N  N     . PRO A 1 56  ? 20.734  -26.113 48.337  1.00 137.06 ? 159  PRO A N     1 
ATOM   429  C  CA    . PRO A 1 56  ? 19.631  -25.942 49.295  1.00 124.16 ? 159  PRO A CA    1 
ATOM   430  C  C     . PRO A 1 56  ? 18.695  -24.802 48.927  1.00 116.56 ? 159  PRO A C     1 
ATOM   431  O  O     . PRO A 1 56  ? 17.489  -25.006 48.755  1.00 110.93 ? 159  PRO A O     1 
ATOM   432  C  CB    . PRO A 1 56  ? 20.357  -25.659 50.616  1.00 118.05 ? 159  PRO A CB    1 
ATOM   433  C  CG    . PRO A 1 56  ? 21.666  -26.326 50.465  1.00 131.46 ? 159  PRO A CG    1 
ATOM   434  C  CD    . PRO A 1 56  ? 22.040  -26.155 49.023  1.00 133.86 ? 159  PRO A CD    1 
ATOM   435  N  N     . HIS A 1 57  ? 19.250  -23.599 48.778  1.00 111.51 ? 160  HIS A N     1 
ATOM   436  C  CA    . HIS A 1 57  ? 18.421  -22.412 48.608  1.00 104.18 ? 160  HIS A CA    1 
ATOM   437  C  C     . HIS A 1 57  ? 17.875  -22.290 47.188  1.00 98.06  ? 160  HIS A C     1 
ATOM   438  O  O     . HIS A 1 57  ? 16.732  -21.860 47.000  1.00 87.55  ? 160  HIS A O     1 
ATOM   439  C  CB    . HIS A 1 57  ? 19.223  -21.166 48.984  1.00 93.69  ? 160  HIS A CB    1 
ATOM   440  C  CG    . HIS A 1 57  ? 18.398  -19.921 49.081  1.00 87.51  ? 160  HIS A CG    1 
ATOM   441  N  ND1   . HIS A 1 57  ? 18.653  -18.798 48.323  1.00 86.46  ? 160  HIS A ND1   1 
ATOM   442  C  CD2   . HIS A 1 57  ? 17.323  -19.622 49.848  1.00 87.65  ? 160  HIS A CD2   1 
ATOM   443  C  CE1   . HIS A 1 57  ? 17.771  -17.861 48.619  1.00 85.54  ? 160  HIS A CE1   1 
ATOM   444  N  NE2   . HIS A 1 57  ? 16.952  -18.335 49.541  1.00 88.44  ? 160  HIS A NE2   1 
ATOM   445  N  N     . SER A 1 58  ? 18.669  -22.669 46.182  1.00 109.80 ? 161  SER A N     1 
ATOM   446  C  CA    . SER A 1 58  ? 18.267  -22.445 44.794  1.00 104.11 ? 161  SER A CA    1 
ATOM   447  C  C     . SER A 1 58  ? 17.101  -23.341 44.394  1.00 98.88  ? 161  SER A C     1 
ATOM   448  O  O     . SER A 1 58  ? 16.195  -22.902 43.675  1.00 88.50  ? 161  SER A O     1 
ATOM   449  C  CB    . SER A 1 58  ? 19.451  -22.671 43.859  1.00 104.81 ? 161  SER A CB    1 
ATOM   450  O  OG    . SER A 1 58  ? 19.915  -24.006 43.948  1.00 110.84 ? 161  SER A OG    1 
ATOM   451  N  N     . ARG A 1 59  ? 17.114  -24.602 44.831  1.00 100.86 ? 162  ARG A N     1 
ATOM   452  C  CA    . ARG A 1 59  ? 15.980  -25.484 44.571  1.00 96.34  ? 162  ARG A CA    1 
ATOM   453  C  C     . ARG A 1 59  ? 14.711  -24.954 45.227  1.00 95.78  ? 162  ARG A C     1 
ATOM   454  O  O     . ARG A 1 59  ? 13.616  -25.075 44.666  1.00 93.06  ? 162  ARG A O     1 
ATOM   455  C  CB    . ARG A 1 59  ? 16.290  -26.897 45.067  1.00 107.01 ? 162  ARG A CB    1 
ATOM   456  C  CG    . ARG A 1 59  ? 17.344  -27.632 44.254  1.00 118.67 ? 162  ARG A CG    1 
ATOM   457  C  CD    . ARG A 1 59  ? 17.928  -28.793 45.044  1.00 134.80 ? 162  ARG A CD    1 
ATOM   458  N  NE    . ARG A 1 59  ? 16.893  -29.653 45.605  1.00 131.47 ? 162  ARG A NE    1 
ATOM   459  C  CZ    . ARG A 1 59  ? 17.111  -30.584 46.523  1.00 130.08 ? 162  ARG A CZ    1 
ATOM   460  N  NH1   . ARG A 1 59  ? 18.320  -30.798 47.018  1.00 127.10 ? 162  ARG A NH1   1 
ATOM   461  N  NH2   . ARG A 1 59  ? 16.091  -31.317 46.960  1.00 126.58 ? 162  ARG A NH2   1 
ATOM   462  N  N     . ALA A 1 60  ? 14.841  -24.360 46.416  1.00 98.06  ? 163  ALA A N     1 
ATOM   463  C  CA    . ALA A 1 60  ? 13.680  -23.786 47.088  1.00 92.32  ? 163  ALA A CA    1 
ATOM   464  C  C     . ALA A 1 60  ? 13.221  -22.506 46.402  1.00 82.47  ? 163  ALA A C     1 
ATOM   465  O  O     . ALA A 1 60  ? 12.016  -22.245 46.304  1.00 81.33  ? 163  ALA A O     1 
ATOM   466  C  CB    . ALA A 1 60  ? 14.002  -23.523 48.559  1.00 103.53 ? 163  ALA A CB    1 
ATOM   467  N  N     . MET A 1 61  ? 14.167  -21.692 45.927  1.00 84.47  ? 164  MET A N     1 
ATOM   468  C  CA    . MET A 1 61  ? 13.814  -20.495 45.172  1.00 96.92  ? 164  MET A CA    1 
ATOM   469  C  C     . MET A 1 61  ? 13.138  -20.826 43.848  1.00 96.94  ? 164  MET A C     1 
ATOM   470  O  O     . MET A 1 61  ? 12.441  -19.971 43.291  1.00 96.17  ? 164  MET A O     1 
ATOM   471  C  CB    . MET A 1 61  ? 15.062  -19.648 44.920  1.00 93.08  ? 164  MET A CB    1 
ATOM   472  C  CG    . MET A 1 61  ? 15.580  -18.924 46.149  1.00 87.47  ? 164  MET A CG    1 
ATOM   473  S  SD    . MET A 1 61  ? 14.661  -17.414 46.500  1.00 98.17  ? 164  MET A SD    1 
ATOM   474  C  CE    . MET A 1 61  ? 15.171  -16.384 45.125  1.00 99.25  ? 164  MET A CE    1 
ATOM   475  N  N     . TYR A 1 62  ? 13.326  -22.043 43.336  1.00 88.87  ? 165  TYR A N     1 
ATOM   476  C  CA    . TYR A 1 62  ? 12.695  -22.435 42.081  1.00 78.93  ? 165  TYR A CA    1 
ATOM   477  C  C     . TYR A 1 62  ? 11.260  -22.902 42.301  1.00 82.09  ? 165  TYR A C     1 
ATOM   478  O  O     . TYR A 1 62  ? 10.348  -22.491 41.576  1.00 83.96  ? 165  TYR A O     1 
ATOM   479  C  CB    . TYR A 1 62  ? 13.524  -23.527 41.403  1.00 85.07  ? 165  TYR A CB    1 
ATOM   480  C  CG    . TYR A 1 62  ? 12.816  -24.222 40.263  1.00 89.14  ? 165  TYR A CG    1 
ATOM   481  C  CD1   . TYR A 1 62  ? 12.471  -23.532 39.107  1.00 81.41  ? 165  TYR A CD1   1 
ATOM   482  C  CD2   . TYR A 1 62  ? 12.501  -25.573 40.339  1.00 86.07  ? 165  TYR A CD2   1 
ATOM   483  C  CE1   . TYR A 1 62  ? 11.824  -24.166 38.063  1.00 80.65  ? 165  TYR A CE1   1 
ATOM   484  C  CE2   . TYR A 1 62  ? 11.857  -26.216 39.300  1.00 92.95  ? 165  TYR A CE2   1 
ATOM   485  C  CZ    . TYR A 1 62  ? 11.522  -25.509 38.164  1.00 85.86  ? 165  TYR A CZ    1 
ATOM   486  O  OH    . TYR A 1 62  ? 10.878  -26.149 37.129  1.00 86.97  ? 165  TYR A OH    1 
ATOM   487  N  N     . VAL A 1 63  ? 11.041  -23.759 43.301  1.00 85.48  ? 166  VAL A N     1 
ATOM   488  C  CA    . VAL A 1 63  ? 9.703   -24.291 43.540  1.00 85.68  ? 166  VAL A CA    1 
ATOM   489  C  C     . VAL A 1 63  ? 8.798   -23.223 44.142  1.00 83.31  ? 166  VAL A C     1 
ATOM   490  O  O     . VAL A 1 63  ? 7.616   -23.120 43.789  1.00 85.32  ? 166  VAL A O     1 
ATOM   491  C  CB    . VAL A 1 63  ? 9.776   -25.541 44.435  1.00 81.78  ? 166  VAL A CB    1 
ATOM   492  C  CG1   . VAL A 1 63  ? 8.401   -26.173 44.578  1.00 82.09  ? 166  VAL A CG1   1 
ATOM   493  C  CG2   . VAL A 1 63  ? 10.772  -26.541 43.871  1.00 82.59  ? 166  VAL A CG2   1 
ATOM   494  N  N     . TYR A 1 64  ? 9.333   -22.411 45.057  1.00 81.50  ? 167  TYR A N     1 
ATOM   495  C  CA    . TYR A 1 64  ? 8.579   -21.360 45.739  1.00 81.04  ? 167  TYR A CA    1 
ATOM   496  C  C     . TYR A 1 64  ? 9.279   -20.029 45.492  1.00 82.29  ? 167  TYR A C     1 
ATOM   497  O  O     . TYR A 1 64  ? 9.975   -19.507 46.377  1.00 87.11  ? 167  TYR A O     1 
ATOM   498  C  CB    . TYR A 1 64  ? 8.449   -21.653 47.232  1.00 84.73  ? 167  TYR A CB    1 
ATOM   499  C  CG    . TYR A 1 64  ? 7.887   -23.025 47.530  1.00 83.64  ? 167  TYR A CG    1 
ATOM   500  C  CD1   . TYR A 1 64  ? 6.520   -23.262 47.477  1.00 82.29  ? 167  TYR A CD1   1 
ATOM   501  C  CD2   . TYR A 1 64  ? 8.725   -24.084 47.859  1.00 83.71  ? 167  TYR A CD2   1 
ATOM   502  C  CE1   . TYR A 1 64  ? 6.001   -24.515 47.743  1.00 83.73  ? 167  TYR A CE1   1 
ATOM   503  C  CE2   . TYR A 1 64  ? 8.215   -25.341 48.129  1.00 84.51  ? 167  TYR A CE2   1 
ATOM   504  C  CZ    . TYR A 1 64  ? 6.852   -25.551 48.069  1.00 85.92  ? 167  TYR A CZ    1 
ATOM   505  O  OH    . TYR A 1 64  ? 6.338   -26.799 48.336  1.00 89.23  ? 167  TYR A OH    1 
ATOM   506  N  N     . PRO A 1 65  ? 9.114   -19.447 44.302  1.00 81.86  ? 168  PRO A N     1 
ATOM   507  C  CA    . PRO A 1 65  ? 9.811   -18.200 44.000  1.00 78.50  ? 168  PRO A CA    1 
ATOM   508  C  C     . PRO A 1 65  ? 9.202   -17.040 44.759  1.00 73.87  ? 168  PRO A C     1 
ATOM   509  O  O     . PRO A 1 65  ? 7.980   -17.000 44.992  1.00 67.89  ? 168  PRO A O     1 
ATOM   510  C  CB    . PRO A 1 65  ? 9.610   -18.044 42.482  1.00 77.54  ? 168  PRO A CB    1 
ATOM   511  C  CG    . PRO A 1 65  ? 8.326   -18.750 42.217  1.00 77.09  ? 168  PRO A CG    1 
ATOM   512  C  CD    . PRO A 1 65  ? 8.282   -19.908 43.176  1.00 80.87  ? 168  PRO A CD    1 
ATOM   513  N  N     . PRO A 1 66  ? 10.013  -16.065 45.177  1.00 74.37  ? 169  PRO A N     1 
ATOM   514  C  CA    . PRO A 1 66  ? 9.477   -14.909 45.907  1.00 74.22  ? 169  PRO A CA    1 
ATOM   515  C  C     . PRO A 1 66  ? 8.480   -14.108 45.087  1.00 75.61  ? 169  PRO A C     1 
ATOM   516  O  O     . PRO A 1 66  ? 8.870   -13.315 44.225  1.00 87.85  ? 169  PRO A O     1 
ATOM   517  C  CB    . PRO A 1 66  ? 10.729  -14.080 46.223  1.00 75.05  ? 169  PRO A CB    1 
ATOM   518  C  CG    . PRO A 1 66  ? 11.855  -15.058 46.176  1.00 80.63  ? 169  PRO A CG    1 
ATOM   519  C  CD    . PRO A 1 66  ? 11.484  -16.045 45.108  1.00 81.27  ? 169  PRO A CD    1 
ATOM   520  N  N     . ASN A 1 67  ? 7.190   -14.309 45.347  1.00 80.61  ? 170  ASN A N     1 
ATOM   521  C  CA    . ASN A 1 67  ? 6.153   -13.548 44.662  1.00 84.55  ? 170  ASN A CA    1 
ATOM   522  C  C     . ASN A 1 67  ? 6.162   -12.106 45.153  1.00 80.98  ? 170  ASN A C     1 
ATOM   523  O  O     . ASN A 1 67  ? 5.418   -11.747 46.071  1.00 82.38  ? 170  ASN A O     1 
ATOM   524  C  CB    . ASN A 1 67  ? 4.782   -14.193 44.878  1.00 84.98  ? 170  ASN A CB    1 
ATOM   525  C  CG    . ASN A 1 67  ? 3.672   -13.455 44.160  1.00 92.28  ? 170  ASN A CG    1 
ATOM   526  O  OD1   . ASN A 1 67  ? 2.778   -12.890 44.790  1.00 94.95  ? 170  ASN A OD1   1 
ATOM   527  N  ND2   . ASN A 1 67  ? 3.725   -13.452 42.833  1.00 104.34 ? 170  ASN A ND2   1 
ATOM   528  N  N     . VAL A 1 68  ? 7.010   -11.275 44.549  1.00 86.15  ? 171  VAL A N     1 
ATOM   529  C  CA    . VAL A 1 68  ? 7.204   -9.898  44.974  1.00 86.18  ? 171  VAL A CA    1 
ATOM   530  C  C     . VAL A 1 68  ? 6.842   -8.969  43.820  1.00 82.80  ? 171  VAL A C     1 
ATOM   531  O  O     . VAL A 1 68  ? 6.659   -9.395  42.680  1.00 86.93  ? 171  VAL A O     1 
ATOM   532  C  CB    . VAL A 1 68  ? 8.644   -9.633  45.452  1.00 87.33  ? 171  VAL A CB    1 
ATOM   533  C  CG1   . VAL A 1 68  ? 8.980   -10.516 46.644  1.00 81.16  ? 171  VAL A CG1   1 
ATOM   534  C  CG2   . VAL A 1 68  ? 9.627   -9.869  44.318  1.00 80.00  ? 171  VAL A CG2   1 
ATOM   535  N  N     . GLU A 1 69  ? 6.737   -7.683  44.139  1.00 85.47  ? 172  GLU A N     1 
ATOM   536  C  CA    . GLU A 1 69  ? 6.502   -6.662  43.135  1.00 85.24  ? 172  GLU A CA    1 
ATOM   537  C  C     . GLU A 1 69  ? 7.840   -6.156  42.600  1.00 89.74  ? 172  GLU A C     1 
ATOM   538  O  O     . GLU A 1 69  ? 8.913   -6.601  43.011  1.00 89.19  ? 172  GLU A O     1 
ATOM   539  C  CB    . GLU A 1 69  ? 5.656   -5.529  43.711  1.00 90.61  ? 172  GLU A CB    1 
ATOM   540  C  CG    . GLU A 1 69  ? 4.257   -5.965  44.109  1.00 95.51  ? 172  GLU A CG    1 
ATOM   541  C  CD    . GLU A 1 69  ? 3.354   -4.798  44.447  1.00 106.16 ? 172  GLU A CD    1 
ATOM   542  O  OE1   . GLU A 1 69  ? 3.830   -3.645  44.392  1.00 104.70 ? 172  GLU A OE1   1 
ATOM   543  O  OE2   . GLU A 1 69  ? 2.168   -5.034  44.763  1.00 115.17 ? 172  GLU A OE2   1 
ATOM   544  N  N     . SER A 1 70  ? 7.777   -5.206  41.667  1.00 110.07 ? 173  SER A N     1 
ATOM   545  C  CA    . SER A 1 70  ? 8.982   -4.795  40.956  1.00 104.92 ? 173  SER A CA    1 
ATOM   546  C  C     . SER A 1 70  ? 9.782   -3.754  41.730  1.00 99.46  ? 173  SER A C     1 
ATOM   547  O  O     . SER A 1 70  ? 11.016  -3.819  41.761  1.00 105.91 ? 173  SER A O     1 
ATOM   548  C  CB    . SER A 1 70  ? 8.615   -4.262  39.571  1.00 101.49 ? 173  SER A CB    1 
ATOM   549  O  OG    . SER A 1 70  ? 7.986   -5.267  38.795  1.00 101.18 ? 173  SER A OG    1 
ATOM   550  N  N     . SER A 1 71  ? 9.110   -2.790  42.356  1.00 94.76  ? 174  SER A N     1 
ATOM   551  C  CA    . SER A 1 71  ? 9.811   -1.709  43.030  1.00 94.30  ? 174  SER A CA    1 
ATOM   552  C  C     . SER A 1 71  ? 9.694   -1.852  44.539  1.00 102.02 ? 174  SER A C     1 
ATOM   553  O  O     . SER A 1 71  ? 8.585   -2.049  45.054  1.00 99.40  ? 174  SER A O     1 
ATOM   554  C  CB    . SER A 1 71  ? 9.254   -0.352  42.593  1.00 92.59  ? 174  SER A CB    1 
ATOM   555  O  OG    . SER A 1 71  ? 10.062  0.704   43.080  1.00 94.88  ? 174  SER A OG    1 
ATOM   556  N  N     . PRO A 1 72  ? 10.805  -1.766  45.275  1.00 101.45 ? 175  PRO A N     1 
ATOM   557  C  CA    . PRO A 1 72  ? 10.709  -1.815  46.742  1.00 98.78  ? 175  PRO A CA    1 
ATOM   558  C  C     . PRO A 1 72  ? 9.983   -0.621  47.335  1.00 100.87 ? 175  PRO A C     1 
ATOM   559  O  O     . PRO A 1 72  ? 9.404   -0.743  48.422  1.00 102.96 ? 175  PRO A O     1 
ATOM   560  C  CB    . PRO A 1 72  ? 12.178  -1.860  47.192  1.00 91.90  ? 175  PRO A CB    1 
ATOM   561  C  CG    . PRO A 1 72  ? 12.940  -2.321  45.987  1.00 102.75 ? 175  PRO A CG    1 
ATOM   562  C  CD    . PRO A 1 72  ? 12.201  -1.768  44.810  1.00 100.15 ? 175  PRO A CD    1 
ATOM   563  N  N     . GLU A 1 73  ? 9.992   0.526   46.660  1.00 95.40  ? 176  GLU A N     1 
ATOM   564  C  CA    . GLU A 1 73  ? 9.360   1.717   47.204  1.00 101.58 ? 176  GLU A CA    1 
ATOM   565  C  C     . GLU A 1 73  ? 7.840   1.619   47.100  1.00 101.45 ? 176  GLU A C     1 
ATOM   566  O  O     . GLU A 1 73  ? 7.289   0.870   46.288  1.00 99.00  ? 176  GLU A O     1 
ATOM   567  C  CB    . GLU A 1 73  ? 9.854   2.970   46.481  1.00 112.35 ? 176  GLU A CB    1 
ATOM   568  C  CG    . GLU A 1 73  ? 9.375   3.088   45.045  1.00 113.94 ? 176  GLU A CG    1 
ATOM   569  C  CD    . GLU A 1 73  ? 9.929   4.313   44.343  1.00 127.62 ? 176  GLU A CD    1 
ATOM   570  O  OE1   . GLU A 1 73  ? 10.529  5.171   45.025  1.00 127.78 ? 176  GLU A OE1   1 
ATOM   571  O  OE2   . GLU A 1 73  ? 9.767   4.415   43.109  1.00 142.21 ? 176  GLU A OE2   1 
ATOM   572  N  N     . LEU A 1 74  ? 7.161   2.397   47.944  1.00 98.20  ? 177  LEU A N     1 
ATOM   573  C  CA    . LEU A 1 74  ? 5.710   2.402   48.006  1.00 97.48  ? 177  LEU A CA    1 
ATOM   574  C  C     . LEU A 1 74  ? 5.152   3.738   47.525  1.00 97.93  ? 177  LEU A C     1 
ATOM   575  O  O     . LEU A 1 74  ? 5.807   4.777   47.660  1.00 95.39  ? 177  LEU A O     1 
ATOM   576  C  CB    . LEU A 1 74  ? 5.209   2.149   49.434  1.00 95.86  ? 177  LEU A CB    1 
ATOM   577  C  CG    . LEU A 1 74  ? 5.808   0.996   50.239  1.00 96.24  ? 177  LEU A CG    1 
ATOM   578  C  CD1   . LEU A 1 74  ? 5.080   0.850   51.567  1.00 93.55  ? 177  LEU A CD1   1 
ATOM   579  C  CD2   . LEU A 1 74  ? 5.762   -0.301  49.458  1.00 94.59  ? 177  LEU A CD2   1 
ATOM   580  N  N     . PRO A 1 75  ? 3.949   3.744   46.954  1.00 99.12  ? 178  PRO A N     1 
ATOM   581  C  CA    . PRO A 1 75  ? 3.267   5.015   46.691  1.00 98.83  ? 178  PRO A CA    1 
ATOM   582  C  C     . PRO A 1 75  ? 2.998   5.763   47.988  1.00 102.22 ? 178  PRO A C     1 
ATOM   583  O  O     . PRO A 1 75  ? 2.961   5.185   49.076  1.00 99.45  ? 178  PRO A O     1 
ATOM   584  C  CB    . PRO A 1 75  ? 1.960   4.588   46.010  1.00 96.49  ? 178  PRO A CB    1 
ATOM   585  C  CG    . PRO A 1 75  ? 2.242   3.229   45.463  1.00 94.57  ? 178  PRO A CG    1 
ATOM   586  C  CD    . PRO A 1 75  ? 3.204   2.592   46.419  1.00 93.75  ? 178  PRO A CD    1 
ATOM   587  N  N     . LYS A 1 76  ? 2.803   7.076   47.858  1.00 104.28 ? 179  LYS A N     1 
ATOM   588  C  CA    . LYS A 1 76  ? 2.618   7.911   49.041  1.00 103.23 ? 179  LYS A CA    1 
ATOM   589  C  C     . LYS A 1 76  ? 1.309   7.589   49.754  1.00 104.97 ? 179  LYS A C     1 
ATOM   590  O  O     . LYS A 1 76  ? 1.255   7.593   50.990  1.00 109.21 ? 179  LYS A O     1 
ATOM   591  C  CB    . LYS A 1 76  ? 2.678   9.389   48.653  1.00 108.07 ? 179  LYS A CB    1 
ATOM   592  C  CG    . LYS A 1 76  ? 4.021   9.807   48.075  1.00 119.85 ? 179  LYS A CG    1 
ATOM   593  C  CD    . LYS A 1 76  ? 4.022   11.261  47.635  1.00 122.73 ? 179  LYS A CD    1 
ATOM   594  C  CE    . LYS A 1 76  ? 5.340   11.626  46.968  1.00 120.31 ? 179  LYS A CE    1 
ATOM   595  N  NZ    . LYS A 1 76  ? 5.347   13.027  46.464  1.00 116.66 ? 179  LYS A NZ    1 
ATOM   596  N  N     . HIS A 1 77  ? 0.246   7.301   49.000  1.00 103.72 ? 180  HIS A N     1 
ATOM   597  C  CA    . HIS A 1 77  ? -1.021  6.947   49.628  1.00 104.78 ? 180  HIS A CA    1 
ATOM   598  C  C     . HIS A 1 77  ? -0.987  5.554   50.243  1.00 106.43 ? 180  HIS A C     1 
ATOM   599  O  O     . HIS A 1 77  ? -1.830  5.243   51.091  1.00 109.55 ? 180  HIS A O     1 
ATOM   600  C  CB    . HIS A 1 77  ? -2.163  7.044   48.615  1.00 105.29 ? 180  HIS A CB    1 
ATOM   601  C  CG    . HIS A 1 77  ? -2.248  5.873   47.687  1.00 108.19 ? 180  HIS A CG    1 
ATOM   602  N  ND1   . HIS A 1 77  ? -1.264  5.577   46.768  1.00 107.44 ? 180  HIS A ND1   1 
ATOM   603  C  CD2   . HIS A 1 77  ? -3.202  4.924   47.536  1.00 110.85 ? 180  HIS A CD2   1 
ATOM   604  C  CE1   . HIS A 1 77  ? -1.607  4.495   46.093  1.00 103.27 ? 180  HIS A CE1   1 
ATOM   605  N  NE2   . HIS A 1 77  ? -2.780  4.080   46.538  1.00 107.74 ? 180  HIS A NE2   1 
ATOM   606  N  N     . ILE A 1 78  ? -0.039  4.710   49.832  1.00 106.36 ? 181  ILE A N     1 
ATOM   607  C  CA    . ILE A 1 78  ? 0.125   3.407   50.468  1.00 107.40 ? 181  ILE A CA    1 
ATOM   608  C  C     . ILE A 1 78  ? 0.929   3.539   51.754  1.00 106.85 ? 181  ILE A C     1 
ATOM   609  O  O     . ILE A 1 78  ? 0.612   2.903   52.766  1.00 107.10 ? 181  ILE A O     1 
ATOM   610  C  CB    . ILE A 1 78  ? 0.777   2.416   49.485  1.00 109.05 ? 181  ILE A CB    1 
ATOM   611  C  CG1   . ILE A 1 78  ? -0.189  2.080   48.347  1.00 112.95 ? 181  ILE A CG1   1 
ATOM   612  C  CG2   . ILE A 1 78  ? 1.220   1.149   50.205  1.00 99.06  ? 181  ILE A CG2   1 
ATOM   613  N  N     . TYR A 1 79  ? 1.976   4.369   51.741  1.00 103.85 ? 182  TYR A N     1 
ATOM   614  C  CA    . TYR A 1 79  ? 2.763   4.588   52.949  1.00 106.49 ? 182  TYR A CA    1 
ATOM   615  C  C     . TYR A 1 79  ? 1.942   5.270   54.035  1.00 110.16 ? 182  TYR A C     1 
ATOM   616  O  O     . TYR A 1 79  ? 2.134   4.992   55.225  1.00 111.13 ? 182  TYR A O     1 
ATOM   617  C  CB    . TYR A 1 79  ? 4.007   5.417   52.622  1.00 106.22 ? 182  TYR A CB    1 
ATOM   618  C  CG    . TYR A 1 79  ? 4.867   5.738   53.825  1.00 110.54 ? 182  TYR A CG    1 
ATOM   619  C  CD1   . TYR A 1 79  ? 5.856   4.860   54.249  1.00 110.12 ? 182  TYR A CD1   1 
ATOM   620  C  CD2   . TYR A 1 79  ? 4.693   6.921   54.534  1.00 111.83 ? 182  TYR A CD2   1 
ATOM   621  C  CE1   . TYR A 1 79  ? 6.645   5.149   55.347  1.00 116.15 ? 182  TYR A CE1   1 
ATOM   622  C  CE2   . TYR A 1 79  ? 5.475   7.217   55.634  1.00 125.64 ? 182  TYR A CE2   1 
ATOM   623  C  CZ    . TYR A 1 79  ? 6.450   6.328   56.036  1.00 125.32 ? 182  TYR A CZ    1 
ATOM   624  O  OH    . TYR A 1 79  ? 7.231   6.621   57.131  1.00 118.17 ? 182  TYR A OH    1 
ATOM   625  N  N     . ASN A 1 80  ? 1.025   6.161   53.652  1.00 109.84 ? 183  ASN A N     1 
ATOM   626  C  CA    . ASN A 1 80  ? 0.181   6.837   54.630  1.00 105.10 ? 183  ASN A CA    1 
ATOM   627  C  C     . ASN A 1 80  ? -0.817  5.900   55.296  1.00 105.14 ? 183  ASN A C     1 
ATOM   628  O  O     . ASN A 1 80  ? -1.410  6.280   56.311  1.00 118.57 ? 183  ASN A O     1 
ATOM   629  C  CB    . ASN A 1 80  ? -0.559  8.002   53.973  1.00 105.78 ? 183  ASN A CB    1 
ATOM   630  C  CG    . ASN A 1 80  ? 0.372   9.125   53.563  1.00 108.92 ? 183  ASN A CG    1 
ATOM   631  O  OD1   . ASN A 1 80  ? 1.524   9.181   53.995  1.00 107.84 ? 183  ASN A OD1   1 
ATOM   632  N  ND2   . ASN A 1 80  ? -0.125  10.033  52.731  1.00 103.43 ? 183  ASN A ND2   1 
ATOM   633  N  N     . LYS A 1 81  ? -1.019  4.701   54.756  1.00 103.94 ? 184  LYS A N     1 
ATOM   634  C  CA    . LYS A 1 81  ? -1.819  3.680   55.418  1.00 106.09 ? 184  LYS A CA    1 
ATOM   635  C  C     . LYS A 1 81  ? -1.048  2.957   56.516  1.00 111.43 ? 184  LYS A C     1 
ATOM   636  O  O     . LYS A 1 81  ? -1.552  1.971   57.064  1.00 113.05 ? 184  LYS A O     1 
ATOM   637  C  CB    . LYS A 1 81  ? -2.338  2.665   54.395  1.00 107.37 ? 184  LYS A CB    1 
ATOM   638  C  CG    . LYS A 1 81  ? -3.313  3.240   53.379  1.00 111.76 ? 184  LYS A CG    1 
ATOM   639  C  CD    . LYS A 1 81  ? -3.863  2.152   52.470  1.00 107.25 ? 184  LYS A CD    1 
ATOM   640  C  CE    . LYS A 1 81  ? -4.917  2.702   51.523  1.00 109.31 ? 184  LYS A CE    1 
ATOM   641  N  NZ    . LYS A 1 81  ? -5.523  1.628   50.688  1.00 109.48 ? 184  LYS A NZ    1 
ATOM   642  N  N     . LEU A 1 82  ? 0.154   3.422   56.841  1.00 111.28 ? 185  LEU A N     1 
ATOM   643  C  CA    . LEU A 1 82  ? 0.999   2.816   57.857  1.00 113.10 ? 185  LEU A CA    1 
ATOM   644  C  C     . LEU A 1 82  ? 1.160   3.756   59.044  1.00 123.99 ? 185  LEU A C     1 
ATOM   645  O  O     . LEU A 1 82  ? 1.070   4.980   58.907  1.00 120.92 ? 185  LEU A O     1 
ATOM   646  C  CB    . LEU A 1 82  ? 2.378   2.466   57.291  1.00 108.61 ? 185  LEU A CB    1 
ATOM   647  C  CG    . LEU A 1 82  ? 2.595   1.029   56.821  1.00 101.49 ? 185  LEU A CG    1 
ATOM   648  C  CD1   . LEU A 1 82  ? 1.470   0.590   55.909  1.00 99.40  ? 185  LEU A CD1   1 
ATOM   649  C  CD2   . LEU A 1 82  ? 3.935   0.898   56.116  1.00 98.81  ? 185  LEU A CD2   1 
ATOM   650  N  N     . ASP A 1 83  ? 1.402   3.167   60.212  1.00 132.06 ? 186  ASP A N     1 
ATOM   651  C  CA    . ASP A 1 83  ? 1.683   3.922   61.429  1.00 133.40 ? 186  ASP A CA    1 
ATOM   652  C  C     . ASP A 1 83  ? 3.192   4.106   61.518  1.00 133.64 ? 186  ASP A C     1 
ATOM   653  O  O     . ASP A 1 83  ? 3.923   3.167   61.844  1.00 141.00 ? 186  ASP A O     1 
ATOM   654  C  CB    . ASP A 1 83  ? 1.131   3.198   62.654  1.00 138.49 ? 186  ASP A CB    1 
ATOM   655  C  CG    . ASP A 1 83  ? 1.419   3.934   63.950  1.00 147.36 ? 186  ASP A CG    1 
ATOM   656  O  OD1   . ASP A 1 83  ? 1.759   5.134   63.899  1.00 163.77 ? 186  ASP A OD1   1 
ATOM   657  O  OD2   . ASP A 1 83  ? 1.308   3.307   65.024  1.00 149.96 ? 186  ASP A OD2   1 
ATOM   658  N  N     . LYS A 1 84  ? 3.658   5.322   61.221  1.00 121.92 ? 187  LYS A N     1 
ATOM   659  C  CA    . LYS A 1 84  ? 5.088   5.642   61.223  1.00 121.39 ? 187  LYS A CA    1 
ATOM   660  C  C     . LYS A 1 84  ? 5.858   4.694   60.304  1.00 120.95 ? 187  LYS A C     1 
ATOM   661  O  O     . LYS A 1 84  ? 6.990   4.298   60.590  1.00 120.11 ? 187  LYS A O     1 
ATOM   662  C  CB    . LYS A 1 84  ? 5.655   5.616   62.646  1.00 129.24 ? 187  LYS A CB    1 
ATOM   663  C  CG    . LYS A 1 84  ? 6.938   6.411   62.843  1.00 130.16 ? 187  LYS A CG    1 
ATOM   664  C  CD    . LYS A 1 84  ? 7.446   6.274   64.271  1.00 140.12 ? 187  LYS A CD    1 
ATOM   665  C  CE    . LYS A 1 84  ? 8.735   7.052   64.485  1.00 143.40 ? 187  LYS A CE    1 
ATOM   666  N  NZ    . LYS A 1 84  ? 9.235   6.919   65.883  1.00 129.36 ? 187  LYS A NZ    1 
ATOM   667  N  N     . GLY A 1 85  ? 5.231   4.321   59.191  1.00 117.14 ? 188  GLY A N     1 
ATOM   668  C  CA    . GLY A 1 85  ? 5.840   3.377   58.275  1.00 109.55 ? 188  GLY A CA    1 
ATOM   669  C  C     . GLY A 1 85  ? 6.012   1.984   58.836  1.00 105.01 ? 188  GLY A C     1 
ATOM   670  O  O     . GLY A 1 85  ? 6.985   1.303   58.495  1.00 101.16 ? 188  GLY A O     1 
ATOM   671  N  N     . GLN A 1 86  ? 5.093   1.537   59.690  1.00 107.40 ? 189  GLN A N     1 
ATOM   672  C  CA    . GLN A 1 86  ? 5.180   0.224   60.314  1.00 101.54 ? 189  GLN A CA    1 
ATOM   673  C  C     . GLN A 1 86  ? 3.867   -0.523  60.143  1.00 95.33  ? 189  GLN A C     1 
ATOM   674  O  O     . GLN A 1 86  ? 2.787   0.048   60.320  1.00 96.52  ? 189  GLN A O     1 
ATOM   675  C  CB    . GLN A 1 86  ? 5.526   0.335   61.802  1.00 103.01 ? 189  GLN A CB    1 
ATOM   676  C  CG    . GLN A 1 86  ? 6.935   0.828   62.077  1.00 104.01 ? 189  GLN A CG    1 
ATOM   677  C  CD    . GLN A 1 86  ? 7.239   0.927   63.559  1.00 100.50 ? 189  GLN A CD    1 
ATOM   678  O  OE1   . GLN A 1 86  ? 6.375   1.287   64.361  1.00 99.02  ? 189  GLN A OE1   1 
ATOM   679  N  NE2   . GLN A 1 86  ? 8.470   0.600   63.931  1.00 96.33  ? 189  GLN A NE2   1 
ATOM   680  N  N     . ILE A 1 87  ? 3.970   -1.802  59.797  1.00 92.33  ? 190  ILE A N     1 
ATOM   681  C  CA    . ILE A 1 87  ? 2.817   -2.679  59.642  1.00 94.00  ? 190  ILE A CA    1 
ATOM   682  C  C     . ILE A 1 87  ? 2.747   -3.603  60.844  1.00 93.71  ? 190  ILE A C     1 
ATOM   683  O  O     . ILE A 1 87  ? 3.762   -3.905  61.485  1.00 94.06  ? 190  ILE A O     1 
ATOM   684  C  CB    . ILE A 1 87  ? 2.891   -3.494  58.333  1.00 100.05 ? 190  ILE A CB    1 
ATOM   685  C  CG1   . ILE A 1 87  ? 4.232   -4.225  58.240  1.00 96.31  ? 190  ILE A CG1   1 
ATOM   686  C  CG2   . ILE A 1 87  ? 2.674   -2.601  57.126  1.00 90.92  ? 190  ILE A CG2   1 
ATOM   687  C  CD1   . ILE A 1 87  ? 4.381   -5.065  56.996  1.00 104.35 ? 190  ILE A CD1   1 
ATOM   688  N  N     . ILE A 1 88  ? 1.541   -4.063  61.154  1.00 92.72  ? 191  ILE A N     1 
ATOM   689  C  CA    . ILE A 1 88  ? 1.327   -5.042  62.211  1.00 99.87  ? 191  ILE A CA    1 
ATOM   690  C  C     . ILE A 1 88  ? 1.089   -6.391  61.547  1.00 95.68  ? 191  ILE A C     1 
ATOM   691  O  O     . ILE A 1 88  ? 0.095   -6.583  60.839  1.00 102.67 ? 191  ILE A O     1 
ATOM   692  C  CB    . ILE A 1 88  ? 0.164   -4.647  63.134  1.00 106.41 ? 191  ILE A CB    1 
ATOM   693  C  CG1   . ILE A 1 88  ? -1.010  -4.084  62.330  1.00 128.52 ? 191  ILE A CG1   1 
ATOM   694  C  CG2   . ILE A 1 88  ? 0.629   -3.639  64.177  1.00 100.69 ? 191  ILE A CG2   1 
ATOM   695  C  CD1   . ILE A 1 88  ? -2.168  -3.621  63.192  1.00 119.58 ? 191  ILE A CD1   1 
ATOM   696  N  N     . VAL A 1 89  ? 2.014   -7.323  61.757  1.00 84.73  ? 192  VAL A N     1 
ATOM   697  C  CA    . VAL A 1 89  ? 1.885   -8.683  61.252  1.00 84.09  ? 192  VAL A CA    1 
ATOM   698  C  C     . VAL A 1 89  ? 1.482   -9.589  62.405  1.00 89.07  ? 192  VAL A C     1 
ATOM   699  O  O     . VAL A 1 89  ? 1.803   -9.333  63.571  1.00 90.27  ? 192  VAL A O     1 
ATOM   700  C  CB    . VAL A 1 89  ? 3.189   -9.172  60.585  1.00 85.47  ? 192  VAL A CB    1 
ATOM   701  C  CG1   . VAL A 1 89  ? 3.531   -8.298  59.390  1.00 94.48  ? 192  VAL A CG1   1 
ATOM   702  C  CG2   . VAL A 1 89  ? 4.331   -9.180  61.585  1.00 84.63  ? 192  VAL A CG2   1 
ATOM   703  N  N     . VAL A 1 90  ? 0.763   -10.657 62.080  1.00 88.70  ? 193  VAL A N     1 
ATOM   704  C  CA    . VAL A 1 90  ? 0.271   -11.609 63.068  1.00 79.80  ? 193  VAL A CA    1 
ATOM   705  C  C     . VAL A 1 90  ? 0.934   -12.947 62.784  1.00 82.20  ? 193  VAL A C     1 
ATOM   706  O  O     . VAL A 1 90  ? 0.685   -13.564 61.740  1.00 85.97  ? 193  VAL A O     1 
ATOM   707  C  CB    . VAL A 1 90  ? -1.258  -11.732 63.041  1.00 82.02  ? 193  VAL A CB    1 
ATOM   708  C  CG1   . VAL A 1 90  ? -1.726  -12.736 64.081  1.00 84.11  ? 193  VAL A CG1   1 
ATOM   709  C  CG2   . VAL A 1 90  ? -1.899  -10.375 63.278  1.00 82.59  ? 193  VAL A CG2   1 
ATOM   710  N  N     . ILE A 1 91  ? 1.775   -13.397 63.705  1.00 86.55  ? 194  ILE A N     1 
ATOM   711  C  CA    . ILE A 1 91  ? 2.483   -14.662 63.561  1.00 85.74  ? 194  ILE A CA    1 
ATOM   712  C  C     . ILE A 1 91  ? 1.702   -15.748 64.287  1.00 79.20  ? 194  ILE A C     1 
ATOM   713  O  O     . ILE A 1 91  ? 1.295   -15.568 65.441  1.00 85.67  ? 194  ILE A O     1 
ATOM   714  C  CB    . ILE A 1 91  ? 3.917   -14.554 64.104  1.00 83.19  ? 194  ILE A CB    1 
ATOM   715  C  CG1   . ILE A 1 91  ? 4.727   -13.582 63.242  1.00 89.11  ? 194  ILE A CG1   1 
ATOM   716  C  CG2   . ILE A 1 91  ? 4.574   -15.921 64.153  1.00 74.43  ? 194  ILE A CG2   1 
ATOM   717  C  CD1   . ILE A 1 91  ? 6.198   -13.557 63.565  1.00 101.01 ? 194  ILE A CD1   1 
ATOM   718  N  N     . TRP A 1 92  ? 1.481   -16.870 63.609  1.00 76.62  ? 195  TRP A N     1 
ATOM   719  C  CA    . TRP A 1 92  ? 0.773   -18.007 64.176  1.00 80.68  ? 195  TRP A CA    1 
ATOM   720  C  C     . TRP A 1 92  ? 1.726   -19.180 64.364  1.00 84.97  ? 195  TRP A C     1 
ATOM   721  O  O     . TRP A 1 92  ? 2.774   -19.270 63.718  1.00 84.59  ? 195  TRP A O     1 
ATOM   722  C  CB    . TRP A 1 92  ? -0.404  -18.421 63.288  1.00 81.67  ? 195  TRP A CB    1 
ATOM   723  C  CG    . TRP A 1 92  ? -1.457  -17.364 63.155  1.00 86.77  ? 195  TRP A CG    1 
ATOM   724  C  CD1   . TRP A 1 92  ? -1.438  -16.290 62.315  1.00 87.19  ? 195  TRP A CD1   1 
ATOM   725  C  CD2   . TRP A 1 92  ? -2.689  -17.283 63.882  1.00 90.36  ? 195  TRP A CD2   1 
ATOM   726  N  NE1   . TRP A 1 92  ? -2.579  -15.542 62.476  1.00 87.66  ? 195  TRP A NE1   1 
ATOM   727  C  CE2   . TRP A 1 92  ? -3.364  -16.131 63.432  1.00 87.54  ? 195  TRP A CE2   1 
ATOM   728  C  CE3   . TRP A 1 92  ? -3.286  -18.071 64.871  1.00 87.38  ? 195  TRP A CE3   1 
ATOM   729  C  CZ2   . TRP A 1 92  ? -4.605  -15.748 63.935  1.00 86.12  ? 195  TRP A CZ2   1 
ATOM   730  C  CZ3   . TRP A 1 92  ? -4.518  -17.689 65.369  1.00 88.87  ? 195  TRP A CZ3   1 
ATOM   731  C  CH2   . TRP A 1 92  ? -5.164  -16.539 64.900  1.00 87.85  ? 195  TRP A CH2   1 
ATOM   732  N  N     . VAL A 1 93  ? 1.346   -20.084 65.262  1.00 88.68  ? 196  VAL A N     1 
ATOM   733  C  CA    . VAL A 1 93  ? 2.170   -21.240 65.599  1.00 86.98  ? 196  VAL A CA    1 
ATOM   734  C  C     . VAL A 1 93  ? 1.259   -22.363 66.075  1.00 88.81  ? 196  VAL A C     1 
ATOM   735  O  O     . VAL A 1 93  ? 0.308   -22.133 66.827  1.00 90.88  ? 196  VAL A O     1 
ATOM   736  C  CB    . VAL A 1 93  ? 3.234   -20.881 66.663  1.00 81.43  ? 196  VAL A CB    1 
ATOM   737  C  CG1   . VAL A 1 93  ? 2.593   -20.162 67.842  1.00 86.07  ? 196  VAL A CG1   1 
ATOM   738  C  CG2   . VAL A 1 93  ? 3.975   -22.127 67.130  1.00 69.56  ? 196  VAL A CG2   1 
ATOM   739  N  N     . ILE A 1 94  ? 1.546   -23.578 65.620  1.00 93.52  ? 197  ILE A N     1 
ATOM   740  C  CA    . ILE A 1 94  ? 0.820   -24.756 66.079  1.00 97.30  ? 197  ILE A CA    1 
ATOM   741  C  C     . ILE A 1 94  ? 1.424   -25.216 67.399  1.00 93.78  ? 197  ILE A C     1 
ATOM   742  O  O     . ILE A 1 94  ? 2.649   -25.327 67.532  1.00 91.25  ? 197  ILE A O     1 
ATOM   743  C  CB    . ILE A 1 94  ? 0.863   -25.868 65.019  1.00 95.12  ? 197  ILE A CB    1 
ATOM   744  C  CG1   . ILE A 1 94  ? 0.169   -25.401 63.738  1.00 87.65  ? 197  ILE A CG1   1 
ATOM   745  C  CG2   . ILE A 1 94  ? 0.207   -27.134 65.543  1.00 104.65 ? 197  ILE A CG2   1 
ATOM   746  C  CD1   . ILE A 1 94  ? 0.071   -26.467 62.670  1.00 117.28 ? 197  ILE A CD1   1 
ATOM   747  N  N     . VAL A 1 95  ? 0.566   -25.477 68.385  1.00 103.45 ? 198  VAL A N     1 
ATOM   748  C  CA    . VAL A 1 95  ? 1.018   -25.803 69.726  1.00 101.32 ? 198  VAL A CA    1 
ATOM   749  C  C     . VAL A 1 95  ? 0.718   -27.247 70.118  1.00 111.15 ? 198  VAL A C     1 
ATOM   750  O  O     . VAL A 1 95  ? 1.471   -27.827 70.909  1.00 116.85 ? 198  VAL A O     1 
ATOM   751  C  CB    . VAL A 1 95  ? 0.414   -24.823 70.753  1.00 93.59  ? 198  VAL A CB    1 
ATOM   752  C  CG1   . VAL A 1 95  ? 0.929   -23.414 70.501  1.00 90.34  ? 198  VAL A CG1   1 
ATOM   753  C  CG2   . VAL A 1 95  ? -1.106  -24.854 70.691  1.00 98.36  ? 198  VAL A CG2   1 
ATOM   754  N  N     . SER A 1 96  ? -0.347  -27.841 69.598  1.00 131.69 ? 199  SER A N     1 
ATOM   755  C  CA    . SER A 1 96  ? -0.712  -29.219 69.875  1.00 136.62 ? 199  SER A CA    1 
ATOM   756  C  C     . SER A 1 96  ? -0.759  -30.008 68.573  1.00 141.74 ? 199  SER A C     1 
ATOM   757  O  O     . SER A 1 96  ? -0.929  -29.430 67.493  1.00 134.97 ? 199  SER A O     1 
ATOM   758  C  CB    . SER A 1 96  ? -2.076  -29.294 70.577  1.00 142.07 ? 199  SER A CB    1 
ATOM   759  O  OG    . SER A 1 96  ? -3.130  -29.051 69.663  1.00 139.11 ? 199  SER A OG    1 
ATOM   760  N  N     . PRO A 1 97  ? -0.617  -31.338 68.634  1.00 135.86 ? 200  PRO A N     1 
ATOM   761  C  CA    . PRO A 1 97  ? -0.682  -32.138 67.402  1.00 133.69 ? 200  PRO A CA    1 
ATOM   762  C  C     . PRO A 1 97  ? -2.083  -32.223 66.811  1.00 131.82 ? 200  PRO A C     1 
ATOM   763  O  O     . PRO A 1 97  ? -2.333  -33.032 65.913  1.00 130.25 ? 200  PRO A O     1 
ATOM   764  C  CB    . PRO A 1 97  ? -0.180  -33.515 67.854  1.00 135.91 ? 200  PRO A CB    1 
ATOM   765  C  CG    . PRO A 1 97  ? -0.474  -33.560 69.313  1.00 137.73 ? 200  PRO A CG    1 
ATOM   766  C  CD    . PRO A 1 97  ? -0.269  -32.159 69.808  1.00 136.50 ? 200  PRO A CD    1 
ATOM   767  N  N     . ASN A 1 98  ? -3.003  -31.394 67.305  1.00 131.16 ? 201  ASN A N     1 
ATOM   768  C  CA    . ASN A 1 98  ? -4.370  -31.335 66.807  1.00 131.14 ? 201  ASN A CA    1 
ATOM   769  C  C     . ASN A 1 98  ? -4.637  -30.040 66.043  1.00 127.25 ? 201  ASN A C     1 
ATOM   770  O  O     . ASN A 1 98  ? -5.781  -29.586 65.958  1.00 125.42 ? 201  ASN A O     1 
ATOM   771  C  CB    . ASN A 1 98  ? -5.362  -31.491 67.957  1.00 133.40 ? 201  ASN A CB    1 
ATOM   772  C  CG    . ASN A 1 98  ? -5.043  -32.680 68.843  1.00 137.76 ? 201  ASN A CG    1 
ATOM   773  O  OD1   . ASN A 1 98  ? -4.459  -33.666 68.392  1.00 136.04 ? 201  ASN A OD1   1 
ATOM   774  N  ND2   . ASN A 1 98  ? -5.422  -32.591 70.112  1.00 141.05 ? 201  ASN A ND2   1 
ATOM   775  N  N     . ASN A 1 99  ? -3.582  -29.436 65.495  1.00 122.93 ? 202  ASN A N     1 
ATOM   776  C  CA    . ASN A 1 99  ? -3.654  -28.206 64.707  1.00 121.66 ? 202  ASN A CA    1 
ATOM   777  C  C     . ASN A 1 99  ? -4.207  -27.026 65.502  1.00 120.92 ? 202  ASN A C     1 
ATOM   778  O  O     . ASN A 1 99  ? -4.729  -26.072 64.916  1.00 119.27 ? 202  ASN A O     1 
ATOM   779  C  CB    . ASN A 1 99  ? -4.473  -28.407 63.426  1.00 125.12 ? 202  ASN A CB    1 
ATOM   780  C  CG    . ASN A 1 99  ? -3.811  -29.364 62.455  1.00 116.31 ? 202  ASN A CG    1 
ATOM   781  O  OD1   . ASN A 1 99  ? -2.587  -29.507 62.443  1.00 114.39 ? 202  ASN A OD1   1 
ATOM   782  N  ND2   . ASN A 1 99  ? -4.617  -30.023 61.632  1.00 113.21 ? 202  ASN A ND2   1 
ATOM   783  N  N     . ASP A 1 100 ? -4.106  -27.066 66.828  1.00 121.41 ? 203  ASP A N     1 
ATOM   784  C  CA    . ASP A 1 100 ? -4.459  -25.903 67.629  1.00 115.68 ? 203  ASP A CA    1 
ATOM   785  C  C     . ASP A 1 100 ? -3.395  -24.826 67.466  1.00 110.23 ? 203  ASP A C     1 
ATOM   786  O  O     . ASP A 1 100 ? -2.193  -25.107 67.500  1.00 109.54 ? 203  ASP A O     1 
ATOM   787  C  CB    . ASP A 1 100 ? -4.605  -26.288 69.101  1.00 132.54 ? 203  ASP A CB    1 
ATOM   788  C  CG    . ASP A 1 100 ? -5.652  -27.363 69.321  1.00 142.92 ? 203  ASP A CG    1 
ATOM   789  O  OD1   . ASP A 1 100 ? -6.227  -27.848 68.323  1.00 139.81 ? 203  ASP A OD1   1 
ATOM   790  O  OD2   . ASP A 1 100 ? -5.898  -27.724 70.492  1.00 134.49 ? 203  ASP A OD2   1 
ATOM   791  N  N     . LYS A 1 101 ? -3.839  -23.586 67.287  1.00 104.74 ? 204  LYS A N     1 
ATOM   792  C  CA    . LYS A 1 101 ? -2.956  -22.490 66.918  1.00 101.19 ? 204  LYS A CA    1 
ATOM   793  C  C     . LYS A 1 101 ? -3.069  -21.338 67.907  1.00 93.96  ? 204  LYS A C     1 
ATOM   794  O  O     . LYS A 1 101 ? -4.170  -20.969 68.327  1.00 94.52  ? 204  LYS A O     1 
ATOM   795  C  CB    . LYS A 1 101 ? -3.271  -21.995 65.501  1.00 102.48 ? 204  LYS A CB    1 
ATOM   796  C  CG    . LYS A 1 101 ? -4.731  -21.631 65.278  1.00 105.61 ? 204  LYS A CG    1 
ATOM   797  C  CD    . LYS A 1 101 ? -5.020  -21.370 63.811  1.00 104.27 ? 204  LYS A CD    1 
ATOM   798  C  CE    . LYS A 1 101 ? -4.742  -22.607 62.971  1.00 112.42 ? 204  LYS A CE    1 
ATOM   799  N  NZ    . LYS A 1 101 ? -5.501  -23.794 63.456  1.00 112.96 ? 204  LYS A NZ    1 
ATOM   800  N  N     . GLN A 1 102 ? -1.920  -20.782 68.275  1.00 96.52  ? 205  GLN A N     1 
ATOM   801  C  CA    . GLN A 1 102 ? -1.826  -19.543 69.030  1.00 96.56  ? 205  GLN A CA    1 
ATOM   802  C  C     . GLN A 1 102 ? -1.268  -18.448 68.131  1.00 96.86  ? 205  GLN A C     1 
ATOM   803  O  O     . GLN A 1 102 ? -0.758  -18.708 67.039  1.00 97.03  ? 205  GLN A O     1 
ATOM   804  C  CB    . GLN A 1 102 ? -0.941  -19.718 70.270  1.00 99.99  ? 205  GLN A CB    1 
ATOM   805  C  CG    . GLN A 1 102 ? -1.490  -20.688 71.301  1.00 102.19 ? 205  GLN A CG    1 
ATOM   806  C  CD    . GLN A 1 102 ? -0.589  -20.810 72.513  1.00 106.95 ? 205  GLN A CD    1 
ATOM   807  O  OE1   . GLN A 1 102 ? -0.879  -21.560 73.446  1.00 113.00 ? 205  GLN A OE1   1 
ATOM   808  N  NE2   . GLN A 1 102 ? 0.512   -20.068 72.506  1.00 105.71 ? 205  GLN A NE2   1 
ATOM   809  N  N     . LYS A 1 103 ? -1.365  -17.207 68.601  1.00 87.14  ? 206  LYS A N     1 
ATOM   810  C  CA    . LYS A 1 103 ? -0.921  -16.068 67.813  1.00 83.28  ? 206  LYS A CA    1 
ATOM   811  C  C     . LYS A 1 103 ? -0.264  -15.035 68.714  1.00 84.77  ? 206  LYS A C     1 
ATOM   812  O  O     . LYS A 1 103 ? -0.539  -14.963 69.915  1.00 91.54  ? 206  LYS A O     1 
ATOM   813  C  CB    . LYS A 1 103 ? -2.084  -15.419 67.047  1.00 85.76  ? 206  LYS A CB    1 
ATOM   814  C  CG    . LYS A 1 103 ? -2.992  -14.562 67.914  1.00 82.70  ? 206  LYS A CG    1 
ATOM   815  C  CD    . LYS A 1 103 ? -4.135  -13.962 67.117  1.00 82.43  ? 206  LYS A CD    1 
ATOM   816  C  CE    . LYS A 1 103 ? -5.005  -13.078 67.995  1.00 88.74  ? 206  LYS A CE    1 
ATOM   817  N  NZ    . LYS A 1 103 ? -6.162  -12.511 67.249  1.00 91.31  ? 206  LYS A NZ    1 
ATOM   818  N  N     . TYR A 1 104 ? 0.617   -14.238 68.115  1.00 87.41  ? 207  TYR A N     1 
ATOM   819  C  CA    . TYR A 1 104 ? 1.194   -13.073 68.772  1.00 86.90  ? 207  TYR A CA    1 
ATOM   820  C  C     . TYR A 1 104 ? 1.538   -12.055 67.698  1.00 89.71  ? 207  TYR A C     1 
ATOM   821  O  O     . TYR A 1 104 ? 2.145   -12.403 66.681  1.00 83.86  ? 207  TYR A O     1 
ATOM   822  C  CB    . TYR A 1 104 ? 2.429   -13.439 69.605  1.00 79.72  ? 207  TYR A CB    1 
ATOM   823  C  CG    . TYR A 1 104 ? 3.508   -14.203 68.869  1.00 74.07  ? 207  TYR A CG    1 
ATOM   824  C  CD1   . TYR A 1 104 ? 3.394   -15.571 68.652  1.00 75.17  ? 207  TYR A CD1   1 
ATOM   825  C  CD2   . TYR A 1 104 ? 4.657   -13.563 68.422  1.00 80.26  ? 207  TYR A CD2   1 
ATOM   826  C  CE1   . TYR A 1 104 ? 4.384   -16.276 67.992  1.00 82.20  ? 207  TYR A CE1   1 
ATOM   827  C  CE2   . TYR A 1 104 ? 5.654   -14.261 67.762  1.00 84.46  ? 207  TYR A CE2   1 
ATOM   828  C  CZ    . TYR A 1 104 ? 5.512   -15.617 67.550  1.00 87.07  ? 207  TYR A CZ    1 
ATOM   829  O  OH    . TYR A 1 104 ? 6.499   -16.316 66.894  1.00 89.45  ? 207  TYR A OH    1 
ATOM   830  N  N     . THR A 1 105 ? 1.138   -10.808 67.921  1.00 89.05  ? 208  THR A N     1 
ATOM   831  C  CA    . THR A 1 105 ? 1.215   -9.766  66.908  1.00 84.42  ? 208  THR A CA    1 
ATOM   832  C  C     . THR A 1 105 ? 2.489   -8.949  67.072  1.00 89.10  ? 208  THR A C     1 
ATOM   833  O  O     . THR A 1 105 ? 2.872   -8.586  68.189  1.00 86.84  ? 208  THR A O     1 
ATOM   834  C  CB    . THR A 1 105 ? -0.008  -8.850  66.986  1.00 86.22  ? 208  THR A CB    1 
ATOM   835  O  OG1   . THR A 1 105 ? -1.199  -9.645  66.950  1.00 82.72  ? 208  THR A OG1   1 
ATOM   836  C  CG2   . THR A 1 105 ? -0.027  -7.877  65.816  1.00 97.58  ? 208  THR A CG2   1 
ATOM   837  N  N     . LEU A 1 106 ? 3.141   -8.665  65.950  1.00 89.74  ? 209  LEU A N     1 
ATOM   838  C  CA    . LEU A 1 106 ? 4.341   -7.846  65.901  1.00 87.78  ? 209  LEU A CA    1 
ATOM   839  C  C     . LEU A 1 106 ? 4.036   -6.534  65.191  1.00 86.62  ? 209  LEU A C     1 
ATOM   840  O  O     . LEU A 1 106 ? 3.086   -6.432  64.413  1.00 93.78  ? 209  LEU A O     1 
ATOM   841  C  CB    . LEU A 1 106 ? 5.483   -8.572  65.179  1.00 82.13  ? 209  LEU A CB    1 
ATOM   842  C  CG    . LEU A 1 106 ? 6.200   -9.746  65.852  1.00 95.83  ? 209  LEU A CG    1 
ATOM   843  C  CD1   . LEU A 1 106 ? 5.292   -10.955 66.024  1.00 104.71 ? 209  LEU A CD1   1 
ATOM   844  C  CD2   . LEU A 1 106 ? 7.432   -10.126 65.049  1.00 109.93 ? 209  LEU A CD2   1 
ATOM   845  N  N     . LYS A 1 107 ? 4.853   -5.523  65.475  1.00 87.44  ? 210  LYS A N     1 
ATOM   846  C  CA    . LYS A 1 107 ? 4.783   -4.240  64.783  1.00 88.89  ? 210  LYS A CA    1 
ATOM   847  C  C     . LYS A 1 107 ? 6.196   -3.865  64.362  1.00 92.53  ? 210  LYS A C     1 
ATOM   848  O  O     . LYS A 1 107 ? 7.015   -3.471  65.199  1.00 96.89  ? 210  LYS A O     1 
ATOM   849  C  CB    . LYS A 1 107 ? 4.163   -3.153  65.659  1.00 93.34  ? 210  LYS A CB    1 
ATOM   850  C  CG    . LYS A 1 107 ? 4.008   -1.824  64.938  1.00 99.49  ? 210  LYS A CG    1 
ATOM   851  C  CD    . LYS A 1 107 ? 3.362   -0.775  65.821  1.00 115.91 ? 210  LYS A CD    1 
ATOM   852  C  CE    . LYS A 1 107 ? 3.206   0.541   65.077  1.00 122.97 ? 210  LYS A CE    1 
ATOM   853  N  NZ    . LYS A 1 107 ? 2.588   1.590   65.932  1.00 145.09 ? 210  LYS A NZ    1 
ATOM   854  N  N     . ILE A 1 108 ? 6.479   -3.992  63.069  1.00 102.31 ? 211  ILE A N     1 
ATOM   855  C  CA    . ILE A 1 108 ? 7.818   -3.807  62.535  1.00 98.66  ? 211  ILE A CA    1 
ATOM   856  C  C     . ILE A 1 108 ? 7.735   -2.872  61.335  1.00 94.06  ? 211  ILE A C     1 
ATOM   857  O  O     . ILE A 1 108 ? 6.672   -2.678  60.742  1.00 94.94  ? 211  ILE A O     1 
ATOM   858  C  CB    . ILE A 1 108 ? 8.462   -5.160  62.152  1.00 95.25  ? 211  ILE A CB    1 
ATOM   859  C  CG1   . ILE A 1 108 ? 9.980   -5.029  61.992  1.00 102.48 ? 211  ILE A CG1   1 
ATOM   860  C  CG2   . ILE A 1 108 ? 7.806   -5.733  60.901  1.00 87.85  ? 211  ILE A CG2   1 
ATOM   861  C  CD1   . ILE A 1 108 ? 10.713  -6.354  62.062  1.00 104.84 ? 211  ILE A CD1   1 
ATOM   862  N  N     . ASN A 1 109 ? 8.874   -2.266  61.002  1.00 97.88  ? 212  ASN A N     1 
ATOM   863  C  CA    . ASN A 1 109 ? 8.950   -1.413  59.824  1.00 100.62 ? 212  ASN A CA    1 
ATOM   864  C  C     . ASN A 1 109 ? 8.652   -2.221  58.566  1.00 98.12  ? 212  ASN A C     1 
ATOM   865  O  O     . ASN A 1 109 ? 8.910   -3.425  58.498  1.00 93.36  ? 212  ASN A O     1 
ATOM   866  C  CB    . ASN A 1 109 ? 10.333  -0.770  59.721  1.00 98.77  ? 212  ASN A CB    1 
ATOM   867  C  CG    . ASN A 1 109 ? 10.675  0.073   60.931  1.00 97.32  ? 212  ASN A CG    1 
ATOM   868  O  OD1   . ASN A 1 109 ? 11.085  -0.448  61.967  1.00 110.58 ? 212  ASN A OD1   1 
ATOM   869  N  ND2   . ASN A 1 109 ? 10.512  1.385   60.805  1.00 97.02  ? 212  ASN A ND2   1 
ATOM   870  N  N     . HIS A 1 110 ? 8.096   -1.545  57.559  1.00 102.94 ? 213  HIS A N     1 
ATOM   871  C  CA    . HIS A 1 110 ? 7.708   -2.246  56.339  1.00 99.09  ? 213  HIS A CA    1 
ATOM   872  C  C     . HIS A 1 110 ? 8.919   -2.656  55.511  1.00 100.41 ? 213  HIS A C     1 
ATOM   873  O  O     . HIS A 1 110 ? 8.880   -3.688  54.831  1.00 107.82 ? 213  HIS A O     1 
ATOM   874  C  CB    . HIS A 1 110 ? 6.766   -1.374  55.506  1.00 94.28  ? 213  HIS A CB    1 
ATOM   875  C  CG    . HIS A 1 110 ? 7.396   -0.117  54.994  1.00 98.51  ? 213  HIS A CG    1 
ATOM   876  N  ND1   . HIS A 1 110 ? 8.218   -0.092  53.888  1.00 95.55  ? 213  HIS A ND1   1 
ATOM   877  C  CD2   . HIS A 1 110 ? 7.324   1.161   55.437  1.00 103.22 ? 213  HIS A CD2   1 
ATOM   878  C  CE1   . HIS A 1 110 ? 8.626   1.146   53.672  1.00 104.94 ? 213  HIS A CE1   1 
ATOM   879  N  NE2   . HIS A 1 110 ? 8.098   1.926   54.598  1.00 103.84 ? 213  HIS A NE2   1 
ATOM   880  N  N     . ASP A 1 111 ? 9.999   -1.878  55.561  1.00 99.02  ? 214  ASP A N     1 
ATOM   881  C  CA    . ASP A 1 111 ? 11.168  -2.098  54.720  1.00 101.22 ? 214  ASP A CA    1 
ATOM   882  C  C     . ASP A 1 111 ? 12.129  -3.138  55.281  1.00 100.25 ? 214  ASP A C     1 
ATOM   883  O  O     . ASP A 1 111 ? 13.284  -3.190  54.842  1.00 104.64 ? 214  ASP A O     1 
ATOM   884  C  CB    . ASP A 1 111 ? 11.913  -0.778  54.508  1.00 108.31 ? 214  ASP A CB    1 
ATOM   885  C  CG    . ASP A 1 111 ? 12.474  -0.216  55.799  1.00 108.27 ? 214  ASP A CG    1 
ATOM   886  O  OD1   . ASP A 1 111 ? 11.808  -0.359  56.845  1.00 107.64 ? 214  ASP A OD1   1 
ATOM   887  O  OD2   . ASP A 1 111 ? 13.582  0.358   55.770  1.00 117.82 ? 214  ASP A OD2   1 
ATOM   888  N  N     . CYS A 1 112 ? 11.695  -3.968  56.222  1.00 98.89  ? 215  CYS A N     1 
ATOM   889  C  CA    . CYS A 1 112 ? 12.597  -4.884  56.901  1.00 101.84 ? 215  CYS A CA    1 
ATOM   890  C  C     . CYS A 1 112 ? 12.633  -6.242  56.210  1.00 98.49  ? 215  CYS A C     1 
ATOM   891  O  O     . CYS A 1 112 ? 11.645  -6.698  55.627  1.00 95.21  ? 215  CYS A O     1 
ATOM   892  C  CB    . CYS A 1 112 ? 12.187  -5.060  58.362  1.00 111.06 ? 215  CYS A CB    1 
ATOM   893  S  SG    . CYS A 1 112 ? 10.642  -5.957  58.576  1.00 140.94 ? 215  CYS A SG    1 
ATOM   894  N  N     . VAL A 1 113 ? 13.794  -6.884  56.288  1.00 105.19 ? 216  VAL A N     1 
ATOM   895  C  CA    . VAL A 1 113 ? 14.022  -8.225  55.757  1.00 100.67 ? 216  VAL A CA    1 
ATOM   896  C  C     . VAL A 1 113 ? 13.146  -9.206  56.529  1.00 101.19 ? 216  VAL A C     1 
ATOM   897  O  O     . VAL A 1 113 ? 12.914  -9.003  57.730  1.00 98.13  ? 216  VAL A O     1 
ATOM   898  C  CB    . VAL A 1 113 ? 15.511  -8.597  55.856  1.00 105.57 ? 216  VAL A CB    1 
ATOM   899  C  CG1   . VAL A 1 113 ? 15.807  -9.924  55.171  1.00 101.69 ? 216  VAL A CG1   1 
ATOM   900  C  CG2   . VAL A 1 113 ? 16.374  -7.486  55.275  1.00 108.87 ? 216  VAL A CG2   1 
ATOM   901  N  N     . PRO A 1 114 ? 12.620  -10.259 55.894  1.00 102.73 ? 217  PRO A N     1 
ATOM   902  C  CA    . PRO A 1 114 ? 11.904  -11.291 56.662  1.00 107.28 ? 217  PRO A CA    1 
ATOM   903  C  C     . PRO A 1 114 ? 12.718  -11.873 57.804  1.00 97.43  ? 217  PRO A C     1 
ATOM   904  O  O     . PRO A 1 114 ? 12.141  -12.275 58.824  1.00 95.14  ? 217  PRO A O     1 
ATOM   905  C  CB    . PRO A 1 114 ? 11.586  -12.351 55.600  1.00 98.10  ? 217  PRO A CB    1 
ATOM   906  C  CG    . PRO A 1 114 ? 11.485  -11.584 54.336  1.00 86.99  ? 217  PRO A CG    1 
ATOM   907  C  CD    . PRO A 1 114 ? 12.498  -10.474 54.441  1.00 92.46  ? 217  PRO A CD    1 
ATOM   908  N  N     . GLU A 1 115 ? 14.045  -11.931 57.665  1.00 104.40 ? 218  GLU A N     1 
ATOM   909  C  CA    . GLU A 1 115 ? 14.880  -12.438 58.749  1.00 105.99 ? 218  GLU A CA    1 
ATOM   910  C  C     . GLU A 1 115 ? 14.799  -11.543 59.979  1.00 100.22 ? 218  GLU A C     1 
ATOM   911  O  O     . GLU A 1 115 ? 14.914  -12.031 61.109  1.00 103.80 ? 218  GLU A O     1 
ATOM   912  C  CB    . GLU A 1 115 ? 16.328  -12.567 58.275  1.00 112.32 ? 218  GLU A CB    1 
ATOM   913  C  CG    . GLU A 1 115 ? 17.205  -13.410 59.181  1.00 103.20 ? 218  GLU A CG    1 
ATOM   914  C  CD    . GLU A 1 115 ? 18.641  -13.487 58.701  1.00 118.56 ? 218  GLU A CD    1 
ATOM   915  O  OE1   . GLU A 1 115 ? 18.958  -12.862 57.667  1.00 142.43 ? 218  GLU A OE1   1 
ATOM   916  O  OE2   . GLU A 1 115 ? 19.453  -14.174 59.357  1.00 106.71 ? 218  GLU A OE2   1 
ATOM   917  N  N     . GLN A 1 116 ? 14.599  -10.238 59.782  1.00 102.06 ? 219  GLN A N     1 
ATOM   918  C  CA    . GLN A 1 116 ? 14.432  -9.336  60.916  1.00 93.48  ? 219  GLN A CA    1 
ATOM   919  C  C     . GLN A 1 116 ? 13.066  -9.503  61.570  1.00 95.59  ? 219  GLN A C     1 
ATOM   920  O  O     . GLN A 1 116 ? 12.931  -9.289  62.780  1.00 99.68  ? 219  GLN A O     1 
ATOM   921  C  CB    . GLN A 1 116 ? 14.639  -7.889  60.471  1.00 96.05  ? 219  GLN A CB    1 
ATOM   922  C  CG    . GLN A 1 116 ? 16.073  -7.564  60.086  1.00 95.37  ? 219  GLN A CG    1 
ATOM   923  C  CD    . GLN A 1 116 ? 16.220  -6.175  59.495  1.00 99.58  ? 219  GLN A CD    1 
ATOM   924  O  OE1   . GLN A 1 116 ? 15.309  -5.665  58.841  1.00 97.59  ? 219  GLN A OE1   1 
ATOM   925  N  NE2   . GLN A 1 116 ? 17.371  -5.552  59.725  1.00 94.29  ? 219  GLN A NE2   1 
ATOM   926  N  N     . VAL A 1 117 ? 12.046  -9.876  60.793  1.00 98.23  ? 220  VAL A N     1 
ATOM   927  C  CA    . VAL A 1 117 ? 10.743  -10.185 61.378  1.00 95.55  ? 220  VAL A CA    1 
ATOM   928  C  C     . VAL A 1 117 ? 10.856  -11.384 62.308  1.00 94.68  ? 220  VAL A C     1 
ATOM   929  O  O     . VAL A 1 117 ? 10.244  -11.418 63.383  1.00 104.54 ? 220  VAL A O     1 
ATOM   930  C  CB    . VAL A 1 117 ? 9.699   -10.422 60.271  1.00 93.33  ? 220  VAL A CB    1 
ATOM   931  C  CG1   . VAL A 1 117 ? 8.377   -10.877 60.870  1.00 89.15  ? 220  VAL A CG1   1 
ATOM   932  C  CG2   . VAL A 1 117 ? 9.503   -9.163  59.451  1.00 93.95  ? 220  VAL A CG2   1 
ATOM   933  N  N     . ILE A 1 118 ? 11.645  -12.385 61.912  1.00 92.79  ? 221  ILE A N     1 
ATOM   934  C  CA    . ILE A 1 118 ? 11.878  -13.534 62.778  1.00 90.84  ? 221  ILE A CA    1 
ATOM   935  C  C     . ILE A 1 118 ? 12.643  -13.116 64.027  1.00 99.09  ? 221  ILE A C     1 
ATOM   936  O  O     . ILE A 1 118 ? 12.418  -13.663 65.114  1.00 103.36 ? 221  ILE A O     1 
ATOM   937  C  CB    . ILE A 1 118 ? 12.617  -14.638 62.002  1.00 93.50  ? 221  ILE A CB    1 
ATOM   938  C  CG1   . ILE A 1 118 ? 11.847  -14.992 60.728  1.00 97.01  ? 221  ILE A CG1   1 
ATOM   939  C  CG2   . ILE A 1 118 ? 12.807  -15.873 62.869  1.00 89.36  ? 221  ILE A CG2   1 
ATOM   940  C  CD1   . ILE A 1 118 ? 12.544  -16.012 59.857  1.00 89.92  ? 221  ILE A CD1   1 
ATOM   941  N  N     . ALA A 1 119 ? 13.547  -12.140 63.902  1.00 98.31  ? 222  ALA A N     1 
ATOM   942  C  CA    . ALA A 1 119 ? 14.271  -11.650 65.071  1.00 96.38  ? 222  ALA A CA    1 
ATOM   943  C  C     . ALA A 1 119 ? 13.325  -11.003 66.073  1.00 99.20  ? 222  ALA A C     1 
ATOM   944  O  O     . ALA A 1 119 ? 13.456  -11.209 67.285  1.00 97.95  ? 222  ALA A O     1 
ATOM   945  C  CB    . ALA A 1 119 ? 15.355  -10.662 64.642  1.00 94.81  ? 222  ALA A CB    1 
ATOM   946  N  N     . GLU A 1 120 ? 12.363  -10.216 65.586  1.00 100.12 ? 223  GLU A N     1 
ATOM   947  C  CA    . GLU A 1 120 ? 11.382  -9.613  66.481  1.00 99.66  ? 223  GLU A CA    1 
ATOM   948  C  C     . GLU A 1 120 ? 10.425  -10.656 67.043  1.00 100.79 ? 223  GLU A C     1 
ATOM   949  O  O     . GLU A 1 120 ? 9.881   -10.472 68.138  1.00 105.36 ? 223  GLU A O     1 
ATOM   950  C  CB    . GLU A 1 120 ? 10.614  -8.511  65.747  1.00 95.77  ? 223  GLU A CB    1 
ATOM   951  C  CG    . GLU A 1 120 ? 9.672   -7.701  66.626  1.00 104.83 ? 223  GLU A CG    1 
ATOM   952  C  CD    . GLU A 1 120 ? 10.400  -6.889  67.682  1.00 126.76 ? 223  GLU A CD    1 
ATOM   953  O  OE1   . GLU A 1 120 ? 11.587  -6.559  67.474  1.00 124.84 ? 223  GLU A OE1   1 
ATOM   954  O  OE2   . GLU A 1 120 ? 9.782   -6.580  68.723  1.00 123.01 ? 223  GLU A OE2   1 
ATOM   955  N  N     . ALA A 1 121 ? 10.217  -11.758 66.319  1.00 98.06  ? 224  ALA A N     1 
ATOM   956  C  CA    . ALA A 1 121 ? 9.366   -12.828 66.830  1.00 102.49 ? 224  ALA A CA    1 
ATOM   957  C  C     . ALA A 1 121 ? 10.011  -13.529 68.019  1.00 100.09 ? 224  ALA A C     1 
ATOM   958  O  O     . ALA A 1 121 ? 9.324   -13.897 68.978  1.00 94.20  ? 224  ALA A O     1 
ATOM   959  C  CB    . ALA A 1 121 ? 9.061   -13.832 65.720  1.00 92.26  ? 224  ALA A CB    1 
ATOM   960  N  N     . ILE A 1 122 ? 11.330  -13.726 67.971  1.00 99.22  ? 225  ILE A N     1 
ATOM   961  C  CA    . ILE A 1 122 ? 12.027  -14.367 69.081  1.00 100.65 ? 225  ILE A CA    1 
ATOM   962  C  C     . ILE A 1 122 ? 11.996  -13.474 70.315  1.00 100.45 ? 225  ILE A C     1 
ATOM   963  O  O     . ILE A 1 122 ? 11.859  -13.959 71.445  1.00 105.68 ? 225  ILE A O     1 
ATOM   964  C  CB    . ILE A 1 122 ? 13.466  -14.726 68.668  1.00 104.10 ? 225  ILE A CB    1 
ATOM   965  C  CG1   . ILE A 1 122 ? 13.449  -15.723 67.507  1.00 100.89 ? 225  ILE A CG1   1 
ATOM   966  C  CG2   . ILE A 1 122 ? 14.242  -15.291 69.847  1.00 105.12 ? 225  ILE A CG2   1 
ATOM   967  C  CD1   . ILE A 1 122 ? 14.826  -16.151 67.045  1.00 109.29 ? 225  ILE A CD1   1 
ATOM   968  N  N     . ARG A 1 123 ? 12.113  -12.158 70.121  1.00 101.32 ? 226  ARG A N     1 
ATOM   969  C  CA    . ARG A 1 123 ? 12.005  -11.228 71.241  1.00 99.24  ? 226  ARG A CA    1 
ATOM   970  C  C     . ARG A 1 123 ? 10.645  -11.347 71.919  1.00 100.27 ? 226  ARG A C     1 
ATOM   971  O  O     . ARG A 1 123 ? 10.553  -11.332 73.152  1.00 105.06 ? 226  ARG A O     1 
ATOM   972  C  CB    . ARG A 1 123 ? 12.244  -9.797  70.752  1.00 102.67 ? 226  ARG A CB    1 
ATOM   973  C  CG    . ARG A 1 123 ? 12.802  -8.826  71.791  1.00 100.09 ? 226  ARG A CG    1 
ATOM   974  C  CD    . ARG A 1 123 ? 11.754  -8.382  72.804  1.00 111.35 ? 226  ARG A CD    1 
ATOM   975  N  NE    . ARG A 1 123 ? 10.507  -7.978  72.167  1.00 108.06 ? 226  ARG A NE    1 
ATOM   976  C  CZ    . ARG A 1 123 ? 10.250  -6.752  71.734  1.00 113.06 ? 226  ARG A CZ    1 
ATOM   977  N  NH1   . ARG A 1 123 ? 11.137  -5.777  71.850  1.00 111.33 ? 226  ARG A NH1   1 
ATOM   978  N  NH2   . ARG A 1 123 ? 9.074   -6.497  71.167  1.00 108.28 ? 226  ARG A NH2   1 
ATOM   979  N  N     . LYS A 1 124 ? 9.578   -11.475 71.128  1.00 100.84 ? 227  LYS A N     1 
ATOM   980  C  CA    . LYS A 1 124 ? 8.238   -11.548 71.699  1.00 97.60  ? 227  LYS A CA    1 
ATOM   981  C  C     . LYS A 1 124 ? 8.003   -12.881 72.400  1.00 104.62 ? 227  LYS A C     1 
ATOM   982  O  O     . LYS A 1 124 ? 7.341   -12.932 73.443  1.00 120.50 ? 227  LYS A O     1 
ATOM   983  C  CB    . LYS A 1 124 ? 7.195   -11.325 70.604  1.00 88.37  ? 227  LYS A CB    1 
ATOM   984  C  CG    . LYS A 1 124 ? 5.803   -10.996 71.115  1.00 87.87  ? 227  LYS A CG    1 
ATOM   985  C  CD    . LYS A 1 124 ? 5.752   -9.596  71.702  1.00 98.91  ? 227  LYS A CD    1 
ATOM   986  C  CE    . LYS A 1 124 ? 4.360   -9.258  72.214  1.00 95.60  ? 227  LYS A CE    1 
ATOM   987  N  NZ    . LYS A 1 124 ? 4.307   -7.890  72.805  1.00 97.94  ? 227  LYS A NZ    1 
ATOM   988  N  N     . LYS A 1 125 ? 8.544   -13.971 71.849  1.00 98.36  ? 228  LYS A N     1 
ATOM   989  C  CA    . LYS A 1 125 ? 8.289   -15.294 72.409  1.00 100.15 ? 228  LYS A CA    1 
ATOM   990  C  C     . LYS A 1 125 ? 9.133   -15.566 73.649  1.00 105.27 ? 228  LYS A C     1 
ATOM   991  O  O     . LYS A 1 125 ? 8.660   -16.210 74.592  1.00 116.11 ? 228  LYS A O     1 
ATOM   992  C  CB    . LYS A 1 125 ? 8.541   -16.370 71.353  1.00 103.68 ? 228  LYS A CB    1 
ATOM   993  C  CG    . LYS A 1 125 ? 7.416   -16.526 70.349  1.00 107.37 ? 228  LYS A CG    1 
ATOM   994  C  CD    . LYS A 1 125 ? 6.146   -17.025 71.021  1.00 106.89 ? 228  LYS A CD    1 
ATOM   995  C  CE    . LYS A 1 125 ? 6.340   -18.416 71.603  1.00 123.23 ? 228  LYS A CE    1 
ATOM   996  N  NZ    . LYS A 1 125 ? 6.709   -19.410 70.556  1.00 103.96 ? 228  LYS A NZ    1 
ATOM   997  N  N     . THR A 1 126 ? 10.377  -15.092 73.673  1.00 104.03 ? 229  THR A N     1 
ATOM   998  C  CA    . THR A 1 126 ? 11.266  -15.350 74.806  1.00 110.14 ? 229  THR A CA    1 
ATOM   999  C  C     . THR A 1 126 ? 11.048  -14.386 75.967  1.00 108.65 ? 229  THR A C     1 
ATOM   1000 O  O     . THR A 1 126 ? 12.006  -13.991 76.637  1.00 107.43 ? 229  THR A O     1 
ATOM   1001 C  CB    . THR A 1 126 ? 12.720  -15.310 74.341  1.00 103.82 ? 229  THR A CB    1 
ATOM   1002 O  OG1   . THR A 1 126 ? 13.019  -14.016 73.806  1.00 101.24 ? 229  THR A OG1   1 
ATOM   1003 C  CG2   . THR A 1 126 ? 12.970  -16.372 73.279  1.00 104.99 ? 229  THR A CG2   1 
ATOM   1004 N  N     . ARG A 1 127 ? 9.800   -13.992 76.227  1.00 103.68 ? 230  ARG A N     1 
ATOM   1005 C  CA    . ARG A 1 127 ? 9.525   -13.154 77.388  1.00 109.88 ? 230  ARG A CA    1 
ATOM   1006 C  C     . ARG A 1 127 ? 9.430   -13.990 78.659  1.00 109.44 ? 230  ARG A C     1 
ATOM   1007 O  O     . ARG A 1 127 ? 9.911   -13.572 79.718  1.00 106.42 ? 230  ARG A O     1 
ATOM   1008 C  CB    . ARG A 1 127 ? 8.238   -12.358 77.176  1.00 109.10 ? 230  ARG A CB    1 
ATOM   1009 C  CG    . ARG A 1 127 ? 8.060   -11.220 78.165  1.00 99.72  ? 230  ARG A CG    1 
ATOM   1010 C  CD    . ARG A 1 127 ? 6.698   -10.557 78.033  1.00 104.65 ? 230  ARG A CD    1 
ATOM   1011 N  NE    . ARG A 1 127 ? 6.604   -9.366  78.868  1.00 100.57 ? 230  ARG A NE    1 
ATOM   1012 C  CZ    . ARG A 1 127 ? 5.474   -8.733  79.150  1.00 98.98  ? 230  ARG A CZ    1 
ATOM   1013 N  NH1   . ARG A 1 127 ? 4.313   -9.148  78.673  1.00 99.78  ? 230  ARG A NH1   1 
ATOM   1014 N  NH2   . ARG A 1 127 ? 5.510   -7.658  79.931  1.00 101.00 ? 230  ARG A NH2   1 
ATOM   1015 N  N     . SER A 1 128 ? 8.820   -15.169 78.569  1.00 109.00 ? 231  SER A N     1 
ATOM   1016 C  CA    . SER A 1 128 ? 8.744   -16.101 79.684  1.00 98.64  ? 231  SER A CA    1 
ATOM   1017 C  C     . SER A 1 128 ? 10.016  -16.923 79.852  1.00 114.47 ? 231  SER A C     1 
ATOM   1018 O  O     . SER A 1 128 ? 10.018  -17.884 80.629  1.00 123.73 ? 231  SER A O     1 
ATOM   1019 C  CB    . SER A 1 128 ? 7.542   -17.032 79.508  1.00 98.39  ? 231  SER A CB    1 
ATOM   1020 O  OG    . SER A 1 128 ? 7.598   -17.709 78.264  1.00 116.55 ? 231  SER A OG    1 
ATOM   1021 N  N     . MET A 1 129 ? 11.087  -16.577 79.139  1.00 129.50 ? 232  MET A N     1 
ATOM   1022 C  CA    . MET A 1 129 ? 12.364  -17.261 79.286  1.00 120.64 ? 232  MET A CA    1 
ATOM   1023 C  C     . MET A 1 129 ? 13.295  -16.564 80.268  1.00 123.89 ? 232  MET A C     1 
ATOM   1024 O  O     . MET A 1 129 ? 14.235  -17.198 80.763  1.00 125.72 ? 232  MET A O     1 
ATOM   1025 C  CB    . MET A 1 129 ? 13.058  -17.382 77.924  1.00 131.08 ? 232  MET A CB    1 
ATOM   1026 C  CG    . MET A 1 129 ? 12.239  -18.099 76.858  1.00 131.53 ? 232  MET A CG    1 
ATOM   1027 S  SD    . MET A 1 129 ? 12.214  -19.893 77.036  1.00 165.15 ? 232  MET A SD    1 
ATOM   1028 C  CE    . MET A 1 129 ? 13.929  -20.290 76.710  1.00 125.28 ? 232  MET A CE    1 
ATOM   1029 N  N     . LEU A 1 130 ? 13.054  -15.283 80.557  1.00 121.14 ? 233  LEU A N     1 
ATOM   1030 C  CA    . LEU A 1 130 ? 13.852  -14.502 81.504  1.00 119.89 ? 233  LEU A CA    1 
ATOM   1031 C  C     . LEU A 1 130 ? 15.329  -14.492 81.102  1.00 121.99 ? 233  LEU A C     1 
ATOM   1032 O  O     . LEU A 1 130 ? 16.215  -14.898 81.857  1.00 120.78 ? 233  LEU A O     1 
ATOM   1033 C  CB    . LEU A 1 130 ? 13.666  -15.017 82.936  1.00 117.70 ? 233  LEU A CB    1 
ATOM   1034 C  CG    . LEU A 1 130 ? 12.590  -14.344 83.795  1.00 115.52 ? 233  LEU A CG    1 
ATOM   1035 C  CD1   . LEU A 1 130 ? 12.992  -12.917 84.139  1.00 117.12 ? 233  LEU A CD1   1 
ATOM   1036 C  CD2   . LEU A 1 130 ? 11.231  -14.367 83.108  1.00 107.23 ? 233  LEU A CD2   1 
ATOM   1037 N  N     . LEU A 1 131 ? 15.577  -14.012 79.888  1.00 125.48 ? 234  LEU A N     1 
ATOM   1038 C  CA    . LEU A 1 131 ? 16.918  -13.918 79.332  1.00 122.12 ? 234  LEU A CA    1 
ATOM   1039 C  C     . LEU A 1 131 ? 17.445  -12.494 79.449  1.00 119.66 ? 234  LEU A C     1 
ATOM   1040 O  O     . LEU A 1 131 ? 16.686  -11.523 79.384  1.00 120.50 ? 234  LEU A O     1 
ATOM   1041 C  CB    . LEU A 1 131 ? 16.934  -14.358 77.866  1.00 123.42 ? 234  LEU A CB    1 
ATOM   1042 C  CG    . LEU A 1 131 ? 17.381  -15.790 77.561  1.00 123.19 ? 234  LEU A CG    1 
ATOM   1043 C  CD1   . LEU A 1 131 ? 16.560  -16.802 78.340  1.00 123.64 ? 234  LEU A CD1   1 
ATOM   1044 C  CD2   . LEU A 1 131 ? 17.299  -16.064 76.067  1.00 128.33 ? 234  LEU A CD2   1 
ATOM   1045 N  N     . SER A 1 132 ? 18.759  -12.378 79.622  1.00 121.30 ? 235  SER A N     1 
ATOM   1046 C  CA    . SER A 1 132 ? 19.401  -11.077 79.717  1.00 125.11 ? 235  SER A CA    1 
ATOM   1047 C  C     . SER A 1 132 ? 19.592  -10.483 78.323  1.00 131.26 ? 235  SER A C     1 
ATOM   1048 O  O     . SER A 1 132 ? 19.233  -11.081 77.305  1.00 130.97 ? 235  SER A O     1 
ATOM   1049 C  CB    . SER A 1 132 ? 20.732  -11.193 80.457  1.00 125.29 ? 235  SER A CB    1 
ATOM   1050 O  OG    . SER A 1 132 ? 21.635  -12.031 79.759  1.00 123.13 ? 235  SER A OG    1 
ATOM   1051 N  N     . SER A 1 133 ? 20.170  -9.280  78.277  1.00 135.95 ? 236  SER A N     1 
ATOM   1052 C  CA    . SER A 1 133 ? 20.391  -8.617  76.996  1.00 139.26 ? 236  SER A CA    1 
ATOM   1053 C  C     . SER A 1 133 ? 21.398  -9.380  76.144  1.00 142.21 ? 236  SER A C     1 
ATOM   1054 O  O     . SER A 1 133 ? 21.203  -9.535  74.932  1.00 137.05 ? 236  SER A O     1 
ATOM   1055 C  CB    . SER A 1 133 ? 20.856  -7.178  77.223  1.00 140.94 ? 236  SER A CB    1 
ATOM   1056 O  OG    . SER A 1 133 ? 22.038  -7.141  78.003  1.00 154.18 ? 236  SER A OG    1 
ATOM   1057 N  N     . GLU A 1 134 ? 22.480  -9.867  76.757  1.00 158.10 ? 237  GLU A N     1 
ATOM   1058 C  CA    . GLU A 1 134 ? 23.444  -10.669 76.012  1.00 154.81 ? 237  GLU A CA    1 
ATOM   1059 C  C     . GLU A 1 134 ? 22.880  -12.040 75.663  1.00 157.84 ? 237  GLU A C     1 
ATOM   1060 O  O     . GLU A 1 134 ? 23.204  -12.590 74.604  1.00 164.40 ? 237  GLU A O     1 
ATOM   1061 C  CB    . GLU A 1 134 ? 24.743  -10.819 76.807  1.00 151.49 ? 237  GLU A CB    1 
ATOM   1062 C  CG    . GLU A 1 134 ? 25.549  -9.536  76.955  1.00 166.41 ? 237  GLU A CG    1 
ATOM   1063 C  CD    . GLU A 1 134 ? 25.028  -8.636  78.059  1.00 179.92 ? 237  GLU A CD    1 
ATOM   1064 O  OE1   . GLU A 1 134 ? 24.183  -9.094  78.856  1.00 174.18 ? 237  GLU A OE1   1 
ATOM   1065 O  OE2   . GLU A 1 134 ? 25.468  -7.468  78.130  1.00 184.01 ? 237  GLU A OE2   1 
ATOM   1066 N  N     . GLN A 1 135 ? 22.040  -12.606 76.534  1.00 135.07 ? 238  GLN A N     1 
ATOM   1067 C  CA    . GLN A 1 135 ? 21.448  -13.908 76.248  1.00 130.62 ? 238  GLN A CA    1 
ATOM   1068 C  C     . GLN A 1 135 ? 20.468  -13.842 75.086  1.00 132.29 ? 238  GLN A C     1 
ATOM   1069 O  O     . GLN A 1 135 ? 20.342  -14.811 74.329  1.00 128.06 ? 238  GLN A O     1 
ATOM   1070 C  CB    . GLN A 1 135 ? 20.751  -14.456 77.491  1.00 126.09 ? 238  GLN A CB    1 
ATOM   1071 C  CG    . GLN A 1 135 ? 21.689  -15.029 78.534  1.00 124.74 ? 238  GLN A CG    1 
ATOM   1072 C  CD    . GLN A 1 135 ? 20.942  -15.649 79.696  1.00 117.00 ? 238  GLN A CD    1 
ATOM   1073 O  OE1   . GLN A 1 135 ? 19.916  -15.131 80.136  1.00 115.79 ? 238  GLN A OE1   1 
ATOM   1074 N  NE2   . GLN A 1 135 ? 21.448  -16.771 80.193  1.00 117.42 ? 238  GLN A NE2   1 
ATOM   1075 N  N     . LEU A 1 136 ? 19.763  -12.719 74.932  1.00 129.69 ? 239  LEU A N     1 
ATOM   1076 C  CA    . LEU A 1 136 ? 18.832  -12.586 73.816  1.00 123.07 ? 239  LEU A CA    1 
ATOM   1077 C  C     . LEU A 1 136 ? 19.561  -12.585 72.478  1.00 125.16 ? 239  LEU A C     1 
ATOM   1078 O  O     . LEU A 1 136 ? 19.024  -13.082 71.483  1.00 125.06 ? 239  LEU A O     1 
ATOM   1079 C  CB    . LEU A 1 136 ? 17.998  -11.315 73.973  1.00 117.19 ? 239  LEU A CB    1 
ATOM   1080 C  CG    . LEU A 1 136 ? 16.817  -11.163 73.010  1.00 111.18 ? 239  LEU A CG    1 
ATOM   1081 C  CD1   . LEU A 1 136 ? 15.867  -12.343 73.142  1.00 105.97 ? 239  LEU A CD1   1 
ATOM   1082 C  CD2   . LEU A 1 136 ? 16.083  -9.853  73.252  1.00 99.19  ? 239  LEU A CD2   1 
ATOM   1083 N  N     . LYS A 1 137 ? 20.782  -12.047 72.435  1.00 126.00 ? 240  LYS A N     1 
ATOM   1084 C  CA    . LYS A 1 137 ? 21.544  -12.052 71.191  1.00 125.15 ? 240  LYS A CA    1 
ATOM   1085 C  C     . LYS A 1 137 ? 21.970  -13.460 70.795  1.00 126.72 ? 240  LYS A C     1 
ATOM   1086 O  O     . LYS A 1 137 ? 22.080  -13.758 69.600  1.00 126.29 ? 240  LYS A O     1 
ATOM   1087 C  CB    . LYS A 1 137 ? 22.770  -11.147 71.316  1.00 121.53 ? 240  LYS A CB    1 
ATOM   1088 C  CG    . LYS A 1 137 ? 22.445  -9.676  71.510  1.00 120.56 ? 240  LYS A CG    1 
ATOM   1089 C  CD    . LYS A 1 137 ? 23.711  -8.831  71.528  1.00 125.78 ? 240  LYS A CD    1 
ATOM   1090 C  CE    . LYS A 1 137 ? 24.651  -9.264  72.643  1.00 132.81 ? 240  LYS A CE    1 
ATOM   1091 N  NZ    . LYS A 1 137 ? 25.899  -8.452  72.672  1.00 117.80 ? 240  LYS A NZ    1 
ATOM   1092 N  N     . LEU A 1 138 ? 22.210  -14.337 71.773  1.00 126.39 ? 241  LEU A N     1 
ATOM   1093 C  CA    . LEU A 1 138 ? 22.657  -15.691 71.460  1.00 129.42 ? 241  LEU A CA    1 
ATOM   1094 C  C     . LEU A 1 138 ? 21.558  -16.490 70.770  1.00 125.64 ? 241  LEU A C     1 
ATOM   1095 O  O     . LEU A 1 138 ? 21.783  -17.086 69.710  1.00 124.51 ? 241  LEU A O     1 
ATOM   1096 C  CB    . LEU A 1 138 ? 23.119  -16.402 72.732  1.00 131.88 ? 241  LEU A CB    1 
ATOM   1097 C  CG    . LEU A 1 138 ? 23.578  -17.854 72.565  1.00 130.01 ? 241  LEU A CG    1 
ATOM   1098 C  CD1   . LEU A 1 138 ? 24.864  -17.929 71.754  1.00 125.77 ? 241  LEU A CD1   1 
ATOM   1099 C  CD2   . LEU A 1 138 ? 23.752  -18.530 73.917  1.00 141.31 ? 241  LEU A CD2   1 
ATOM   1100 N  N     . CYS A 1 139 ? 20.358  -16.513 71.358  1.00 127.51 ? 242  CYS A N     1 
ATOM   1101 C  CA    . CYS A 1 139 ? 19.273  -17.306 70.790  1.00 125.81 ? 242  CYS A CA    1 
ATOM   1102 C  C     . CYS A 1 139 ? 18.827  -16.769 69.437  1.00 123.53 ? 242  CYS A C     1 
ATOM   1103 O  O     . CYS A 1 139 ? 18.388  -17.545 68.579  1.00 120.15 ? 242  CYS A O     1 
ATOM   1104 C  CB    . CYS A 1 139 ? 18.090  -17.352 71.756  1.00 119.75 ? 242  CYS A CB    1 
ATOM   1105 S  SG    . CYS A 1 139 ? 17.307  -15.752 72.054  1.00 143.63 ? 242  CYS A SG    1 
ATOM   1106 N  N     . VAL A 1 140 ? 18.924  -15.455 69.226  1.00 123.63 ? 243  VAL A N     1 
ATOM   1107 C  CA    . VAL A 1 140 ? 18.582  -14.885 67.926  1.00 124.92 ? 243  VAL A CA    1 
ATOM   1108 C  C     . VAL A 1 140 ? 19.571  -15.358 66.868  1.00 119.30 ? 243  VAL A C     1 
ATOM   1109 O  O     . VAL A 1 140 ? 19.209  -16.086 65.938  1.00 118.90 ? 243  VAL A O     1 
ATOM   1110 C  CB    . VAL A 1 140 ? 18.526  -13.349 68.005  1.00 120.57 ? 243  VAL A CB    1 
ATOM   1111 C  CG1   . VAL A 1 140 ? 18.439  -12.747 66.613  1.00 109.80 ? 243  VAL A CG1   1 
ATOM   1112 C  CG2   . VAL A 1 140 ? 17.335  -12.909 68.840  1.00 113.81 ? 243  VAL A CG2   1 
ATOM   1113 N  N     . LEU A 1 141 ? 20.845  -14.983 67.017  1.00 119.98 ? 244  LEU A N     1 
ATOM   1114 C  CA    . LEU A 1 141 ? 21.861  -15.359 66.040  1.00 116.70 ? 244  LEU A CA    1 
ATOM   1115 C  C     . LEU A 1 141 ? 21.984  -16.869 65.874  1.00 121.08 ? 244  LEU A C     1 
ATOM   1116 O  O     . LEU A 1 141 ? 22.552  -17.327 64.876  1.00 136.67 ? 244  LEU A O     1 
ATOM   1117 C  CB    . LEU A 1 141 ? 23.212  -14.765 66.439  1.00 118.20 ? 244  LEU A CB    1 
ATOM   1118 C  CG    . LEU A 1 141 ? 23.236  -13.241 66.575  1.00 117.79 ? 244  LEU A CG    1 
ATOM   1119 C  CD1   . LEU A 1 141 ? 24.622  -12.754 66.965  1.00 115.66 ? 244  LEU A CD1   1 
ATOM   1120 C  CD2   . LEU A 1 141 ? 22.770  -12.579 65.287  1.00 117.51 ? 244  LEU A CD2   1 
ATOM   1121 N  N     . GLU A 1 142 ? 21.469  -17.651 66.824  1.00 119.88 ? 245  GLU A N     1 
ATOM   1122 C  CA    . GLU A 1 142 ? 21.438  -19.099 66.665  1.00 123.00 ? 245  GLU A CA    1 
ATOM   1123 C  C     . GLU A 1 142 ? 20.232  -19.556 65.852  1.00 123.82 ? 245  GLU A C     1 
ATOM   1124 O  O     . GLU A 1 142 ? 20.314  -20.567 65.145  1.00 125.23 ? 245  GLU A O     1 
ATOM   1125 C  CB    . GLU A 1 142 ? 21.446  -19.773 68.040  1.00 125.46 ? 245  GLU A CB    1 
ATOM   1126 C  CG    . GLU A 1 142 ? 21.311  -21.288 68.016  1.00 129.27 ? 245  GLU A CG    1 
ATOM   1127 C  CD    . GLU A 1 142 ? 19.971  -21.760 68.550  1.00 134.14 ? 245  GLU A CD    1 
ATOM   1128 O  OE1   . GLU A 1 142 ? 19.147  -20.903 68.934  1.00 128.08 ? 245  GLU A OE1   1 
ATOM   1129 O  OE2   . GLU A 1 142 ? 19.743  -22.987 68.588  1.00 136.55 ? 245  GLU A OE2   1 
ATOM   1130 N  N     . TYR A 1 143 ? 19.115  -18.825 65.922  1.00 120.67 ? 246  TYR A N     1 
ATOM   1131 C  CA    . TYR A 1 143 ? 17.902  -19.197 65.207  1.00 120.84 ? 246  TYR A CA    1 
ATOM   1132 C  C     . TYR A 1 143 ? 17.509  -18.225 64.102  1.00 120.76 ? 246  TYR A C     1 
ATOM   1133 O  O     . TYR A 1 143 ? 16.794  -18.630 63.178  1.00 120.57 ? 246  TYR A O     1 
ATOM   1134 C  CB    . TYR A 1 143 ? 16.727  -19.339 66.187  1.00 129.30 ? 246  TYR A CB    1 
ATOM   1135 C  CG    . TYR A 1 143 ? 16.680  -20.678 66.892  1.00 130.47 ? 246  TYR A CG    1 
ATOM   1136 C  CD1   . TYR A 1 143 ? 17.171  -21.823 66.279  1.00 128.74 ? 246  TYR A CD1   1 
ATOM   1137 C  CD2   . TYR A 1 143 ? 16.146  -20.797 68.170  1.00 138.02 ? 246  TYR A CD2   1 
ATOM   1138 C  CE1   . TYR A 1 143 ? 17.131  -23.050 66.915  1.00 137.89 ? 246  TYR A CE1   1 
ATOM   1139 C  CE2   . TYR A 1 143 ? 16.103  -22.020 68.817  1.00 139.79 ? 246  TYR A CE2   1 
ATOM   1140 C  CZ    . TYR A 1 143 ? 16.598  -23.143 68.184  1.00 145.38 ? 246  TYR A CZ    1 
ATOM   1141 O  OH    . TYR A 1 143 ? 16.557  -24.362 68.822  1.00 155.87 ? 246  TYR A OH    1 
ATOM   1142 N  N     . GLN A 1 144 ? 17.945  -16.967 64.172  1.00 117.02 ? 247  GLN A N     1 
ATOM   1143 C  CA    . GLN A 1 144 ? 17.692  -16.008 63.101  1.00 109.53 ? 247  GLN A CA    1 
ATOM   1144 C  C     . GLN A 1 144 ? 18.456  -16.456 61.864  1.00 116.05 ? 247  GLN A C     1 
ATOM   1145 O  O     . GLN A 1 144 ? 19.678  -16.312 61.789  1.00 122.86 ? 247  GLN A O     1 
ATOM   1146 C  CB    . GLN A 1 144 ? 18.109  -14.603 63.527  1.00 105.89 ? 247  GLN A CB    1 
ATOM   1147 C  CG    . GLN A 1 144 ? 17.573  -13.493 62.654  1.00 98.48  ? 247  GLN A CG    1 
ATOM   1148 C  CD    . GLN A 1 144 ? 18.284  -12.176 62.891  1.00 103.47 ? 247  GLN A CD    1 
ATOM   1149 O  OE1   . GLN A 1 144 ? 19.339  -12.131 63.523  1.00 110.83 ? 247  GLN A OE1   1 
ATOM   1150 N  NE2   . GLN A 1 144 ? 17.707  -11.093 62.381  1.00 103.14 ? 247  GLN A NE2   1 
ATOM   1151 N  N     . GLY A 1 145 ? 17.736  -17.009 60.892  1.00 108.23 ? 248  GLY A N     1 
ATOM   1152 C  CA    . GLY A 1 145 ? 18.357  -17.615 59.726  1.00 107.11 ? 248  GLY A CA    1 
ATOM   1153 C  C     . GLY A 1 145 ? 18.150  -19.110 59.619  1.00 106.37 ? 248  GLY A C     1 
ATOM   1154 O  O     . GLY A 1 145 ? 18.678  -19.724 58.681  1.00 105.64 ? 248  GLY A O     1 
ATOM   1155 N  N     . LYS A 1 146 ? 17.417  -19.733 60.541  1.00 104.51 ? 249  LYS A N     1 
ATOM   1156 C  CA    . LYS A 1 146 ? 17.083  -21.150 60.454  1.00 102.11 ? 249  LYS A CA    1 
ATOM   1157 C  C     . LYS A 1 146 ? 15.587  -21.374 60.286  1.00 98.03  ? 249  LYS A C     1 
ATOM   1158 O  O     . LYS A 1 146 ? 15.133  -22.525 60.322  1.00 95.65  ? 249  LYS A O     1 
ATOM   1159 C  CB    . LYS A 1 146 ? 17.597  -21.898 61.688  1.00 107.69 ? 249  LYS A CB    1 
ATOM   1160 C  CG    . LYS A 1 146 ? 19.110  -21.860 61.842  1.00 108.78 ? 249  LYS A CG    1 
ATOM   1161 C  CD    . LYS A 1 146 ? 19.585  -22.797 62.938  1.00 117.08 ? 249  LYS A CD    1 
ATOM   1162 C  CE    . LYS A 1 146 ? 21.104  -22.842 63.001  1.00 121.84 ? 249  LYS A CE    1 
ATOM   1163 N  NZ    . LYS A 1 146 ? 21.591  -23.721 64.100  1.00 136.45 ? 249  LYS A NZ    1 
ATOM   1164 N  N     . TYR A 1 147 ? 14.812  -20.307 60.105  1.00 98.26  ? 250  TYR A N     1 
ATOM   1165 C  CA    . TYR A 1 147 ? 13.375  -20.393 59.898  1.00 98.25  ? 250  TYR A CA    1 
ATOM   1166 C  C     . TYR A 1 147 ? 12.977  -19.495 58.735  1.00 94.09  ? 250  TYR A C     1 
ATOM   1167 O  O     . TYR A 1 147 ? 13.734  -18.617 58.312  1.00 91.33  ? 250  TYR A O     1 
ATOM   1168 C  CB    . TYR A 1 147 ? 12.597  -20.001 61.163  1.00 96.49  ? 250  TYR A CB    1 
ATOM   1169 C  CG    . TYR A 1 147 ? 12.670  -21.033 62.265  1.00 96.69  ? 250  TYR A CG    1 
ATOM   1170 C  CD1   . TYR A 1 147 ? 13.738  -21.056 63.152  1.00 102.63 ? 250  TYR A CD1   1 
ATOM   1171 C  CD2   . TYR A 1 147 ? 11.671  -21.987 62.415  1.00 96.31  ? 250  TYR A CD2   1 
ATOM   1172 C  CE1   . TYR A 1 147 ? 13.810  -22.001 64.160  1.00 106.80 ? 250  TYR A CE1   1 
ATOM   1173 C  CE2   . TYR A 1 147 ? 11.733  -22.934 63.420  1.00 103.19 ? 250  TYR A CE2   1 
ATOM   1174 C  CZ    . TYR A 1 147 ? 12.805  -22.937 64.289  1.00 106.81 ? 250  TYR A CZ    1 
ATOM   1175 O  OH    . TYR A 1 147 ? 12.870  -23.879 65.291  1.00 108.51 ? 250  TYR A OH    1 
ATOM   1176 N  N     . ILE A 1 148 ? 11.772  -19.729 58.222  1.00 93.74  ? 251  ILE A N     1 
ATOM   1177 C  CA    . ILE A 1 148 ? 11.259  -19.030 57.049  1.00 93.82  ? 251  ILE A CA    1 
ATOM   1178 C  C     . ILE A 1 148 ? 9.818   -18.619 57.318  1.00 93.55  ? 251  ILE A C     1 
ATOM   1179 O  O     . ILE A 1 148 ? 9.051   -19.371 57.927  1.00 92.56  ? 251  ILE A O     1 
ATOM   1180 C  CB    . ILE A 1 148 ? 11.357  -19.910 55.781  1.00 89.29  ? 251  ILE A CB    1 
ATOM   1181 C  CG1   . ILE A 1 148 ? 12.815  -20.076 55.353  1.00 89.56  ? 251  ILE A CG1   1 
ATOM   1182 C  CG2   . ILE A 1 148 ? 10.539  -19.327 54.639  1.00 89.93  ? 251  ILE A CG2   1 
ATOM   1183 C  CD1   . ILE A 1 148 ? 13.498  -18.772 55.001  1.00 97.92  ? 251  ILE A CD1   1 
ATOM   1184 N  N     . LEU A 1 149 ? 9.456   -17.416 56.874  1.00 90.25  ? 252  LEU A N     1 
ATOM   1185 C  CA    . LEU A 1 149 ? 8.076   -16.959 56.952  1.00 86.67  ? 252  LEU A CA    1 
ATOM   1186 C  C     . LEU A 1 149 ? 7.241   -17.591 55.844  1.00 91.77  ? 252  LEU A C     1 
ATOM   1187 O  O     . LEU A 1 149 ? 7.690   -17.715 54.700  1.00 81.69  ? 252  LEU A O     1 
ATOM   1188 C  CB    . LEU A 1 149 ? 8.011   -15.434 56.847  1.00 83.63  ? 252  LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1 149 ? 8.703   -14.623 57.943  1.00 90.19  ? 252  LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1 149 ? 8.586   -13.132 57.661  1.00 89.30  ? 252  LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1 149 ? 8.119   -14.959 59.306  1.00 85.51  ? 252  LEU A CD2   1 
ATOM   1192 N  N     . LYS A 1 150 ? 6.018   -17.987 56.190  1.00 90.53  ? 253  LYS A N     1 
ATOM   1193 C  CA    . LYS A 1 150 ? 5.087   -18.575 55.238  1.00 81.98  ? 253  LYS A CA    1 
ATOM   1194 C  C     . LYS A 1 150 ? 3.710   -17.962 55.439  1.00 83.03  ? 253  LYS A C     1 
ATOM   1195 O  O     . LYS A 1 150 ? 3.257   -17.799 56.575  1.00 85.35  ? 253  LYS A O     1 
ATOM   1196 C  CB    . LYS A 1 150 ? 5.009   -20.099 55.399  1.00 81.52  ? 253  LYS A CB    1 
ATOM   1197 C  CG    . LYS A 1 150 ? 3.850   -20.752 54.659  1.00 81.91  ? 253  LYS A CG    1 
ATOM   1198 C  CD    . LYS A 1 150 ? 3.722   -22.219 55.034  1.00 81.46  ? 253  LYS A CD    1 
ATOM   1199 C  CE    . LYS A 1 150 ? 2.265   -22.639 55.156  1.00 84.18  ? 253  LYS A CE    1 
ATOM   1200 N  NZ    . LYS A 1 150 ? 1.722   -23.222 53.903  1.00 88.18  ? 253  LYS A NZ    1 
ATOM   1201 N  N     . VAL A 1 151 ? 3.054   -17.613 54.330  1.00 85.69  ? 254  VAL A N     1 
ATOM   1202 C  CA    . VAL A 1 151 ? 1.688   -17.113 54.407  1.00 84.09  ? 254  VAL A CA    1 
ATOM   1203 C  C     . VAL A 1 151 ? 0.780   -18.217 54.928  1.00 84.26  ? 254  VAL A C     1 
ATOM   1204 O  O     . VAL A 1 151 ? 0.873   -19.377 54.507  1.00 85.34  ? 254  VAL A O     1 
ATOM   1205 C  CB    . VAL A 1 151 ? 1.219   -16.607 53.032  1.00 88.75  ? 254  VAL A CB    1 
ATOM   1206 C  CG1   . VAL A 1 151 ? -0.173  -15.997 53.132  1.00 86.35  ? 254  VAL A CG1   1 
ATOM   1207 C  CG2   . VAL A 1 151 ? 2.208   -15.601 52.470  1.00 85.93  ? 254  VAL A CG2   1 
ATOM   1208 N  N     . CYS A 1 152 ? -0.097  -17.861 55.863  1.00 87.13  ? 255  CYS A N     1 
ATOM   1209 C  CA    . CYS A 1 152 ? -1.021  -18.824 56.448  1.00 94.80  ? 255  CYS A CA    1 
ATOM   1210 C  C     . CYS A 1 152 ? -2.180  -19.065 55.490  1.00 94.42  ? 255  CYS A C     1 
ATOM   1211 O  O     . CYS A 1 152 ? -2.963  -18.150 55.211  1.00 93.12  ? 255  CYS A O     1 
ATOM   1212 C  CB    . CYS A 1 152 ? -1.533  -18.324 57.798  1.00 98.89  ? 255  CYS A CB    1 
ATOM   1213 S  SG    . CYS A 1 152 ? -0.261  -18.160 59.074  1.00 92.05  ? 255  CYS A SG    1 
ATOM   1214 N  N     . GLY A 1 153 ? -2.290  -20.291 54.984  1.00 91.85  ? 256  GLY A N     1 
ATOM   1215 C  CA    . GLY A 1 153 ? -3.386  -20.641 54.103  1.00 94.87  ? 256  GLY A CA    1 
ATOM   1216 C  C     . GLY A 1 153 ? -2.957  -21.232 52.776  1.00 98.78  ? 256  GLY A C     1 
ATOM   1217 O  O     . GLY A 1 153 ? -3.564  -22.196 52.299  1.00 96.08  ? 256  GLY A O     1 
ATOM   1218 N  N     . CYS A 1 154 ? -1.919  -20.668 52.169  1.00 91.34  ? 257  CYS A N     1 
ATOM   1219 C  CA    . CYS A 1 154 ? -1.428  -21.109 50.870  1.00 99.30  ? 257  CYS A CA    1 
ATOM   1220 C  C     . CYS A 1 154 ? 0.038   -21.529 50.989  1.00 99.59  ? 257  CYS A C     1 
ATOM   1221 O  O     . CYS A 1 154 ? 0.608   -21.575 52.082  1.00 92.33  ? 257  CYS A O     1 
ATOM   1222 C  CB    . CYS A 1 154 ? -1.616  -20.007 49.825  1.00 88.79  ? 257  CYS A CB    1 
ATOM   1223 S  SG    . CYS A 1 154 ? -0.747  -18.469 50.205  1.00 89.21  ? 257  CYS A SG    1 
ATOM   1224 N  N     . ASP A 1 155 ? 0.648   -21.834 49.844  1.00 99.77  ? 258  ASP A N     1 
ATOM   1225 C  CA    . ASP A 1 155 ? 2.037   -22.286 49.779  1.00 92.39  ? 258  ASP A CA    1 
ATOM   1226 C  C     . ASP A 1 155 ? 2.982   -21.175 49.342  1.00 91.80  ? 258  ASP A C     1 
ATOM   1227 O  O     . ASP A 1 155 ? 3.913   -21.413 48.567  1.00 94.66  ? 258  ASP A O     1 
ATOM   1228 C  CB    . ASP A 1 155 ? 2.159   -23.486 48.846  1.00 90.33  ? 258  ASP A CB    1 
ATOM   1229 C  CG    . ASP A 1 155 ? 1.463   -24.717 49.387  1.00 110.13 ? 258  ASP A CG    1 
ATOM   1230 O  OD1   . ASP A 1 155 ? 0.859   -24.629 50.477  1.00 109.61 ? 258  ASP A OD1   1 
ATOM   1231 O  OD2   . ASP A 1 155 ? 1.521   -25.773 48.722  1.00 110.79 ? 258  ASP A OD2   1 
ATOM   1232 N  N     . GLU A 1 156 ? 2.769   -19.954 49.819  1.00 86.36  ? 259  GLU A N     1 
ATOM   1233 C  CA    . GLU A 1 156 ? 3.642   -18.831 49.509  1.00 85.26  ? 259  GLU A CA    1 
ATOM   1234 C  C     . GLU A 1 156 ? 4.644   -18.637 50.640  1.00 78.91  ? 259  GLU A C     1 
ATOM   1235 O  O     . GLU A 1 156 ? 4.285   -18.701 51.818  1.00 83.31  ? 259  GLU A O     1 
ATOM   1236 C  CB    . GLU A 1 156 ? 2.830   -17.553 49.290  1.00 83.80  ? 259  GLU A CB    1 
ATOM   1237 C  CG    . GLU A 1 156 ? 3.662   -16.350 48.877  1.00 85.88  ? 259  GLU A CG    1 
ATOM   1238 C  CD    . GLU A 1 156 ? 2.811   -15.170 48.446  1.00 103.44 ? 259  GLU A CD    1 
ATOM   1239 O  OE1   . GLU A 1 156 ? 1.601   -15.366 48.205  1.00 112.35 ? 259  GLU A OE1   1 
ATOM   1240 O  OE2   . GLU A 1 156 ? 3.352   -14.047 48.349  1.00 101.75 ? 259  GLU A OE2   1 
ATOM   1241 N  N     . TYR A 1 157 ? 5.903   -18.403 50.274  1.00 75.48  ? 260  TYR A N     1 
ATOM   1242 C  CA    . TYR A 1 157 ? 6.992   -18.301 51.233  1.00 72.12  ? 260  TYR A CA    1 
ATOM   1243 C  C     . TYR A 1 157 ? 7.751   -16.997 51.029  1.00 73.85  ? 260  TYR A C     1 
ATOM   1244 O  O     . TYR A 1 157 ? 7.556   -16.279 50.045  1.00 83.36  ? 260  TYR A O     1 
ATOM   1245 C  CB    . TYR A 1 157 ? 7.950   -19.495 51.116  1.00 75.90  ? 260  TYR A CB    1 
ATOM   1246 C  CG    . TYR A 1 157 ? 7.337   -20.816 51.521  1.00 85.42  ? 260  TYR A CG    1 
ATOM   1247 C  CD1   . TYR A 1 157 ? 6.498   -21.509 50.656  1.00 87.62  ? 260  TYR A CD1   1 
ATOM   1248 C  CD2   . TYR A 1 157 ? 7.601   -21.375 52.765  1.00 83.37  ? 260  TYR A CD2   1 
ATOM   1249 C  CE1   . TYR A 1 157 ? 5.936   -22.718 51.021  1.00 90.46  ? 260  TYR A CE1   1 
ATOM   1250 C  CE2   . TYR A 1 157 ? 7.044   -22.585 53.139  1.00 87.73  ? 260  TYR A CE2   1 
ATOM   1251 C  CZ    . TYR A 1 157 ? 6.213   -23.251 52.262  1.00 95.95  ? 260  TYR A CZ    1 
ATOM   1252 O  OH    . TYR A 1 157 ? 5.655   -24.455 52.626  1.00 103.92 ? 260  TYR A OH    1 
ATOM   1253 N  N     . PHE A 1 158 ? 8.629   -16.699 51.985  1.00 77.98  ? 261  PHE A N     1 
ATOM   1254 C  CA    . PHE A 1 158 ? 9.475   -15.505 51.986  1.00 73.39  ? 261  PHE A CA    1 
ATOM   1255 C  C     . PHE A 1 158 ? 10.923  -15.983 52.065  1.00 79.81  ? 261  PHE A C     1 
ATOM   1256 O  O     . PHE A 1 158 ? 11.535  -15.975 53.135  1.00 91.80  ? 261  PHE A O     1 
ATOM   1257 C  CB    . PHE A 1 158 ? 9.125   -14.561 53.168  1.00 75.28  ? 261  PHE A CB    1 
ATOM   1258 C  CG    . PHE A 1 158 ? 7.738   -13.977 53.105  1.00 77.33  ? 261  PHE A CG    1 
ATOM   1259 C  CD1   . PHE A 1 158 ? 6.620   -14.779 53.270  1.00 87.84  ? 261  PHE A CD1   1 
ATOM   1260 C  CD2   . PHE A 1 158 ? 7.555   -12.618 52.918  1.00 79.16  ? 261  PHE A CD2   1 
ATOM   1261 C  CE1   . PHE A 1 158 ? 5.348   -14.240 53.221  1.00 91.16  ? 261  PHE A CE1   1 
ATOM   1262 C  CE2   . PHE A 1 158 ? 6.283   -12.074 52.871  1.00 83.10  ? 261  PHE A CE2   1 
ATOM   1263 C  CZ    . PHE A 1 158 ? 5.180   -12.886 53.023  1.00 82.26  ? 261  PHE A CZ    1 
ATOM   1264 N  N     . LEU A 1 159 ? 11.472  -16.398 50.923  1.00 80.44  ? 262  LEU A N     1 
ATOM   1265 C  CA    . LEU A 1 159 ? 12.781  -17.037 50.880  1.00 73.90  ? 262  LEU A CA    1 
ATOM   1266 C  C     . LEU A 1 159 ? 13.911  -16.094 50.490  1.00 75.84  ? 262  LEU A C     1 
ATOM   1267 O  O     . LEU A 1 159 ? 15.049  -16.549 50.347  1.00 82.75  ? 262  LEU A O     1 
ATOM   1268 C  CB    . LEU A 1 159 ? 12.756  -18.221 49.908  1.00 77.66  ? 262  LEU A CB    1 
ATOM   1269 C  CG    . LEU A 1 159 ? 11.938  -19.447 50.315  1.00 81.37  ? 262  LEU A CG    1 
ATOM   1270 C  CD1   . LEU A 1 159 ? 11.962  -20.492 49.212  1.00 84.94  ? 262  LEU A CD1   1 
ATOM   1271 C  CD2   . LEU A 1 159 ? 12.468  -20.029 51.610  1.00 92.39  ? 262  LEU A CD2   1 
ATOM   1272 N  N     . GLU A 1 160 ? 13.640  -14.802 50.321  1.00 74.90  ? 263  GLU A N     1 
ATOM   1273 C  CA    . GLU A 1 160 ? 14.658  -13.872 49.850  1.00 98.99  ? 263  GLU A CA    1 
ATOM   1274 C  C     . GLU A 1 160 ? 14.620  -12.598 50.681  1.00 87.90  ? 263  GLU A C     1 
ATOM   1275 O  O     . GLU A 1 160 ? 13.571  -12.203 51.197  1.00 84.52  ? 263  GLU A O     1 
ATOM   1276 C  CB    . GLU A 1 160 ? 14.466  -13.544 48.358  1.00 93.48  ? 263  GLU A CB    1 
ATOM   1277 C  CG    . GLU A 1 160 ? 15.581  -12.708 47.737  1.00 92.28  ? 263  GLU A CG    1 
ATOM   1278 C  CD    . GLU A 1 160 ? 16.895  -13.459 47.631  1.00 108.70 ? 263  GLU A CD    1 
ATOM   1279 O  OE1   . GLU A 1 160 ? 16.871  -14.708 47.608  1.00 114.89 ? 263  GLU A OE1   1 
ATOM   1280 O  OE2   . GLU A 1 160 ? 17.952  -12.797 47.569  1.00 116.29 ? 263  GLU A OE2   1 
ATOM   1281 N  N     . LYS A 1 161 ? 15.783  -11.951 50.796  1.00 90.57  ? 264  LYS A N     1 
ATOM   1282 C  CA    . LYS A 1 161 ? 15.917  -10.701 51.538  1.00 87.30  ? 264  LYS A CA    1 
ATOM   1283 C  C     . LYS A 1 161 ? 15.218  -9.536  50.847  1.00 93.38  ? 264  LYS A C     1 
ATOM   1284 O  O     . LYS A 1 161 ? 15.835  -8.491  50.614  1.00 106.56 ? 264  LYS A O     1 
ATOM   1285 C  CB    . LYS A 1 161 ? 17.393  -10.351 51.737  1.00 91.14  ? 264  LYS A CB    1 
ATOM   1286 C  CG    . LYS A 1 161 ? 18.172  -11.325 52.597  1.00 104.71 ? 264  LYS A CG    1 
ATOM   1287 C  CD    . LYS A 1 161 ? 19.496  -10.713 53.030  1.00 111.45 ? 264  LYS A CD    1 
ATOM   1288 C  CE    . LYS A 1 161 ? 19.276  -9.394  53.760  1.00 114.12 ? 264  LYS A CE    1 
ATOM   1289 N  NZ    . LYS A 1 161 ? 20.551  -8.767  54.206  1.00 116.70 ? 264  LYS A NZ    1 
ATOM   1290 N  N     . TYR A 1 162 ? 13.939  -9.696  50.514  1.00 90.47  ? 265  TYR A N     1 
ATOM   1291 C  CA    . TYR A 1 162 ? 13.243  -8.525  50.004  1.00 97.57  ? 265  TYR A CA    1 
ATOM   1292 C  C     . TYR A 1 162 ? 12.636  -7.732  51.155  1.00 92.48  ? 265  TYR A C     1 
ATOM   1293 O  O     . TYR A 1 162 ? 12.273  -8.306  52.186  1.00 88.01  ? 265  TYR A O     1 
ATOM   1294 C  CB    . TYR A 1 162 ? 12.129  -8.933  49.040  1.00 89.18  ? 265  TYR A CB    1 
ATOM   1295 C  CG    . TYR A 1 162 ? 12.581  -9.354  47.661  1.00 91.05  ? 265  TYR A CG    1 
ATOM   1296 C  CD1   . TYR A 1 162 ? 12.936  -8.409  46.706  1.00 99.97  ? 265  TYR A CD1   1 
ATOM   1297 C  CD2   . TYR A 1 162 ? 12.623  -10.695 47.302  1.00 87.59  ? 265  TYR A CD2   1 
ATOM   1298 C  CE1   . TYR A 1 162 ? 13.339  -8.788  45.441  1.00 78.42  ? 265  TYR A CE1   1 
ATOM   1299 C  CE2   . TYR A 1 162 ? 13.025  -11.084 46.037  1.00 88.67  ? 265  TYR A CE2   1 
ATOM   1300 C  CZ    . TYR A 1 162 ? 13.383  -10.127 45.111  1.00 89.83  ? 265  TYR A CZ    1 
ATOM   1301 O  OH    . TYR A 1 162 ? 13.785  -10.510 43.851  1.00 99.59  ? 265  TYR A OH    1 
ATOM   1302 N  N     . PRO A 1 163 ? 12.527  -6.412  51.017  1.00 91.59  ? 266  PRO A N     1 
ATOM   1303 C  CA    . PRO A 1 163 ? 11.712  -5.643  51.962  1.00 89.33  ? 266  PRO A CA    1 
ATOM   1304 C  C     . PRO A 1 163 ? 10.323  -6.253  52.078  1.00 90.76  ? 266  PRO A C     1 
ATOM   1305 O  O     . PRO A 1 163 ? 9.694   -6.599  51.075  1.00 93.91  ? 266  PRO A O     1 
ATOM   1306 C  CB    . PRO A 1 163 ? 11.676  -4.247  51.337  1.00 85.30  ? 266  PRO A CB    1 
ATOM   1307 C  CG    . PRO A 1 163 ? 12.964  -4.156  50.590  1.00 89.32  ? 266  PRO A CG    1 
ATOM   1308 C  CD    . PRO A 1 163 ? 13.233  -5.543  50.059  1.00 99.04  ? 266  PRO A CD    1 
ATOM   1309 N  N     . LEU A 1 164 ? 9.856   -6.406  53.320  1.00 95.01  ? 267  LEU A N     1 
ATOM   1310 C  CA    . LEU A 1 164 ? 8.624   -7.151  53.566  1.00 90.74  ? 267  LEU A CA    1 
ATOM   1311 C  C     . LEU A 1 164 ? 7.448   -6.557  52.800  1.00 80.90  ? 267  LEU A C     1 
ATOM   1312 O  O     . LEU A 1 164 ? 6.587   -7.293  52.306  1.00 86.51  ? 267  LEU A O     1 
ATOM   1313 C  CB    . LEU A 1 164 ? 8.324   -7.191  55.064  1.00 101.78 ? 267  LEU A CB    1 
ATOM   1314 C  CG    . LEU A 1 164 ? 7.120   -8.042  55.476  1.00 95.32  ? 267  LEU A CG    1 
ATOM   1315 C  CD1   . LEU A 1 164 ? 7.358   -9.506  55.140  1.00 103.57 ? 267  LEU A CD1   1 
ATOM   1316 C  CD2   . LEU A 1 164 ? 6.813   -7.872  56.953  1.00 93.67  ? 267  LEU A CD2   1 
ATOM   1317 N  N     . SER A 1 165 ? 7.403   -5.230  52.678  1.00 75.88  ? 268  SER A N     1 
ATOM   1318 C  CA    . SER A 1 165 ? 6.316   -4.579  51.958  1.00 84.16  ? 268  SER A CA    1 
ATOM   1319 C  C     . SER A 1 165 ? 6.384   -4.801  50.451  1.00 91.33  ? 268  SER A C     1 
ATOM   1320 O  O     . SER A 1 165 ? 5.412   -4.492  49.754  1.00 83.73  ? 268  SER A O     1 
ATOM   1321 C  CB    . SER A 1 165 ? 6.316   -3.082  52.268  1.00 81.52  ? 268  SER A CB    1 
ATOM   1322 O  OG    . SER A 1 165 ? 7.615   -2.534  52.128  1.00 77.41  ? 268  SER A OG    1 
ATOM   1323 N  N     . GLN A 1 166 ? 7.496   -5.329  49.934  1.00 85.72  ? 269  GLN A N     1 
ATOM   1324 C  CA    . GLN A 1 166 ? 7.606   -5.577  48.503  1.00 89.14  ? 269  GLN A CA    1 
ATOM   1325 C  C     . GLN A 1 166 ? 6.917   -6.872  48.091  1.00 92.17  ? 269  GLN A C     1 
ATOM   1326 O  O     . GLN A 1 166 ? 6.502   -7.004  46.934  1.00 93.30  ? 269  GLN A O     1 
ATOM   1327 C  CB    . GLN A 1 166 ? 9.078   -5.602  48.085  1.00 97.69  ? 269  GLN A CB    1 
ATOM   1328 C  CG    . GLN A 1 166 ? 9.303   -5.595  46.582  1.00 88.48  ? 269  GLN A CG    1 
ATOM   1329 C  CD    . GLN A 1 166 ? 10.747  -5.322  46.215  1.00 102.57 ? 269  GLN A CD    1 
ATOM   1330 O  OE1   . GLN A 1 166 ? 11.589  -5.100  47.086  1.00 100.10 ? 269  GLN A OE1   1 
ATOM   1331 N  NE2   . GLN A 1 166 ? 11.041  -5.333  44.920  1.00 104.16 ? 269  GLN A NE2   1 
ATOM   1332 N  N     . TYR A 1 167 ? 6.789   -7.832  49.006  1.00 81.56  ? 270  TYR A N     1 
ATOM   1333 C  CA    . TYR A 1 167 ? 6.022   -9.036  48.713  1.00 80.98  ? 270  TYR A CA    1 
ATOM   1334 C  C     . TYR A 1 167 ? 4.571   -8.673  48.423  1.00 84.95  ? 270  TYR A C     1 
ATOM   1335 O  O     . TYR A 1 167 ? 3.992   -7.793  49.066  1.00 78.31  ? 270  TYR A O     1 
ATOM   1336 C  CB    . TYR A 1 167 ? 6.098   -10.020 49.881  1.00 77.73  ? 270  TYR A CB    1 
ATOM   1337 C  CG    . TYR A 1 167 ? 7.405   -10.775 49.972  1.00 73.58  ? 270  TYR A CG    1 
ATOM   1338 C  CD1   . TYR A 1 167 ? 8.530   -10.192 50.540  1.00 76.44  ? 270  TYR A CD1   1 
ATOM   1339 C  CD2   . TYR A 1 167 ? 7.510   -12.077 49.499  1.00 70.97  ? 270  TYR A CD2   1 
ATOM   1340 C  CE1   . TYR A 1 167 ? 9.725   -10.881 50.630  1.00 74.75  ? 270  TYR A CE1   1 
ATOM   1341 C  CE2   . TYR A 1 167 ? 8.701   -12.775 49.583  1.00 66.40  ? 270  TYR A CE2   1 
ATOM   1342 C  CZ    . TYR A 1 167 ? 9.806   -12.172 50.149  1.00 71.66  ? 270  TYR A CZ    1 
ATOM   1343 O  OH    . TYR A 1 167 ? 10.996  -12.861 50.236  1.00 71.21  ? 270  TYR A OH    1 
ATOM   1344 N  N     . LYS A 1 168 ? 3.984   -9.359  47.439  1.00 85.40  ? 271  LYS A N     1 
ATOM   1345 C  CA    . LYS A 1 168 ? 2.647   -8.991  46.983  1.00 85.01  ? 271  LYS A CA    1 
ATOM   1346 C  C     . LYS A 1 168 ? 1.604   -9.204  48.071  1.00 76.57  ? 271  LYS A C     1 
ATOM   1347 O  O     . LYS A 1 168 ? 0.702   -8.375  48.237  1.00 76.26  ? 271  LYS A O     1 
ATOM   1348 C  CB    . LYS A 1 168 ? 2.279   -9.781  45.727  1.00 92.50  ? 271  LYS A CB    1 
ATOM   1349 C  CG    . LYS A 1 168 ? 3.009   -9.324  44.478  1.00 89.64  ? 271  LYS A CG    1 
ATOM   1350 C  CD    . LYS A 1 168 ? 2.498   -10.047 43.246  1.00 94.86  ? 271  LYS A CD    1 
ATOM   1351 C  CE    . LYS A 1 168 ? 3.161   -9.520  41.987  1.00 96.80  ? 271  LYS A CE    1 
ATOM   1352 N  NZ    . LYS A 1 168 ? 2.677   -10.226 40.770  1.00 96.31  ? 271  LYS A NZ    1 
ATOM   1353 N  N     . TYR A 1 169 ? 1.705   -10.305 48.821  1.00 81.45  ? 272  TYR A N     1 
ATOM   1354 C  CA    . TYR A 1 169 ? 0.727   -10.564 49.873  1.00 79.99  ? 272  TYR A CA    1 
ATOM   1355 C  C     . TYR A 1 169 ? 0.761   -9.477  50.939  1.00 76.59  ? 272  TYR A C     1 
ATOM   1356 O  O     . TYR A 1 169 ? -0.289  -9.009  51.394  1.00 70.36  ? 272  TYR A O     1 
ATOM   1357 C  CB    . TYR A 1 169 ? 0.972   -11.934 50.505  1.00 79.28  ? 272  TYR A CB    1 
ATOM   1358 C  CG    . TYR A 1 169 ? 0.135   -12.176 51.741  1.00 83.98  ? 272  TYR A CG    1 
ATOM   1359 C  CD1   . TYR A 1 169 ? -1.192  -12.568 51.638  1.00 80.98  ? 272  TYR A CD1   1 
ATOM   1360 C  CD2   . TYR A 1 169 ? 0.670   -12.002 53.012  1.00 88.93  ? 272  TYR A CD2   1 
ATOM   1361 C  CE1   . TYR A 1 169 ? -1.963  -12.784 52.765  1.00 90.53  ? 272  TYR A CE1   1 
ATOM   1362 C  CE2   . TYR A 1 169 ? -0.093  -12.214 54.144  1.00 84.59  ? 272  TYR A CE2   1 
ATOM   1363 C  CZ    . TYR A 1 169 ? -1.409  -12.605 54.015  1.00 87.76  ? 272  TYR A CZ    1 
ATOM   1364 O  OH    . TYR A 1 169 ? -2.172  -12.819 55.141  1.00 93.33  ? 272  TYR A OH    1 
ATOM   1365 N  N     . ILE A 1 170 ? 1.961   -9.059  51.347  1.00 72.47  ? 273  ILE A N     1 
ATOM   1366 C  CA    . ILE A 1 170 ? 2.082   -8.038  52.382  1.00 77.76  ? 273  ILE A CA    1 
ATOM   1367 C  C     . ILE A 1 170 ? 1.525   -6.708  51.888  1.00 75.65  ? 273  ILE A C     1 
ATOM   1368 O  O     . ILE A 1 170 ? 0.761   -6.037  52.591  1.00 80.65  ? 273  ILE A O     1 
ATOM   1369 C  CB    . ILE A 1 170 ? 3.546   -7.902  52.834  1.00 80.68  ? 273  ILE A CB    1 
ATOM   1370 C  CG1   . ILE A 1 170 ? 4.081   -9.245  53.337  1.00 79.67  ? 273  ILE A CG1   1 
ATOM   1371 C  CG2   . ILE A 1 170 ? 3.676   -6.831  53.902  1.00 80.64  ? 273  ILE A CG2   1 
ATOM   1372 C  CD1   . ILE A 1 170 ? 3.283   -9.834  54.472  1.00 78.17  ? 273  ILE A CD1   1 
ATOM   1373 N  N     . ARG A 1 171 ? 1.898   -6.307  50.670  1.00 83.34  ? 274  ARG A N     1 
ATOM   1374 C  CA    . ARG A 1 171 ? 1.422   -5.030  50.148  1.00 81.05  ? 274  ARG A CA    1 
ATOM   1375 C  C     . ARG A 1 171 ? -0.064  -5.078  49.815  1.00 77.32  ? 274  ARG A C     1 
ATOM   1376 O  O     . ARG A 1 171 ? -0.747  -4.050  49.891  1.00 79.10  ? 274  ARG A O     1 
ATOM   1377 C  CB    . ARG A 1 171 ? 2.232   -4.618  48.919  1.00 85.35  ? 274  ARG A CB    1 
ATOM   1378 C  CG    . ARG A 1 171 ? 2.010   -3.170  48.512  1.00 88.59  ? 274  ARG A CG    1 
ATOM   1379 C  CD    . ARG A 1 171 ? 2.867   -2.767  47.329  1.00 92.86  ? 274  ARG A CD    1 
ATOM   1380 N  NE    . ARG A 1 171 ? 4.292   -2.897  47.607  1.00 97.81  ? 274  ARG A NE    1 
ATOM   1381 C  CZ    . ARG A 1 171 ? 5.251   -2.407  46.834  1.00 101.16 ? 274  ARG A CZ    1 
ATOM   1382 N  NH1   . ARG A 1 171 ? 4.972   -1.723  45.736  1.00 93.74  ? 274  ARG A NH1   1 
ATOM   1383 N  NH2   . ARG A 1 171 ? 6.522   -2.601  47.174  1.00 106.44 ? 274  ARG A NH2   1 
ATOM   1384 N  N     . SER A 1 172 ? -0.584  -6.251  49.449  1.00 73.01  ? 275  SER A N     1 
ATOM   1385 C  CA    . SER A 1 172 ? -2.024  -6.380  49.254  1.00 76.53  ? 275  SER A CA    1 
ATOM   1386 C  C     . SER A 1 172 ? -2.766  -6.222  50.575  1.00 90.12  ? 275  SER A C     1 
ATOM   1387 O  O     . SER A 1 172 ? -3.872  -5.670  50.610  1.00 93.92  ? 275  SER A O     1 
ATOM   1388 C  CB    . SER A 1 172 ? -2.353  -7.724  48.605  1.00 78.62  ? 275  SER A CB    1 
ATOM   1389 O  OG    . SER A 1 172 ? -3.723  -7.799  48.252  1.00 89.85  ? 275  SER A OG    1 
ATOM   1390 N  N     . CYS A 1 173 ? -2.172  -6.700  51.674  1.00 84.90  ? 276  CYS A N     1 
ATOM   1391 C  CA    . CYS A 1 173 ? -2.759  -6.471  52.991  1.00 78.48  ? 276  CYS A CA    1 
ATOM   1392 C  C     . CYS A 1 173 ? -2.755  -4.990  53.342  1.00 83.72  ? 276  CYS A C     1 
ATOM   1393 O  O     . CYS A 1 173 ? -3.721  -4.477  53.920  1.00 87.58  ? 276  CYS A O     1 
ATOM   1394 C  CB    . CYS A 1 173 ? -2.003  -7.271  54.055  1.00 74.70  ? 276  CYS A CB    1 
ATOM   1395 S  SG    . CYS A 1 173 ? -2.289  -9.061  54.041  1.00 69.84  ? 276  CYS A SG    1 
ATOM   1396 N  N     . ILE A 1 174 ? -1.674  -4.286  52.998  1.00 77.04  ? 277  ILE A N     1 
ATOM   1397 C  CA    . ILE A 1 174 ? -1.565  -2.865  53.319  1.00 77.24  ? 277  ILE A CA    1 
ATOM   1398 C  C     . ILE A 1 174 ? -2.655  -2.072  52.609  1.00 91.93  ? 277  ILE A C     1 
ATOM   1399 O  O     . ILE A 1 174 ? -3.342  -1.242  53.217  1.00 96.30  ? 277  ILE A O     1 
ATOM   1400 C  CB    . ILE A 1 174 ? -0.165  -2.343  52.954  1.00 82.83  ? 277  ILE A CB    1 
ATOM   1401 C  CG1   . ILE A 1 174 ? 0.900   -3.015  53.822  1.00 80.73  ? 277  ILE A CG1   1 
ATOM   1402 C  CG2   . ILE A 1 174 ? -0.112  -0.831  53.083  1.00 88.42  ? 277  ILE A CG2   1 
ATOM   1403 C  CD1   . ILE A 1 174 ? 2.317   -2.663  53.427  1.00 78.38  ? 277  ILE A CD1   1 
ATOM   1404 N  N     . MET A 1 175 ? -2.828  -2.314  51.308  1.00 106.54 ? 278  MET A N     1 
ATOM   1405 C  CA    . MET A 1 175 ? -3.814  -1.562  50.537  1.00 98.52  ? 278  MET A CA    1 
ATOM   1406 C  C     . MET A 1 175 ? -5.232  -1.864  51.004  1.00 96.51  ? 278  MET A C     1 
ATOM   1407 O  O     . MET A 1 175 ? -6.077  -0.963  51.060  1.00 99.37  ? 278  MET A O     1 
ATOM   1408 C  CB    . MET A 1 175 ? -3.660  -1.874  49.049  1.00 104.95 ? 278  MET A CB    1 
ATOM   1409 C  CG    . MET A 1 175 ? -2.301  -1.502  48.479  1.00 111.06 ? 278  MET A CG    1 
ATOM   1410 S  SD    . MET A 1 175 ? -2.078  -2.075  46.785  1.00 111.64 ? 278  MET A SD    1 
ATOM   1411 C  CE    . MET A 1 175 ? -0.459  -1.406  46.412  1.00 116.37 ? 278  MET A CE    1 
ATOM   1412 N  N     . LEU A 1 176 ? -5.512  -3.121  51.342  1.00 94.53  ? 279  LEU A N     1 
ATOM   1413 C  CA    . LEU A 1 176 ? -6.832  -3.520  51.811  1.00 99.24  ? 279  LEU A CA    1 
ATOM   1414 C  C     . LEU A 1 176 ? -7.049  -3.234  53.291  1.00 100.78 ? 279  LEU A C     1 
ATOM   1415 O  O     . LEU A 1 176 ? -8.133  -3.527  53.809  1.00 101.66 ? 279  LEU A O     1 
ATOM   1416 C  CB    . LEU A 1 176 ? -7.056  -5.008  51.532  1.00 97.83  ? 279  LEU A CB    1 
ATOM   1417 C  CG    . LEU A 1 176 ? -7.055  -5.411  50.056  1.00 106.60 ? 279  LEU A CG    1 
ATOM   1418 C  CD1   . LEU A 1 176 ? -7.006  -6.922  49.906  1.00 111.67 ? 279  LEU A CD1   1 
ATOM   1419 C  CD2   . LEU A 1 176 ? -8.273  -4.843  49.349  1.00 109.62 ? 279  LEU A CD2   1 
ATOM   1420 N  N     . GLY A 1 177 ? -6.058  -2.674  53.980  1.00 100.26 ? 280  GLY A N     1 
ATOM   1421 C  CA    . GLY A 1 177 ? -6.201  -2.385  55.393  1.00 95.49  ? 280  GLY A CA    1 
ATOM   1422 C  C     . GLY A 1 177 ? -6.247  -3.599  56.289  1.00 95.44  ? 280  GLY A C     1 
ATOM   1423 O  O     . GLY A 1 177 ? -6.702  -3.496  57.430  1.00 99.55  ? 280  GLY A O     1 
ATOM   1424 N  N     . ARG A 1 178 ? -5.787  -4.749  55.809  1.00 94.81  ? 281  ARG A N     1 
ATOM   1425 C  CA    . ARG A 1 178 ? -5.809  -5.981  56.582  1.00 93.33  ? 281  ARG A CA    1 
ATOM   1426 C  C     . ARG A 1 178 ? -4.451  -6.241  57.226  1.00 91.31  ? 281  ARG A C     1 
ATOM   1427 O  O     . ARG A 1 178 ? -3.465  -5.541  56.981  1.00 81.04  ? 281  ARG A O     1 
ATOM   1428 C  CB    . ARG A 1 178 ? -6.214  -7.165  55.700  1.00 92.68  ? 281  ARG A CB    1 
ATOM   1429 C  CG    . ARG A 1 178 ? -7.627  -7.082  55.156  1.00 97.10  ? 281  ARG A CG    1 
ATOM   1430 C  CD    . ARG A 1 178 ? -8.223  -8.470  55.004  1.00 109.93 ? 281  ARG A CD    1 
ATOM   1431 N  NE    . ARG A 1 178 ? -7.304  -9.387  54.342  1.00 118.43 ? 281  ARG A NE    1 
ATOM   1432 C  CZ    . ARG A 1 178 ? -7.298  -9.629  53.038  1.00 126.31 ? 281  ARG A CZ    1 
ATOM   1433 N  NH1   . ARG A 1 178 ? -8.159  -9.044  52.223  1.00 117.42 ? 281  ARG A NH1   1 
ATOM   1434 N  NH2   . ARG A 1 178 ? -6.406  -10.482 52.540  1.00 122.22 ? 281  ARG A NH2   1 
ATOM   1435 N  N     . MET A 1 179 ? -4.414  -7.276  58.064  1.00 99.99  ? 282  MET A N     1 
ATOM   1436 C  CA    . MET A 1 179 ? -3.209  -7.668  58.774  1.00 91.31  ? 282  MET A CA    1 
ATOM   1437 C  C     . MET A 1 179 ? -2.633  -8.939  58.175  1.00 80.61  ? 282  MET A C     1 
ATOM   1438 O  O     . MET A 1 179 ? -3.379  -9.895  57.924  1.00 75.88  ? 282  MET A O     1 
ATOM   1439 C  CB    . MET A 1 179 ? -3.503  -7.881  60.265  1.00 87.11  ? 282  MET A CB    1 
ATOM   1440 C  CG    . MET A 1 179 ? -3.482  -6.601  61.088  1.00 102.90 ? 282  MET A CG    1 
ATOM   1441 S  SD    . MET A 1 179 ? -3.807  -6.866  62.844  1.00 96.82  ? 282  MET A SD    1 
ATOM   1442 C  CE    . MET A 1 179 ? -5.580  -7.126  62.829  1.00 91.23  ? 282  MET A CE    1 
ATOM   1443 N  N     . PRO A 1 180 ? -1.327  -8.983  57.924  1.00 73.83  ? 283  PRO A N     1 
ATOM   1444 C  CA    . PRO A 1 180 ? -0.716  -10.222 57.429  1.00 76.96  ? 283  PRO A CA    1 
ATOM   1445 C  C     . PRO A 1 180 ? -0.793  -11.334 58.464  1.00 83.81  ? 283  PRO A C     1 
ATOM   1446 O  O     . PRO A 1 180 ? -0.564  -11.117 59.657  1.00 86.41  ? 283  PRO A O     1 
ATOM   1447 C  CB    . PRO A 1 180 ? 0.738   -9.815  57.157  1.00 81.22  ? 283  PRO A CB    1 
ATOM   1448 C  CG    . PRO A 1 180 ? 0.698   -8.326  57.004  1.00 83.47  ? 283  PRO A CG    1 
ATOM   1449 C  CD    . PRO A 1 180 ? -0.380  -7.857  57.928  1.00 76.56  ? 283  PRO A CD    1 
ATOM   1450 N  N     . ASN A 1 181 ? -1.119  -12.534 57.994  1.00 79.36  ? 284  ASN A N     1 
ATOM   1451 C  CA    . ASN A 1 181 ? -1.165  -13.735 58.826  1.00 80.63  ? 284  ASN A CA    1 
ATOM   1452 C  C     . ASN A 1 181 ? -0.053  -14.666 58.355  1.00 84.86  ? 284  ASN A C     1 
ATOM   1453 O  O     . ASN A 1 181 ? -0.199  -15.365 57.348  1.00 89.59  ? 284  ASN A O     1 
ATOM   1454 C  CB    . ASN A 1 181 ? -2.531  -14.407 58.746  1.00 86.25  ? 284  ASN A CB    1 
ATOM   1455 C  CG    . ASN A 1 181 ? -3.578  -13.696 59.576  1.00 89.54  ? 284  ASN A CG    1 
ATOM   1456 O  OD1   . ASN A 1 181 ? -3.290  -12.701 60.244  1.00 85.26  ? 284  ASN A OD1   1 
ATOM   1457 N  ND2   . ASN A 1 181 ? -4.805  -14.201 59.536  1.00 95.25  ? 284  ASN A ND2   1 
ATOM   1458 N  N     . LEU A 1 182 ? 1.056   -14.671 59.087  1.00 86.26  ? 285  LEU A N     1 
ATOM   1459 C  CA    . LEU A 1 182 ? 2.246   -15.423 58.723  1.00 88.82  ? 285  LEU A CA    1 
ATOM   1460 C  C     . LEU A 1 182 ? 2.550   -16.467 59.791  1.00 85.02  ? 285  LEU A C     1 
ATOM   1461 O  O     . LEU A 1 182 ? 2.000   -16.444 60.894  1.00 90.40  ? 285  LEU A O     1 
ATOM   1462 C  CB    . LEU A 1 182 ? 3.448   -14.487 58.538  1.00 87.08  ? 285  LEU A CB    1 
ATOM   1463 C  CG    . LEU A 1 182 ? 3.192   -13.214 57.729  1.00 82.35  ? 285  LEU A CG    1 
ATOM   1464 C  CD1   . LEU A 1 182 ? 4.441   -12.345 57.683  1.00 75.46  ? 285  LEU A CD1   1 
ATOM   1465 C  CD2   . LEU A 1 182 ? 2.716   -13.555 56.324  1.00 96.90  ? 285  LEU A CD2   1 
ATOM   1466 N  N     . MET A 1 183 ? 3.440   -17.395 59.446  1.00 84.00  ? 286  MET A N     1 
ATOM   1467 C  CA    . MET A 1 183 ? 3.896   -18.400 60.393  1.00 81.15  ? 286  MET A CA    1 
ATOM   1468 C  C     . MET A 1 183 ? 5.351   -18.732 60.095  1.00 81.91  ? 286  MET A C     1 
ATOM   1469 O  O     . MET A 1 183 ? 5.864   -18.445 59.011  1.00 86.25  ? 286  MET A O     1 
ATOM   1470 C  CB    . MET A 1 183 ? 3.036   -19.668 60.341  1.00 86.68  ? 286  MET A CB    1 
ATOM   1471 C  CG    . MET A 1 183 ? 3.522   -20.710 59.347  1.00 96.89  ? 286  MET A CG    1 
ATOM   1472 S  SD    . MET A 1 183 ? 2.799   -22.334 59.651  1.00 127.50 ? 286  MET A SD    1 
ATOM   1473 C  CE    . MET A 1 183 ? 3.763   -23.349 58.534  1.00 122.33 ? 286  MET A CE    1 
ATOM   1474 N  N     . LEU A 1 184 ? 6.011   -19.341 61.074  1.00 89.62  ? 287  LEU A N     1 
ATOM   1475 C  CA    . LEU A 1 184 ? 7.415   -19.703 60.957  1.00 87.82  ? 287  LEU A CA    1 
ATOM   1476 C  C     . LEU A 1 184 ? 7.559   -21.181 60.616  1.00 92.92  ? 287  LEU A C     1 
ATOM   1477 O  O     . LEU A 1 184 ? 6.770   -22.020 61.058  1.00 94.56  ? 287  LEU A O     1 
ATOM   1478 C  CB    . LEU A 1 184 ? 8.174   -19.394 62.249  1.00 84.86  ? 287  LEU A CB    1 
ATOM   1479 C  CG    . LEU A 1 184 ? 8.758   -17.986 62.409  1.00 82.87  ? 287  LEU A CG    1 
ATOM   1480 C  CD1   . LEU A 1 184 ? 7.668   -16.932 62.510  1.00 80.97  ? 287  LEU A CD1   1 
ATOM   1481 C  CD2   . LEU A 1 184 ? 9.681   -17.921 63.616  1.00 84.23  ? 287  LEU A CD2   1 
ATOM   1482 N  N     . MET A 1 185 ? 8.583   -21.487 59.823  1.00 100.76 ? 288  MET A N     1 
ATOM   1483 C  CA    . MET A 1 185 ? 8.869   -22.856 59.420  1.00 103.09 ? 288  MET A CA    1 
ATOM   1484 C  C     . MET A 1 185 ? 10.370  -22.997 59.230  1.00 96.87  ? 288  MET A C     1 
ATOM   1485 O  O     . MET A 1 185 ? 10.997  -22.143 58.597  1.00 97.68  ? 288  MET A O     1 
ATOM   1486 C  CB    . MET A 1 185 ? 8.122   -23.222 58.133  1.00 100.34 ? 288  MET A CB    1 
ATOM   1487 C  CG    . MET A 1 185 ? 8.311   -24.660 57.689  1.00 102.36 ? 288  MET A CG    1 
ATOM   1488 S  SD    . MET A 1 185 ? 7.183   -25.110 56.358  1.00 128.99 ? 288  MET A SD    1 
ATOM   1489 C  CE    . MET A 1 185 ? 7.757   -26.762 55.966  1.00 124.30 ? 288  MET A CE    1 
ATOM   1490 N  N     . ALA A 1 186 ? 10.938  -24.064 59.782  1.00 100.08 ? 289  ALA A N     1 
ATOM   1491 C  CA    . ALA A 1 186 ? 12.377  -24.269 59.709  1.00 106.55 ? 289  ALA A CA    1 
ATOM   1492 C  C     . ALA A 1 186 ? 12.812  -24.560 58.278  1.00 102.12 ? 289  ALA A C     1 
ATOM   1493 O  O     . ALA A 1 186 ? 12.122  -25.260 57.531  1.00 103.01 ? 289  ALA A O     1 
ATOM   1494 C  CB    . ALA A 1 186 ? 12.796  -25.414 60.629  1.00 105.35 ? 289  ALA A CB    1 
ATOM   1495 N  N     . LYS A 1 187 ? 13.970  -24.011 57.898  1.00 98.81  ? 290  LYS A N     1 
ATOM   1496 C  CA    . LYS A 1 187 ? 14.498  -24.236 56.555  1.00 99.19  ? 290  LYS A CA    1 
ATOM   1497 C  C     . LYS A 1 187 ? 14.702  -25.720 56.281  1.00 104.92 ? 290  LYS A C     1 
ATOM   1498 O  O     . LYS A 1 187 ? 14.391  -26.204 55.187  1.00 110.96 ? 290  LYS A O     1 
ATOM   1499 C  CB    . LYS A 1 187 ? 15.815  -23.482 56.370  1.00 94.87  ? 290  LYS A CB    1 
ATOM   1500 C  CG    . LYS A 1 187 ? 15.686  -21.971 56.317  1.00 91.53  ? 290  LYS A CG    1 
ATOM   1501 C  CD    . LYS A 1 187 ? 17.051  -21.317 56.154  1.00 92.48  ? 290  LYS A CD    1 
ATOM   1502 C  CE    . LYS A 1 187 ? 16.931  -19.817 55.937  1.00 95.78  ? 290  LYS A CE    1 
ATOM   1503 N  NZ    . LYS A 1 187 ? 16.235  -19.139 57.066  1.00 98.26  ? 290  LYS A NZ    1 
ATOM   1504 N  N     . GLU A 1 188 ? 15.224  -26.459 57.264  1.00 107.19 ? 291  GLU A N     1 
ATOM   1505 C  CA    . GLU A 1 188 ? 15.523  -27.871 57.049  1.00 112.37 ? 291  GLU A CA    1 
ATOM   1506 C  C     . GLU A 1 188 ? 14.260  -28.691 56.818  1.00 116.67 ? 291  GLU A C     1 
ATOM   1507 O  O     . GLU A 1 188 ? 14.305  -29.710 56.119  1.00 111.90 ? 291  GLU A O     1 
ATOM   1508 C  CB    . GLU A 1 188 ? 16.317  -28.432 58.231  1.00 115.22 ? 291  GLU A CB    1 
ATOM   1509 C  CG    . GLU A 1 188 ? 15.610  -28.355 59.580  1.00 120.66 ? 291  GLU A CG    1 
ATOM   1510 C  CD    . GLU A 1 188 ? 15.829  -27.032 60.294  1.00 133.14 ? 291  GLU A CD    1 
ATOM   1511 O  OE1   . GLU A 1 188 ? 15.955  -25.992 59.614  1.00 132.11 ? 291  GLU A OE1   1 
ATOM   1512 O  OE2   . GLU A 1 188 ? 15.878  -27.034 61.543  1.00 147.28 ? 291  GLU A OE2   1 
ATOM   1513 N  N     . SER A 1 189 ? 13.127  -28.269 57.386  1.00 111.41 ? 292  SER A N     1 
ATOM   1514 C  CA    . SER A 1 189 ? 11.877  -28.975 57.127  1.00 111.76 ? 292  SER A CA    1 
ATOM   1515 C  C     . SER A 1 189 ? 11.354  -28.682 55.727  1.00 114.27 ? 292  SER A C     1 
ATOM   1516 O  O     . SER A 1 189 ? 10.713  -29.543 55.113  1.00 113.50 ? 292  SER A O     1 
ATOM   1517 C  CB    . SER A 1 189 ? 10.831  -28.605 58.179  1.00 104.15 ? 292  SER A CB    1 
ATOM   1518 O  OG    . SER A 1 189 ? 10.534  -27.220 58.142  1.00 103.69 ? 292  SER A OG    1 
ATOM   1519 N  N     . LEU A 1 190 ? 11.616  -27.481 55.208  1.00 109.62 ? 293  LEU A N     1 
ATOM   1520 C  CA    . LEU A 1 190 ? 11.210  -27.151 53.847  1.00 111.64 ? 293  LEU A CA    1 
ATOM   1521 C  C     . LEU A 1 190 ? 12.185  -27.725 52.826  1.00 109.65 ? 293  LEU A C     1 
ATOM   1522 O  O     . LEU A 1 190 ? 11.770  -28.179 51.754  1.00 105.20 ? 293  LEU A O     1 
ATOM   1523 C  CB    . LEU A 1 190 ? 11.090  -25.632 53.694  1.00 112.55 ? 293  LEU A CB    1 
ATOM   1524 C  CG    . LEU A 1 190 ? 10.457  -25.038 52.429  1.00 103.11 ? 293  LEU A CG    1 
ATOM   1525 C  CD1   . LEU A 1 190 ? 11.484  -24.844 51.319  1.00 103.83 ? 293  LEU A CD1   1 
ATOM   1526 C  CD2   . LEU A 1 190 ? 9.296   -25.898 51.947  1.00 102.91 ? 293  LEU A CD2   1 
ATOM   1527 N  N     . TYR A 1 191 ? 13.483  -27.717 53.142  1.00 103.60 ? 294  TYR A N     1 
ATOM   1528 C  CA    . TYR A 1 191 ? 14.473  -28.258 52.217  1.00 100.06 ? 294  TYR A CA    1 
ATOM   1529 C  C     . TYR A 1 191 ? 14.360  -29.772 52.091  1.00 107.33 ? 294  TYR A C     1 
ATOM   1530 O  O     . TYR A 1 191 ? 14.628  -30.323 51.017  1.00 116.21 ? 294  TYR A O     1 
ATOM   1531 C  CB    . TYR A 1 191 ? 15.885  -27.873 52.664  1.00 94.92  ? 294  TYR A CB    1 
ATOM   1532 C  CG    . TYR A 1 191 ? 16.184  -26.391 52.603  1.00 95.22  ? 294  TYR A CG    1 
ATOM   1533 C  CD1   . TYR A 1 191 ? 15.336  -25.513 51.938  1.00 101.02 ? 294  TYR A CD1   1 
ATOM   1534 C  CD2   . TYR A 1 191 ? 17.322  -25.870 53.205  1.00 97.76  ? 294  TYR A CD2   1 
ATOM   1535 C  CE1   . TYR A 1 191 ? 15.611  -24.159 51.881  1.00 100.58 ? 294  TYR A CE1   1 
ATOM   1536 C  CE2   . TYR A 1 191 ? 17.605  -24.519 53.154  1.00 98.97  ? 294  TYR A CE2   1 
ATOM   1537 C  CZ    . TYR A 1 191 ? 16.747  -23.668 52.491  1.00 102.05 ? 294  TYR A CZ    1 
ATOM   1538 O  OH    . TYR A 1 191 ? 17.027  -22.322 52.438  1.00 108.92 ? 294  TYR A OH    1 
ATOM   1539 N  N     . SER A 1 192 ? 13.972  -30.458 53.168  1.00 109.21 ? 295  SER A N     1 
ATOM   1540 C  CA    . SER A 1 192 ? 13.841  -31.910 53.119  1.00 112.45 ? 295  SER A CA    1 
ATOM   1541 C  C     . SER A 1 192 ? 12.665  -32.355 52.260  1.00 105.68 ? 295  SER A C     1 
ATOM   1542 O  O     . SER A 1 192 ? 12.679  -33.480 51.749  1.00 100.48 ? 295  SER A O     1 
ATOM   1543 C  CB    . SER A 1 192 ? 13.696  -32.475 54.533  1.00 109.90 ? 295  SER A CB    1 
ATOM   1544 O  OG    . SER A 1 192 ? 12.551  -31.945 55.179  1.00 113.52 ? 295  SER A OG    1 
ATOM   1545 N  N     . GLN A 1 193 ? 11.655  -31.506 52.093  1.00 102.84 ? 296  GLN A N     1 
ATOM   1546 C  CA    . GLN A 1 193 ? 10.512  -31.822 51.247  1.00 115.64 ? 296  GLN A CA    1 
ATOM   1547 C  C     . GLN A 1 193 ? 10.762  -31.516 49.776  1.00 114.36 ? 296  GLN A C     1 
ATOM   1548 O  O     . GLN A 1 193 ? 9.897   -31.811 48.944  1.00 111.97 ? 296  GLN A O     1 
ATOM   1549 C  CB    . GLN A 1 193 ? 9.278   -31.058 51.734  1.00 115.79 ? 296  GLN A CB    1 
ATOM   1550 C  CG    . GLN A 1 193 ? 8.881   -31.391 53.162  1.00 121.29 ? 296  GLN A CG    1 
ATOM   1551 C  CD    . GLN A 1 193 ? 8.010   -30.322 53.790  1.00 136.89 ? 296  GLN A CD    1 
ATOM   1552 O  OE1   . GLN A 1 193 ? 7.755   -29.279 53.188  1.00 144.44 ? 296  GLN A OE1   1 
ATOM   1553 N  NE2   . GLN A 1 193 ? 7.551   -30.575 55.011  1.00 132.97 ? 296  GLN A NE2   1 
ATOM   1554 N  N     . LEU A 1 194 ? 11.911  -30.940 49.440  1.00 114.01 ? 297  LEU A N     1 
ATOM   1555 C  CA    . LEU A 1 194 ? 12.233  -30.634 48.052  1.00 113.68 ? 297  LEU A CA    1 
ATOM   1556 C  C     . LEU A 1 194 ? 12.837  -31.860 47.379  1.00 118.42 ? 297  LEU A C     1 
ATOM   1557 O  O     . LEU A 1 194 ? 13.922  -32.299 47.777  1.00 120.51 ? 297  LEU A O     1 
ATOM   1558 C  CB    . LEU A 1 194 ? 13.211  -29.469 47.975  1.00 112.95 ? 297  LEU A CB    1 
ATOM   1559 C  CG    . LEU A 1 194 ? 12.773  -28.135 48.580  1.00 106.76 ? 297  LEU A CG    1 
ATOM   1560 C  CD1   . LEU A 1 194 ? 13.952  -27.180 48.650  1.00 101.67 ? 297  LEU A CD1   1 
ATOM   1561 C  CD2   . LEU A 1 194 ? 11.635  -27.528 47.777  1.00 97.51  ? 297  LEU A CD2   1 
ATOM   1562 N  N     . PRO A 1 195 ? 12.182  -32.441 46.378  1.00 122.72 ? 298  PRO A N     1 
ATOM   1563 C  CA    . PRO A 1 195 ? 12.774  -33.583 45.678  1.00 123.93 ? 298  PRO A CA    1 
ATOM   1564 C  C     . PRO A 1 195 ? 13.934  -33.149 44.795  1.00 129.04 ? 298  PRO A C     1 
ATOM   1565 O  O     . PRO A 1 195 ? 14.033  -31.998 44.363  1.00 128.23 ? 298  PRO A O     1 
ATOM   1566 C  CB    . PRO A 1 195 ? 11.613  -34.131 44.837  1.00 125.82 ? 298  PRO A CB    1 
ATOM   1567 C  CG    . PRO A 1 195 ? 10.372  -33.492 45.405  1.00 120.69 ? 298  PRO A CG    1 
ATOM   1568 C  CD    . PRO A 1 195 ? 10.815  -32.160 45.913  1.00 120.67 ? 298  PRO A CD    1 
ATOM   1569 N  N     . MET A 1 196 ? 14.824  -34.101 44.531  1.00 135.50 ? 299  MET A N     1 
ATOM   1570 C  CA    . MET A 1 196 ? 15.985  -33.841 43.691  1.00 141.60 ? 299  MET A CA    1 
ATOM   1571 C  C     . MET A 1 196 ? 15.590  -33.894 42.221  1.00 147.93 ? 299  MET A C     1 
ATOM   1572 O  O     . MET A 1 196 ? 14.907  -34.826 41.786  1.00 144.25 ? 299  MET A O     1 
ATOM   1573 C  CB    . MET A 1 196 ? 17.090  -34.859 43.973  1.00 142.16 ? 299  MET A CB    1 
ATOM   1574 C  CG    . MET A 1 196 ? 18.351  -34.641 43.151  1.00 144.82 ? 299  MET A CG    1 
ATOM   1575 S  SD    . MET A 1 196 ? 19.411  -36.099 43.083  1.00 157.37 ? 299  MET A SD    1 
ATOM   1576 C  CE    . MET A 1 196 ? 18.376  -37.226 42.149  1.00 135.27 ? 299  MET A CE    1 
ATOM   1577 N  N     . ASP A 1 197 ? 16.020  -32.893 41.459  1.00 164.71 ? 300  ASP A N     1 
ATOM   1578 C  CA    . ASP A 1 197 ? 15.804  -32.898 40.020  1.00 162.94 ? 300  ASP A CA    1 
ATOM   1579 C  C     . ASP A 1 197 ? 16.854  -33.769 39.342  1.00 164.10 ? 300  ASP A C     1 
ATOM   1580 O  O     . ASP A 1 197 ? 18.037  -33.731 39.693  1.00 166.34 ? 300  ASP A O     1 
ATOM   1581 C  CB    . ASP A 1 197 ? 15.846  -31.474 39.461  1.00 153.07 ? 300  ASP A CB    1 
ATOM   1582 C  CG    . ASP A 1 197 ? 17.136  -30.750 39.798  1.00 161.74 ? 300  ASP A CG    1 
ATOM   1583 O  OD1   . ASP A 1 197 ? 18.152  -30.985 39.110  1.00 155.48 ? 300  ASP A OD1   1 
ATOM   1584 O  OD2   . ASP A 1 197 ? 17.132  -29.943 40.752  1.00 165.40 ? 300  ASP A OD2   1 
ATOM   1585 N  N     . CYS A 1 198 ? 16.410  -34.567 38.369  1.00 161.26 ? 301  CYS A N     1 
ATOM   1586 C  CA    . CYS A 1 198 ? 17.265  -35.538 37.683  1.00 157.81 ? 301  CYS A CA    1 
ATOM   1587 C  C     . CYS A 1 198 ? 17.073  -35.373 36.177  1.00 153.73 ? 301  CYS A C     1 
ATOM   1588 O  O     . CYS A 1 198 ? 16.406  -36.181 35.527  1.00 163.28 ? 301  CYS A O     1 
ATOM   1589 C  CB    . CYS A 1 198 ? 16.950  -36.959 38.151  1.00 168.34 ? 301  CYS A CB    1 
ATOM   1590 S  SG    . CYS A 1 198 ? 15.183  -37.329 38.273  1.00 176.48 ? 301  CYS A SG    1 
ATOM   1591 N  N     . PHE A 1 199 ? 17.666  -34.318 35.624  1.00 141.35 ? 302  PHE A N     1 
ATOM   1592 C  CA    . PHE A 1 199 ? 17.619  -34.071 34.190  1.00 129.82 ? 302  PHE A CA    1 
ATOM   1593 C  C     . PHE A 1 199 ? 18.764  -34.801 33.502  1.00 124.73 ? 302  PHE A C     1 
ATOM   1594 O  O     . PHE A 1 199 ? 19.925  -34.668 33.902  1.00 125.51 ? 302  PHE A O     1 
ATOM   1595 C  CB    . PHE A 1 199 ? 17.695  -32.574 33.889  1.00 117.57 ? 302  PHE A CB    1 
ATOM   1596 C  CG    . PHE A 1 199 ? 17.925  -32.260 32.437  1.00 115.13 ? 302  PHE A CG    1 
ATOM   1597 C  CD1   . PHE A 1 199 ? 16.885  -32.332 31.526  1.00 110.14 ? 302  PHE A CD1   1 
ATOM   1598 C  CD2   . PHE A 1 199 ? 19.183  -31.895 31.983  1.00 112.58 ? 302  PHE A CD2   1 
ATOM   1599 C  CE1   . PHE A 1 199 ? 17.093  -32.046 30.190  1.00 109.25 ? 302  PHE A CE1   1 
ATOM   1600 C  CE2   . PHE A 1 199 ? 19.398  -31.609 30.648  1.00 113.65 ? 302  PHE A CE2   1 
ATOM   1601 C  CZ    . PHE A 1 199 ? 18.351  -31.684 29.750  1.00 120.29 ? 302  PHE A CZ    1 
ATOM   1602 N  N     . THR A 1 200 ? 18.433  -35.570 32.470  1.00 120.91 ? 303  THR A N     1 
ATOM   1603 C  CA    . THR A 1 200 ? 19.424  -36.264 31.664  1.00 118.35 ? 303  THR A CA    1 
ATOM   1604 C  C     . THR A 1 200 ? 19.197  -35.937 30.197  1.00 113.37 ? 303  THR A C     1 
ATOM   1605 O  O     . THR A 1 200 ? 18.062  -35.728 29.758  1.00 113.09 ? 303  THR A O     1 
ATOM   1606 C  CB    . THR A 1 200 ? 19.372  -37.786 31.878  1.00 116.82 ? 303  THR A CB    1 
ATOM   1607 O  OG1   . THR A 1 200 ? 20.266  -38.431 30.962  1.00 109.50 ? 303  THR A OG1   1 
ATOM   1608 C  CG2   . THR A 1 200 ? 17.960  -38.311 31.662  1.00 119.76 ? 303  THR A CG2   1 
ATOM   1609 N  N     . MET A 1 201 ? 20.288  -35.881 29.446  1.00 112.07 ? 304  MET A N     1 
ATOM   1610 C  CA    . MET A 1 201 ? 20.188  -35.631 28.015  1.00 110.88 ? 304  MET A CA    1 
ATOM   1611 C  C     . MET A 1 201 ? 19.474  -36.800 27.345  1.00 106.46 ? 304  MET A C     1 
ATOM   1612 O  O     . MET A 1 201 ? 19.853  -37.957 27.559  1.00 103.78 ? 304  MET A O     1 
ATOM   1613 C  CB    . MET A 1 201 ? 21.572  -35.427 27.405  1.00 118.36 ? 304  MET A CB    1 
ATOM   1614 C  CG    . MET A 1 201 ? 22.271  -34.163 27.882  1.00 125.79 ? 304  MET A CG    1 
ATOM   1615 S  SD    . MET A 1 201 ? 21.470  -32.656 27.296  1.00 116.10 ? 304  MET A SD    1 
ATOM   1616 C  CE    . MET A 1 201 ? 22.000  -32.637 25.587  1.00 119.93 ? 304  MET A CE    1 
ATOM   1617 N  N     . PRO A 1 202 ? 18.441  -36.546 26.545  1.00 108.60 ? 305  PRO A N     1 
ATOM   1618 C  CA    . PRO A 1 202 ? 17.689  -37.650 25.933  1.00 114.40 ? 305  PRO A CA    1 
ATOM   1619 C  C     . PRO A 1 202 ? 18.478  -38.390 24.863  1.00 117.55 ? 305  PRO A C     1 
ATOM   1620 O  O     . PRO A 1 202 ? 19.619  -38.030 24.553  1.00 114.20 ? 305  PRO A O     1 
ATOM   1621 C  CB    . PRO A 1 202 ? 16.462  -36.946 25.340  1.00 108.52 ? 305  PRO A CB    1 
ATOM   1622 C  CG    . PRO A 1 202 ? 16.918  -35.545 25.102  1.00 108.45 ? 305  PRO A CG    1 
ATOM   1623 C  CD    . PRO A 1 202 ? 17.874  -35.229 26.210  1.00 106.24 ? 305  PRO A CD    1 
ATOM   1624 N  N     . SER A 1 203 ? 17.870  -39.433 24.293  1.00 118.21 ? 306  SER A N     1 
ATOM   1625 C  CA    . SER A 1 203 ? 18.570  -40.257 23.314  1.00 124.71 ? 306  SER A CA    1 
ATOM   1626 C  C     . SER A 1 203 ? 18.825  -39.505 22.015  1.00 122.07 ? 306  SER A C     1 
ATOM   1627 O  O     . SER A 1 203 ? 19.852  -39.730 21.364  1.00 125.99 ? 306  SER A O     1 
ATOM   1628 C  CB    . SER A 1 203 ? 17.776  -41.534 23.041  1.00 133.84 ? 306  SER A CB    1 
ATOM   1629 O  OG    . SER A 1 203 ? 17.609  -42.292 24.227  1.00 136.58 ? 306  SER A OG    1 
ATOM   1630 N  N     . TYR A 1 204 ? 17.916  -38.615 21.621  1.00 119.35 ? 307  TYR A N     1 
ATOM   1631 C  CA    . TYR A 1 204 ? 18.095  -37.852 20.393  1.00 117.85 ? 307  TYR A CA    1 
ATOM   1632 C  C     . TYR A 1 204 ? 19.095  -36.711 20.541  1.00 122.48 ? 307  TYR A C     1 
ATOM   1633 O  O     . TYR A 1 204 ? 19.315  -35.977 19.572  1.00 123.82 ? 307  TYR A O     1 
ATOM   1634 C  CB    . TYR A 1 204 ? 16.749  -37.304 19.904  1.00 109.70 ? 307  TYR A CB    1 
ATOM   1635 C  CG    . TYR A 1 204 ? 16.050  -36.380 20.876  1.00 104.21 ? 307  TYR A CG    1 
ATOM   1636 C  CD1   . TYR A 1 204 ? 16.341  -35.022 20.908  1.00 102.34 ? 307  TYR A CD1   1 
ATOM   1637 C  CD2   . TYR A 1 204 ? 15.085  -36.862 21.751  1.00 105.46 ? 307  TYR A CD2   1 
ATOM   1638 C  CE1   . TYR A 1 204 ? 15.703  -34.174 21.791  1.00 99.67  ? 307  TYR A CE1   1 
ATOM   1639 C  CE2   . TYR A 1 204 ? 14.437  -36.019 22.636  1.00 100.32 ? 307  TYR A CE2   1 
ATOM   1640 C  CZ    . TYR A 1 204 ? 14.750  -34.676 22.651  1.00 97.24  ? 307  TYR A CZ    1 
ATOM   1641 O  OH    . TYR A 1 204 ? 14.112  -33.831 23.530  1.00 95.08  ? 307  TYR A OH    1 
ATOM   1642 N  N     . SER A 1 205 ? 19.699  -36.542 21.720  1.00 125.11 ? 308  SER A N     1 
ATOM   1643 C  CA    . SER A 1 205 ? 20.714  -35.510 21.895  1.00 129.38 ? 308  SER A CA    1 
ATOM   1644 C  C     . SER A 1 205 ? 21.965  -35.789 21.073  1.00 129.35 ? 308  SER A C     1 
ATOM   1645 O  O     . SER A 1 205 ? 22.729  -34.859 20.794  1.00 129.60 ? 308  SER A O     1 
ATOM   1646 C  CB    . SER A 1 205 ? 21.081  -35.373 23.374  1.00 121.69 ? 308  SER A CB    1 
ATOM   1647 O  OG    . SER A 1 205 ? 21.623  -36.578 23.884  1.00 123.12 ? 308  SER A OG    1 
ATOM   1648 N  N     . ARG A 1 206 ? 22.190  -37.040 20.685  1.00 138.85 ? 309  ARG A N     1 
ATOM   1649 C  CA    . ARG A 1 206 ? 23.294  -37.409 19.811  1.00 154.54 ? 309  ARG A CA    1 
ATOM   1650 C  C     . ARG A 1 206 ? 22.774  -37.562 18.388  1.00 153.16 ? 309  ARG A C     1 
ATOM   1651 O  O     . ARG A 1 206 ? 21.766  -38.240 18.160  1.00 152.30 ? 309  ARG A O     1 
ATOM   1652 C  CB    . ARG A 1 206 ? 23.953  -38.705 20.285  1.00 156.02 ? 309  ARG A CB    1 
ATOM   1653 C  CG    . ARG A 1 206 ? 24.584  -38.605 21.665  1.00 164.77 ? 309  ARG A CG    1 
ATOM   1654 C  CD    . ARG A 1 206 ? 25.157  -39.939 22.114  1.00 175.17 ? 309  ARG A CD    1 
ATOM   1655 N  NE    . ARG A 1 206 ? 24.116  -40.932 22.346  1.00 175.90 ? 309  ARG A NE    1 
ATOM   1656 C  CZ    . ARG A 1 206 ? 23.525  -41.137 23.515  1.00 180.30 ? 309  ARG A CZ    1 
ATOM   1657 N  NH1   . ARG A 1 206 ? 23.848  -40.432 24.587  1.00 180.76 ? 309  ARG A NH1   1 
ATOM   1658 N  NH2   . ARG A 1 206 ? 22.586  -42.075 23.612  1.00 174.44 ? 309  ARG A NH2   1 
ATOM   1659 N  N     . ARG A 1 207 ? 23.456  -36.926 17.440  1.00 148.45 ? 310  ARG A N     1 
ATOM   1660 C  CA    . ARG A 1 207 ? 23.035  -36.945 16.043  1.00 150.84 ? 310  ARG A CA    1 
ATOM   1661 C  C     . ARG A 1 207 ? 23.069  -38.355 15.461  1.00 147.49 ? 310  ARG A C     1 
ATOM   1662 O  O     . ARG A 1 207 ? 22.101  -38.805 14.848  1.00 138.67 ? 310  ARG A O     1 
ATOM   1663 C  CB    . ARG A 1 207 ? 23.918  -36.016 15.208  1.00 151.64 ? 310  ARG A CB    1 
ATOM   1664 C  CG    . ARG A 1 207 ? 23.585  -36.012 13.727  1.00 153.94 ? 310  ARG A CG    1 
ATOM   1665 C  CD    . ARG A 1 207 ? 24.492  -35.062 12.966  1.00 158.02 ? 310  ARG A CD    1 
ATOM   1666 N  NE    . ARG A 1 207 ? 24.432  -33.711 13.509  1.00 155.09 ? 310  ARG A NE    1 
ATOM   1667 C  CZ    . ARG A 1 207 ? 23.536  -32.801 13.154  1.00 152.41 ? 310  ARG A CZ    1 
ATOM   1668 N  NH1   . ARG A 1 207 ? 22.606  -33.063 12.249  1.00 151.44 ? 310  ARG A NH1   1 
ATOM   1669 N  NH2   . ARG A 1 207 ? 23.572  -31.599 13.721  1.00 150.07 ? 310  ARG A NH2   1 
ATOM   1670 N  N     . THR A 1 221 ? 29.683  -22.181 -1.388  1.00 112.00 ? 324  THR A N     1 
ATOM   1671 C  CA    . THR A 1 221 ? 28.484  -21.351 -1.377  1.00 117.25 ? 324  THR A CA    1 
ATOM   1672 C  C     . THR A 1 221 ? 28.775  -19.965 -1.945  1.00 114.71 ? 324  THR A C     1 
ATOM   1673 O  O     . THR A 1 221 ? 29.931  -19.553 -2.035  1.00 116.50 ? 324  THR A O     1 
ATOM   1674 C  CB    . THR A 1 221 ? 27.909  -21.203 0.047   1.00 115.45 ? 324  THR A CB    1 
ATOM   1675 O  OG1   . THR A 1 221 ? 28.855  -20.524 0.881   1.00 119.47 ? 324  THR A OG1   1 
ATOM   1676 C  CG2   . THR A 1 221 ? 27.608  -22.568 0.644   1.00 113.65 ? 324  THR A CG2   1 
ATOM   1677 N  N     . LYS A 1 222 ? 27.720  -19.251 -2.327  1.00 113.14 ? 325  LYS A N     1 
ATOM   1678 C  CA    . LYS A 1 222 ? 27.830  -17.910 -2.881  1.00 115.06 ? 325  LYS A CA    1 
ATOM   1679 C  C     . LYS A 1 222 ? 27.049  -16.928 -2.020  1.00 115.21 ? 325  LYS A C     1 
ATOM   1680 O  O     . LYS A 1 222 ? 25.946  -17.234 -1.557  1.00 109.15 ? 325  LYS A O     1 
ATOM   1681 C  CB    . LYS A 1 222 ? 27.316  -17.861 -4.322  1.00 114.96 ? 325  LYS A CB    1 
ATOM   1682 C  CG    . LYS A 1 222 ? 28.156  -18.655 -5.305  1.00 123.29 ? 325  LYS A CG    1 
ATOM   1683 C  CD    . LYS A 1 222 ? 27.598  -18.550 -6.713  1.00 130.26 ? 325  LYS A CD    1 
ATOM   1684 C  CE    . LYS A 1 222 ? 28.547  -19.168 -7.725  1.00 144.69 ? 325  LYS A CE    1 
ATOM   1685 N  NZ    . LYS A 1 222 ? 29.870  -18.487 -7.731  1.00 143.93 ? 325  LYS A NZ    1 
ATOM   1686 N  N     . SER A 1 223 ? 27.626  -15.749 -1.809  1.00 113.59 ? 326  SER A N     1 
ATOM   1687 C  CA    . SER A 1 223 ? 26.956  -14.718 -1.032  1.00 108.79 ? 326  SER A CA    1 
ATOM   1688 C  C     . SER A 1 223 ? 25.721  -14.211 -1.768  1.00 106.24 ? 326  SER A C     1 
ATOM   1689 O  O     . SER A 1 223 ? 25.629  -14.275 -2.996  1.00 117.56 ? 326  SER A O     1 
ATOM   1690 C  CB    . SER A 1 223 ? 27.910  -13.557 -0.750  1.00 108.38 ? 326  SER A CB    1 
ATOM   1691 O  OG    . SER A 1 223 ? 27.242  -12.491 -0.097  1.00 105.12 ? 326  SER A OG    1 
ATOM   1692 N  N     . LEU A 1 224 ? 24.756  -13.709 -0.995  1.00 107.99 ? 327  LEU A N     1 
ATOM   1693 C  CA    . LEU A 1 224 ? 23.569  -13.111 -1.594  1.00 110.53 ? 327  LEU A CA    1 
ATOM   1694 C  C     . LEU A 1 224 ? 23.923  -11.876 -2.409  1.00 112.31 ? 327  LEU A C     1 
ATOM   1695 O  O     . LEU A 1 224 ? 23.243  -11.562 -3.393  1.00 109.31 ? 327  LEU A O     1 
ATOM   1696 C  CB    . LEU A 1 224 ? 22.557  -12.753 -0.503  1.00 110.24 ? 327  LEU A CB    1 
ATOM   1697 C  CG    . LEU A 1 224 ? 21.227  -12.136 -0.946  1.00 109.28 ? 327  LEU A CG    1 
ATOM   1698 C  CD1   . LEU A 1 224 ? 20.305  -13.196 -1.533  1.00 108.81 ? 327  LEU A CD1   1 
ATOM   1699 C  CD2   . LEU A 1 224 ? 20.556  -11.406 0.207   1.00 99.94  ? 327  LEU A CD2   1 
ATOM   1700 N  N     . TRP A 1 225 ? 24.990  -11.178 -2.028  1.00 117.40 ? 328  TRP A N     1 
ATOM   1701 C  CA    . TRP A 1 225 ? 25.365  -9.908  -2.631  1.00 117.80 ? 328  TRP A CA    1 
ATOM   1702 C  C     . TRP A 1 225 ? 26.247  -10.067 -3.863  1.00 114.94 ? 328  TRP A C     1 
ATOM   1703 O  O     . TRP A 1 225 ? 26.767  -9.069  -4.372  1.00 116.89 ? 328  TRP A O     1 
ATOM   1704 C  CB    . TRP A 1 225 ? 26.061  -9.027  -1.591  1.00 116.83 ? 328  TRP A CB    1 
ATOM   1705 C  CG    . TRP A 1 225 ? 25.155  -8.610  -0.467  1.00 119.42 ? 328  TRP A CG    1 
ATOM   1706 C  CD1   . TRP A 1 225 ? 23.844  -8.957  -0.295  1.00 118.75 ? 328  TRP A CD1   1 
ATOM   1707 C  CD2   . TRP A 1 225 ? 25.491  -7.763  0.637   1.00 126.87 ? 328  TRP A CD2   1 
ATOM   1708 N  NE1   . TRP A 1 225 ? 23.346  -8.381  0.848   1.00 111.76 ? 328  TRP A NE1   1 
ATOM   1709 C  CE2   . TRP A 1 225 ? 24.337  -7.642  1.438   1.00 116.47 ? 328  TRP A CE2   1 
ATOM   1710 C  CE3   . TRP A 1 225 ? 26.656  -7.096  1.027   1.00 126.60 ? 328  TRP A CE3   1 
ATOM   1711 C  CZ2   . TRP A 1 225 ? 24.315  -6.882  2.604   1.00 119.43 ? 328  TRP A CZ2   1 
ATOM   1712 C  CZ3   . TRP A 1 225 ? 26.632  -6.343  2.184   1.00 122.51 ? 328  TRP A CZ3   1 
ATOM   1713 C  CH2   . TRP A 1 225 ? 25.470  -6.241  2.958   1.00 124.00 ? 328  TRP A CH2   1 
ATOM   1714 N  N     . VAL A 1 226 ? 26.428  -11.293 -4.352  1.00 116.97 ? 329  VAL A N     1 
ATOM   1715 C  CA    . VAL A 1 226 ? 27.153  -11.536 -5.595  1.00 114.74 ? 329  VAL A CA    1 
ATOM   1716 C  C     . VAL A 1 226 ? 26.227  -11.928 -6.737  1.00 112.85 ? 329  VAL A C     1 
ATOM   1717 O  O     . VAL A 1 226 ? 26.690  -12.023 -7.886  1.00 121.07 ? 329  VAL A O     1 
ATOM   1718 C  CB    . VAL A 1 226 ? 28.249  -12.608 -5.408  1.00 111.46 ? 329  VAL A CB    1 
ATOM   1719 C  CG1   . VAL A 1 226 ? 27.660  -14.009 -5.525  1.00 109.46 ? 329  VAL A CG1   1 
ATOM   1720 C  CG2   . VAL A 1 226 ? 29.391  -12.401 -6.398  1.00 133.07 ? 329  VAL A CG2   1 
ATOM   1721 N  N     . ILE A 1 227 ? 24.942  -12.138 -6.468  1.00 113.17 ? 330  ILE A N     1 
ATOM   1722 C  CA    . ILE A 1 227 ? 23.989  -12.585 -7.477  1.00 116.91 ? 330  ILE A CA    1 
ATOM   1723 C  C     . ILE A 1 227 ? 23.479  -11.359 -8.226  1.00 116.12 ? 330  ILE A C     1 
ATOM   1724 O  O     . ILE A 1 227 ? 22.711  -10.563 -7.681  1.00 116.27 ? 330  ILE A O     1 
ATOM   1725 C  CB    . ILE A 1 227 ? 22.835  -13.371 -6.845  1.00 113.01 ? 330  ILE A CB    1 
ATOM   1726 C  CG1   . ILE A 1 227 ? 23.371  -14.407 -5.852  1.00 104.99 ? 330  ILE A CG1   1 
ATOM   1727 C  CG2   . ILE A 1 227 ? 21.998  -14.039 -7.921  1.00 118.78 ? 330  ILE A CG2   1 
ATOM   1728 C  CD1   . ILE A 1 227 ? 24.320  -15.416 -6.461  1.00 106.40 ? 330  ILE A CD1   1 
ATOM   1729 N  N     . ASN A 1 228 ? 23.897  -11.210 -9.483  1.00 120.84 ? 331  ASN A N     1 
ATOM   1730 C  CA    . ASN A 1 228 ? 23.505  -10.066 -10.306 1.00 123.23 ? 331  ASN A CA    1 
ATOM   1731 C  C     . ASN A 1 228 ? 22.286  -10.460 -11.132 1.00 116.60 ? 331  ASN A C     1 
ATOM   1732 O  O     . ASN A 1 228 ? 22.397  -10.885 -12.283 1.00 118.38 ? 331  ASN A O     1 
ATOM   1733 C  CB    . ASN A 1 228 ? 24.661  -9.616  -11.190 1.00 117.60 ? 331  ASN A CB    1 
ATOM   1734 C  CG    . ASN A 1 228 ? 24.420  -8.255  -11.820 1.00 119.58 ? 331  ASN A CG    1 
ATOM   1735 O  OD1   . ASN A 1 228 ? 23.305  -7.733  -11.797 1.00 111.93 ? 331  ASN A OD1   1 
ATOM   1736 N  ND2   . ASN A 1 228 ? 25.470  -7.676  -12.391 1.00 132.61 ? 331  ASN A ND2   1 
ATOM   1737 N  N     . SER A 1 229 ? 21.108  -10.311 -10.532 1.00 116.98 ? 332  SER A N     1 
ATOM   1738 C  CA    . SER A 1 229 ? 19.833  -10.585 -11.184 1.00 110.10 ? 332  SER A CA    1 
ATOM   1739 C  C     . SER A 1 229 ? 18.726  -10.108 -10.255 1.00 113.20 ? 332  SER A C     1 
ATOM   1740 O  O     . SER A 1 229 ? 18.962  -9.807  -9.082  1.00 113.70 ? 332  SER A O     1 
ATOM   1741 C  CB    . SER A 1 229 ? 19.661  -12.071 -11.512 1.00 110.02 ? 332  SER A CB    1 
ATOM   1742 O  OG    . SER A 1 229 ? 19.491  -12.837 -10.331 1.00 113.80 ? 332  SER A OG    1 
ATOM   1743 N  N     . ALA A 1 230 ? 17.513  -10.050 -10.790 1.00 109.37 ? 333  ALA A N     1 
ATOM   1744 C  CA    . ALA A 1 230 ? 16.341  -9.671  -10.015 1.00 100.59 ? 333  ALA A CA    1 
ATOM   1745 C  C     . ALA A 1 230 ? 15.629  -10.914 -9.495  1.00 109.12 ? 333  ALA A C     1 
ATOM   1746 O  O     . ALA A 1 230 ? 15.865  -12.036 -9.948  1.00 115.50 ? 333  ALA A O     1 
ATOM   1747 C  CB    . ALA A 1 230 ? 15.386  -8.821  -10.856 1.00 99.85  ? 333  ALA A CB    1 
ATOM   1748 N  N     . LEU A 1 231 ? 14.744  -10.698 -8.524  1.00 104.72 ? 334  LEU A N     1 
ATOM   1749 C  CA    . LEU A 1 231 ? 13.988  -11.796 -7.939  1.00 101.87 ? 334  LEU A CA    1 
ATOM   1750 C  C     . LEU A 1 231 ? 12.919  -12.277 -8.912  1.00 101.99 ? 334  LEU A C     1 
ATOM   1751 O  O     . LEU A 1 231 ? 12.111  -11.485 -9.404  1.00 105.47 ? 334  LEU A O     1 
ATOM   1752 C  CB    . LEU A 1 231 ? 13.350  -11.356 -6.622  1.00 100.70 ? 334  LEU A CB    1 
ATOM   1753 C  CG    . LEU A 1 231 ? 12.467  -12.371 -5.891  1.00 96.98  ? 334  LEU A CG    1 
ATOM   1754 C  CD1   . LEU A 1 231 ? 13.272  -13.589 -5.466  1.00 94.99  ? 334  LEU A CD1   1 
ATOM   1755 C  CD2   . LEU A 1 231 ? 11.791  -11.725 -4.691  1.00 92.64  ? 334  LEU A CD2   1 
ATOM   1756 N  N     . ARG A 1 232 ? 12.922  -13.579 -9.196  1.00 95.38  ? 335  ARG A N     1 
ATOM   1757 C  CA    . ARG A 1 232 ? 11.924  -14.188 -10.064 1.00 100.05 ? 335  ARG A CA    1 
ATOM   1758 C  C     . ARG A 1 232 ? 11.452  -15.492 -9.444  1.00 99.20  ? 335  ARG A C     1 
ATOM   1759 O  O     . ARG A 1 232 ? 12.266  -16.365 -9.133  1.00 101.98 ? 335  ARG A O     1 
ATOM   1760 C  CB    . ARG A 1 232 ? 12.480  -14.446 -11.469 1.00 112.00 ? 335  ARG A CB    1 
ATOM   1761 C  CG    . ARG A 1 232 ? 12.770  -13.190 -12.267 1.00 110.00 ? 335  ARG A CG    1 
ATOM   1762 C  CD    . ARG A 1 232 ? 13.307  -13.543 -13.639 1.00 114.45 ? 335  ARG A CD    1 
ATOM   1763 N  NE    . ARG A 1 232 ? 13.779  -12.372 -14.365 1.00 120.94 ? 335  ARG A NE    1 
ATOM   1764 C  CZ    . ARG A 1 232 ? 14.428  -12.422 -15.520 1.00 119.33 ? 335  ARG A CZ    1 
ATOM   1765 N  NH1   . ARG A 1 232 ? 14.698  -13.575 -16.111 1.00 107.17 ? 335  ARG A NH1   1 
ATOM   1766 N  NH2   . ARG A 1 232 ? 14.820  -11.289 -16.094 1.00 121.58 ? 335  ARG A NH2   1 
ATOM   1767 N  N     . ILE A 1 233 ? 10.139  -15.618 -9.269  1.00 99.92  ? 336  ILE A N     1 
ATOM   1768 C  CA    . ILE A 1 233 ? 9.520   -16.813 -8.713  1.00 104.01 ? 336  ILE A CA    1 
ATOM   1769 C  C     . ILE A 1 233 ? 8.552   -17.376 -9.743  1.00 105.81 ? 336  ILE A C     1 
ATOM   1770 O  O     . ILE A 1 233 ? 7.794   -16.628 -10.372 1.00 107.77 ? 336  ILE A O     1 
ATOM   1771 C  CB    . ILE A 1 233 ? 8.798   -16.511 -7.384  1.00 99.12  ? 336  ILE A CB    1 
ATOM   1772 C  CG1   . ILE A 1 233 ? 9.776   -15.895 -6.381  1.00 99.63  ? 336  ILE A CG1   1 
ATOM   1773 C  CG2   . ILE A 1 233 ? 8.172   -17.774 -6.813  1.00 92.08  ? 336  ILE A CG2   1 
ATOM   1774 C  CD1   . ILE A 1 233 ? 9.133   -15.452 -5.089  1.00 87.95  ? 336  ILE A CD1   1 
ATOM   1775 N  N     . LYS A 1 234 ? 8.582   -18.693 -9.916  1.00 102.47 ? 337  LYS A N     1 
ATOM   1776 C  CA    . LYS A 1 234 ? 7.762   -19.377 -10.906 1.00 106.11 ? 337  LYS A CA    1 
ATOM   1777 C  C     . LYS A 1 234 ? 6.590   -20.060 -10.211 1.00 102.99 ? 337  LYS A C     1 
ATOM   1778 O  O     . LYS A 1 234 ? 6.789   -20.854 -9.285  1.00 106.55 ? 337  LYS A O     1 
ATOM   1779 C  CB    . LYS A 1 234 ? 8.598   -20.395 -11.683 1.00 110.74 ? 337  LYS A CB    1 
ATOM   1780 C  CG    . LYS A 1 234 ? 7.833   -21.180 -12.733 1.00 107.84 ? 337  LYS A CG    1 
ATOM   1781 C  CD    . LYS A 1 234 ? 8.726   -22.235 -13.369 1.00 109.34 ? 337  LYS A CD    1 
ATOM   1782 C  CE    . LYS A 1 234 ? 7.953   -23.128 -14.322 1.00 113.04 ? 337  LYS A CE    1 
ATOM   1783 N  NZ    . LYS A 1 234 ? 8.809   -24.221 -14.860 1.00 127.46 ? 337  LYS A NZ    1 
ATOM   1784 N  N     . ILE A 1 235 ? 5.375   -19.738 -10.649 1.00 102.88 ? 338  ILE A N     1 
ATOM   1785 C  CA    . ILE A 1 235 ? 4.165   -20.434 -10.225 1.00 100.95 ? 338  ILE A CA    1 
ATOM   1786 C  C     . ILE A 1 235 ? 3.829   -21.473 -11.285 1.00 107.92 ? 338  ILE A C     1 
ATOM   1787 O  O     . ILE A 1 235 ? 3.788   -21.158 -12.481 1.00 107.21 ? 338  ILE A O     1 
ATOM   1788 C  CB    . ILE A 1 235 ? 2.995   -19.456 -10.012 1.00 96.59  ? 338  ILE A CB    1 
ATOM   1789 C  CG1   . ILE A 1 235 ? 3.086   -18.780 -8.639  1.00 110.82 ? 338  ILE A CG1   1 
ATOM   1790 C  CG2   . ILE A 1 235 ? 1.658   -20.169 -10.158 1.00 98.66  ? 338  ILE A CG2   1 
ATOM   1791 C  CD1   . ILE A 1 235 ? 4.088   -17.650 -8.560  1.00 109.47 ? 338  ILE A CD1   1 
ATOM   1792 N  N     . LEU A 1 236 ? 3.599   -22.712 -10.853 1.00 108.61 ? 339  LEU A N     1 
ATOM   1793 C  CA    . LEU A 1 236 ? 3.364   -23.804 -11.791 1.00 113.01 ? 339  LEU A CA    1 
ATOM   1794 C  C     . LEU A 1 236 ? 1.878   -24.102 -11.940 1.00 120.84 ? 339  LEU A C     1 
ATOM   1795 O  O     . LEU A 1 236 ? 1.224   -23.587 -12.853 1.00 125.41 ? 339  LEU A O     1 
ATOM   1796 C  CB    . LEU A 1 236 ? 4.112   -25.065 -11.348 1.00 114.08 ? 339  LEU A CB    1 
ATOM   1797 C  CG    . LEU A 1 236 ? 5.573   -25.187 -11.788 1.00 120.25 ? 339  LEU A CG    1 
ATOM   1798 C  CD1   . LEU A 1 236 ? 6.444   -24.150 -11.099 1.00 107.28 ? 339  LEU A CD1   1 
ATOM   1799 C  CD2   . LEU A 1 236 ? 6.100   -26.593 -11.535 1.00 126.64 ? 339  LEU A CD2   1 
ATOM   1800 N  N     . CYS A 1 237 ? 1.339   -24.937 -11.055 1.00 123.73 ? 340  CYS A N     1 
ATOM   1801 C  CA    . CYS A 1 237 ? -0.054  -25.349 -11.120 1.00 134.83 ? 340  CYS A CA    1 
ATOM   1802 C  C     . CYS A 1 237 ? -0.617  -25.402 -9.706  1.00 135.74 ? 340  CYS A C     1 
ATOM   1803 O  O     . CYS A 1 237 ? 0.069   -25.086 -8.729  1.00 127.59 ? 340  CYS A O     1 
ATOM   1804 C  CB    . CYS A 1 237 ? -0.195  -26.701 -11.830 1.00 137.43 ? 340  CYS A CB    1 
ATOM   1805 S  SG    . CYS A 1 237 ? 0.639   -28.070 -11.002 1.00 137.48 ? 340  CYS A SG    1 
ATOM   1806 N  N     . ALA A 1 238 ? -1.881  -25.806 -9.599  1.00 142.71 ? 341  ALA A N     1 
ATOM   1807 C  CA    . ALA A 1 238 ? -2.547  -25.903 -8.307  1.00 143.43 ? 341  ALA A CA    1 
ATOM   1808 C  C     . ALA A 1 238 ? -3.537  -27.056 -8.341  1.00 152.25 ? 341  ALA A C     1 
ATOM   1809 O  O     . ALA A 1 238 ? -4.354  -27.148 -9.262  1.00 160.29 ? 341  ALA A O     1 
ATOM   1810 C  CB    . ALA A 1 238 ? -3.263  -24.595 -7.953  1.00 136.67 ? 341  ALA A CB    1 
ATOM   1811 N  N     . THR A 1 239 ? -3.459  -27.926 -7.341  1.00 146.28 ? 342  THR A N     1 
ATOM   1812 C  CA    . THR A 1 239 ? -4.365  -29.054 -7.196  1.00 150.39 ? 342  THR A CA    1 
ATOM   1813 C  C     . THR A 1 239 ? -5.269  -28.842 -5.988  1.00 158.72 ? 342  THR A C     1 
ATOM   1814 O  O     . THR A 1 239 ? -5.068  -27.928 -5.183  1.00 156.96 ? 342  THR A O     1 
ATOM   1815 C  CB    . THR A 1 239 ? -3.588  -30.369 -7.061  1.00 149.16 ? 342  THR A CB    1 
ATOM   1816 O  OG1   . THR A 1 239 ? -4.490  -31.428 -6.719  1.00 156.60 ? 342  THR A OG1   1 
ATOM   1817 C  CG2   . THR A 1 239 ? -2.518  -30.250 -5.989  1.00 144.34 ? 342  THR A CG2   1 
ATOM   1818 N  N     . TYR A 1 240 ? -6.282  -29.703 -5.878  1.00 183.66 ? 343  TYR A N     1 
ATOM   1819 C  CA    . TYR A 1 240 ? -7.278  -29.656 -4.807  1.00 188.03 ? 343  TYR A CA    1 
ATOM   1820 C  C     . TYR A 1 240 ? -8.000  -28.313 -4.736  1.00 184.73 ? 343  TYR A C     1 
ATOM   1821 O  O     . TYR A 1 240 ? -8.582  -27.975 -3.701  1.00 182.28 ? 343  TYR A O     1 
ATOM   1822 C  CB    . TYR A 1 240 ? -6.653  -29.978 -3.443  1.00 185.33 ? 343  TYR A CB    1 
ATOM   1823 C  CG    . TYR A 1 240 ? -6.154  -31.398 -3.297  1.00 199.08 ? 343  TYR A CG    1 
ATOM   1824 C  CD1   . TYR A 1 240 ? -7.001  -32.412 -2.871  1.00 198.21 ? 343  TYR A CD1   1 
ATOM   1825 C  CD2   . TYR A 1 240 ? -4.832  -31.722 -3.572  1.00 204.52 ? 343  TYR A CD2   1 
ATOM   1826 C  CE1   . TYR A 1 240 ? -6.548  -33.711 -2.731  1.00 207.61 ? 343  TYR A CE1   1 
ATOM   1827 C  CE2   . TYR A 1 240 ? -4.369  -33.017 -3.435  1.00 212.56 ? 343  TYR A CE2   1 
ATOM   1828 C  CZ    . TYR A 1 240 ? -5.232  -34.007 -3.014  1.00 215.93 ? 343  TYR A CZ    1 
ATOM   1829 O  OH    . TYR A 1 240 ? -4.776  -35.298 -2.877  1.00 216.63 ? 343  TYR A OH    1 
ATOM   1830 N  N     . VAL A 1 241 ? -7.978  -27.536 -5.821  1.00 166.22 ? 344  VAL A N     1 
ATOM   1831 C  CA    . VAL A 1 241 ? -8.608  -26.219 -5.799  1.00 162.49 ? 344  VAL A CA    1 
ATOM   1832 C  C     . VAL A 1 241 ? -10.127 -26.353 -5.758  1.00 168.99 ? 344  VAL A C     1 
ATOM   1833 O  O     . VAL A 1 241 ? -10.810 -25.594 -5.059  1.00 164.52 ? 344  VAL A O     1 
ATOM   1834 C  CB    . VAL A 1 241 ? -8.132  -25.380 -7.000  1.00 156.60 ? 344  VAL A CB    1 
ATOM   1835 C  CG1   . VAL A 1 241 ? -8.300  -26.153 -8.302  1.00 158.54 ? 344  VAL A CG1   1 
ATOM   1836 C  CG2   . VAL A 1 241 ? -8.872  -24.051 -7.057  1.00 151.33 ? 344  VAL A CG2   1 
ATOM   1837 N  N     . ASN A 1 242 ? -10.673 -27.325 -6.487  1.00 174.40 ? 345  ASN A N     1 
ATOM   1838 C  CA    . ASN A 1 242 ? -12.111 -27.594 -6.523  1.00 171.91 ? 345  ASN A CA    1 
ATOM   1839 C  C     . ASN A 1 242 ? -12.915 -26.356 -6.916  1.00 170.90 ? 345  ASN A C     1 
ATOM   1840 O  O     . ASN A 1 242 ? -13.549 -25.720 -6.073  1.00 168.80 ? 345  ASN A O     1 
ATOM   1841 C  CB    . ASN A 1 242 ? -12.590 -28.126 -5.168  1.00 171.81 ? 345  ASN A CB    1 
ATOM   1842 C  CG    . ASN A 1 242 ? -14.021 -28.625 -5.211  1.00 175.28 ? 345  ASN A CG    1 
ATOM   1843 O  OD1   . ASN A 1 242 ? -14.276 -29.790 -5.516  1.00 180.70 ? 345  ASN A OD1   1 
ATOM   1844 N  ND2   . ASN A 1 242 ? -14.965 -27.742 -4.902  1.00 173.24 ? 345  ASN A ND2   1 
ATOM   1845 N  N     . LYS A 1 250 ? -13.087 -16.714 -13.042 1.00 147.74 ? 353  LYS A N     1 
ATOM   1846 C  CA    . LYS A 1 250 ? -11.993 -17.678 -13.005 1.00 143.55 ? 353  LYS A CA    1 
ATOM   1847 C  C     . LYS A 1 250 ? -11.103 -17.455 -11.785 1.00 138.47 ? 353  LYS A C     1 
ATOM   1848 O  O     . LYS A 1 250 ? -11.545 -16.891 -10.784 1.00 134.88 ? 353  LYS A O     1 
ATOM   1849 C  CB    . LYS A 1 250 ? -11.173 -17.601 -14.292 1.00 138.31 ? 353  LYS A CB    1 
ATOM   1850 C  CG    . LYS A 1 250 ? -10.893 -16.188 -14.769 1.00 136.91 ? 353  LYS A CG    1 
ATOM   1851 C  CD    . LYS A 1 250 ? -10.340 -16.199 -16.183 1.00 150.58 ? 353  LYS A CD    1 
ATOM   1852 C  CE    . LYS A 1 250 ? -11.295 -16.896 -17.140 1.00 142.07 ? 353  LYS A CE    1 
ATOM   1853 N  NZ    . LYS A 1 250 ? -10.757 -16.948 -18.525 1.00 127.78 ? 353  LYS A NZ    1 
ATOM   1854 N  N     . ILE A 1 251 ? -9.848  -17.898 -11.866 1.00 136.44 ? 354  ILE A N     1 
ATOM   1855 C  CA    . ILE A 1 251 ? -8.936  -17.851 -10.731 1.00 137.56 ? 354  ILE A CA    1 
ATOM   1856 C  C     . ILE A 1 251 ? -7.547  -17.438 -11.199 1.00 128.72 ? 354  ILE A C     1 
ATOM   1857 O  O     . ILE A 1 251 ? -7.123  -17.754 -12.314 1.00 131.93 ? 354  ILE A O     1 
ATOM   1858 C  CB    . ILE A 1 251 ? -8.871  -19.206 -9.991  1.00 128.67 ? 354  ILE A CB    1 
ATOM   1859 N  N     . TYR A 1 252 ? -6.837  -16.726 -10.326 1.00 121.59 ? 355  TYR A N     1 
ATOM   1860 C  CA    . TYR A 1 252 ? -5.456  -16.333 -10.561 1.00 114.97 ? 355  TYR A CA    1 
ATOM   1861 C  C     . TYR A 1 252 ? -4.707  -16.385 -9.237  1.00 122.20 ? 355  TYR A C     1 
ATOM   1862 O  O     . TYR A 1 252 ? -5.298  -16.574 -8.170  1.00 120.65 ? 355  TYR A O     1 
ATOM   1863 C  CB    . TYR A 1 252 ? -5.361  -14.935 -11.190 1.00 117.49 ? 355  TYR A CB    1 
ATOM   1864 C  CG    . TYR A 1 252 ? -5.908  -13.822 -10.323 1.00 125.66 ? 355  TYR A CG    1 
ATOM   1865 C  CD1   . TYR A 1 252 ? -5.087  -13.141 -9.431  1.00 128.39 ? 355  TYR A CD1   1 
ATOM   1866 C  CD2   . TYR A 1 252 ? -7.243  -13.448 -10.399 1.00 132.14 ? 355  TYR A CD2   1 
ATOM   1867 C  CE1   . TYR A 1 252 ? -5.581  -12.123 -8.637  1.00 125.41 ? 355  TYR A CE1   1 
ATOM   1868 C  CE2   . TYR A 1 252 ? -7.747  -12.431 -9.608  1.00 139.79 ? 355  TYR A CE2   1 
ATOM   1869 C  CZ    . TYR A 1 252 ? -6.911  -11.772 -8.730  1.00 137.52 ? 355  TYR A CZ    1 
ATOM   1870 O  OH    . TYR A 1 252 ? -7.406  -10.759 -7.941  1.00 131.06 ? 355  TYR A OH    1 
ATOM   1871 N  N     . VAL A 1 253 ? -3.390  -16.212 -9.309  1.00 119.50 ? 356  VAL A N     1 
ATOM   1872 C  CA    . VAL A 1 253 ? -2.526  -16.233 -8.133  1.00 112.76 ? 356  VAL A CA    1 
ATOM   1873 C  C     . VAL A 1 253 ? -1.882  -14.862 -7.989  1.00 113.79 ? 356  VAL A C     1 
ATOM   1874 O  O     . VAL A 1 253 ? -1.231  -14.373 -8.921  1.00 109.98 ? 356  VAL A O     1 
ATOM   1875 C  CB    . VAL A 1 253 ? -1.459  -17.336 -8.222  1.00 108.08 ? 356  VAL A CB    1 
ATOM   1876 C  CG1   . VAL A 1 253 ? -0.435  -17.171 -7.109  1.00 91.79  ? 356  VAL A CG1   1 
ATOM   1877 C  CG2   . VAL A 1 253 ? -2.113  -18.707 -8.143  1.00 109.88 ? 356  VAL A CG2   1 
ATOM   1878 N  N     . ARG A 1 254 ? -2.068  -14.245 -6.826  1.00 113.60 ? 357  ARG A N     1 
ATOM   1879 C  CA    . ARG A 1 254 ? -1.488  -12.948 -6.508  1.00 108.51 ? 357  ARG A CA    1 
ATOM   1880 C  C     . ARG A 1 254 ? -0.334  -13.149 -5.540  1.00 103.99 ? 357  ARG A C     1 
ATOM   1881 O  O     . ARG A 1 254 ? -0.493  -13.818 -4.514  1.00 111.10 ? 357  ARG A O     1 
ATOM   1882 C  CB    . ARG A 1 254 ? -2.537  -12.017 -5.898  1.00 107.64 ? 357  ARG A CB    1 
ATOM   1883 C  CG    . ARG A 1 254 ? -2.078  -10.580 -5.729  1.00 109.50 ? 357  ARG A CG    1 
ATOM   1884 C  CD    . ARG A 1 254 ? -3.237  -9.690  -5.315  1.00 112.14 ? 357  ARG A CD    1 
ATOM   1885 N  NE    . ARG A 1 254 ? -3.126  -8.347  -5.872  1.00 110.12 ? 357  ARG A NE    1 
ATOM   1886 C  CZ    . ARG A 1 254 ? -2.487  -7.343  -5.288  1.00 111.32 ? 357  ARG A CZ    1 
ATOM   1887 N  NH1   . ARG A 1 254 ? -1.878  -7.496  -4.123  1.00 115.32 ? 357  ARG A NH1   1 
ATOM   1888 N  NH2   . ARG A 1 254 ? -2.460  -6.155  -5.885  1.00 102.02 ? 357  ARG A NH2   1 
ATOM   1889 N  N     . THR A 1 255 ? 0.819   -12.576 -5.862  1.00 101.37 ? 358  THR A N     1 
ATOM   1890 C  CA    . THR A 1 255 ? 2.022   -12.729 -5.059  1.00 108.08 ? 358  THR A CA    1 
ATOM   1891 C  C     . THR A 1 255 ? 2.429   -11.386 -4.460  1.00 107.68 ? 358  THR A C     1 
ATOM   1892 O  O     . THR A 1 255 ? 1.799   -10.351 -4.697  1.00 105.60 ? 358  THR A O     1 
ATOM   1893 C  CB    . THR A 1 255 ? 3.162   -13.315 -5.896  1.00 104.03 ? 358  THR A CB    1 
ATOM   1894 O  OG1   . THR A 1 255 ? 3.548   -12.374 -6.903  1.00 106.97 ? 358  THR A OG1   1 
ATOM   1895 C  CG2   . THR A 1 255 ? 2.723   -14.611 -6.560  1.00 103.56 ? 358  THR A CG2   1 
ATOM   1896 N  N     . GLY A 1 256 ? 3.503   -11.416 -3.676  1.00 101.87 ? 359  GLY A N     1 
ATOM   1897 C  CA    . GLY A 1 256 ? 4.040   -10.222 -3.056  1.00 86.63  ? 359  GLY A CA    1 
ATOM   1898 C  C     . GLY A 1 256 ? 5.216   -10.529 -2.154  1.00 95.01  ? 359  GLY A C     1 
ATOM   1899 O  O     . GLY A 1 256 ? 5.279   -11.608 -1.559  1.00 103.69 ? 359  GLY A O     1 
ATOM   1900 N  N     . ILE A 1 257 ? 6.157   -9.596  -2.045  1.00 94.03  ? 360  ILE A N     1 
ATOM   1901 C  CA    . ILE A 1 257 ? 7.330   -9.753  -1.193  1.00 94.89  ? 360  ILE A CA    1 
ATOM   1902 C  C     . ILE A 1 257 ? 7.215   -8.736  -0.067  1.00 99.00  ? 360  ILE A C     1 
ATOM   1903 O  O     . ILE A 1 257 ? 7.284   -7.523  -0.303  1.00 96.55  ? 360  ILE A O     1 
ATOM   1904 C  CB    . ILE A 1 257 ? 8.637   -9.574  -1.976  1.00 89.14  ? 360  ILE A CB    1 
ATOM   1905 C  CG1   . ILE A 1 257 ? 8.636   -10.463 -3.221  1.00 104.40 ? 360  ILE A CG1   1 
ATOM   1906 C  CG2   . ILE A 1 257 ? 9.833   -9.899  -1.093  1.00 83.46  ? 360  ILE A CG2   1 
ATOM   1907 C  CD1   . ILE A 1 257 ? 8.491   -11.938 -2.919  1.00 98.14  ? 360  ILE A CD1   1 
ATOM   1908 N  N     . TYR A 1 258 ? 7.040   -9.225  1.158   1.00 102.54 ? 361  TYR A N     1 
ATOM   1909 C  CA    . TYR A 1 258 ? 6.864   -8.377  2.325   1.00 99.21  ? 361  TYR A CA    1 
ATOM   1910 C  C     . TYR A 1 258 ? 8.006   -8.581  3.309   1.00 92.79  ? 361  TYR A C     1 
ATOM   1911 O  O     . TYR A 1 258 ? 8.609   -9.657  3.377   1.00 87.01  ? 361  TYR A O     1 
ATOM   1912 C  CB    . TYR A 1 258 ? 5.527   -8.659  3.025   1.00 96.74  ? 361  TYR A CB    1 
ATOM   1913 C  CG    . TYR A 1 258 ? 4.320   -8.243  2.218   1.00 111.91 ? 361  TYR A CG    1 
ATOM   1914 C  CD1   . TYR A 1 258 ? 3.812   -9.064  1.219   1.00 102.95 ? 361  TYR A CD1   1 
ATOM   1915 C  CD2   . TYR A 1 258 ? 3.688   -7.028  2.453   1.00 104.77 ? 361  TYR A CD2   1 
ATOM   1916 C  CE1   . TYR A 1 258 ? 2.711   -8.687  0.478   1.00 101.75 ? 361  TYR A CE1   1 
ATOM   1917 C  CE2   . TYR A 1 258 ? 2.585   -6.643  1.717   1.00 104.14 ? 361  TYR A CE2   1 
ATOM   1918 C  CZ    . TYR A 1 258 ? 2.101   -7.476  0.730   1.00 109.07 ? 361  TYR A CZ    1 
ATOM   1919 O  OH    . TYR A 1 258 ? 1.002   -7.099  -0.007  1.00 111.73 ? 361  TYR A OH    1 
ATOM   1920 N  N     . HIS A 1 259 ? 8.300   -7.527  4.064   1.00 102.88 ? 362  HIS A N     1 
ATOM   1921 C  CA    . HIS A 1 259 ? 9.218   -7.592  5.194   1.00 104.17 ? 362  HIS A CA    1 
ATOM   1922 C  C     . HIS A 1 259 ? 8.420   -7.358  6.473   1.00 101.29 ? 362  HIS A C     1 
ATOM   1923 O  O     . HIS A 1 259 ? 8.594   -6.361  7.178   1.00 106.74 ? 362  HIS A O     1 
ATOM   1924 C  CB    . HIS A 1 259 ? 10.353  -6.568  5.029   1.00 101.15 ? 362  HIS A CB    1 
ATOM   1925 C  CG    . HIS A 1 259 ? 11.370  -6.606  6.129   1.00 106.60 ? 362  HIS A CG    1 
ATOM   1926 N  ND1   . HIS A 1 259 ? 11.404  -5.674  7.144   1.00 105.73 ? 362  HIS A ND1   1 
ATOM   1927 C  CD2   . HIS A 1 259 ? 12.388  -7.465  6.373   1.00 106.30 ? 362  HIS A CD2   1 
ATOM   1928 C  CE1   . HIS A 1 259 ? 12.400  -5.956  7.965   1.00 97.92  ? 362  HIS A CE1   1 
ATOM   1929 N  NE2   . HIS A 1 259 ? 13.013  -7.038  7.519   1.00 96.43  ? 362  HIS A NE2   1 
ATOM   1930 N  N     . GLY A 1 260 ? 7.514   -8.292  6.755   1.00 104.45 ? 363  GLY A N     1 
ATOM   1931 C  CA    . GLY A 1 260 ? 6.664   -8.201  7.924   1.00 102.91 ? 363  GLY A CA    1 
ATOM   1932 C  C     . GLY A 1 260 ? 5.637   -7.092  7.836   1.00 105.49 ? 363  GLY A C     1 
ATOM   1933 O  O     . GLY A 1 260 ? 5.645   -6.164  8.651   1.00 119.01 ? 363  GLY A O     1 
ATOM   1934 N  N     . GLY A 1 261 ? 4.747   -7.172  6.847   1.00 98.75  ? 364  GLY A N     1 
ATOM   1935 C  CA    . GLY A 1 261 ? 3.683   -6.208  6.684   1.00 99.26  ? 364  GLY A CA    1 
ATOM   1936 C  C     . GLY A 1 261 ? 4.015   -5.023  5.802   1.00 100.45 ? 364  GLY A C     1 
ATOM   1937 O  O     . GLY A 1 261 ? 3.095   -4.346  5.327   1.00 98.40  ? 364  GLY A O     1 
ATOM   1938 N  N     . GLU A 1 262 ? 5.298   -4.746  5.573   1.00 104.98 ? 365  GLU A N     1 
ATOM   1939 C  CA    . GLU A 1 262 ? 5.706   -3.659  4.696   1.00 109.79 ? 365  GLU A CA    1 
ATOM   1940 C  C     . GLU A 1 262 ? 6.032   -4.217  3.322   1.00 116.05 ? 365  GLU A C     1 
ATOM   1941 O  O     . GLU A 1 262 ? 6.925   -5.072  3.211   1.00 108.27 ? 365  GLU A O     1 
ATOM   1942 C  CB    . GLU A 1 262 ? 6.916   -2.931  5.270   1.00 117.27 ? 365  GLU A CB    1 
ATOM   1943 C  CG    . GLU A 1 262 ? 6.636   -2.165  6.554   1.00 143.31 ? 365  GLU A CG    1 
ATOM   1944 C  CD    . GLU A 1 262 ? 7.902   -1.645  7.212   1.00 144.48 ? 365  GLU A CD    1 
ATOM   1945 O  OE1   . GLU A 1 262 ? 8.923   -2.366  7.193   1.00 127.62 ? 365  GLU A OE1   1 
ATOM   1946 O  OE2   . GLU A 1 262 ? 7.878   -0.515  7.745   1.00 135.63 ? 365  GLU A OE2   1 
ATOM   1947 N  N     . PRO A 1 263 ? 5.348   -3.787  2.261   1.00 106.45 ? 366  PRO A N     1 
ATOM   1948 C  CA    . PRO A 1 263 ? 5.648   -4.320  0.924   1.00 102.39 ? 366  PRO A CA    1 
ATOM   1949 C  C     . PRO A 1 263 ? 7.023   -3.869  0.452   1.00 101.54 ? 366  PRO A C     1 
ATOM   1950 O  O     . PRO A 1 263 ? 7.322   -2.674  0.418   1.00 100.20 ? 366  PRO A O     1 
ATOM   1951 C  CB    . PRO A 1 263 ? 4.531   -3.739  0.046   1.00 101.48 ? 366  PRO A CB    1 
ATOM   1952 C  CG    . PRO A 1 263 ? 3.467   -3.288  1.007   1.00 101.04 ? 366  PRO A CG    1 
ATOM   1953 C  CD    . PRO A 1 263 ? 4.196   -2.872  2.243   1.00 103.92 ? 366  PRO A CD    1 
ATOM   1954 N  N     . LEU A 1 264 ? 7.863   -4.841  0.093   1.00 100.31 ? 367  LEU A N     1 
ATOM   1955 C  CA    . LEU A 1 264 ? 9.195   -4.523  -0.409  1.00 102.68 ? 367  LEU A CA    1 
ATOM   1956 C  C     . LEU A 1 264 ? 9.151   -4.092  -1.870  1.00 102.31 ? 367  LEU A C     1 
ATOM   1957 O  O     . LEU A 1 264 ? 9.896   -3.194  -2.278  1.00 101.07 ? 367  LEU A O     1 
ATOM   1958 C  CB    . LEU A 1 264 ? 10.122  -5.725  -0.231  1.00 101.81 ? 367  LEU A CB    1 
ATOM   1959 C  CG    . LEU A 1 264 ? 10.471  -6.071  1.218   1.00 95.01  ? 367  LEU A CG    1 
ATOM   1960 C  CD1   . LEU A 1 264 ? 11.249  -7.372  1.290   1.00 87.71  ? 367  LEU A CD1   1 
ATOM   1961 C  CD2   . LEU A 1 264 ? 11.259  -4.936  1.855   1.00 93.06  ? 367  LEU A CD2   1 
ATOM   1962 N  N     . CYS A 1 265 ? 8.290   -4.720  -2.665  1.00 104.11 ? 368  CYS A N     1 
ATOM   1963 C  CA    . CYS A 1 265 ? 8.080   -4.340  -4.053  1.00 108.98 ? 368  CYS A CA    1 
ATOM   1964 C  C     . CYS A 1 265 ? 6.596   -4.457  -4.365  1.00 113.21 ? 368  CYS A C     1 
ATOM   1965 O  O     . CYS A 1 265 ? 5.814   -4.999  -3.579  1.00 108.76 ? 368  CYS A O     1 
ATOM   1966 C  CB    . CYS A 1 265 ? 8.909   -5.206  -5.011  1.00 107.14 ? 368  CYS A CB    1 
ATOM   1967 S  SG    . CYS A 1 265 ? 8.529   -6.973  -4.947  1.00 110.81 ? 368  CYS A SG    1 
ATOM   1968 N  N     . ASP A 1 266 ? 6.210   -3.937  -5.527  1.00 113.10 ? 369  ASP A N     1 
ATOM   1969 C  CA    . ASP A 1 266 ? 4.811   -3.970  -5.927  1.00 113.86 ? 369  ASP A CA    1 
ATOM   1970 C  C     . ASP A 1 266 ? 4.366   -5.401  -6.205  1.00 114.12 ? 369  ASP A C     1 
ATOM   1971 O  O     . ASP A 1 266 ? 5.100   -6.194  -6.802  1.00 121.28 ? 369  ASP A O     1 
ATOM   1972 C  CB    . ASP A 1 266 ? 4.592   -3.098  -7.161  1.00 120.34 ? 369  ASP A CB    1 
ATOM   1973 C  CG    . ASP A 1 266 ? 4.840   -1.628  -6.885  1.00 132.27 ? 369  ASP A CG    1 
ATOM   1974 O  OD1   . ASP A 1 266 ? 5.948   -1.290  -6.416  1.00 136.11 ? 369  ASP A OD1   1 
ATOM   1975 O  OD2   . ASP A 1 266 ? 3.929   -0.812  -7.138  1.00 141.27 ? 369  ASP A OD2   1 
ATOM   1976 N  N     . ASN A 1 267 ? 3.156   -5.728  -5.760  1.00 114.22 ? 370  ASN A N     1 
ATOM   1977 C  CA    . ASN A 1 267 ? 2.617   -7.063  -5.967  1.00 110.96 ? 370  ASN A CA    1 
ATOM   1978 C  C     . ASN A 1 267 ? 2.316   -7.294  -7.442  1.00 112.26 ? 370  ASN A C     1 
ATOM   1979 O  O     . ASN A 1 267 ? 1.799   -6.412  -8.133  1.00 110.01 ? 370  ASN A O     1 
ATOM   1980 C  CB    . ASN A 1 267 ? 1.347   -7.256  -5.138  1.00 107.51 ? 370  ASN A CB    1 
ATOM   1981 C  CG    . ASN A 1 267 ? 1.541   -6.889  -3.681  1.00 114.44 ? 370  ASN A CG    1 
ATOM   1982 O  OD1   . ASN A 1 267 ? 0.684   -6.249  -3.071  1.00 126.59 ? 370  ASN A OD1   1 
ATOM   1983 N  ND2   . ASN A 1 267 ? 2.676   -7.284  -3.117  1.00 111.58 ? 370  ASN A ND2   1 
ATOM   1984 N  N     . VAL A 1 268 ? 2.648   -8.488  -7.925  1.00 113.40 ? 371  VAL A N     1 
ATOM   1985 C  CA    . VAL A 1 268 ? 2.388   -8.865  -9.307  1.00 116.67 ? 371  VAL A CA    1 
ATOM   1986 C  C     . VAL A 1 268 ? 1.368   -9.997  -9.322  1.00 117.26 ? 371  VAL A C     1 
ATOM   1987 O  O     . VAL A 1 268 ? 1.211   -10.748 -8.354  1.00 111.64 ? 371  VAL A O     1 
ATOM   1988 C  CB    . VAL A 1 268 ? 3.676   -9.269  -10.055 1.00 113.97 ? 371  VAL A CB    1 
ATOM   1989 C  CG1   . VAL A 1 268 ? 4.747   -8.203  -9.879  1.00 112.74 ? 371  VAL A CG1   1 
ATOM   1990 C  CG2   . VAL A 1 268 ? 4.175   -10.621 -9.578  1.00 109.70 ? 371  VAL A CG2   1 
ATOM   1991 N  N     . ASN A 1 269 ? 0.663   -10.112 -10.444 1.00 118.19 ? 372  ASN A N     1 
ATOM   1992 C  CA    . ASN A 1 269 ? -0.401  -11.090 -10.608 1.00 118.84 ? 372  ASN A CA    1 
ATOM   1993 C  C     . ASN A 1 269 ? -0.115  -11.988 -11.803 1.00 118.49 ? 372  ASN A C     1 
ATOM   1994 O  O     . ASN A 1 269 ? 0.455   -11.552 -12.808 1.00 113.68 ? 372  ASN A O     1 
ATOM   1995 C  CB    . ASN A 1 269 ? -1.761  -10.405 -10.796 1.00 125.96 ? 372  ASN A CB    1 
ATOM   1996 C  CG    . ASN A 1 269 ? -2.247  -9.720  -9.536  1.00 136.72 ? 372  ASN A CG    1 
ATOM   1997 O  OD1   . ASN A 1 269 ? -2.964  -10.315 -8.733  1.00 124.07 ? 372  ASN A OD1   1 
ATOM   1998 N  ND2   . ASN A 1 269 ? -1.860  -8.463  -9.356  1.00 145.95 ? 372  ASN A ND2   1 
ATOM   1999 N  N     . THR A 1 270 ? -0.522  -13.249 -11.683 1.00 114.40 ? 373  THR A N     1 
ATOM   2000 C  CA    . THR A 1 270 ? -0.383  -14.203 -12.770 1.00 113.76 ? 373  THR A CA    1 
ATOM   2001 C  C     . THR A 1 270 ? -1.523  -14.027 -13.771 1.00 122.83 ? 373  THR A C     1 
ATOM   2002 O  O     . THR A 1 270 ? -2.384  -13.153 -13.630 1.00 122.00 ? 373  THR A O     1 
ATOM   2003 C  CB    . THR A 1 270 ? -0.356  -15.631 -12.230 1.00 112.79 ? 373  THR A CB    1 
ATOM   2004 O  OG1   . THR A 1 270 ? -1.632  -15.950 -11.662 1.00 115.84 ? 373  THR A OG1   1 
ATOM   2005 C  CG2   . THR A 1 270 ? 0.719   -15.780 -11.165 1.00 116.33 ? 373  THR A CG2   1 
ATOM   2006 N  N     . GLN A 1 271 ? -1.528  -14.873 -14.796 1.00 125.04 ? 374  GLN A N     1 
ATOM   2007 C  CA    . GLN A 1 271 ? -2.582  -14.835 -15.796 1.00 125.69 ? 374  GLN A CA    1 
ATOM   2008 C  C     . GLN A 1 271 ? -3.911  -15.284 -15.193 1.00 129.19 ? 374  GLN A C     1 
ATOM   2009 O  O     . GLN A 1 271 ? -3.968  -15.908 -14.129 1.00 118.10 ? 374  GLN A O     1 
ATOM   2010 C  CB    . GLN A 1 271 ? -2.223  -15.723 -16.989 1.00 127.11 ? 374  GLN A CB    1 
ATOM   2011 C  CG    . GLN A 1 271 ? -0.918  -15.354 -17.683 1.00 131.38 ? 374  GLN A CG    1 
ATOM   2012 C  CD    . GLN A 1 271 ? -1.010  -14.056 -18.461 1.00 127.49 ? 374  GLN A CD    1 
ATOM   2013 O  OE1   . GLN A 1 271 ? -0.883  -12.968 -17.898 1.00 126.36 ? 374  GLN A OE1   1 
ATOM   2014 N  NE2   . GLN A 1 271 ? -1.230  -14.165 -19.766 1.00 131.52 ? 374  GLN A NE2   1 
ATOM   2015 N  N     . ARG A 1 272 ? -4.993  -14.955 -15.895 1.00 146.04 ? 375  ARG A N     1 
ATOM   2016 C  CA    . ARG A 1 272 ? -6.343  -15.324 -15.474 1.00 143.23 ? 375  ARG A CA    1 
ATOM   2017 C  C     . ARG A 1 272 ? -6.719  -16.621 -16.180 1.00 138.54 ? 375  ARG A C     1 
ATOM   2018 O  O     . ARG A 1 272 ? -7.093  -16.616 -17.356 1.00 146.60 ? 375  ARG A O     1 
ATOM   2019 C  CB    . ARG A 1 272 ? -7.329  -14.205 -15.791 1.00 145.33 ? 375  ARG A CB    1 
ATOM   2020 C  CG    . ARG A 1 272 ? -6.942  -12.852 -15.215 1.00 155.28 ? 375  ARG A CG    1 
ATOM   2021 C  CD    . ARG A 1 272 ? -7.908  -11.765 -15.664 1.00 157.88 ? 375  ARG A CD    1 
ATOM   2022 N  NE    . ARG A 1 272 ? -7.537  -10.452 -15.150 1.00 164.36 ? 375  ARG A NE    1 
ATOM   2023 C  CZ    . ARG A 1 272 ? -7.987  -9.937  -14.014 1.00 159.36 ? 375  ARG A CZ    1 
ATOM   2024 N  NH1   . ARG A 1 272 ? -8.830  -10.601 -13.241 1.00 147.53 ? 375  ARG A NH1   1 
ATOM   2025 N  NH2   . ARG A 1 272 ? -7.581  -8.726  -13.644 1.00 164.18 ? 375  ARG A NH2   1 
ATOM   2026 N  N     . VAL A 1 273 ? -6.619  -17.737 -15.465 1.00 139.56 ? 376  VAL A N     1 
ATOM   2027 C  CA    . VAL A 1 273 ? -6.907  -19.050 -16.039 1.00 138.04 ? 376  VAL A CA    1 
ATOM   2028 C  C     . VAL A 1 273 ? -8.169  -19.616 -15.398 1.00 140.76 ? 376  VAL A C     1 
ATOM   2029 O  O     . VAL A 1 273 ? -8.453  -19.329 -14.225 1.00 144.51 ? 376  VAL A O     1 
ATOM   2030 C  CB    . VAL A 1 273 ? -5.717  -20.009 -15.867 1.00 133.21 ? 376  VAL A CB    1 
ATOM   2031 C  CG1   . VAL A 1 273 ? -4.447  -19.386 -16.431 1.00 125.93 ? 376  VAL A CG1   1 
ATOM   2032 C  CG2   . VAL A 1 273 ? -5.528  -20.386 -14.402 1.00 131.64 ? 376  VAL A CG2   1 
ATOM   2033 N  N     . PRO A 1 274 ? -8.963  -20.398 -16.121 1.00 145.61 ? 377  PRO A N     1 
ATOM   2034 C  CA    . PRO A 1 274 ? -10.124 -21.050 -15.510 1.00 150.07 ? 377  PRO A CA    1 
ATOM   2035 C  C     . PRO A 1 274 ? -9.702  -22.248 -14.668 1.00 156.99 ? 377  PRO A C     1 
ATOM   2036 O  O     . PRO A 1 274 ? -8.569  -22.728 -14.732 1.00 159.47 ? 377  PRO A O     1 
ATOM   2037 C  CB    . PRO A 1 274 ? -10.963 -21.482 -16.717 1.00 150.67 ? 377  PRO A CB    1 
ATOM   2038 C  CG    . PRO A 1 274 ? -9.967  -21.661 -17.810 1.00 153.71 ? 377  PRO A CG    1 
ATOM   2039 C  CD    . PRO A 1 274 ? -8.902  -20.623 -17.576 1.00 149.11 ? 377  PRO A CD    1 
ATOM   2040 N  N     . CYS A 1 275 ? -10.653 -22.731 -13.868 1.00 162.76 ? 378  CYS A N     1 
ATOM   2041 C  CA    . CYS A 1 275 ? -10.411 -23.848 -12.963 1.00 170.59 ? 378  CYS A CA    1 
ATOM   2042 C  C     . CYS A 1 275 ? -10.378 -25.196 -13.673 1.00 183.71 ? 378  CYS A C     1 
ATOM   2043 O  O     . CYS A 1 275 ? -10.151 -26.216 -13.013 1.00 190.13 ? 378  CYS A O     1 
ATOM   2044 C  CB    . CYS A 1 275 ? -11.481 -23.865 -11.866 1.00 166.44 ? 378  CYS A CB    1 
ATOM   2045 S  SG    . CYS A 1 275 ? -11.102 -24.908 -10.433 1.00 181.41 ? 378  CYS A SG    1 
ATOM   2046 N  N     . SER A 1 276 ? -10.595 -25.228 -14.991 1.00 183.37 ? 379  SER A N     1 
ATOM   2047 C  CA    . SER A 1 276 ? -10.596 -26.493 -15.720 1.00 198.29 ? 379  SER A CA    1 
ATOM   2048 C  C     . SER A 1 276 ? -9.267  -27.221 -15.556 1.00 207.43 ? 379  SER A C     1 
ATOM   2049 O  O     . SER A 1 276 ? -9.213  -28.336 -15.026 1.00 208.80 ? 379  SER A O     1 
ATOM   2050 C  CB    . SER A 1 276 ? -10.900 -26.242 -17.199 1.00 196.91 ? 379  SER A CB    1 
ATOM   2051 O  OG    . SER A 1 276 ? -9.882  -25.463 -17.805 1.00 197.39 ? 379  SER A OG    1 
ATOM   2052 N  N     . ASN A 1 277 ? -8.178  -26.598 -16.004 1.00 201.59 ? 380  ASN A N     1 
ATOM   2053 C  CA    . ASN A 1 277 ? -6.830  -27.134 -15.834 1.00 196.85 ? 380  ASN A CA    1 
ATOM   2054 C  C     . ASN A 1 277 ? -5.981  -26.051 -15.183 1.00 189.23 ? 380  ASN A C     1 
ATOM   2055 O  O     . ASN A 1 277 ? -5.333  -25.255 -15.876 1.00 192.81 ? 380  ASN A O     1 
ATOM   2056 C  CB    . ASN A 1 277 ? -6.234  -27.586 -17.166 1.00 196.95 ? 380  ASN A CB    1 
ATOM   2057 C  CG    . ASN A 1 277 ? -4.872  -28.234 -17.005 1.00 189.60 ? 380  ASN A CG    1 
ATOM   2058 O  OD1   . ASN A 1 277 ? -4.550  -28.776 -15.947 1.00 192.05 ? 380  ASN A OD1   1 
ATOM   2059 N  ND2   . ASN A 1 277 ? -4.063  -28.179 -18.057 1.00 179.26 ? 380  ASN A ND2   1 
ATOM   2060 N  N     . PRO A 1 278 ? -5.974  -25.981 -13.846 1.00 185.74 ? 381  PRO A N     1 
ATOM   2061 C  CA    . PRO A 1 278 ? -5.175  -24.954 -13.161 1.00 175.87 ? 381  PRO A CA    1 
ATOM   2062 C  C     . PRO A 1 278 ? -3.697  -25.053 -13.495 1.00 176.01 ? 381  PRO A C     1 
ATOM   2063 O  O     . PRO A 1 278 ? -2.983  -25.897 -12.946 1.00 181.46 ? 381  PRO A O     1 
ATOM   2064 C  CB    . PRO A 1 278 ? -5.435  -25.238 -11.675 1.00 164.99 ? 381  PRO A CB    1 
ATOM   2065 C  CG    . PRO A 1 278 ? -6.734  -25.969 -11.649 1.00 174.54 ? 381  PRO A CG    1 
ATOM   2066 C  CD    . PRO A 1 278 ? -6.760  -26.792 -12.902 1.00 184.77 ? 381  PRO A CD    1 
ATOM   2067 N  N     . ARG A 1 279 ? -3.236  -24.195 -14.401 1.00 155.64 ? 382  ARG A N     1 
ATOM   2068 C  CA    . ARG A 1 279 ? -1.848  -24.191 -14.838 1.00 142.79 ? 382  ARG A CA    1 
ATOM   2069 C  C     . ARG A 1 279 ? -1.434  -22.759 -15.140 1.00 131.24 ? 382  ARG A C     1 
ATOM   2070 O  O     . ARG A 1 279 ? -2.202  -21.995 -15.730 1.00 130.40 ? 382  ARG A O     1 
ATOM   2071 C  CB    . ARG A 1 279 ? -1.644  -25.068 -16.081 1.00 146.82 ? 382  ARG A CB    1 
ATOM   2072 C  CG    . ARG A 1 279 ? -0.767  -26.293 -15.863 1.00 141.67 ? 382  ARG A CG    1 
ATOM   2073 C  CD    . ARG A 1 279 ? -1.573  -27.477 -15.353 1.00 152.13 ? 382  ARG A CD    1 
ATOM   2074 N  NE    . ARG A 1 279 ? -0.753  -28.674 -15.208 1.00 152.99 ? 382  ARG A NE    1 
ATOM   2075 N  N     . TRP A 1 280 ? -0.217  -22.404 -14.732 1.00 123.92 ? 383  TRP A N     1 
ATOM   2076 C  CA    . TRP A 1 280 ? 0.332   -21.086 -15.023 1.00 119.86 ? 383  TRP A CA    1 
ATOM   2077 C  C     . TRP A 1 280 ? 1.681   -21.206 -15.723 1.00 113.91 ? 383  TRP A C     1 
ATOM   2078 O  O     . TRP A 1 280 ? 1.879   -20.622 -16.792 1.00 119.98 ? 383  TRP A O     1 
ATOM   2079 C  CB    . TRP A 1 280 ? 0.455   -20.260 -13.740 1.00 119.62 ? 383  TRP A CB    1 
ATOM   2080 C  CG    . TRP A 1 280 ? -0.872  -19.816 -13.191 1.00 117.15 ? 383  TRP A CG    1 
ATOM   2081 C  CD1   . TRP A 1 280 ? -1.560  -18.686 -13.527 1.00 116.13 ? 383  TRP A CD1   1 
ATOM   2082 C  CD2   . TRP A 1 280 ? -1.670  -20.495 -12.214 1.00 122.62 ? 383  TRP A CD2   1 
ATOM   2083 N  NE1   . TRP A 1 280 ? -2.735  -18.618 -12.819 1.00 115.43 ? 383  TRP A NE1   1 
ATOM   2084 C  CE2   . TRP A 1 280 ? -2.826  -19.717 -12.005 1.00 120.82 ? 383  TRP A CE2   1 
ATOM   2085 C  CE3   . TRP A 1 280 ? -1.519  -21.684 -11.493 1.00 130.11 ? 383  TRP A CE3   1 
ATOM   2086 C  CZ2   . TRP A 1 280 ? -3.825  -20.089 -11.107 1.00 122.25 ? 383  TRP A CZ2   1 
ATOM   2087 C  CZ3   . TRP A 1 280 ? -2.512  -22.052 -10.602 1.00 131.84 ? 383  TRP A CZ3   1 
ATOM   2088 C  CH2   . TRP A 1 280 ? -3.650  -21.257 -10.418 1.00 126.67 ? 383  TRP A CH2   1 
ATOM   2089 N  N     . ASN A 1 281 ? 2.609   -21.956 -15.123 1.00 113.24 ? 384  ASN A N     1 
ATOM   2090 C  CA    . ASN A 1 281 ? 3.902   -22.273 -15.736 1.00 109.81 ? 384  ASN A CA    1 
ATOM   2091 C  C     . ASN A 1 281 ? 4.628   -21.014 -16.205 1.00 109.61 ? 384  ASN A C     1 
ATOM   2092 O  O     . ASN A 1 281 ? 5.264   -20.992 -17.261 1.00 126.13 ? 384  ASN A O     1 
ATOM   2093 C  CB    . ASN A 1 281 ? 3.728   -23.263 -16.891 1.00 112.54 ? 384  ASN A CB    1 
ATOM   2094 C  CG    . ASN A 1 281 ? 2.999   -24.524 -16.471 1.00 115.43 ? 384  ASN A CG    1 
ATOM   2095 O  OD1   . ASN A 1 281 ? 2.979   -24.879 -15.293 1.00 130.03 ? 384  ASN A OD1   1 
ATOM   2096 N  ND2   . ASN A 1 281 ? 2.395   -25.209 -17.436 1.00 109.22 ? 384  ASN A ND2   1 
ATOM   2097 N  N     . GLU A 1 282 ? 4.530   -19.952 -15.411 1.00 112.15 ? 385  GLU A N     1 
ATOM   2098 C  CA    . GLU A 1 282 ? 5.083   -18.656 -15.773 1.00 119.42 ? 385  GLU A CA    1 
ATOM   2099 C  C     . GLU A 1 282 ? 5.944   -18.111 -14.645 1.00 115.57 ? 385  GLU A C     1 
ATOM   2100 O  O     . GLU A 1 282 ? 5.614   -18.266 -13.464 1.00 104.22 ? 385  GLU A O     1 
ATOM   2101 C  CB    . GLU A 1 282 ? 3.974   -17.653 -16.102 1.00 118.95 ? 385  GLU A CB    1 
ATOM   2102 C  CG    . GLU A 1 282 ? 2.882   -17.570 -15.051 1.00 122.05 ? 385  GLU A CG    1 
ATOM   2103 C  CD    . GLU A 1 282 ? 1.948   -16.398 -15.274 1.00 122.27 ? 385  GLU A CD    1 
ATOM   2104 O  OE1   . GLU A 1 282 ? 2.445   -15.284 -15.543 1.00 123.41 ? 385  GLU A OE1   1 
ATOM   2105 O  OE2   . GLU A 1 282 ? 0.718   -16.592 -15.186 1.00 122.52 ? 385  GLU A OE2   1 
ATOM   2106 N  N     . TRP A 1 283 ? 7.048   -17.471 -15.021 1.00 120.14 ? 386  TRP A N     1 
ATOM   2107 C  CA    . TRP A 1 283 ? 7.899   -16.771 -14.073 1.00 116.39 ? 386  TRP A CA    1 
ATOM   2108 C  C     . TRP A 1 283 ? 7.381   -15.356 -13.862 1.00 115.25 ? 386  TRP A C     1 
ATOM   2109 O  O     . TRP A 1 283 ? 6.911   -14.706 -14.800 1.00 114.61 ? 386  TRP A O     1 
ATOM   2110 C  CB    . TRP A 1 283 ? 9.345   -16.731 -14.571 1.00 114.75 ? 386  TRP A CB    1 
ATOM   2111 C  CG    . TRP A 1 283 ? 10.039  -18.053 -14.504 1.00 112.41 ? 386  TRP A CG    1 
ATOM   2112 C  CD1   . TRP A 1 283 ? 9.939   -19.077 -15.398 1.00 118.19 ? 386  TRP A CD1   1 
ATOM   2113 C  CD2   . TRP A 1 283 ? 10.944  -18.496 -13.486 1.00 117.06 ? 386  TRP A CD2   1 
ATOM   2114 N  NE1   . TRP A 1 283 ? 10.724  -20.132 -15.000 1.00 114.55 ? 386  TRP A NE1   1 
ATOM   2115 C  CE2   . TRP A 1 283 ? 11.351  -19.800 -13.828 1.00 116.50 ? 386  TRP A CE2   1 
ATOM   2116 C  CE3   . TRP A 1 283 ? 11.448  -17.917 -12.317 1.00 117.70 ? 386  TRP A CE3   1 
ATOM   2117 C  CZ2   . TRP A 1 283 ? 12.239  -20.535 -13.045 1.00 118.20 ? 386  TRP A CZ2   1 
ATOM   2118 C  CZ3   . TRP A 1 283 ? 12.330  -18.648 -11.541 1.00 116.41 ? 386  TRP A CZ3   1 
ATOM   2119 C  CH2   . TRP A 1 283 ? 12.716  -19.943 -11.908 1.00 118.61 ? 386  TRP A CH2   1 
ATOM   2120 N  N     . LEU A 1 284 ? 7.465   -14.885 -12.623 1.00 109.14 ? 387  LEU A N     1 
ATOM   2121 C  CA    . LEU A 1 284 ? 7.045   -13.539 -12.259 1.00 105.19 ? 387  LEU A CA    1 
ATOM   2122 C  C     . LEU A 1 284 ? 8.280   -12.730 -11.891 1.00 103.04 ? 387  LEU A C     1 
ATOM   2123 O  O     . LEU A 1 284 ? 8.997   -13.082 -10.949 1.00 105.23 ? 387  LEU A O     1 
ATOM   2124 C  CB    . LEU A 1 284 ? 6.054   -13.566 -11.096 1.00 104.46 ? 387  LEU A CB    1 
ATOM   2125 C  CG    . LEU A 1 284 ? 4.749   -14.330 -11.326 1.00 107.68 ? 387  LEU A CG    1 
ATOM   2126 C  CD1   . LEU A 1 284 ? 3.858   -14.250 -10.097 1.00 105.48 ? 387  LEU A CD1   1 
ATOM   2127 C  CD2   . LEU A 1 284 ? 4.028   -13.796 -12.553 1.00 115.88 ? 387  LEU A CD2   1 
ATOM   2128 N  N     . ASN A 1 285 ? 8.533   -11.661 -12.638 1.00 103.80 ? 388  ASN A N     1 
ATOM   2129 C  CA    . ASN A 1 285 ? 9.645   -10.770 -12.346 1.00 105.22 ? 388  ASN A CA    1 
ATOM   2130 C  C     . ASN A 1 285 ? 9.194   -9.715  -11.344 1.00 104.46 ? 388  ASN A C     1 
ATOM   2131 O  O     . ASN A 1 285 ? 8.176   -9.045  -11.550 1.00 104.10 ? 388  ASN A O     1 
ATOM   2132 C  CB    . ASN A 1 285 ? 10.173  -10.115 -13.624 1.00 105.71 ? 388  ASN A CB    1 
ATOM   2133 C  CG    . ASN A 1 285 ? 9.126   -9.277  -14.328 1.00 111.30 ? 388  ASN A CG    1 
ATOM   2134 O  OD1   . ASN A 1 285 ? 8.315   -9.791  -15.099 1.00 114.81 ? 388  ASN A OD1   1 
ATOM   2135 N  ND2   . ASN A 1 285 ? 9.140   -7.975  -14.068 1.00 110.13 ? 388  ASN A ND2   1 
ATOM   2136 N  N     . TYR A 1 286 ? 9.941   -9.584  -10.254 1.00 106.66 ? 389  TYR A N     1 
ATOM   2137 C  CA    . TYR A 1 286 ? 9.620   -8.648  -9.190  1.00 110.69 ? 389  TYR A CA    1 
ATOM   2138 C  C     . TYR A 1 286 ? 10.563  -7.454  -9.242  1.00 111.97 ? 389  TYR A C     1 
ATOM   2139 O  O     . TYR A 1 286 ? 11.713  -7.565  -9.678  1.00 113.29 ? 389  TYR A O     1 
ATOM   2140 C  CB    . TYR A 1 286 ? 9.705   -9.325  -7.817  1.00 102.63 ? 389  TYR A CB    1 
ATOM   2141 C  CG    . TYR A 1 286 ? 8.761   -10.496 -7.658  1.00 100.78 ? 389  TYR A CG    1 
ATOM   2142 C  CD1   . TYR A 1 286 ? 7.462   -10.309 -7.205  1.00 108.74 ? 389  TYR A CD1   1 
ATOM   2143 C  CD2   . TYR A 1 286 ? 9.169   -11.788 -7.964  1.00 97.02  ? 389  TYR A CD2   1 
ATOM   2144 C  CE1   . TYR A 1 286 ? 6.596   -11.377 -7.059  1.00 107.78 ? 389  TYR A CE1   1 
ATOM   2145 C  CE2   . TYR A 1 286 ? 8.310   -12.861 -7.824  1.00 95.03  ? 389  TYR A CE2   1 
ATOM   2146 C  CZ    . TYR A 1 286 ? 7.025   -12.650 -7.371  1.00 104.46 ? 389  TYR A CZ    1 
ATOM   2147 O  OH    . TYR A 1 286 ? 6.167   -13.716 -7.229  1.00 113.98 ? 389  TYR A OH    1 
ATOM   2148 N  N     . ASP A 1 287 ? 10.060  -6.304  -8.795  1.00 113.14 ? 390  ASP A N     1 
ATOM   2149 C  CA    . ASP A 1 287 ? 10.837  -5.067  -8.777  1.00 111.79 ? 390  ASP A CA    1 
ATOM   2150 C  C     . ASP A 1 287 ? 11.707  -5.006  -7.518  1.00 114.10 ? 390  ASP A C     1 
ATOM   2151 O  O     . ASP A 1 287 ? 11.559  -4.141  -6.655  1.00 113.64 ? 390  ASP A O     1 
ATOM   2152 C  CB    . ASP A 1 287 ? 9.906   -3.865  -8.873  1.00 108.52 ? 390  ASP A CB    1 
ATOM   2153 C  CG    . ASP A 1 287 ? 10.653  -2.554  -9.030  1.00 112.44 ? 390  ASP A CG    1 
ATOM   2154 O  OD1   . ASP A 1 287 ? 11.874  -2.586  -9.297  1.00 114.62 ? 390  ASP A OD1   1 
ATOM   2155 O  OD2   . ASP A 1 287 ? 10.017  -1.489  -8.880  1.00 115.13 ? 390  ASP A OD2   1 
ATOM   2156 N  N     . ILE A 1 288 ? 12.632  -5.958  -7.425  1.00 111.60 ? 391  ILE A N     1 
ATOM   2157 C  CA    . ILE A 1 288 ? 13.545  -6.034  -6.288  1.00 119.05 ? 391  ILE A CA    1 
ATOM   2158 C  C     . ILE A 1 288 ? 14.817  -6.749  -6.724  1.00 115.57 ? 391  ILE A C     1 
ATOM   2159 O  O     . ILE A 1 288 ? 14.766  -7.837  -7.307  1.00 106.04 ? 391  ILE A O     1 
ATOM   2160 C  CB    . ILE A 1 288 ? 12.899  -6.739  -5.075  1.00 112.92 ? 391  ILE A CB    1 
ATOM   2161 C  CG1   . ILE A 1 288 ? 13.942  -7.004  -3.988  1.00 105.43 ? 391  ILE A CG1   1 
ATOM   2162 C  CG2   . ILE A 1 288 ? 12.204  -8.027  -5.495  1.00 116.31 ? 391  ILE A CG2   1 
ATOM   2163 N  N     . TYR A 1 289 ? 15.957  -6.121  -6.452  1.00 131.26 ? 392  TYR A N     1 
ATOM   2164 C  CA    . TYR A 1 289 ? 17.250  -6.740  -6.703  1.00 129.39 ? 392  TYR A CA    1 
ATOM   2165 C  C     . TYR A 1 289 ? 17.462  -7.902  -5.738  1.00 122.09 ? 392  TYR A C     1 
ATOM   2166 O  O     . TYR A 1 289 ? 17.157  -7.799  -4.547  1.00 124.26 ? 392  TYR A O     1 
ATOM   2167 C  CB    . TYR A 1 289 ? 18.359  -5.699  -6.536  1.00 137.00 ? 392  TYR A CB    1 
ATOM   2168 C  CG    . TYR A 1 289 ? 19.615  -5.943  -7.344  1.00 129.72 ? 392  TYR A CG    1 
ATOM   2169 C  CD1   . TYR A 1 289 ? 19.662  -6.921  -8.327  1.00 138.90 ? 392  TYR A CD1   1 
ATOM   2170 C  CD2   . TYR A 1 289 ? 20.758  -5.186  -7.118  1.00 141.28 ? 392  TYR A CD2   1 
ATOM   2171 C  CE1   . TYR A 1 289 ? 20.816  -7.140  -9.064  1.00 139.43 ? 392  TYR A CE1   1 
ATOM   2172 C  CE2   . TYR A 1 289 ? 21.913  -5.396  -7.847  1.00 148.09 ? 392  TYR A CE2   1 
ATOM   2173 C  CZ    . TYR A 1 289 ? 21.938  -6.373  -8.817  1.00 136.86 ? 392  TYR A CZ    1 
ATOM   2174 O  OH    . TYR A 1 289 ? 23.089  -6.582  -9.541  1.00 130.39 ? 392  TYR A OH    1 
ATOM   2175 N  N     . ILE A 1 290 ? 17.977  -9.019  -6.263  1.00 111.23 ? 393  ILE A N     1 
ATOM   2176 C  CA    . ILE A 1 290 ? 18.225  -10.191 -5.416  1.00 108.01 ? 393  ILE A CA    1 
ATOM   2177 C  C     . ILE A 1 290 ? 19.130  -9.869  -4.231  1.00 111.67 ? 393  ILE A C     1 
ATOM   2178 O  O     . ILE A 1 290 ? 18.769  -10.219 -3.096  1.00 113.67 ? 393  ILE A O     1 
ATOM   2179 C  CB    . ILE A 1 290 ? 18.755  -11.358 -6.267  1.00 109.45 ? 393  ILE A CB    1 
ATOM   2180 C  CG1   . ILE A 1 290 ? 17.605  -12.097 -6.950  1.00 108.98 ? 393  ILE A CG1   1 
ATOM   2181 C  CG2   . ILE A 1 290 ? 19.562  -12.324 -5.409  1.00 108.36 ? 393  ILE A CG2   1 
ATOM   2182 C  CD1   . ILE A 1 290 ? 16.834  -13.011 -6.023  1.00 110.71 ? 393  ILE A CD1   1 
ATOM   2183 N  N     . PRO A 1 291 ? 20.292  -9.221  -4.403  1.00 114.39 ? 394  PRO A N     1 
ATOM   2184 C  CA    . PRO A 1 291 ? 21.140  -8.947  -3.231  1.00 113.25 ? 394  PRO A CA    1 
ATOM   2185 C  C     . PRO A 1 291 ? 20.524  -7.981  -2.235  1.00 112.44 ? 394  PRO A C     1 
ATOM   2186 O  O     . PRO A 1 291 ? 20.956  -7.960  -1.076  1.00 120.78 ? 394  PRO A O     1 
ATOM   2187 C  CB    . PRO A 1 291 ? 22.419  -8.365  -3.850  1.00 117.44 ? 394  PRO A CB    1 
ATOM   2188 C  CG    . PRO A 1 291 ? 21.996  -7.832  -5.161  1.00 116.10 ? 394  PRO A CG    1 
ATOM   2189 C  CD    . PRO A 1 291 ? 20.941  -8.771  -5.648  1.00 115.61 ? 394  PRO A CD    1 
ATOM   2190 N  N     . ASP A 1 292 ? 19.532  -7.189  -2.634  1.00 107.35 ? 395  ASP A N     1 
ATOM   2191 C  CA    . ASP A 1 292 ? 18.914  -6.214  -1.747  1.00 111.26 ? 395  ASP A CA    1 
ATOM   2192 C  C     . ASP A 1 292 ? 17.770  -6.796  -0.923  1.00 111.20 ? 395  ASP A C     1 
ATOM   2193 O  O     . ASP A 1 292 ? 17.096  -6.048  -0.207  1.00 107.04 ? 395  ASP A O     1 
ATOM   2194 C  CB    . ASP A 1 292 ? 18.424  -5.009  -2.553  1.00 111.57 ? 395  ASP A CB    1 
ATOM   2195 C  CG    . ASP A 1 292 ? 19.533  -4.017  -2.846  1.00 114.69 ? 395  ASP A CG    1 
ATOM   2196 O  OD1   . ASP A 1 292 ? 20.602  -4.447  -3.328  1.00 123.73 ? 395  ASP A OD1   1 
ATOM   2197 O  OD2   . ASP A 1 292 ? 19.338  -2.809  -2.596  1.00 107.76 ? 395  ASP A OD2   1 
ATOM   2198 N  N     . LEU A 1 293 ? 17.539  -8.103  -1.000  1.00 108.33 ? 396  LEU A N     1 
ATOM   2199 C  CA    . LEU A 1 293 ? 16.529  -8.721  -0.155  1.00 102.34 ? 396  LEU A CA    1 
ATOM   2200 C  C     . LEU A 1 293 ? 16.999  -8.735  1.299   1.00 97.74  ? 396  LEU A C     1 
ATOM   2201 O  O     . LEU A 1 293 ? 18.168  -9.025  1.572   1.00 97.68  ? 396  LEU A O     1 
ATOM   2202 C  CB    . LEU A 1 293 ? 16.232  -10.147 -0.616  1.00 99.05  ? 396  LEU A CB    1 
ATOM   2203 C  CG    . LEU A 1 293 ? 15.248  -10.327 -1.770  1.00 101.05 ? 396  LEU A CG    1 
ATOM   2204 C  CD1   . LEU A 1 293 ? 15.113  -11.800 -2.115  1.00 101.45 ? 396  LEU A CD1   1 
ATOM   2205 C  CD2   . LEU A 1 293 ? 13.894  -9.733  -1.416  1.00 96.53  ? 396  LEU A CD2   1 
ATOM   2206 N  N     . PRO A 1 294 ? 16.123  -8.423  2.247   1.00 96.39  ? 397  PRO A N     1 
ATOM   2207 C  CA    . PRO A 1 294 ? 16.500  -8.484  3.660   1.00 96.54  ? 397  PRO A CA    1 
ATOM   2208 C  C     . PRO A 1 294 ? 16.480  -9.919  4.175   1.00 92.87  ? 397  PRO A C     1 
ATOM   2209 O  O     . PRO A 1 294 ? 16.010  -10.846 3.513   1.00 89.67  ? 397  PRO A O     1 
ATOM   2210 C  CB    . PRO A 1 294 ? 15.429  -7.631  4.344   1.00 94.58  ? 397  PRO A CB    1 
ATOM   2211 C  CG    . PRO A 1 294 ? 14.235  -7.789  3.468   1.00 96.62  ? 397  PRO A CG    1 
ATOM   2212 C  CD    . PRO A 1 294 ? 14.754  -7.911  2.060   1.00 94.69  ? 397  PRO A CD    1 
ATOM   2213 N  N     . ARG A 1 295 ? 17.007  -10.084 5.390   1.00 93.45  ? 398  ARG A N     1 
ATOM   2214 C  CA    . ARG A 1 295 ? 17.084  -11.413 5.990   1.00 90.06  ? 398  ARG A CA    1 
ATOM   2215 C  C     . ARG A 1 295 ? 15.698  -11.967 6.297   1.00 87.43  ? 398  ARG A C     1 
ATOM   2216 O  O     . ARG A 1 295 ? 15.458  -13.171 6.143   1.00 87.18  ? 398  ARG A O     1 
ATOM   2217 C  CB    . ARG A 1 295 ? 17.939  -11.364 7.257   1.00 87.69  ? 398  ARG A CB    1 
ATOM   2218 C  CG    . ARG A 1 295 ? 18.057  -12.694 7.982   1.00 87.83  ? 398  ARG A CG    1 
ATOM   2219 C  CD    . ARG A 1 295 ? 18.593  -13.776 7.062   1.00 88.11  ? 398  ARG A CD    1 
ATOM   2220 N  NE    . ARG A 1 295 ? 18.689  -15.070 7.727   1.00 85.58  ? 398  ARG A NE    1 
ATOM   2221 C  CZ    . ARG A 1 295 ? 17.682  -15.923 7.853   1.00 81.02  ? 398  ARG A CZ    1 
ATOM   2222 N  NH1   . ARG A 1 295 ? 16.474  -15.638 7.394   1.00 77.86  ? 398  ARG A NH1   1 
ATOM   2223 N  NH2   . ARG A 1 295 ? 17.892  -17.091 8.454   1.00 82.12  ? 398  ARG A NH2   1 
ATOM   2224 N  N     . ALA A 1 296 ? 14.772  -11.107 6.727   1.00 88.32  ? 399  ALA A N     1 
ATOM   2225 C  CA    . ALA A 1 296 ? 13.418  -11.520 7.078   1.00 90.13  ? 399  ALA A CA    1 
ATOM   2226 C  C     . ALA A 1 296 ? 12.443  -11.408 5.910   1.00 92.17  ? 399  ALA A C     1 
ATOM   2227 O  O     . ALA A 1 296 ? 11.236  -11.238 6.131   1.00 90.34  ? 399  ALA A O     1 
ATOM   2228 C  CB    . ALA A 1 296 ? 12.915  -10.703 8.269   1.00 90.70  ? 399  ALA A CB    1 
ATOM   2229 N  N     . ALA A 1 297 ? 12.930  -11.502 4.676   1.00 102.23 ? 400  ALA A N     1 
ATOM   2230 C  CA    . ALA A 1 297 ? 12.061  -11.369 3.514   1.00 99.99  ? 400  ALA A CA    1 
ATOM   2231 C  C     . ALA A 1 297 ? 11.145  -12.580 3.384   1.00 90.63  ? 400  ALA A C     1 
ATOM   2232 O  O     . ALA A 1 297 ? 11.568  -13.724 3.573   1.00 99.32  ? 400  ALA A O     1 
ATOM   2233 C  CB    . ALA A 1 297 ? 12.894  -11.200 2.245   1.00 92.16  ? 400  ALA A CB    1 
ATOM   2234 N  N     . ARG A 1 298 ? 9.880   -12.322 3.057   1.00 78.38  ? 401  ARG A N     1 
ATOM   2235 C  CA    . ARG A 1 298 ? 8.878   -13.369 2.926   1.00 92.87  ? 401  ARG A CA    1 
ATOM   2236 C  C     . ARG A 1 298 ? 8.099   -13.192 1.631   1.00 102.51 ? 401  ARG A C     1 
ATOM   2237 O  O     . ARG A 1 298 ? 7.931   -12.076 1.132   1.00 99.33  ? 401  ARG A O     1 
ATOM   2238 C  CB    . ARG A 1 298 ? 7.903   -13.370 4.116   1.00 90.07  ? 401  ARG A CB    1 
ATOM   2239 C  CG    . ARG A 1 298 ? 8.566   -13.587 5.468   1.00 102.53 ? 401  ARG A CG    1 
ATOM   2240 C  CD    . ARG A 1 298 ? 7.555   -13.593 6.609   1.00 95.52  ? 401  ARG A CD    1 
ATOM   2241 N  NE    . ARG A 1 298 ? 6.774   -12.362 6.670   1.00 94.78  ? 401  ARG A NE    1 
ATOM   2242 C  CZ    . ARG A 1 298 ? 5.472   -12.287 6.427   1.00 104.88 ? 401  ARG A CZ    1 
ATOM   2243 N  NH1   . ARG A 1 298 ? 4.762   -13.362 6.129   1.00 113.02 ? 401  ARG A NH1   1 
ATOM   2244 N  NH2   . ARG A 1 298 ? 4.867   -11.104 6.491   1.00 100.59 ? 401  ARG A NH2   1 
ATOM   2245 N  N     . LEU A 1 299 ? 7.625   -14.311 1.091   1.00 88.99  ? 402  LEU A N     1 
ATOM   2246 C  CA    . LEU A 1 299 ? 6.729   -14.315 -0.058  1.00 93.94  ? 402  LEU A CA    1 
ATOM   2247 C  C     . LEU A 1 299 ? 5.309   -14.548 0.438   1.00 90.00  ? 402  LEU A C     1 
ATOM   2248 O  O     . LEU A 1 299 ? 5.042   -15.539 1.126   1.00 90.01  ? 402  LEU A O     1 
ATOM   2249 C  CB    . LEU A 1 299 ? 7.128   -15.392 -1.068  1.00 95.81  ? 402  LEU A CB    1 
ATOM   2250 C  CG    . LEU A 1 299 ? 6.104   -15.695 -2.168  1.00 95.25  ? 402  LEU A CG    1 
ATOM   2251 C  CD1   . LEU A 1 299 ? 5.876   -14.482 -3.059  1.00 96.58  ? 402  LEU A CD1   1 
ATOM   2252 C  CD2   . LEU A 1 299 ? 6.529   -16.901 -2.995  1.00 100.24 ? 402  LEU A CD2   1 
ATOM   2253 N  N     . CYS A 1 300 ? 4.406   -13.634 0.095   1.00 88.75  ? 403  CYS A N     1 
ATOM   2254 C  CA    . CYS A 1 300 ? 3.001   -13.725 0.477   1.00 97.38  ? 403  CYS A CA    1 
ATOM   2255 C  C     . CYS A 1 300 ? 2.176   -13.902 -0.791  1.00 101.62 ? 403  CYS A C     1 
ATOM   2256 O  O     . CYS A 1 300 ? 2.101   -12.990 -1.622  1.00 105.59 ? 403  CYS A O     1 
ATOM   2257 C  CB    . CYS A 1 300 ? 2.566   -12.486 1.258   1.00 100.56 ? 403  CYS A CB    1 
ATOM   2258 S  SG    . CYS A 1 300 ? 3.489   -12.223 2.793   1.00 102.96 ? 403  CYS A SG    1 
ATOM   2259 N  N     . LEU A 1 301 ? 1.566   -15.074 -0.942  1.00 100.96 ? 404  LEU A N     1 
ATOM   2260 C  CA    . LEU A 1 301 ? 0.790   -15.409 -2.125  1.00 116.58 ? 404  LEU A CA    1 
ATOM   2261 C  C     . LEU A 1 301 ? -0.622  -15.820 -1.731  1.00 107.93 ? 404  LEU A C     1 
ATOM   2262 O  O     . LEU A 1 301 ? -0.924  -16.063 -0.559  1.00 101.88 ? 404  LEU A O     1 
ATOM   2263 C  CB    . LEU A 1 301 ? 1.470   -16.524 -2.934  1.00 108.89 ? 404  LEU A CB    1 
ATOM   2264 C  CG    . LEU A 1 301 ? 2.019   -17.745 -2.189  1.00 115.45 ? 404  LEU A CG    1 
ATOM   2265 C  CD1   . LEU A 1 301 ? 0.925   -18.738 -1.815  1.00 111.31 ? 404  LEU A CD1   1 
ATOM   2266 C  CD2   . LEU A 1 301 ? 3.087   -18.423 -3.024  1.00 108.00 ? 404  LEU A CD2   1 
ATOM   2267 N  N     . SER A 1 302 ? -1.489  -15.903 -2.738  1.00 111.36 ? 405  SER A N     1 
ATOM   2268 C  CA    . SER A 1 302 ? -2.874  -16.302 -2.532  1.00 112.23 ? 405  SER A CA    1 
ATOM   2269 C  C     . SER A 1 302 ? -3.483  -16.670 -3.875  1.00 112.79 ? 405  SER A C     1 
ATOM   2270 O  O     . SER A 1 302 ? -3.025  -16.222 -4.929  1.00 113.82 ? 405  SER A O     1 
ATOM   2271 C  CB    . SER A 1 302 ? -3.690  -15.191 -1.862  1.00 110.59 ? 405  SER A CB    1 
ATOM   2272 O  OG    . SER A 1 302 ? -3.818  -14.069 -2.718  1.00 113.60 ? 405  SER A OG    1 
ATOM   2273 N  N     . ILE A 1 303 ? -4.525  -17.493 -3.820  1.00 118.02 ? 406  ILE A N     1 
ATOM   2274 C  CA    . ILE A 1 303 ? -5.309  -17.863 -4.993  1.00 114.67 ? 406  ILE A CA    1 
ATOM   2275 C  C     . ILE A 1 303 ? -6.596  -17.050 -4.946  1.00 119.11 ? 406  ILE A C     1 
ATOM   2276 O  O     . ILE A 1 303 ? -7.456  -17.282 -4.091  1.00 123.56 ? 406  ILE A O     1 
ATOM   2277 C  CB    . ILE A 1 303 ? -5.598  -19.369 -5.033  1.00 111.03 ? 406  ILE A CB    1 
ATOM   2278 C  CG1   . ILE A 1 303 ? -4.294  -20.161 -5.131  1.00 110.25 ? 406  ILE A CG1   1 
ATOM   2279 C  CG2   . ILE A 1 303 ? -6.518  -19.704 -6.196  1.00 114.73 ? 406  ILE A CG2   1 
ATOM   2280 C  CD1   . ILE A 1 303 ? -4.494  -21.660 -5.193  1.00 113.01 ? 406  ILE A CD1   1 
ATOM   2281 N  N     . CYS A 1 304 ? -6.732  -16.094 -5.859  1.00 122.02 ? 407  CYS A N     1 
ATOM   2282 C  CA    . CYS A 1 304 ? -7.864  -15.183 -5.874  1.00 127.90 ? 407  CYS A CA    1 
ATOM   2283 C  C     . CYS A 1 304 ? -8.785  -15.487 -7.048  1.00 133.55 ? 407  CYS A C     1 
ATOM   2284 O  O     . CYS A 1 304 ? -8.374  -16.055 -8.063  1.00 133.96 ? 407  CYS A O     1 
ATOM   2285 C  CB    . CYS A 1 304 ? -7.393  -13.726 -5.947  1.00 127.16 ? 407  CYS A CB    1 
ATOM   2286 S  SG    . CYS A 1 304 ? -6.184  -13.266 -4.689  1.00 120.35 ? 407  CYS A SG    1 
ATOM   2287 N  N     . SER A 1 305 ? -10.045 -15.096 -6.893  1.00 135.14 ? 408  SER A N     1 
ATOM   2288 C  CA    . SER A 1 305 ? -11.063 -15.248 -7.921  1.00 138.47 ? 408  SER A CA    1 
ATOM   2289 C  C     . SER A 1 305 ? -11.450 -13.882 -8.474  1.00 140.36 ? 408  SER A C     1 
ATOM   2290 O  O     . SER A 1 305 ? -11.118 -12.836 -7.910  1.00 141.95 ? 408  SER A O     1 
ATOM   2291 C  CB    . SER A 1 305 ? -12.294 -15.971 -7.364  1.00 143.96 ? 408  SER A CB    1 
ATOM   2292 O  OG    . SER A 1 305 ? -12.845 -15.264 -6.266  1.00 147.81 ? 408  SER A OG    1 
ATOM   2293 N  N     . VAL A 1 306 ? -12.166 -13.902 -9.597  1.00 144.78 ? 409  VAL A N     1 
ATOM   2294 C  CA    . VAL A 1 306 ? -12.580 -12.671 -10.262 1.00 149.53 ? 409  VAL A CA    1 
ATOM   2295 C  C     . VAL A 1 306 ? -13.781 -12.941 -11.160 1.00 155.60 ? 409  VAL A C     1 
ATOM   2296 O  O     . VAL A 1 306 ? -13.760 -13.856 -11.992 1.00 148.62 ? 409  VAL A O     1 
ATOM   2297 C  CB    . VAL A 1 306 ? -11.414 -12.053 -11.058 1.00 143.22 ? 409  VAL A CB    1 
ATOM   2298 C  CG1   . VAL A 1 306 ? -10.707 -13.116 -11.890 1.00 140.68 ? 409  VAL A CG1   1 
ATOM   2299 C  CG2   . VAL A 1 306 ? -11.912 -10.920 -11.941 1.00 144.52 ? 409  VAL A CG2   1 
ATOM   2300 N  N     . LYS A 1 307 ? -14.839 -12.153 -10.990 1.00 160.70 ? 410  LYS A N     1 
ATOM   2301 C  CA    . LYS A 1 307 ? -16.032 -12.276 -11.820 1.00 158.96 ? 410  LYS A CA    1 
ATOM   2302 C  C     . LYS A 1 307 ? -16.379 -10.938 -12.465 1.00 162.81 ? 410  LYS A C     1 
ATOM   2303 O  O     . LYS A 1 307 ? -16.244 -9.885  -11.842 1.00 168.36 ? 410  LYS A O     1 
ATOM   2304 C  CB    . LYS A 1 307 ? -17.221 -12.786 -11.000 1.00 164.44 ? 410  LYS A CB    1 
ATOM   2305 C  CG    . LYS A 1 307 ? -17.187 -14.277 -10.682 1.00 163.85 ? 410  LYS A CG    1 
ATOM   2306 C  CD    . LYS A 1 307 ? -16.333 -14.580 -9.460  1.00 161.72 ? 410  LYS A CD    1 
ATOM   2307 C  CE    . LYS A 1 307 ? -16.323 -16.068 -9.150  1.00 161.60 ? 410  LYS A CE    1 
ATOM   2308 N  NZ    . LYS A 1 307 ? -17.693 -16.593 -8.895  1.00 168.75 ? 410  LYS A NZ    1 
ATOM   2309 N  N     . GLU A 1 314 ? -13.561 -5.150  -10.445 1.00 141.40 ? 417  GLU A N     1 
ATOM   2310 C  CA    . GLU A 1 314 ? -14.764 -5.967  -10.343 1.00 149.85 ? 417  GLU A CA    1 
ATOM   2311 C  C     . GLU A 1 314 ? -14.780 -6.761  -9.038  1.00 157.54 ? 417  GLU A C     1 
ATOM   2312 O  O     . GLU A 1 314 ? -14.341 -6.268  -7.999  1.00 159.11 ? 417  GLU A O     1 
ATOM   2313 C  CB    . GLU A 1 314 ? -14.884 -6.910  -11.547 1.00 153.83 ? 417  GLU A CB    1 
ATOM   2314 C  CG    . GLU A 1 314 ? -13.639 -7.738  -11.845 1.00 150.86 ? 417  GLU A CG    1 
ATOM   2315 C  CD    . GLU A 1 314 ? -12.598 -6.977  -12.643 1.00 138.83 ? 417  GLU A CD    1 
ATOM   2316 O  OE1   . GLU A 1 314 ? -12.943 -5.926  -13.223 1.00 138.00 ? 417  GLU A OE1   1 
ATOM   2317 O  OE2   . GLU A 1 314 ? -11.434 -7.430  -12.686 1.00 132.50 ? 417  GLU A OE2   1 
ATOM   2318 N  N     . GLU A 1 315 ? -15.285 -7.995  -9.097  1.00 163.55 ? 418  GLU A N     1 
ATOM   2319 C  CA    . GLU A 1 315 ? -15.476 -8.814  -7.900  1.00 174.48 ? 418  GLU A CA    1 
ATOM   2320 C  C     . GLU A 1 315 ? -14.235 -9.675  -7.672  1.00 167.34 ? 418  GLU A C     1 
ATOM   2321 O  O     . GLU A 1 315 ? -14.167 -10.847 -8.047  1.00 170.33 ? 418  GLU A O     1 
ATOM   2322 C  CB    . GLU A 1 315 ? -16.734 -9.663  -8.032  1.00 181.13 ? 418  GLU A CB    1 
ATOM   2323 C  CG    . GLU A 1 315 ? -17.965 -8.881  -8.465  1.00 183.23 ? 418  GLU A CG    1 
ATOM   2324 C  CD    . GLU A 1 315 ? -18.359 -7.805  -7.470  1.00 186.45 ? 418  GLU A CD    1 
ATOM   2325 O  OE1   . GLU A 1 315 ? -18.156 -8.010  -6.254  1.00 172.62 ? 418  GLU A OE1   1 
ATOM   2326 O  OE2   . GLU A 1 315 ? -18.869 -6.751  -7.905  1.00 195.16 ? 418  GLU A OE2   1 
ATOM   2327 N  N     . HIS A 1 316 ? -13.236 -9.072  -7.032  1.00 154.12 ? 419  HIS A N     1 
ATOM   2328 C  CA    . HIS A 1 316 ? -12.021 -9.777  -6.643  1.00 148.94 ? 419  HIS A CA    1 
ATOM   2329 C  C     . HIS A 1 316 ? -12.201 -10.337 -5.237  1.00 149.96 ? 419  HIS A C     1 
ATOM   2330 O  O     . HIS A 1 316 ? -12.373 -9.577  -4.278  1.00 147.63 ? 419  HIS A O     1 
ATOM   2331 C  CB    . HIS A 1 316 ? -10.807 -8.850  -6.703  1.00 144.96 ? 419  HIS A CB    1 
ATOM   2332 C  CG    . HIS A 1 316 ? -10.442 -8.421  -8.090  1.00 146.72 ? 419  HIS A CG    1 
ATOM   2333 N  ND1   . HIS A 1 316 ? -9.676  -9.198  -8.932  1.00 142.95 ? 419  HIS A ND1   1 
ATOM   2334 C  CD2   . HIS A 1 316 ? -10.734 -7.293  -8.780  1.00 143.71 ? 419  HIS A CD2   1 
ATOM   2335 C  CE1   . HIS A 1 316 ? -9.514  -8.569  -10.082 1.00 142.62 ? 419  HIS A CE1   1 
ATOM   2336 N  NE2   . HIS A 1 316 ? -10.145 -7.411  -10.016 1.00 142.59 ? 419  HIS A NE2   1 
ATOM   2337 N  N     . CYS A 1 317 ? -12.161 -11.664 -5.116  1.00 153.28 ? 420  CYS A N     1 
ATOM   2338 C  CA    . CYS A 1 317 ? -12.411 -12.336 -3.851  1.00 153.49 ? 420  CYS A CA    1 
ATOM   2339 C  C     . CYS A 1 317 ? -11.324 -13.374 -3.597  1.00 145.48 ? 420  CYS A C     1 
ATOM   2340 O  O     . CYS A 1 317 ? -11.075 -14.234 -4.460  1.00 155.17 ? 420  CYS A O     1 
ATOM   2341 C  CB    . CYS A 1 317 ? -13.795 -13.000 -3.855  1.00 153.16 ? 420  CYS A CB    1 
ATOM   2342 S  SG    . CYS A 1 317 ? -14.189 -13.928 -2.357  1.00 170.26 ? 420  CYS A SG    1 
ATOM   2343 N  N     . PRO A 1 318 ? -10.659 -13.334 -2.445  1.00 140.59 ? 421  PRO A N     1 
ATOM   2344 C  CA    . PRO A 1 318 ? -9.641  -14.347 -2.148  1.00 137.39 ? 421  PRO A CA    1 
ATOM   2345 C  C     . PRO A 1 318 ? -10.269 -15.691 -1.815  1.00 136.68 ? 421  PRO A C     1 
ATOM   2346 O  O     . PRO A 1 318 ? -11.368 -15.772 -1.260  1.00 135.69 ? 421  PRO A O     1 
ATOM   2347 C  CB    . PRO A 1 318 ? -8.904  -13.763 -0.938  1.00 134.95 ? 421  PRO A CB    1 
ATOM   2348 C  CG    . PRO A 1 318 ? -9.920  -12.897 -0.272  1.00 136.33 ? 421  PRO A CG    1 
ATOM   2349 C  CD    . PRO A 1 318 ? -10.764 -12.322 -1.379  1.00 143.84 ? 421  PRO A CD    1 
ATOM   2350 N  N     . LEU A 1 319 ? -9.550  -16.755 -2.162  1.00 130.50 ? 422  LEU A N     1 
ATOM   2351 C  CA    . LEU A 1 319 ? -10.008 -18.120 -1.934  1.00 127.79 ? 422  LEU A CA    1 
ATOM   2352 C  C     . LEU A 1 319 ? -9.137  -18.891 -0.956  1.00 121.06 ? 422  LEU A C     1 
ATOM   2353 O  O     . LEU A 1 319 ? -9.663  -19.643 -0.131  1.00 124.05 ? 422  LEU A O     1 
ATOM   2354 C  CB    . LEU A 1 319 ? -10.077 -18.883 -3.266  1.00 127.45 ? 422  LEU A CB    1 
ATOM   2355 C  CG    . LEU A 1 319 ? -10.852 -18.201 -4.397  1.00 133.20 ? 422  LEU A CG    1 
ATOM   2356 C  CD1   . LEU A 1 319 ? -10.797 -19.034 -5.669  1.00 132.71 ? 422  LEU A CD1   1 
ATOM   2357 C  CD2   . LEU A 1 319 ? -12.293 -17.940 -3.985  1.00 135.42 ? 422  LEU A CD2   1 
ATOM   2358 N  N     . ALA A 1 320 ? -7.817  -18.728 -1.026  1.00 116.54 ? 423  ALA A N     1 
ATOM   2359 C  CA    . ALA A 1 320 ? -6.903  -19.388 -0.105  1.00 113.92 ? 423  ALA A CA    1 
ATOM   2360 C  C     . ALA A 1 320 ? -5.571  -18.653 -0.136  1.00 111.55 ? 423  ALA A C     1 
ATOM   2361 O  O     . ALA A 1 320 ? -5.145  -18.180 -1.192  1.00 111.46 ? 423  ALA A O     1 
ATOM   2362 C  CB    . ALA A 1 320 ? -6.709  -20.866 -0.463  1.00 117.94 ? 423  ALA A CB    1 
ATOM   2363 N  N     . TRP A 1 321 ? -4.921  -18.568 1.021   1.00 105.28 ? 424  TRP A N     1 
ATOM   2364 C  CA    . TRP A 1 321 ? -3.690  -17.809 1.180   1.00 102.36 ? 424  TRP A CA    1 
ATOM   2365 C  C     . TRP A 1 321 ? -2.558  -18.725 1.632   1.00 98.27  ? 424  TRP A C     1 
ATOM   2366 O  O     . TRP A 1 321 ? -2.769  -19.877 2.017   1.00 96.74  ? 424  TRP A O     1 
ATOM   2367 C  CB    . TRP A 1 321 ? -3.876  -16.668 2.188   1.00 106.23 ? 424  TRP A CB    1 
ATOM   2368 C  CG    . TRP A 1 321 ? -4.080  -17.153 3.588   1.00 105.92 ? 424  TRP A CG    1 
ATOM   2369 C  CD1   . TRP A 1 321 ? -5.241  -17.614 4.136   1.00 105.18 ? 424  TRP A CD1   1 
ATOM   2370 C  CD2   . TRP A 1 321 ? -3.089  -17.234 4.620   1.00 104.75 ? 424  TRP A CD2   1 
ATOM   2371 N  NE1   . TRP A 1 321 ? -5.035  -17.975 5.445   1.00 111.24 ? 424  TRP A NE1   1 
ATOM   2372 C  CE2   . TRP A 1 321 ? -3.723  -17.751 5.767   1.00 108.21 ? 424  TRP A CE2   1 
ATOM   2373 C  CE3   . TRP A 1 321 ? -1.729  -16.919 4.685   1.00 103.65 ? 424  TRP A CE3   1 
ATOM   2374 C  CZ2   . TRP A 1 321 ? -3.043  -17.959 6.965   1.00 103.89 ? 424  TRP A CZ2   1 
ATOM   2375 C  CZ3   . TRP A 1 321 ? -1.056  -17.126 5.875   1.00 107.39 ? 424  TRP A CZ3   1 
ATOM   2376 C  CH2   . TRP A 1 321 ? -1.713  -17.642 6.999   1.00 106.39 ? 424  TRP A CH2   1 
ATOM   2377 N  N     . GLY A 1 322 ? -1.341  -18.187 1.586   1.00 97.13  ? 425  GLY A N     1 
ATOM   2378 C  CA    . GLY A 1 322 ? -0.162  -18.918 2.010   1.00 98.01  ? 425  GLY A CA    1 
ATOM   2379 C  C     . GLY A 1 322 ? 1.085   -18.057 2.015   1.00 100.71 ? 425  GLY A C     1 
ATOM   2380 O  O     . GLY A 1 322 ? 1.253   -17.197 1.145   1.00 103.24 ? 425  GLY A O     1 
ATOM   2381 N  N     . ASN A 1 323 ? 1.967   -18.275 2.989   1.00 98.83  ? 426  ASN A N     1 
ATOM   2382 C  CA    . ASN A 1 323 ? 3.192   -17.501 3.122   1.00 98.49  ? 426  ASN A CA    1 
ATOM   2383 C  C     . ASN A 1 323 ? 4.386   -18.437 3.250   1.00 98.21  ? 426  ASN A C     1 
ATOM   2384 O  O     . ASN A 1 323 ? 4.260   -19.571 3.721   1.00 100.10 ? 426  ASN A O     1 
ATOM   2385 C  CB    . ASN A 1 323 ? 3.136   -16.561 4.336   1.00 98.88  ? 426  ASN A CB    1 
ATOM   2386 C  CG    . ASN A 1 323 ? 2.020   -15.539 4.234   1.00 100.41 ? 426  ASN A CG    1 
ATOM   2387 O  OD1   . ASN A 1 323 ? 1.621   -15.144 3.138   1.00 97.67  ? 426  ASN A OD1   1 
ATOM   2388 N  ND2   . ASN A 1 323 ? 1.512   -15.104 5.381   1.00 103.38 ? 426  ASN A ND2   1 
ATOM   2389 N  N     . ILE A 1 324 ? 5.548   -17.946 2.828   1.00 95.04  ? 427  ILE A N     1 
ATOM   2390 C  CA    . ILE A 1 324 ? 6.782   -18.723 2.865   1.00 96.69  ? 427  ILE A CA    1 
ATOM   2391 C  C     . ILE A 1 324 ? 7.956   -17.764 2.994   1.00 94.28  ? 427  ILE A C     1 
ATOM   2392 O  O     . ILE A 1 324 ? 8.006   -16.728 2.324   1.00 96.08  ? 427  ILE A O     1 
ATOM   2393 C  CB    . ILE A 1 324 ? 6.924   -19.621 1.614   1.00 93.70  ? 427  ILE A CB    1 
ATOM   2394 C  CG1   . ILE A 1 324 ? 8.325   -20.236 1.549   1.00 93.09  ? 427  ILE A CG1   1 
ATOM   2395 C  CG2   . ILE A 1 324 ? 6.611   -18.835 0.349   1.00 94.11  ? 427  ILE A CG2   1 
ATOM   2396 C  CD1   . ILE A 1 324 ? 8.550   -21.131 0.359   1.00 98.03  ? 427  ILE A CD1   1 
ATOM   2397 N  N     . ASN A 1 325 ? 8.900   -18.111 3.867   1.00 84.59  ? 428  ASN A N     1 
ATOM   2398 C  CA    . ASN A 1 325 ? 10.107  -17.316 4.043   1.00 86.68  ? 428  ASN A CA    1 
ATOM   2399 C  C     . ASN A 1 325 ? 11.052  -17.536 2.867   1.00 100.82 ? 428  ASN A C     1 
ATOM   2400 O  O     . ASN A 1 325 ? 11.294  -18.677 2.460   1.00 103.34 ? 428  ASN A O     1 
ATOM   2401 C  CB    . ASN A 1 325 ? 10.805  -17.690 5.350   1.00 96.93  ? 428  ASN A CB    1 
ATOM   2402 C  CG    . ASN A 1 325 ? 9.850   -17.759 6.525   1.00 92.55  ? 428  ASN A CG    1 
ATOM   2403 O  OD1   . ASN A 1 325 ? 8.962   -16.918 6.674   1.00 84.80  ? 428  ASN A OD1   1 
ATOM   2404 N  ND2   . ASN A 1 325 ? 10.026  -18.770 7.367   1.00 75.64  ? 428  ASN A ND2   1 
ATOM   2405 N  N     . LEU A 1 326 ? 11.590  -16.442 2.323   1.00 101.51 ? 429  LEU A N     1 
ATOM   2406 C  CA    . LEU A 1 326 ? 12.578  -16.550 1.254   1.00 91.90  ? 429  LEU A CA    1 
ATOM   2407 C  C     . LEU A 1 326 ? 13.908  -17.111 1.742   1.00 92.74  ? 429  LEU A C     1 
ATOM   2408 O  O     . LEU A 1 326 ? 14.737  -17.503 0.914   1.00 101.86 ? 429  LEU A O     1 
ATOM   2409 C  CB    . LEU A 1 326 ? 12.797  -15.185 0.599   1.00 90.62  ? 429  LEU A CB    1 
ATOM   2410 C  CG    . LEU A 1 326 ? 11.594  -14.598 -0.142  1.00 91.66  ? 429  LEU A CG    1 
ATOM   2411 C  CD1   . LEU A 1 326 ? 11.929  -13.241 -0.742  1.00 87.76  ? 429  LEU A CD1   1 
ATOM   2412 C  CD2   . LEU A 1 326 ? 11.104  -15.557 -1.217  1.00 91.31  ? 429  LEU A CD2   1 
ATOM   2413 N  N     . PHE A 1 327 ? 14.135  -17.151 3.051   1.00 99.58  ? 430  PHE A N     1 
ATOM   2414 C  CA    . PHE A 1 327 ? 15.313  -17.771 3.636   1.00 97.24  ? 430  PHE A CA    1 
ATOM   2415 C  C     . PHE A 1 327 ? 14.876  -18.809 4.659   1.00 92.69  ? 430  PHE A C     1 
ATOM   2416 O  O     . PHE A 1 327 ? 13.871  -18.626 5.352   1.00 92.26  ? 430  PHE A O     1 
ATOM   2417 C  CB    . PHE A 1 327 ? 16.222  -16.737 4.309   1.00 90.24  ? 430  PHE A CB    1 
ATOM   2418 C  CG    . PHE A 1 327 ? 16.876  -15.785 3.351   1.00 95.00  ? 430  PHE A CG    1 
ATOM   2419 C  CD1   . PHE A 1 327 ? 18.080  -16.109 2.747   1.00 99.81  ? 430  PHE A CD1   1 
ATOM   2420 C  CD2   . PHE A 1 327 ? 16.295  -14.561 3.063   1.00 91.95  ? 430  PHE A CD2   1 
ATOM   2421 C  CE1   . PHE A 1 327 ? 18.688  -15.235 1.870   1.00 93.63  ? 430  PHE A CE1   1 
ATOM   2422 C  CE2   . PHE A 1 327 ? 16.899  -13.681 2.188   1.00 83.67  ? 430  PHE A CE2   1 
ATOM   2423 C  CZ    . PHE A 1 327 ? 18.097  -14.019 1.590   1.00 91.78  ? 430  PHE A CZ    1 
ATOM   2424 N  N     . ASP A 1 328 ? 15.628  -19.901 4.749   1.00 96.00  ? 431  ASP A N     1 
ATOM   2425 C  CA    . ASP A 1 328 ? 15.355  -20.930 5.738   1.00 96.32  ? 431  ASP A CA    1 
ATOM   2426 C  C     . ASP A 1 328 ? 16.148  -20.619 7.008   1.00 105.85 ? 431  ASP A C     1 
ATOM   2427 O  O     . ASP A 1 328 ? 16.805  -19.579 7.113   1.00 103.99 ? 431  ASP A O     1 
ATOM   2428 C  CB    . ASP A 1 328 ? 15.665  -22.313 5.166   1.00 98.94  ? 431  ASP A CB    1 
ATOM   2429 C  CG    . ASP A 1 328 ? 17.149  -22.551 4.985   1.00 102.07 ? 431  ASP A CG    1 
ATOM   2430 O  OD1   . ASP A 1 328 ? 17.912  -21.565 4.959   1.00 114.25 ? 431  ASP A OD1   1 
ATOM   2431 O  OD2   . ASP A 1 328 ? 17.552  -23.727 4.865   1.00 101.82 ? 431  ASP A OD2   1 
ATOM   2432 N  N     . TYR A 1 329 ? 16.104  -21.524 7.989   1.00 102.94 ? 432  TYR A N     1 
ATOM   2433 C  CA    . TYR A 1 329 ? 16.737  -21.261 9.277   1.00 93.66  ? 432  TYR A CA    1 
ATOM   2434 C  C     . TYR A 1 329 ? 18.260  -21.323 9.225   1.00 98.28  ? 432  TYR A C     1 
ATOM   2435 O  O     . TYR A 1 329 ? 18.908  -20.987 10.222  1.00 98.57  ? 432  TYR A O     1 
ATOM   2436 C  CB    . TYR A 1 329 ? 16.211  -22.242 10.326  1.00 88.22  ? 432  TYR A CB    1 
ATOM   2437 C  CG    . TYR A 1 329 ? 16.712  -23.662 10.174  1.00 84.74  ? 432  TYR A CG    1 
ATOM   2438 C  CD1   . TYR A 1 329 ? 16.153  -24.524 9.239   1.00 94.47  ? 432  TYR A CD1   1 
ATOM   2439 C  CD2   . TYR A 1 329 ? 17.735  -24.144 10.978  1.00 82.91  ? 432  TYR A CD2   1 
ATOM   2440 C  CE1   . TYR A 1 329 ? 16.610  -25.824 9.104   1.00 95.39  ? 432  TYR A CE1   1 
ATOM   2441 C  CE2   . TYR A 1 329 ? 18.195  -25.438 10.853  1.00 85.69  ? 432  TYR A CE2   1 
ATOM   2442 C  CZ    . TYR A 1 329 ? 17.630  -26.275 9.917   1.00 88.85  ? 432  TYR A CZ    1 
ATOM   2443 O  OH    . TYR A 1 329 ? 18.093  -27.566 9.794   1.00 90.58  ? 432  TYR A OH    1 
ATOM   2444 N  N     . THR A 1 330 ? 18.847  -21.735 8.101   1.00 99.45  ? 433  THR A N     1 
ATOM   2445 C  CA    . THR A 1 330 ? 20.295  -21.778 7.946   1.00 101.00 ? 433  THR A CA    1 
ATOM   2446 C  C     . THR A 1 330 ? 20.826  -20.610 7.122   1.00 104.42 ? 433  THR A C     1 
ATOM   2447 O  O     . THR A 1 330 ? 21.962  -20.668 6.638   1.00 107.27 ? 433  THR A O     1 
ATOM   2448 C  CB    . THR A 1 330 ? 20.724  -23.103 7.313   1.00 101.38 ? 433  THR A CB    1 
ATOM   2449 O  OG1   . THR A 1 330 ? 20.356  -23.115 5.928   1.00 116.04 ? 433  THR A OG1   1 
ATOM   2450 C  CG2   . THR A 1 330 ? 20.050  -24.270 8.018   1.00 94.55  ? 433  THR A CG2   1 
ATOM   2451 N  N     . ASP A 1 331 ? 20.022  -19.556 6.954   1.00 113.99 ? 434  ASP A N     1 
ATOM   2452 C  CA    . ASP A 1 331 ? 20.380  -18.385 6.149   1.00 114.17 ? 434  ASP A CA    1 
ATOM   2453 C  C     . ASP A 1 331 ? 20.609  -18.748 4.683   1.00 116.79 ? 434  ASP A C     1 
ATOM   2454 O  O     . ASP A 1 331 ? 21.398  -18.103 3.990   1.00 124.26 ? 434  ASP A O     1 
ATOM   2455 C  CB    . ASP A 1 331 ? 21.608  -17.663 6.715   1.00 113.20 ? 434  ASP A CB    1 
ATOM   2456 C  CG    . ASP A 1 331 ? 21.374  -17.112 8.108   1.00 121.38 ? 434  ASP A CG    1 
ATOM   2457 O  OD1   . ASP A 1 331 ? 20.305  -17.391 8.692   1.00 112.48 ? 434  ASP A OD1   1 
ATOM   2458 O  OD2   . ASP A 1 331 ? 22.261  -16.395 8.619   1.00 123.75 ? 434  ASP A OD2   1 
ATOM   2459 N  N     . THR A 1 332 ? 19.919  -19.777 4.196   1.00 105.26 ? 435  THR A N     1 
ATOM   2460 C  CA    . THR A 1 332 ? 20.042  -20.223 2.814   1.00 106.75 ? 435  THR A CA    1 
ATOM   2461 C  C     . THR A 1 332 ? 18.891  -19.661 1.991   1.00 101.80 ? 435  THR A C     1 
ATOM   2462 O  O     . THR A 1 332 ? 17.735  -19.701 2.424   1.00 97.64  ? 435  THR A O     1 
ATOM   2463 C  CB    . THR A 1 332 ? 20.049  -21.751 2.726   1.00 111.41 ? 435  THR A CB    1 
ATOM   2464 O  OG1   . THR A 1 332 ? 21.117  -22.276 3.522   1.00 114.96 ? 435  THR A OG1   1 
ATOM   2465 C  CG2   . THR A 1 332 ? 20.219  -22.208 1.285   1.00 98.33  ? 435  THR A CG2   1 
ATOM   2466 N  N     . LEU A 1 333 ? 19.210  -19.139 0.809   1.00 106.11 ? 436  LEU A N     1 
ATOM   2467 C  CA    . LEU A 1 333 ? 18.176  -18.660 -0.096  1.00 99.45  ? 436  LEU A CA    1 
ATOM   2468 C  C     . LEU A 1 333 ? 17.409  -19.838 -0.683  1.00 93.46  ? 436  LEU A C     1 
ATOM   2469 O  O     . LEU A 1 333 ? 17.989  -20.876 -1.013  1.00 96.19  ? 436  LEU A O     1 
ATOM   2470 C  CB    . LEU A 1 333 ? 18.793  -17.820 -1.214  1.00 98.16  ? 436  LEU A CB    1 
ATOM   2471 C  CG    . LEU A 1 333 ? 17.808  -17.063 -2.107  1.00 103.04 ? 436  LEU A CG    1 
ATOM   2472 C  CD1   . LEU A 1 333 ? 17.052  -16.016 -1.300  1.00 87.57  ? 436  LEU A CD1   1 
ATOM   2473 C  CD2   . LEU A 1 333 ? 18.523  -16.429 -3.294  1.00 100.58 ? 436  LEU A CD2   1 
ATOM   2474 N  N     . VAL A 1 334 ? 16.092  -19.673 -0.810  1.00 89.99  ? 437  VAL A N     1 
ATOM   2475 C  CA    . VAL A 1 334 ? 15.251  -20.751 -1.313  1.00 100.95 ? 437  VAL A CA    1 
ATOM   2476 C  C     . VAL A 1 334 ? 15.530  -20.980 -2.792  1.00 113.93 ? 437  VAL A C     1 
ATOM   2477 O  O     . VAL A 1 334 ? 15.708  -20.031 -3.569  1.00 118.93 ? 437  VAL A O     1 
ATOM   2478 C  CB    . VAL A 1 334 ? 13.766  -20.437 -1.066  1.00 101.32 ? 437  VAL A CB    1 
ATOM   2479 C  CG1   . VAL A 1 334 ? 13.440  -20.555 0.416   1.00 108.71 ? 437  VAL A CG1   1 
ATOM   2480 C  CG2   . VAL A 1 334 ? 13.425  -19.046 -1.576  1.00 99.22  ? 437  VAL A CG2   1 
ATOM   2481 N  N     . SER A 1 335 ? 15.575  -22.249 -3.188  1.00 120.02 ? 438  SER A N     1 
ATOM   2482 C  CA    . SER A 1 335 ? 15.802  -22.614 -4.578  1.00 115.29 ? 438  SER A CA    1 
ATOM   2483 C  C     . SER A 1 335 ? 15.287  -24.027 -4.797  1.00 115.38 ? 438  SER A C     1 
ATOM   2484 O  O     . SER A 1 335 ? 15.495  -24.905 -3.956  1.00 117.48 ? 438  SER A O     1 
ATOM   2485 C  CB    . SER A 1 335 ? 17.286  -22.521 -4.950  1.00 116.86 ? 438  SER A CB    1 
ATOM   2486 O  OG    . SER A 1 335 ? 18.059  -23.425 -4.181  1.00 127.86 ? 438  SER A OG    1 
ATOM   2487 N  N     . GLY A 1 336 ? 14.616  -24.235 -5.921  1.00 110.78 ? 439  GLY A N     1 
ATOM   2488 C  CA    . GLY A 1 336 ? 14.089  -25.535 -6.283  1.00 109.95 ? 439  GLY A CA    1 
ATOM   2489 C  C     . GLY A 1 336 ? 12.570  -25.561 -6.242  1.00 109.94 ? 439  GLY A C     1 
ATOM   2490 O  O     . GLY A 1 336 ? 11.900  -24.564 -5.968  1.00 106.86 ? 439  GLY A O     1 
ATOM   2491 N  N     . LYS A 1 337 ? 12.041  -26.748 -6.523  1.00 111.25 ? 440  LYS A N     1 
ATOM   2492 C  CA    . LYS A 1 337 ? 10.602  -26.957 -6.577  1.00 114.20 ? 440  LYS A CA    1 
ATOM   2493 C  C     . LYS A 1 337 ? 10.054  -27.220 -5.181  1.00 120.44 ? 440  LYS A C     1 
ATOM   2494 O  O     . LYS A 1 337 ? 10.710  -27.856 -4.351  1.00 128.48 ? 440  LYS A O     1 
ATOM   2495 C  CB    . LYS A 1 337 ? 10.277  -28.129 -7.502  1.00 126.72 ? 440  LYS A CB    1 
ATOM   2496 C  CG    . LYS A 1 337 ? 8.911   -28.059 -8.158  1.00 123.69 ? 440  LYS A CG    1 
ATOM   2497 C  CD    . LYS A 1 337 ? 8.762   -29.154 -9.200  1.00 122.16 ? 440  LYS A CD    1 
ATOM   2498 C  CE    . LYS A 1 337 ? 9.888   -29.103 -10.223 1.00 122.43 ? 440  LYS A CE    1 
ATOM   2499 N  NZ    . LYS A 1 337 ? 9.770   -30.190 -11.236 1.00 120.91 ? 440  LYS A NZ    1 
ATOM   2500 N  N     . MET A 1 338 ? 8.845   -26.724 -4.922  1.00 123.75 ? 441  MET A N     1 
ATOM   2501 C  CA    . MET A 1 338 ? 8.242   -26.882 -3.607  1.00 115.64 ? 441  MET A CA    1 
ATOM   2502 C  C     . MET A 1 338 ? 6.735   -26.697 -3.711  1.00 117.33 ? 441  MET A C     1 
ATOM   2503 O  O     . MET A 1 338 ? 6.260   -25.778 -4.384  1.00 116.64 ? 441  MET A O     1 
ATOM   2504 C  CB    . MET A 1 338 ? 8.823   -25.881 -2.603  1.00 115.48 ? 441  MET A CB    1 
ATOM   2505 C  CG    . MET A 1 338 ? 8.457   -26.180 -1.161  1.00 135.29 ? 441  MET A CG    1 
ATOM   2506 S  SD    . MET A 1 338 ? 8.228   -24.689 -0.176  1.00 148.45 ? 441  MET A SD    1 
ATOM   2507 C  CE    . MET A 1 338 ? 6.764   -24.008 -0.952  1.00 123.69 ? 441  MET A CE    1 
ATOM   2508 N  N     . ALA A 1 339 ? 5.995   -27.572 -3.036  1.00 112.79 ? 442  ALA A N     1 
ATOM   2509 C  CA    . ALA A 1 339 ? 4.549   -27.463 -2.924  1.00 111.36 ? 442  ALA A CA    1 
ATOM   2510 C  C     . ALA A 1 339 ? 4.190   -26.777 -1.612  1.00 116.24 ? 442  ALA A C     1 
ATOM   2511 O  O     . ALA A 1 339 ? 4.846   -26.989 -0.589  1.00 115.54 ? 442  ALA A O     1 
ATOM   2512 C  CB    . ALA A 1 339 ? 3.886   -28.839 -2.999  1.00 107.77 ? 442  ALA A CB    1 
ATOM   2513 N  N     . LEU A 1 340 ? 3.145   -25.952 -1.648  1.00 114.51 ? 443  LEU A N     1 
ATOM   2514 C  CA    . LEU A 1 340 ? 2.740   -25.143 -0.499  1.00 107.66 ? 443  LEU A CA    1 
ATOM   2515 C  C     . LEU A 1 340 ? 1.241   -25.333 -0.283  1.00 109.32 ? 443  LEU A C     1 
ATOM   2516 O  O     . LEU A 1 340 ? 0.425   -24.761 -1.012  1.00 112.49 ? 443  LEU A O     1 
ATOM   2517 C  CB    . LEU A 1 340 ? 3.091   -23.674 -0.721  1.00 106.14 ? 443  LEU A CB    1 
ATOM   2518 C  CG    . LEU A 1 340 ? 3.282   -22.756 0.490   1.00 110.58 ? 443  LEU A CG    1 
ATOM   2519 C  CD1   . LEU A 1 340 ? 3.986   -21.477 0.064   1.00 115.34 ? 443  LEU A CD1   1 
ATOM   2520 C  CD2   . LEU A 1 340 ? 1.963   -22.426 1.171   1.00 112.81 ? 443  LEU A CD2   1 
ATOM   2521 N  N     . ASN A 1 341 ? 0.882   -26.131 0.719   1.00 116.99 ? 444  ASN A N     1 
ATOM   2522 C  CA    . ASN A 1 341 ? -0.520  -26.307 1.077   1.00 120.05 ? 444  ASN A CA    1 
ATOM   2523 C  C     . ASN A 1 341 ? -1.063  -25.013 1.671   1.00 113.36 ? 444  ASN A C     1 
ATOM   2524 O  O     . ASN A 1 341 ? -0.581  -24.546 2.707   1.00 108.44 ? 444  ASN A O     1 
ATOM   2525 C  CB    . ASN A 1 341 ? -0.670  -27.462 2.062   1.00 118.51 ? 444  ASN A CB    1 
ATOM   2526 C  CG    . ASN A 1 341 ? -0.488  -28.816 1.405   1.00 125.16 ? 444  ASN A CG    1 
ATOM   2527 O  OD1   . ASN A 1 341 ? -1.461  -29.512 1.115   1.00 127.70 ? 444  ASN A OD1   1 
ATOM   2528 N  ND2   . ASN A 1 341 ? 0.761   -29.194 1.161   1.00 123.88 ? 444  ASN A ND2   1 
ATOM   2529 N  N     . LEU A 1 342 ? -2.064  -24.432 1.015   1.00 115.52 ? 445  LEU A N     1 
ATOM   2530 C  CA    . LEU A 1 342 ? -2.583  -23.139 1.425   1.00 111.27 ? 445  LEU A CA    1 
ATOM   2531 C  C     . LEU A 1 342 ? -3.495  -23.276 2.642   1.00 116.03 ? 445  LEU A C     1 
ATOM   2532 O  O     . LEU A 1 342 ? -3.856  -24.375 3.069   1.00 118.38 ? 445  LEU A O     1 
ATOM   2533 C  CB    . LEU A 1 342 ? -3.333  -22.471 0.273   1.00 109.46 ? 445  LEU A CB    1 
ATOM   2534 C  CG    . LEU A 1 342 ? -2.502  -22.085 -0.951  1.00 104.51 ? 445  LEU A CG    1 
ATOM   2535 C  CD1   . LEU A 1 342 ? -3.260  -21.086 -1.803  1.00 107.23 ? 445  LEU A CD1   1 
ATOM   2536 C  CD2   . LEU A 1 342 ? -1.149  -21.526 -0.544  1.00 99.33  ? 445  LEU A CD2   1 
ATOM   2537 N  N     . TRP A 1 343 ? -3.870  -22.127 3.204   1.00 120.42 ? 446  TRP A N     1 
ATOM   2538 C  CA    . TRP A 1 343 ? -4.706  -22.060 4.389   1.00 108.23 ? 446  TRP A CA    1 
ATOM   2539 C  C     . TRP A 1 343 ? -6.071  -21.471 4.055   1.00 113.04 ? 446  TRP A C     1 
ATOM   2540 O  O     . TRP A 1 343 ? -6.168  -20.581 3.203   1.00 116.29 ? 446  TRP A O     1 
ATOM   2541 C  CB    . TRP A 1 343 ? -4.044  -21.210 5.479   1.00 106.56 ? 446  TRP A CB    1 
ATOM   2542 C  CG    . TRP A 1 343 ? -2.783  -21.802 6.016   1.00 108.98 ? 446  TRP A CG    1 
ATOM   2543 C  CD1   . TRP A 1 343 ? -1.520  -21.621 5.533   1.00 107.96 ? 446  TRP A CD1   1 
ATOM   2544 C  CD2   . TRP A 1 343 ? -2.661  -22.674 7.144   1.00 113.97 ? 446  TRP A CD2   1 
ATOM   2545 N  NE1   . TRP A 1 343 ? -0.618  -22.329 6.291   1.00 110.02 ? 446  TRP A NE1   1 
ATOM   2546 C  CE2   . TRP A 1 343 ? -1.294  -22.983 7.287   1.00 118.61 ? 446  TRP A CE2   1 
ATOM   2547 C  CE3   . TRP A 1 343 ? -3.575  -23.223 8.047   1.00 110.28 ? 446  TRP A CE3   1 
ATOM   2548 C  CZ2   . TRP A 1 343 ? -0.820  -23.815 8.297   1.00 116.04 ? 446  TRP A CZ2   1 
ATOM   2549 C  CZ3   . TRP A 1 343 ? -3.103  -24.050 9.047   1.00 115.71 ? 446  TRP A CZ3   1 
ATOM   2550 C  CH2   . TRP A 1 343 ? -1.738  -24.337 9.165   1.00 113.48 ? 446  TRP A CH2   1 
ATOM   2551 N  N     . PRO A 1 344 ? -7.136  -21.944 4.702   1.00 114.63 ? 447  PRO A N     1 
ATOM   2552 C  CA    . PRO A 1 344 ? -8.463  -21.374 4.440   1.00 111.74 ? 447  PRO A CA    1 
ATOM   2553 C  C     . PRO A 1 344 ? -8.546  -19.931 4.913   1.00 113.55 ? 447  PRO A C     1 
ATOM   2554 O  O     . PRO A 1 344 ? -7.952  -19.553 5.926   1.00 111.27 ? 447  PRO A O     1 
ATOM   2555 C  CB    . PRO A 1 344 ? -9.405  -22.283 5.238   1.00 107.04 ? 447  PRO A CB    1 
ATOM   2556 C  CG    . PRO A 1 344 ? -8.544  -22.875 6.305   1.00 104.25 ? 447  PRO A CG    1 
ATOM   2557 C  CD    . PRO A 1 344 ? -7.184  -23.035 5.689   1.00 112.15 ? 447  PRO A CD    1 
ATOM   2558 N  N     . VAL A 1 345 ? -9.285  -19.125 4.163   1.00 118.85 ? 448  VAL A N     1 
ATOM   2559 C  CA    . VAL A 1 345 ? -9.412  -17.700 4.495   1.00 127.10 ? 448  VAL A CA    1 
ATOM   2560 C  C     . VAL A 1 345 ? -10.341 -17.546 5.693   1.00 137.25 ? 448  VAL A C     1 
ATOM   2561 O  O     . VAL A 1 345 ? -11.392 -18.211 5.746   1.00 136.59 ? 448  VAL A O     1 
ATOM   2562 C  CB    . VAL A 1 345 ? -9.933  -16.918 3.287   1.00 119.72 ? 448  VAL A CB    1 
ATOM   2563 C  CG1   . VAL A 1 345 ? -9.988  -15.429 3.596   1.00 122.52 ? 448  VAL A CG1   1 
ATOM   2564 C  CG2   . VAL A 1 345 ? -9.057  -17.178 2.076   1.00 120.89 ? 448  VAL A CG2   1 
ATOM   2565 N  N     . PRO A 1 346 ? -10.008 -16.699 6.671   1.00 154.91 ? 449  PRO A N     1 
ATOM   2566 C  CA    . PRO A 1 346 ? -10.890 -16.539 7.835   1.00 153.45 ? 449  PRO A CA    1 
ATOM   2567 C  C     . PRO A 1 346 ? -12.105 -15.677 7.528   1.00 168.77 ? 449  PRO A C     1 
ATOM   2568 O  O     . PRO A 1 346 ? -12.344 -15.318 6.370   1.00 169.32 ? 449  PRO A O     1 
ATOM   2569 C  CB    . PRO A 1 346 ? -9.979  -15.879 8.877   1.00 150.67 ? 449  PRO A CB    1 
ATOM   2570 N  N     . HIS A 1 347 ? -12.879 -15.342 8.558   1.00 156.41 ? 450  HIS A N     1 
ATOM   2571 C  CA    . HIS A 1 347 ? -14.072 -14.528 8.366   1.00 150.40 ? 450  HIS A CA    1 
ATOM   2572 C  C     . HIS A 1 347 ? -13.685 -13.100 8.002   1.00 151.30 ? 450  HIS A C     1 
ATOM   2573 O  O     . HIS A 1 347 ? -12.809 -12.501 8.633   1.00 146.39 ? 450  HIS A O     1 
ATOM   2574 C  CB    . HIS A 1 347 ? -14.932 -14.542 9.628   1.00 137.69 ? 450  HIS A CB    1 
ATOM   2575 N  N     . GLY A 1 348 ? -14.343 -12.555 6.982   1.00 153.14 ? 451  GLY A N     1 
ATOM   2576 C  CA    . GLY A 1 348 ? -14.025 -11.225 6.502   1.00 154.69 ? 451  GLY A CA    1 
ATOM   2577 C  C     . GLY A 1 348 ? -13.031 -11.246 5.360   1.00 165.28 ? 451  GLY A C     1 
ATOM   2578 O  O     . GLY A 1 348 ? -12.029 -11.966 5.416   1.00 167.17 ? 451  GLY A O     1 
ATOM   2579 N  N     . LEU A 1 349 ? -13.294 -10.464 4.318   1.00 170.24 ? 452  LEU A N     1 
ATOM   2580 C  CA    . LEU A 1 349 ? -12.451 -10.419 3.125   1.00 167.43 ? 452  LEU A CA    1 
ATOM   2581 C  C     . LEU A 1 349 ? -11.703 -9.089  3.113   1.00 170.81 ? 452  LEU A C     1 
ATOM   2582 O  O     . LEU A 1 349 ? -12.266 -8.053  2.749   1.00 168.55 ? 452  LEU A O     1 
ATOM   2583 C  CB    . LEU A 1 349 ? -13.287 -10.601 1.862   1.00 157.72 ? 452  LEU A CB    1 
ATOM   2584 N  N     . GLU A 1 350 ? -10.432 -9.123  3.511   1.00 176.95 ? 453  GLU A N     1 
ATOM   2585 C  CA    . GLU A 1 350 ? -9.590  -7.934  3.478   1.00 179.17 ? 453  GLU A CA    1 
ATOM   2586 C  C     . GLU A 1 350 ? -8.799  -7.887  2.177   1.00 178.15 ? 453  GLU A C     1 
ATOM   2587 O  O     . GLU A 1 350 ? -9.293  -8.322  1.132   1.00 172.01 ? 453  GLU A O     1 
ATOM   2588 C  CB    . GLU A 1 350 ? -8.645  -7.908  4.681   1.00 179.79 ? 453  GLU A CB    1 
ATOM   2589 C  CG    . GLU A 1 350 ? -9.354  -7.872  6.023   1.00 185.49 ? 453  GLU A CG    1 
ATOM   2590 C  CD    . GLU A 1 350 ? -8.390  -7.835  7.192   1.00 197.15 ? 453  GLU A CD    1 
ATOM   2591 O  OE1   . GLU A 1 350 ? -7.164  -7.906  6.958   1.00 201.55 ? 453  GLU A OE1   1 
ATOM   2592 O  OE2   . GLU A 1 350 ? -8.858  -7.733  8.345   1.00 186.04 ? 453  GLU A OE2   1 
ATOM   2593 N  N     . ASP A 1 351 ? -7.577  -7.361  2.230   1.00 185.14 ? 454  ASP A N     1 
ATOM   2594 C  CA    . ASP A 1 351 ? -6.722  -7.351  1.052   1.00 182.39 ? 454  ASP A CA    1 
ATOM   2595 C  C     . ASP A 1 351 ? -6.450  -8.777  0.587   1.00 175.71 ? 454  ASP A C     1 
ATOM   2596 O  O     . ASP A 1 351 ? -6.502  -9.731  1.368   1.00 177.24 ? 454  ASP A O     1 
ATOM   2597 C  CB    . ASP A 1 351 ? -5.409  -6.627  1.349   1.00 187.53 ? 454  ASP A CB    1 
ATOM   2598 C  CG    . ASP A 1 351 ? -5.600  -5.137  1.560   1.00 196.29 ? 454  ASP A CG    1 
ATOM   2599 O  OD1   . ASP A 1 351 ? -6.461  -4.544  0.877   1.00 198.44 ? 454  ASP A OD1   1 
ATOM   2600 O  OD2   . ASP A 1 351 ? -4.890  -4.560  2.410   1.00 202.97 ? 454  ASP A OD2   1 
ATOM   2601 N  N     . LEU A 1 352 ? -6.159  -8.916  -0.708  1.00 150.42 ? 455  LEU A N     1 
ATOM   2602 C  CA    . LEU A 1 352 ? -6.034  -10.239 -1.309  1.00 135.47 ? 455  LEU A CA    1 
ATOM   2603 C  C     . LEU A 1 352 ? -4.865  -11.037 -0.743  1.00 126.53 ? 455  LEU A C     1 
ATOM   2604 O  O     . LEU A 1 352 ? -4.851  -12.265 -0.876  1.00 120.82 ? 455  LEU A O     1 
ATOM   2605 C  CB    . LEU A 1 352 ? -5.900  -10.108 -2.825  1.00 131.34 ? 455  LEU A CB    1 
ATOM   2606 C  CG    . LEU A 1 352 ? -7.043  -9.345  -3.499  1.00 135.97 ? 455  LEU A CG    1 
ATOM   2607 C  CD1   . LEU A 1 352 ? -6.890  -9.356  -5.012  1.00 133.37 ? 455  LEU A CD1   1 
ATOM   2608 C  CD2   . LEU A 1 352 ? -8.391  -9.920  -3.087  1.00 140.13 ? 455  LEU A CD2   1 
ATOM   2609 N  N     . LEU A 1 353 ? -3.895  -10.378 -0.118  1.00 120.09 ? 456  LEU A N     1 
ATOM   2610 C  CA    . LEU A 1 353 ? -2.783  -11.053 0.534   1.00 113.32 ? 456  LEU A CA    1 
ATOM   2611 C  C     . LEU A 1 353 ? -2.942  -10.979 2.046   1.00 117.29 ? 456  LEU A C     1 
ATOM   2612 O  O     . LEU A 1 353 ? -3.734  -10.193 2.574   1.00 119.26 ? 456  LEU A O     1 
ATOM   2613 C  CB    . LEU A 1 353 ? -1.443  -10.442 0.109   1.00 106.59 ? 456  LEU A CB    1 
ATOM   2614 C  CG    . LEU A 1 353 ? -1.066  -10.689 -1.352  1.00 109.50 ? 456  LEU A CG    1 
ATOM   2615 C  CD1   . LEU A 1 353 ? 0.269   -10.047 -1.685  1.00 107.46 ? 456  LEU A CD1   1 
ATOM   2616 C  CD2   . LEU A 1 353 ? -1.037  -12.181 -1.645  1.00 107.77 ? 456  LEU A CD2   1 
ATOM   2617 N  N     . ASN A 1 354 ? -2.175  -11.814 2.744   1.00 109.52 ? 457  ASN A N     1 
ATOM   2618 C  CA    . ASN A 1 354 ? -2.251  -11.923 4.202   1.00 111.70 ? 457  ASN A CA    1 
ATOM   2619 C  C     . ASN A 1 354 ? -0.843  -12.009 4.777   1.00 105.16 ? 457  ASN A C     1 
ATOM   2620 O  O     . ASN A 1 354 ? -0.396  -13.072 5.224   1.00 101.25 ? 457  ASN A O     1 
ATOM   2621 C  CB    . ASN A 1 354 ? -3.095  -13.134 4.605   1.00 110.64 ? 457  ASN A CB    1 
ATOM   2622 C  CG    . ASN A 1 354 ? -3.327  -13.212 6.098   1.00 106.69 ? 457  ASN A CG    1 
ATOM   2623 O  OD1   . ASN A 1 354 ? -3.053  -14.233 6.727   1.00 109.20 ? 457  ASN A OD1   1 
ATOM   2624 N  ND2   . ASN A 1 354 ? -3.830  -12.127 6.675   1.00 107.79 ? 457  ASN A ND2   1 
ATOM   2625 N  N     . PRO A 1 355 ? -0.110  -10.892 4.784   1.00 106.42 ? 458  PRO A N     1 
ATOM   2626 C  CA    . PRO A 1 355 ? 1.260   -10.924 5.323   1.00 109.99 ? 458  PRO A CA    1 
ATOM   2627 C  C     . PRO A 1 355 ? 1.318   -11.241 6.804   1.00 123.14 ? 458  PRO A C     1 
ATOM   2628 O  O     . PRO A 1 355 ? 2.269   -11.894 7.252   1.00 120.43 ? 458  PRO A O     1 
ATOM   2629 C  CB    . PRO A 1 355 ? 1.786   -9.510  5.032   1.00 106.94 ? 458  PRO A CB    1 
ATOM   2630 C  CG    . PRO A 1 355 ? 0.883   -8.965  3.966   1.00 109.74 ? 458  PRO A CG    1 
ATOM   2631 C  CD    . PRO A 1 355 ? -0.457  -9.570  4.236   1.00 107.85 ? 458  PRO A CD    1 
ATOM   2632 N  N     . ILE A 1 356 ? 0.324   -10.800 7.579   1.00 150.54 ? 459  ILE A N     1 
ATOM   2633 C  CA    . ILE A 1 356 ? 0.341   -11.015 9.021   1.00 151.24 ? 459  ILE A CA    1 
ATOM   2634 C  C     . ILE A 1 356 ? 0.147   -12.484 9.377   1.00 151.24 ? 459  ILE A C     1 
ATOM   2635 O  O     . ILE A 1 356 ? 0.521   -12.905 10.479  1.00 153.10 ? 459  ILE A O     1 
ATOM   2636 C  CB    . ILE A 1 356 ? -0.732  -10.138 9.693   1.00 160.14 ? 459  ILE A CB    1 
ATOM   2637 C  CG1   . ILE A 1 356 ? -0.722  -8.735  9.086   1.00 165.28 ? 459  ILE A CG1   1 
ATOM   2638 C  CG2   . ILE A 1 356 ? -0.498  -10.052 11.194  1.00 150.97 ? 459  ILE A CG2   1 
ATOM   2639 C  CD1   . ILE A 1 356 ? -1.755  -7.803  9.681   1.00 168.82 ? 459  ILE A CD1   1 
ATOM   2640 N  N     . GLY A 1 357 ? -0.415  -13.278 8.473   1.00 121.69 ? 460  GLY A N     1 
ATOM   2641 C  CA    . GLY A 1 357 ? -0.652  -14.681 8.750   1.00 112.77 ? 460  GLY A CA    1 
ATOM   2642 C  C     . GLY A 1 357 ? 0.636   -15.460 8.945   1.00 107.68 ? 460  GLY A C     1 
ATOM   2643 O  O     . GLY A 1 357 ? 1.745   -14.993 8.689   1.00 110.31 ? 460  GLY A O     1 
ATOM   2644 N  N     . VAL A 1 358 ? 0.468   -16.694 9.423   1.00 98.28  ? 461  VAL A N     1 
ATOM   2645 C  CA    . VAL A 1 358 ? 1.612   -17.562 9.662   1.00 100.26 ? 461  VAL A CA    1 
ATOM   2646 C  C     . VAL A 1 358 ? 2.218   -17.988 8.330   1.00 104.76 ? 461  VAL A C     1 
ATOM   2647 O  O     . VAL A 1 358 ? 1.545   -18.020 7.291   1.00 105.04 ? 461  VAL A O     1 
ATOM   2648 C  CB    . VAL A 1 358 ? 1.199   -18.784 10.505  1.00 98.81  ? 461  VAL A CB    1 
ATOM   2649 C  CG1   . VAL A 1 358 ? 0.429   -19.788 9.655   1.00 96.71  ? 461  VAL A CG1   1 
ATOM   2650 C  CG2   . VAL A 1 358 ? 2.417   -19.432 11.151  1.00 99.36  ? 461  VAL A CG2   1 
ATOM   2651 N  N     . THR A 1 359 ? 3.509   -18.303 8.354   1.00 103.59 ? 462  THR A N     1 
ATOM   2652 C  CA    . THR A 1 359 ? 4.216   -18.802 7.186   1.00 100.63 ? 462  THR A CA    1 
ATOM   2653 C  C     . THR A 1 359 ? 4.462   -20.295 7.348   1.00 106.51 ? 462  THR A C     1 
ATOM   2654 O  O     . THR A 1 359 ? 4.821   -20.760 8.434   1.00 106.16 ? 462  THR A O     1 
ATOM   2655 C  CB    . THR A 1 359 ? 5.546   -18.071 6.985   1.00 96.19  ? 462  THR A CB    1 
ATOM   2656 O  OG1   . THR A 1 359 ? 6.519   -18.583 7.903   1.00 96.63  ? 462  THR A OG1   1 
ATOM   2657 C  CG2   . THR A 1 359 ? 5.373   -16.578 7.223   1.00 95.52  ? 462  THR A CG2   1 
ATOM   2658 N  N     . GLY A 1 360 ? 4.261   -21.044 6.267   1.00 123.76 ? 463  GLY A N     1 
ATOM   2659 C  CA    . GLY A 1 360 ? 4.465   -22.477 6.305   1.00 120.90 ? 463  GLY A CA    1 
ATOM   2660 C  C     . GLY A 1 360 ? 3.319   -23.260 5.701   1.00 123.67 ? 463  GLY A C     1 
ATOM   2661 O  O     . GLY A 1 360 ? 2.203   -22.748 5.572   1.00 112.15 ? 463  GLY A O     1 
ATOM   2662 N  N     . SER A 1 361 ? 3.586   -24.510 5.334   1.00 121.69 ? 464  SER A N     1 
ATOM   2663 C  CA    . SER A 1 361 ? 2.580   -25.331 4.678   1.00 121.39 ? 464  SER A CA    1 
ATOM   2664 C  C     . SER A 1 361 ? 1.529   -25.808 5.676   1.00 115.24 ? 464  SER A C     1 
ATOM   2665 O  O     . SER A 1 361 ? 1.807   -26.015 6.860   1.00 104.44 ? 464  SER A O     1 
ATOM   2666 C  CB    . SER A 1 361 ? 3.238   -26.530 3.993   1.00 115.47 ? 464  SER A CB    1 
ATOM   2667 O  OG    . SER A 1 361 ? 2.297   -27.273 3.240   1.00 113.87 ? 464  SER A OG    1 
ATOM   2668 N  N     . ASN A 1 362 ? 0.310   -25.977 5.180   1.00 116.38 ? 465  ASN A N     1 
ATOM   2669 C  CA    . ASN A 1 362 ? -0.777  -26.483 6.008   1.00 114.09 ? 465  ASN A CA    1 
ATOM   2670 C  C     . ASN A 1 362 ? -0.549  -27.962 6.303   1.00 117.21 ? 465  ASN A C     1 
ATOM   2671 O  O     . ASN A 1 362 ? -0.295  -28.741 5.376   1.00 123.49 ? 465  ASN A O     1 
ATOM   2672 C  CB    . ASN A 1 362 ? -2.114  -26.274 5.293   1.00 115.16 ? 465  ASN A CB    1 
ATOM   2673 C  CG    . ASN A 1 362 ? -3.314  -26.474 6.203   1.00 117.42 ? 465  ASN A CG    1 
ATOM   2674 O  OD1   . ASN A 1 362 ? -3.325  -27.356 7.060   1.00 121.51 ? 465  ASN A OD1   1 
ATOM   2675 N  ND2   . ASN A 1 362 ? -4.339  -25.651 6.010   1.00 112.59 ? 465  ASN A ND2   1 
ATOM   2676 N  N     . PRO A 1 363 ? -0.610  -28.386 7.570   1.00 114.65 ? 466  PRO A N     1 
ATOM   2677 C  CA    . PRO A 1 363 ? -0.482  -29.826 7.856   1.00 116.00 ? 466  PRO A CA    1 
ATOM   2678 C  C     . PRO A 1 363 ? -1.578  -30.658 7.216   1.00 119.70 ? 466  PRO A C     1 
ATOM   2679 O  O     . PRO A 1 363 ? -1.314  -31.772 6.748   1.00 121.39 ? 466  PRO A O     1 
ATOM   2680 C  CB    . PRO A 1 363 ? -0.541  -29.885 9.390   1.00 120.24 ? 466  PRO A CB    1 
ATOM   2681 C  CG    . PRO A 1 363 ? -0.130  -28.522 9.842   1.00 114.72 ? 466  PRO A CG    1 
ATOM   2682 C  CD    . PRO A 1 363 ? -0.654  -27.579 8.801   1.00 120.13 ? 466  PRO A CD    1 
ATOM   2683 N  N     . ASN A 1 364 ? -2.807  -30.147 7.186   1.00 122.31 ? 467  ASN A N     1 
ATOM   2684 C  CA    . ASN A 1 364 ? -3.901  -30.842 6.520   1.00 127.87 ? 467  ASN A CA    1 
ATOM   2685 C  C     . ASN A 1 364 ? -3.677  -30.808 5.014   1.00 134.33 ? 467  ASN A C     1 
ATOM   2686 O  O     . ASN A 1 364 ? -3.683  -29.734 4.404   1.00 141.28 ? 467  ASN A O     1 
ATOM   2687 C  CB    . ASN A 1 364 ? -5.235  -30.194 6.885   1.00 126.66 ? 467  ASN A CB    1 
ATOM   2688 C  CG    . ASN A 1 364 ? -6.428  -31.063 6.528   1.00 138.43 ? 467  ASN A CG    1 
ATOM   2689 O  OD1   . ASN A 1 364 ? -6.343  -31.935 5.663   1.00 147.61 ? 467  ASN A OD1   1 
ATOM   2690 N  ND2   . ASN A 1 364 ? -7.550  -30.824 7.195   1.00 144.70 ? 467  ASN A ND2   1 
ATOM   2691 N  N     . LYS A 1 365 ? -3.476  -31.978 4.412   1.00 134.12 ? 468  LYS A N     1 
ATOM   2692 C  CA    . LYS A 1 365 ? -3.168  -32.055 2.990   1.00 136.03 ? 468  LYS A CA    1 
ATOM   2693 C  C     . LYS A 1 365 ? -4.407  -32.033 2.103   1.00 142.52 ? 468  LYS A C     1 
ATOM   2694 O  O     . LYS A 1 365 ? -4.266  -32.036 0.876   1.00 155.38 ? 468  LYS A O     1 
ATOM   2695 C  CB    . LYS A 1 365 ? -2.341  -33.310 2.698   1.00 138.05 ? 468  LYS A CB    1 
ATOM   2696 C  CG    . LYS A 1 365 ? -0.977  -33.311 3.371   1.00 130.02 ? 468  LYS A CG    1 
ATOM   2697 C  CD    . LYS A 1 365 ? -0.222  -32.023 3.077   1.00 125.46 ? 468  LYS A CD    1 
ATOM   2698 C  CE    . LYS A 1 365 ? 1.114   -31.982 3.798   1.00 121.51 ? 468  LYS A CE    1 
ATOM   2699 N  NZ    . LYS A 1 365 ? 1.803   -30.676 3.607   1.00 118.27 ? 468  LYS A NZ    1 
ATOM   2700 N  N     . GLU A 1 366 ? -5.609  -32.013 2.683   1.00 142.28 ? 469  GLU A N     1 
ATOM   2701 C  CA    . GLU A 1 366 ? -6.815  -31.887 1.873   1.00 147.95 ? 469  GLU A CA    1 
ATOM   2702 C  C     . GLU A 1 366 ? -6.993  -30.473 1.337   1.00 146.99 ? 469  GLU A C     1 
ATOM   2703 O  O     . GLU A 1 366 ? -7.714  -30.280 0.352   1.00 152.65 ? 469  GLU A O     1 
ATOM   2704 C  CB    . GLU A 1 366 ? -8.041  -32.304 2.690   1.00 148.17 ? 469  GLU A CB    1 
ATOM   2705 C  CG    . GLU A 1 366 ? -9.091  -33.079 1.901   1.00 161.12 ? 469  GLU A CG    1 
ATOM   2706 C  CD    . GLU A 1 366 ? -9.935  -32.193 1.004   1.00 157.99 ? 469  GLU A CD    1 
ATOM   2707 O  OE1   . GLU A 1 366 ? -10.200 -31.034 1.388   1.00 159.70 ? 469  GLU A OE1   1 
ATOM   2708 O  OE2   . GLU A 1 366 ? -10.333 -32.656 -0.086  1.00 148.10 ? 469  GLU A OE2   1 
ATOM   2709 N  N     . THR A 1 367 ? -6.343  -29.487 1.956   1.00 142.91 ? 470  THR A N     1 
ATOM   2710 C  CA    . THR A 1 367 ? -6.415  -28.112 1.495   1.00 138.77 ? 470  THR A CA    1 
ATOM   2711 C  C     . THR A 1 367 ? -5.789  -27.990 0.104   1.00 134.36 ? 470  THR A C     1 
ATOM   2712 O  O     . THR A 1 367 ? -4.976  -28.827 -0.298  1.00 136.41 ? 470  THR A O     1 
ATOM   2713 C  CB    . THR A 1 367 ? -5.698  -27.194 2.488   1.00 128.37 ? 470  THR A CB    1 
ATOM   2714 O  OG1   . THR A 1 367 ? -6.004  -25.823 2.205   1.00 128.69 ? 470  THR A OG1   1 
ATOM   2715 C  CG2   . THR A 1 367 ? -4.199  -27.396 2.403   1.00 123.60 ? 470  THR A CG2   1 
ATOM   2716 N  N     . PRO A 1 368 ? -6.183  -26.973 -0.665  1.00 133.86 ? 471  PRO A N     1 
ATOM   2717 C  CA    . PRO A 1 368 ? -5.539  -26.744 -1.964  1.00 137.13 ? 471  PRO A CA    1 
ATOM   2718 C  C     . PRO A 1 368 ? -4.033  -26.570 -1.828  1.00 131.24 ? 471  PRO A C     1 
ATOM   2719 O  O     . PRO A 1 368 ? -3.544  -25.897 -0.919  1.00 125.52 ? 471  PRO A O     1 
ATOM   2720 C  CB    . PRO A 1 368 ? -6.208  -25.461 -2.465  1.00 132.42 ? 471  PRO A CB    1 
ATOM   2721 C  CG    . PRO A 1 368 ? -7.558  -25.495 -1.850  1.00 133.52 ? 471  PRO A CG    1 
ATOM   2722 C  CD    . PRO A 1 368 ? -7.393  -26.146 -0.501  1.00 132.82 ? 471  PRO A CD    1 
ATOM   2723 N  N     . CYS A 1 369 ? -3.300  -27.193 -2.746  1.00 129.11 ? 472  CYS A N     1 
ATOM   2724 C  CA    . CYS A 1 369 ? -1.853  -27.084 -2.803  1.00 127.68 ? 472  CYS A CA    1 
ATOM   2725 C  C     . CYS A 1 369 ? -1.455  -26.034 -3.837  1.00 122.81 ? 472  CYS A C     1 
ATOM   2726 O  O     . CYS A 1 369 ? -2.290  -25.462 -4.541  1.00 130.51 ? 472  CYS A O     1 
ATOM   2727 C  CB    . CYS A 1 369 ? -1.220  -28.437 -3.132  1.00 125.05 ? 472  CYS A CB    1 
ATOM   2728 S  SG    . CYS A 1 369 ? -1.658  -29.777 -2.005  1.00 156.38 ? 472  CYS A SG    1 
ATOM   2729 N  N     . LEU A 1 370 ? -0.152  -25.782 -3.926  1.00 117.74 ? 473  LEU A N     1 
ATOM   2730 C  CA    . LEU A 1 370 ? 0.381   -24.850 -4.917  1.00 116.55 ? 473  LEU A CA    1 
ATOM   2731 C  C     . LEU A 1 370 ? 1.829   -25.223 -5.178  1.00 114.38 ? 473  LEU A C     1 
ATOM   2732 O  O     . LEU A 1 370 ? 2.642   -25.230 -4.248  1.00 108.75 ? 473  LEU A O     1 
ATOM   2733 C  CB    . LEU A 1 370 ? 0.266   -23.404 -4.434  1.00 113.29 ? 473  LEU A CB    1 
ATOM   2734 C  CG    . LEU A 1 370 ? 0.598   -22.323 -5.464  1.00 115.54 ? 473  LEU A CG    1 
ATOM   2735 C  CD1   . LEU A 1 370 ? -0.293  -22.458 -6.690  1.00 113.49 ? 473  LEU A CD1   1 
ATOM   2736 C  CD2   . LEU A 1 370 ? 0.462   -20.938 -4.852  1.00 114.92 ? 473  LEU A CD2   1 
ATOM   2737 N  N     . GLU A 1 371 ? 2.149   -25.539 -6.429  1.00 118.55 ? 474  GLU A N     1 
ATOM   2738 C  CA    . GLU A 1 371 ? 3.497   -25.935 -6.809  1.00 112.32 ? 474  GLU A CA    1 
ATOM   2739 C  C     . GLU A 1 371 ? 4.268   -24.714 -7.294  1.00 106.74 ? 474  GLU A C     1 
ATOM   2740 O  O     . GLU A 1 371 ? 3.779   -23.958 -8.139  1.00 102.57 ? 474  GLU A O     1 
ATOM   2741 C  CB    . GLU A 1 371 ? 3.454   -27.010 -7.896  1.00 112.54 ? 474  GLU A CB    1 
ATOM   2742 C  CG    . GLU A 1 371 ? 4.764   -27.751 -8.097  1.00 120.40 ? 474  GLU A CG    1 
ATOM   2743 C  CD    . GLU A 1 371 ? 4.654   -28.847 -9.141  1.00 142.68 ? 474  GLU A CD    1 
ATOM   2744 O  OE1   . GLU A 1 371 ? 3.614   -28.911 -9.830  1.00 143.39 ? 474  GLU A OE1   1 
ATOM   2745 O  OE2   . GLU A 1 371 ? 5.604   -29.647 -9.271  1.00 144.11 ? 474  GLU A OE2   1 
ATOM   2746 N  N     . LEU A 1 372 ? 5.467   -24.523 -6.752  1.00 107.85 ? 475  LEU A N     1 
ATOM   2747 C  CA    . LEU A 1 372 ? 6.295   -23.371 -7.071  1.00 103.55 ? 475  LEU A CA    1 
ATOM   2748 C  C     . LEU A 1 372 ? 7.707   -23.824 -7.399  1.00 101.35 ? 475  LEU A C     1 
ATOM   2749 O  O     . LEU A 1 372 ? 8.114   -24.946 -7.088  1.00 106.29 ? 475  LEU A O     1 
ATOM   2750 C  CB    . LEU A 1 372 ? 6.356   -22.364 -5.913  1.00 116.39 ? 475  LEU A CB    1 
ATOM   2751 C  CG    . LEU A 1 372 ? 5.100   -21.633 -5.446  1.00 109.12 ? 475  LEU A CG    1 
ATOM   2752 C  CD1   . LEU A 1 372 ? 4.278   -22.497 -4.508  1.00 108.69 ? 475  LEU A CD1   1 
ATOM   2753 C  CD2   . LEU A 1 372 ? 5.507   -20.341 -4.767  1.00 110.98 ? 475  LEU A CD2   1 
ATOM   2754 N  N     . GLU A 1 373 ? 8.458   -22.922 -8.026  1.00 101.11 ? 476  GLU A N     1 
ATOM   2755 C  CA    . GLU A 1 373 ? 9.876   -23.124 -8.285  1.00 109.97 ? 476  GLU A CA    1 
ATOM   2756 C  C     . GLU A 1 373 ? 10.608  -21.819 -8.025  1.00 104.38 ? 476  GLU A C     1 
ATOM   2757 O  O     . GLU A 1 373 ? 10.164  -20.756 -8.469  1.00 104.46 ? 476  GLU A O     1 
ATOM   2758 C  CB    . GLU A 1 373 ? 10.132  -23.597 -9.721  1.00 109.69 ? 476  GLU A CB    1 
ATOM   2759 C  CG    . GLU A 1 373 ? 9.721   -25.033 -9.991  1.00 112.07 ? 476  GLU A CG    1 
ATOM   2760 C  CD    . GLU A 1 373 ? 10.262  -25.553 -11.308 1.00 129.64 ? 476  GLU A CD    1 
ATOM   2761 O  OE1   . GLU A 1 373 ? 11.405  -25.192 -11.662 1.00 139.07 ? 476  GLU A OE1   1 
ATOM   2762 O  OE2   . GLU A 1 373 ? 9.546   -26.315 -11.991 1.00 136.51 ? 476  GLU A OE2   1 
ATOM   2763 N  N     . PHE A 1 374 ? 11.719  -21.901 -7.301  1.00 103.95 ? 477  PHE A N     1 
ATOM   2764 C  CA    . PHE A 1 374 ? 12.556  -20.749 -7.009  1.00 107.04 ? 477  PHE A CA    1 
ATOM   2765 C  C     . PHE A 1 374 ? 13.823  -20.822 -7.850  1.00 109.38 ? 477  PHE A C     1 
ATOM   2766 O  O     . PHE A 1 374 ? 14.355  -21.909 -8.095  1.00 110.19 ? 477  PHE A O     1 
ATOM   2767 C  CB    . PHE A 1 374 ? 12.895  -20.683 -5.518  1.00 112.71 ? 477  PHE A CB    1 
ATOM   2768 C  CG    . PHE A 1 374 ? 11.689  -20.543 -4.631  1.00 105.04 ? 477  PHE A CG    1 
ATOM   2769 C  CD1   . PHE A 1 374 ? 11.020  -21.663 -4.165  1.00 106.99 ? 477  PHE A CD1   1 
ATOM   2770 C  CD2   . PHE A 1 374 ? 11.217  -19.290 -4.275  1.00 100.28 ? 477  PHE A CD2   1 
ATOM   2771 C  CE1   . PHE A 1 374 ? 9.907   -21.536 -3.354  1.00 106.33 ? 477  PHE A CE1   1 
ATOM   2772 C  CE2   . PHE A 1 374 ? 10.106  -19.157 -3.464  1.00 97.53  ? 477  PHE A CE2   1 
ATOM   2773 C  CZ    . PHE A 1 374 ? 9.450   -20.281 -3.004  1.00 99.63  ? 477  PHE A CZ    1 
ATOM   2774 N  N     . ASP A 1 375 ? 14.299  -19.660 -8.287  1.00 116.16 ? 478  ASP A N     1 
ATOM   2775 C  CA    . ASP A 1 375 ? 15.353  -19.598 -9.293  1.00 122.89 ? 478  ASP A CA    1 
ATOM   2776 C  C     . ASP A 1 375 ? 16.666  -20.138 -8.736  1.00 124.59 ? 478  ASP A C     1 
ATOM   2777 O  O     . ASP A 1 375 ? 17.203  -19.605 -7.760  1.00 131.82 ? 478  ASP A O     1 
ATOM   2778 C  CB    . ASP A 1 375 ? 15.526  -18.160 -9.776  1.00 121.59 ? 478  ASP A CB    1 
ATOM   2779 C  CG    . ASP A 1 375 ? 16.240  -18.074 -11.109 1.00 132.30 ? 478  ASP A CG    1 
ATOM   2780 O  OD1   . ASP A 1 375 ? 16.602  -19.133 -11.662 1.00 149.03 ? 478  ASP A OD1   1 
ATOM   2781 O  OD2   . ASP A 1 375 ? 16.434  -16.945 -11.607 1.00 151.81 ? 478  ASP A OD2   1 
ATOM   2782 N  N     . TRP A 1 376 ? 17.180  -21.197 -9.358  1.00 129.95 ? 479  TRP A N     1 
ATOM   2783 C  CA    . TRP A 1 376 ? 18.492  -21.722 -9.016  1.00 129.13 ? 479  TRP A CA    1 
ATOM   2784 C  C     . TRP A 1 376 ? 19.576  -20.954 -9.763  1.00 127.95 ? 479  TRP A C     1 
ATOM   2785 O  O     . TRP A 1 376 ? 19.371  -20.482 -10.885 1.00 133.38 ? 479  TRP A O     1 
ATOM   2786 C  CB    . TRP A 1 376 ? 18.582  -23.213 -9.348  1.00 127.77 ? 479  TRP A CB    1 
ATOM   2787 C  CG    . TRP A 1 376 ? 19.926  -23.818 -9.061  1.00 134.06 ? 479  TRP A CG    1 
ATOM   2788 C  CD1   . TRP A 1 376 ? 20.976  -23.933 -9.925  1.00 132.85 ? 479  TRP A CD1   1 
ATOM   2789 C  CD2   . TRP A 1 376 ? 20.364  -24.391 -7.821  1.00 139.25 ? 479  TRP A CD2   1 
ATOM   2790 N  NE1   . TRP A 1 376 ? 22.039  -24.540 -9.302  1.00 135.49 ? 479  TRP A NE1   1 
ATOM   2791 C  CE2   . TRP A 1 376 ? 21.689  -24.831 -8.010  1.00 138.07 ? 479  TRP A CE2   1 
ATOM   2792 C  CE3   . TRP A 1 376 ? 19.764  -24.574 -6.572  1.00 131.17 ? 479  TRP A CE3   1 
ATOM   2793 C  CZ2   . TRP A 1 376 ? 22.424  -25.443 -6.996  1.00 137.75 ? 479  TRP A CZ2   1 
ATOM   2794 C  CZ3   . TRP A 1 376 ? 20.495  -25.181 -5.567  1.00 135.50 ? 479  TRP A CZ3   1 
ATOM   2795 C  CH2   . TRP A 1 376 ? 21.811  -25.608 -5.785  1.00 137.79 ? 479  TRP A CH2   1 
ATOM   2796 N  N     . PHE A 1 377 ? 20.741  -20.831 -9.129  1.00 123.78 ? 480  PHE A N     1 
ATOM   2797 C  CA    . PHE A 1 377 ? 21.829  -20.057 -9.713  1.00 129.83 ? 480  PHE A CA    1 
ATOM   2798 C  C     . PHE A 1 377 ? 23.022  -20.941 -10.050 1.00 141.98 ? 480  PHE A C     1 
ATOM   2799 O  O     . PHE A 1 377 ? 23.226  -21.298 -11.215 1.00 154.42 ? 480  PHE A O     1 
ATOM   2800 C  CB    . PHE A 1 377 ? 22.242  -18.930 -8.765  1.00 121.83 ? 480  PHE A CB    1 
ATOM   2801 C  CG    . PHE A 1 377 ? 21.119  -17.996 -8.417  1.00 124.94 ? 480  PHE A CG    1 
ATOM   2802 C  CD1   . PHE A 1 377 ? 20.605  -17.128 -9.367  1.00 123.28 ? 480  PHE A CD1   1 
ATOM   2803 C  CD2   . PHE A 1 377 ? 20.572  -17.988 -7.144  1.00 126.36 ? 480  PHE A CD2   1 
ATOM   2804 C  CE1   . PHE A 1 377 ? 19.567  -16.270 -9.056  1.00 122.26 ? 480  PHE A CE1   1 
ATOM   2805 C  CE2   . PHE A 1 377 ? 19.536  -17.130 -6.825  1.00 124.44 ? 480  PHE A CE2   1 
ATOM   2806 C  CZ    . PHE A 1 377 ? 19.033  -16.270 -7.782  1.00 124.59 ? 480  PHE A CZ    1 
ATOM   2807 N  N     . SER A 1 378 ? 23.817  -21.297 -9.044  1.00 137.78 ? 481  SER A N     1 
ATOM   2808 C  CA    . SER A 1 378 ? 24.984  -22.141 -9.268  1.00 147.75 ? 481  SER A CA    1 
ATOM   2809 C  C     . SER A 1 378 ? 25.168  -23.117 -8.114  1.00 146.52 ? 481  SER A C     1 
ATOM   2810 O  O     . SER A 1 378 ? 25.106  -24.335 -8.305  1.00 150.63 ? 481  SER A O     1 
ATOM   2811 C  CB    . SER A 1 378 ? 26.238  -21.285 -9.451  1.00 147.61 ? 481  SER A CB    1 
ATOM   2812 O  OG    . SER A 1 378 ? 26.074  -20.361 -10.512 1.00 157.02 ? 481  SER A OG    1 
ATOM   2813 N  N     . SER A 1 379 ? 25.398  -22.590 -6.917  1.00 137.66 ? 482  SER A N     1 
ATOM   2814 C  CA    . SER A 1 379 ? 25.531  -23.411 -5.722  1.00 135.68 ? 482  SER A CA    1 
ATOM   2815 C  C     . SER A 1 379 ? 24.610  -22.830 -4.651  1.00 128.36 ? 482  SER A C     1 
ATOM   2816 O  O     . SER A 1 379 ? 23.693  -22.048 -4.933  1.00 124.50 ? 482  SER A O     1 
ATOM   2817 C  CB    . SER A 1 379 ? 26.996  -23.481 -5.271  1.00 146.19 ? 482  SER A CB    1 
ATOM   2818 O  OG    . SER A 1 379 ? 27.135  -24.269 -4.101  1.00 127.14 ? 482  SER A OG    1 
ATOM   2819 N  N     . VAL A 1 380 ? 24.855  -23.215 -3.397  1.00 134.57 ? 483  VAL A N     1 
ATOM   2820 C  CA    . VAL A 1 380 ? 24.064  -22.697 -2.288  1.00 116.23 ? 483  VAL A CA    1 
ATOM   2821 C  C     . VAL A 1 380 ? 24.291  -21.198 -2.155  1.00 110.55 ? 483  VAL A C     1 
ATOM   2822 O  O     . VAL A 1 380 ? 25.419  -20.705 -2.282  1.00 117.76 ? 483  VAL A O     1 
ATOM   2823 C  CB    . VAL A 1 380 ? 24.429  -23.437 -0.990  1.00 110.54 ? 483  VAL A CB    1 
ATOM   2824 C  CG1   . VAL A 1 380 ? 23.545  -22.978 0.157   1.00 119.66 ? 483  VAL A CG1   1 
ATOM   2825 C  CG2   . VAL A 1 380 ? 24.321  -24.941 -1.191  1.00 106.60 ? 483  VAL A CG2   1 
ATOM   2826 N  N     . VAL A 1 381 ? 23.211  -20.460 -1.914  1.00 98.46  ? 484  VAL A N     1 
ATOM   2827 C  CA    . VAL A 1 381 ? 23.267  -19.016 -1.722  1.00 108.35 ? 484  VAL A CA    1 
ATOM   2828 C  C     . VAL A 1 381 ? 22.944  -18.723 -0.263  1.00 108.95 ? 484  VAL A C     1 
ATOM   2829 O  O     . VAL A 1 381 ? 21.848  -19.040 0.216   1.00 99.80  ? 484  VAL A O     1 
ATOM   2830 C  CB    . VAL A 1 381 ? 22.308  -18.275 -2.666  1.00 106.47 ? 484  VAL A CB    1 
ATOM   2831 C  CG1   . VAL A 1 381 ? 22.459  -16.771 -2.499  1.00 103.64 ? 484  VAL A CG1   1 
ATOM   2832 C  CG2   . VAL A 1 381 ? 22.567  -18.682 -4.108  1.00 104.79 ? 484  VAL A CG2   1 
ATOM   2833 N  N     . LYS A 1 382 ? 23.899  -18.124 0.441   1.00 108.65 ? 485  LYS A N     1 
ATOM   2834 C  CA    . LYS A 1 382 ? 23.771  -17.817 1.856   1.00 105.63 ? 485  LYS A CA    1 
ATOM   2835 C  C     . LYS A 1 382 ? 23.648  -16.314 2.062   1.00 104.54 ? 485  LYS A C     1 
ATOM   2836 O  O     . LYS A 1 382 ? 24.137  -15.517 1.257   1.00 100.91 ? 485  LYS A O     1 
ATOM   2837 C  CB    . LYS A 1 382 ? 24.978  -18.341 2.642   1.00 109.79 ? 485  LYS A CB    1 
ATOM   2838 C  CG    . LYS A 1 382 ? 24.644  -19.346 3.729   1.00 110.67 ? 485  LYS A CG    1 
ATOM   2839 C  CD    . LYS A 1 382 ? 24.239  -20.688 3.145   1.00 112.25 ? 485  LYS A CD    1 
ATOM   2840 C  CE    . LYS A 1 382 ? 24.171  -21.754 4.227   1.00 121.10 ? 485  LYS A CE    1 
ATOM   2841 N  NZ    . LYS A 1 382 ? 23.772  -23.078 3.674   1.00 127.86 ? 485  LYS A NZ    1 
ATOM   2842 N  N     . PHE A 1 383 ? 22.991  -15.931 3.150   1.00 109.21 ? 486  PHE A N     1 
ATOM   2843 C  CA    . PHE A 1 383 ? 22.972  -14.529 3.532   1.00 106.41 ? 486  PHE A CA    1 
ATOM   2844 C  C     . PHE A 1 383 ? 24.351  -14.131 4.053   1.00 108.18 ? 486  PHE A C     1 
ATOM   2845 O  O     . PHE A 1 383 ? 24.974  -14.893 4.800   1.00 108.52 ? 486  PHE A O     1 
ATOM   2846 C  CB    . PHE A 1 383 ? 21.907  -14.272 4.599   1.00 100.55 ? 486  PHE A CB    1 
ATOM   2847 C  CG    . PHE A 1 383 ? 21.461  -12.837 4.679   1.00 101.93 ? 486  PHE A CG    1 
ATOM   2848 C  CD1   . PHE A 1 383 ? 20.471  -12.358 3.835   1.00 97.16  ? 486  PHE A CD1   1 
ATOM   2849 C  CD2   . PHE A 1 383 ? 22.028  -11.969 5.599   1.00 101.30 ? 486  PHE A CD2   1 
ATOM   2850 C  CE1   . PHE A 1 383 ? 20.056  -11.040 3.904   1.00 92.72  ? 486  PHE A CE1   1 
ATOM   2851 C  CE2   . PHE A 1 383 ? 21.618  -10.649 5.672   1.00 100.55 ? 486  PHE A CE2   1 
ATOM   2852 C  CZ    . PHE A 1 383 ? 20.630  -10.185 4.824   1.00 100.42 ? 486  PHE A CZ    1 
ATOM   2853 N  N     . PRO A 1 384 ? 24.860  -12.961 3.669   1.00 109.19 ? 487  PRO A N     1 
ATOM   2854 C  CA    . PRO A 1 384 ? 26.218  -12.581 4.080   1.00 110.00 ? 487  PRO A CA    1 
ATOM   2855 C  C     . PRO A 1 384 ? 26.341  -12.490 5.594   1.00 119.39 ? 487  PRO A C     1 
ATOM   2856 O  O     . PRO A 1 384 ? 25.444  -12.000 6.283   1.00 110.76 ? 487  PRO A O     1 
ATOM   2857 C  CB    . PRO A 1 384 ? 26.422  -11.216 3.412   1.00 108.24 ? 487  PRO A CB    1 
ATOM   2858 C  CG    . PRO A 1 384 ? 25.041  -10.705 3.154   1.00 107.63 ? 487  PRO A CG    1 
ATOM   2859 C  CD    . PRO A 1 384 ? 24.216  -11.918 2.853   1.00 106.96 ? 487  PRO A CD    1 
ATOM   2860 N  N     . ASP A 1 385 ? 27.468  -12.981 6.107   1.00 122.61 ? 488  ASP A N     1 
ATOM   2861 C  CA    . ASP A 1 385 ? 27.716  -12.961 7.538   1.00 125.57 ? 488  ASP A CA    1 
ATOM   2862 C  C     . ASP A 1 385 ? 27.823  -11.520 8.039   1.00 132.99 ? 488  ASP A C     1 
ATOM   2863 O  O     . ASP A 1 385 ? 27.921  -10.566 7.264   1.00 131.93 ? 488  ASP A O     1 
ATOM   2864 C  CB    . ASP A 1 385 ? 28.983  -13.748 7.872   1.00 125.52 ? 488  ASP A CB    1 
ATOM   2865 C  CG    . ASP A 1 385 ? 30.209  -13.213 7.159   1.00 135.49 ? 488  ASP A CG    1 
ATOM   2866 O  OD1   . ASP A 1 385 ? 30.738  -12.165 7.586   1.00 138.66 ? 488  ASP A OD1   1 
ATOM   2867 O  OD2   . ASP A 1 385 ? 30.647  -13.841 6.173   1.00 151.29 ? 488  ASP A OD2   1 
ATOM   2868 N  N     . MET A 1 386 ? 27.809  -11.375 9.367   1.00 144.26 ? 489  MET A N     1 
ATOM   2869 C  CA    . MET A 1 386 ? 27.773  -10.045 9.967   1.00 145.00 ? 489  MET A CA    1 
ATOM   2870 C  C     . MET A 1 386 ? 29.012  -9.229  9.619   1.00 142.26 ? 489  MET A C     1 
ATOM   2871 O  O     . MET A 1 386 ? 28.918  -8.008  9.451   1.00 146.45 ? 489  MET A O     1 
ATOM   2872 C  CB    . MET A 1 386 ? 27.617  -10.159 11.484  1.00 148.01 ? 489  MET A CB    1 
ATOM   2873 C  CG    . MET A 1 386 ? 27.388  -8.830  12.188  1.00 156.91 ? 489  MET A CG    1 
ATOM   2874 S  SD    . MET A 1 386 ? 25.931  -7.957  11.578  1.00 159.87 ? 489  MET A SD    1 
ATOM   2875 C  CE    . MET A 1 386 ? 25.934  -6.510  12.634  1.00 144.96 ? 489  MET A CE    1 
ATOM   2876 N  N     . SER A 1 387 ? 30.173  -9.876  9.496   1.00 141.96 ? 490  SER A N     1 
ATOM   2877 C  CA    . SER A 1 387 ? 31.390  -9.141  9.165   1.00 146.12 ? 490  SER A CA    1 
ATOM   2878 C  C     . SER A 1 387 ? 31.320  -8.533  7.769   1.00 150.16 ? 490  SER A C     1 
ATOM   2879 O  O     . SER A 1 387 ? 31.864  -7.446  7.542   1.00 156.05 ? 490  SER A O     1 
ATOM   2880 C  CB    . SER A 1 387 ? 32.610  -10.055 9.285   1.00 149.62 ? 490  SER A CB    1 
ATOM   2881 O  OG    . SER A 1 387 ? 32.565  -11.100 8.330   1.00 147.68 ? 490  SER A OG    1 
ATOM   2882 N  N     . VAL A 1 388 ? 30.660  -9.211  6.827   1.00 149.92 ? 491  VAL A N     1 
ATOM   2883 C  CA    . VAL A 1 388 ? 30.493  -8.644  5.493   1.00 145.84 ? 491  VAL A CA    1 
ATOM   2884 C  C     . VAL A 1 388 ? 29.539  -7.458  5.533   1.00 144.67 ? 491  VAL A C     1 
ATOM   2885 O  O     . VAL A 1 388 ? 29.706  -6.491  4.779   1.00 148.02 ? 491  VAL A O     1 
ATOM   2886 C  CB    . VAL A 1 388 ? 30.014  -9.727  4.508   1.00 139.63 ? 491  VAL A CB    1 
ATOM   2887 C  CG1   . VAL A 1 388 ? 29.892  -9.158  3.101   1.00 133.18 ? 491  VAL A CG1   1 
ATOM   2888 C  CG2   . VAL A 1 388 ? 30.963  -10.915 4.523   1.00 138.52 ? 491  VAL A CG2   1 
ATOM   2889 N  N     . ILE A 1 389 ? 28.532  -7.503  6.410   1.00 141.48 ? 492  ILE A N     1 
ATOM   2890 C  CA    . ILE A 1 389 ? 27.609  -6.379  6.545   1.00 138.02 ? 492  ILE A CA    1 
ATOM   2891 C  C     . ILE A 1 389 ? 28.350  -5.140  7.029   1.00 149.29 ? 492  ILE A C     1 
ATOM   2892 O  O     . ILE A 1 389 ? 28.046  -4.014  6.614   1.00 144.58 ? 492  ILE A O     1 
ATOM   2893 C  CB    . ILE A 1 389 ? 26.452  -6.747  7.493   1.00 131.92 ? 492  ILE A CB    1 
ATOM   2894 C  CG1   . ILE A 1 389 ? 25.889  -8.129  7.154   1.00 126.71 ? 492  ILE A CG1   1 
ATOM   2895 C  CG2   . ILE A 1 389 ? 25.353  -5.699  7.420   1.00 130.21 ? 492  ILE A CG2   1 
ATOM   2896 C  CD1   . ILE A 1 389 ? 25.128  -8.183  5.854   1.00 119.82 ? 492  ILE A CD1   1 
ATOM   2897 N  N     . GLU A 1 390 ? 29.334  -5.327  7.914   1.00 169.69 ? 493  GLU A N     1 
ATOM   2898 C  CA    . GLU A 1 390 ? 30.102  -4.194  8.422   1.00 172.90 ? 493  GLU A CA    1 
ATOM   2899 C  C     . GLU A 1 390 ? 30.907  -3.532  7.312   1.00 174.02 ? 493  GLU A C     1 
ATOM   2900 O  O     . GLU A 1 390 ? 31.077  -2.307  7.303   1.00 176.39 ? 493  GLU A O     1 
ATOM   2901 C  CB    . GLU A 1 390 ? 31.031  -4.650  9.549   1.00 182.05 ? 493  GLU A CB    1 
ATOM   2902 C  CG    . GLU A 1 390 ? 30.367  -5.490  10.633  1.00 178.65 ? 493  GLU A CG    1 
ATOM   2903 C  CD    . GLU A 1 390 ? 29.611  -4.661  11.654  1.00 190.37 ? 493  GLU A CD    1 
ATOM   2904 O  OE1   . GLU A 1 390 ? 29.532  -3.426  11.487  1.00 192.58 ? 493  GLU A OE1   1 
ATOM   2905 O  OE2   . GLU A 1 390 ? 29.099  -5.248  12.631  1.00 195.65 ? 493  GLU A OE2   1 
ATOM   2906 N  N     . GLU A 1 391 ? 31.413  -4.329  6.367   1.00 190.37 ? 494  GLU A N     1 
ATOM   2907 C  CA    . GLU A 1 391 ? 32.223  -3.782  5.283   1.00 192.64 ? 494  GLU A CA    1 
ATOM   2908 C  C     . GLU A 1 391 ? 31.402  -2.852  4.399   1.00 192.10 ? 494  GLU A C     1 
ATOM   2909 O  O     . GLU A 1 391 ? 31.847  -1.753  4.048   1.00 192.93 ? 494  GLU A O     1 
ATOM   2910 C  CB    . GLU A 1 391 ? 32.821  -4.920  4.456   1.00 201.66 ? 494  GLU A CB    1 
ATOM   2911 C  CG    . GLU A 1 391 ? 33.603  -5.936  5.270   1.00 205.83 ? 494  GLU A CG    1 
ATOM   2912 C  CD    . GLU A 1 391 ? 33.924  -7.188  4.480   1.00 205.71 ? 494  GLU A CD    1 
ATOM   2913 O  OE1   . GLU A 1 391 ? 33.615  -7.224  3.270   1.00 200.49 ? 494  GLU A OE1   1 
ATOM   2914 O  OE2   . GLU A 1 391 ? 34.480  -8.139  5.069   1.00 207.36 ? 494  GLU A OE2   1 
ATOM   2915 N  N     . HIS A 1 392 ? 30.193  -3.279  4.029   1.00 164.78 ? 495  HIS A N     1 
ATOM   2916 C  CA    . HIS A 1 392 ? 29.354  -2.459  3.163   1.00 155.41 ? 495  HIS A CA    1 
ATOM   2917 C  C     . HIS A 1 392 ? 28.856  -1.216  3.888   1.00 154.31 ? 495  HIS A C     1 
ATOM   2918 O  O     . HIS A 1 392 ? 28.720  -0.148  3.279   1.00 153.24 ? 495  HIS A O     1 
ATOM   2919 C  CB    . HIS A 1 392 ? 28.177  -3.282  2.644   1.00 141.85 ? 495  HIS A CB    1 
ATOM   2920 C  CG    . HIS A 1 392 ? 27.330  -2.561  1.642   1.00 142.02 ? 495  HIS A CG    1 
ATOM   2921 N  ND1   . HIS A 1 392 ? 27.807  -1.518  0.878   1.00 148.00 ? 495  HIS A ND1   1 
ATOM   2922 C  CD2   . HIS A 1 392 ? 26.037  -2.733  1.280   1.00 137.06 ? 495  HIS A CD2   1 
ATOM   2923 C  CE1   . HIS A 1 392 ? 26.844  -1.079  0.087   1.00 146.19 ? 495  HIS A CE1   1 
ATOM   2924 N  NE2   . HIS A 1 392 ? 25.760  -1.799  0.311   1.00 141.01 ? 495  HIS A NE2   1 
ATOM   2925 N  N     . ALA A 1 393 ? 28.579  -1.334  5.189   1.00 153.87 ? 496  ALA A N     1 
ATOM   2926 C  CA    . ALA A 1 393 ? 28.096  -0.185  5.947   1.00 147.97 ? 496  ALA A CA    1 
ATOM   2927 C  C     . ALA A 1 393 ? 29.169  0.889   6.070   1.00 153.57 ? 496  ALA A C     1 
ATOM   2928 O  O     . ALA A 1 393 ? 28.865  2.087   6.023   1.00 151.44 ? 496  ALA A O     1 
ATOM   2929 C  CB    . ALA A 1 393 ? 27.619  -0.632  7.327   1.00 141.87 ? 496  ALA A CB    1 
ATOM   2930 N  N     . ASN A 1 394 ? 30.431  0.482   6.227   1.00 157.29 ? 497  ASN A N     1 
ATOM   2931 C  CA    . ASN A 1 394 ? 31.515  1.455   6.306   1.00 154.34 ? 497  ASN A CA    1 
ATOM   2932 C  C     . ASN A 1 394 ? 31.727  2.170   4.979   1.00 157.44 ? 497  ASN A C     1 
ATOM   2933 O  O     . ASN A 1 394 ? 32.097  3.350   4.965   1.00 157.63 ? 497  ASN A O     1 
ATOM   2934 C  CB    . ASN A 1 394 ? 32.809  0.770   6.747   1.00 151.16 ? 497  ASN A CB    1 
ATOM   2935 C  CG    . ASN A 1 394 ? 32.724  0.212   8.153   1.00 154.36 ? 497  ASN A CG    1 
ATOM   2936 O  OD1   . ASN A 1 394 ? 32.022  0.754   9.006   1.00 156.85 ? 497  ASN A OD1   1 
ATOM   2937 N  ND2   . ASN A 1 394 ? 33.442  -0.877  8.402   1.00 158.69 ? 497  ASN A ND2   1 
ATOM   2938 N  N     . TRP A 1 395 ? 31.495  1.481   3.859   1.00 158.08 ? 498  TRP A N     1 
ATOM   2939 C  CA    . TRP A 1 395 ? 31.751  2.076   2.552   1.00 155.42 ? 498  TRP A CA    1 
ATOM   2940 C  C     . TRP A 1 395 ? 30.670  3.075   2.160   1.00 155.85 ? 498  TRP A C     1 
ATOM   2941 O  O     . TRP A 1 395 ? 30.981  4.150   1.633   1.00 158.43 ? 498  TRP A O     1 
ATOM   2942 C  CB    . TRP A 1 395 ? 31.869  0.983   1.489   1.00 156.19 ? 498  TRP A CB    1 
ATOM   2943 C  CG    . TRP A 1 395 ? 31.880  1.519   0.090   1.00 162.04 ? 498  TRP A CG    1 
ATOM   2944 C  CD1   . TRP A 1 395 ? 32.959  1.990   -0.599  1.00 162.97 ? 498  TRP A CD1   1 
ATOM   2945 C  CD2   . TRP A 1 395 ? 30.757  1.640   -0.792  1.00 157.90 ? 498  TRP A CD2   1 
ATOM   2946 N  NE1   . TRP A 1 395 ? 32.578  2.397   -1.854  1.00 160.23 ? 498  TRP A NE1   1 
ATOM   2947 C  CE2   . TRP A 1 395 ? 31.231  2.192   -1.998  1.00 159.70 ? 498  TRP A CE2   1 
ATOM   2948 C  CE3   . TRP A 1 395 ? 29.397  1.335   -0.678  1.00 157.32 ? 498  TRP A CE3   1 
ATOM   2949 C  CZ2   . TRP A 1 395 ? 30.394  2.445   -3.082  1.00 168.77 ? 498  TRP A CZ2   1 
ATOM   2950 C  CZ3   . TRP A 1 395 ? 28.568  1.587   -1.757  1.00 154.41 ? 498  TRP A CZ3   1 
ATOM   2951 C  CH2   . TRP A 1 395 ? 29.069  2.137   -2.942  1.00 162.91 ? 498  TRP A CH2   1 
ATOM   2952 N  N     . SER A 1 396 ? 29.400  2.744   2.404   1.00 154.22 ? 499  SER A N     1 
ATOM   2953 C  CA    . SER A 1 396 ? 28.312  3.635   2.016   1.00 152.48 ? 499  SER A CA    1 
ATOM   2954 C  C     . SER A 1 396 ? 28.297  4.936   2.808   1.00 158.18 ? 499  SER A C     1 
ATOM   2955 O  O     . SER A 1 396 ? 27.532  5.842   2.456   1.00 159.16 ? 499  SER A O     1 
ATOM   2956 C  CB    . SER A 1 396 ? 26.967  2.920   2.159   1.00 146.96 ? 499  SER A CB    1 
ATOM   2957 O  OG    . SER A 1 396 ? 26.667  2.655   3.519   1.00 145.81 ? 499  SER A OG    1 
ATOM   2958 N  N     . VAL A 1 397 ? 29.100  5.045   3.870   1.00 164.83 ? 500  VAL A N     1 
ATOM   2959 C  CA    . VAL A 1 397 ? 29.291  6.335   4.527   1.00 163.96 ? 500  VAL A CA    1 
ATOM   2960 C  C     . VAL A 1 397 ? 29.933  7.323   3.561   1.00 170.42 ? 500  VAL A C     1 
ATOM   2961 O  O     . VAL A 1 397 ? 29.637  8.525   3.583   1.00 168.46 ? 500  VAL A O     1 
ATOM   2962 C  CB    . VAL A 1 397 ? 30.130  6.158   5.809   1.00 177.48 ? 500  VAL A CB    1 
ATOM   2963 C  CG1   . VAL A 1 397 ? 30.574  7.511   6.372   1.00 184.43 ? 500  VAL A CG1   1 
ATOM   2964 C  CG2   . VAL A 1 397 ? 29.343  5.372   6.858   1.00 167.90 ? 500  VAL A CG2   1 
ATOM   2965 N  N     . SER A 1 398 ? 30.805  6.827   2.684   1.00 169.98 ? 501  SER A N     1 
ATOM   2966 C  CA    . SER A 1 398 ? 31.486  7.657   1.695   1.00 165.36 ? 501  SER A CA    1 
ATOM   2967 C  C     . SER A 1 398 ? 30.790  7.514   0.341   1.00 170.62 ? 501  SER A C     1 
ATOM   2968 O  O     . SER A 1 398 ? 31.319  6.951   -0.618  1.00 180.04 ? 501  SER A O     1 
ATOM   2969 C  CB    . SER A 1 398 ? 32.961  7.273   1.614   1.00 162.59 ? 501  SER A CB    1 
ATOM   2970 O  OG    . SER A 1 398 ? 33.116  5.940   1.151   1.00 164.91 ? 501  SER A OG    1 
ATOM   2971 N  N     . ARG A 1 399 ? 29.570  8.039   0.285   1.00 166.74 ? 502  ARG A N     1 
ATOM   2972 C  CA    . ARG A 1 399 ? 28.781  8.018   -0.944  1.00 166.62 ? 502  ARG A CA    1 
ATOM   2973 C  C     . ARG A 1 399 ? 27.784  9.174   -0.981  1.00 168.49 ? 502  ARG A C     1 
ATOM   2974 O  O     . ARG A 1 399 ? 28.171  10.342  -0.961  1.00 175.29 ? 502  ARG A O     1 
ATOM   2975 C  CB    . ARG A 1 399 ? 28.044  6.684   -1.086  1.00 155.05 ? 502  ARG A CB    1 
ATOM   2976 N  N     . LEU A 1 420 ? 19.327  21.607  14.385  1.00 170.74 ? 523  LEU A N     1 
ATOM   2977 C  CA    . LEU A 1 420 ? 19.830  20.577  15.287  1.00 172.08 ? 523  LEU A CA    1 
ATOM   2978 C  C     . LEU A 1 420 ? 19.146  20.660  16.649  1.00 178.31 ? 523  LEU A C     1 
ATOM   2979 O  O     . LEU A 1 420 ? 18.999  19.653  17.343  1.00 176.61 ? 523  LEU A O     1 
ATOM   2980 C  CB    . LEU A 1 420 ? 21.349  20.703  15.449  1.00 164.03 ? 523  LEU A CB    1 
ATOM   2981 C  CG    . LEU A 1 420 ? 22.047  19.679  16.349  1.00 160.39 ? 523  LEU A CG    1 
ATOM   2982 C  CD1   . LEU A 1 420 ? 21.834  18.265  15.828  1.00 156.48 ? 523  LEU A CD1   1 
ATOM   2983 C  CD2   . LEU A 1 420 ? 23.531  19.990  16.477  1.00 148.67 ? 523  LEU A CD2   1 
ATOM   2984 N  N     . ARG A 1 421 ? 18.718  21.865  17.026  1.00 182.56 ? 524  ARG A N     1 
ATOM   2985 C  CA    . ARG A 1 421 ? 18.126  22.077  18.341  1.00 181.53 ? 524  ARG A CA    1 
ATOM   2986 C  C     . ARG A 1 421 ? 16.861  22.923  18.274  1.00 183.24 ? 524  ARG A C     1 
ATOM   2987 O  O     . ARG A 1 421 ? 15.992  22.808  19.145  1.00 178.22 ? 524  ARG A O     1 
ATOM   2988 C  CB    . ARG A 1 421 ? 19.141  22.735  19.279  1.00 184.23 ? 524  ARG A CB    1 
ATOM   2989 C  CG    . ARG A 1 421 ? 20.139  21.772  19.897  1.00 184.74 ? 524  ARG A CG    1 
ATOM   2990 C  CD    . ARG A 1 421 ? 21.148  22.513  20.759  1.00 188.34 ? 524  ARG A CD    1 
ATOM   2991 N  NE    . ARG A 1 421 ? 20.518  23.555  21.560  1.00 190.77 ? 524  ARG A NE    1 
ATOM   2992 C  CZ    . ARG A 1 421 ? 19.944  23.355  22.739  1.00 192.20 ? 524  ARG A CZ    1 
ATOM   2993 N  NH1   . ARG A 1 421 ? 19.895  22.152  23.288  1.00 187.93 ? 524  ARG A NH1   1 
ATOM   2994 N  NH2   . ARG A 1 421 ? 19.405  24.386  23.382  1.00 190.70 ? 524  ARG A NH2   1 
ATOM   2995 N  N     . GLU A 1 422 ? 16.746  23.779  17.255  1.00 189.23 ? 525  GLU A N     1 
ATOM   2996 C  CA    . GLU A 1 422 ? 15.599  24.681  17.183  1.00 189.91 ? 525  GLU A CA    1 
ATOM   2997 C  C     . GLU A 1 422 ? 14.303  23.912  16.950  1.00 188.99 ? 525  GLU A C     1 
ATOM   2998 O  O     . GLU A 1 422 ? 13.276  24.214  17.568  1.00 190.65 ? 525  GLU A O     1 
ATOM   2999 C  CB    . GLU A 1 422 ? 15.818  25.736  16.093  1.00 191.71 ? 525  GLU A CB    1 
ATOM   3000 C  CG    . GLU A 1 422 ? 15.839  25.221  14.654  1.00 195.25 ? 525  GLU A CG    1 
ATOM   3001 C  CD    . GLU A 1 422 ? 17.106  24.463  14.306  1.00 191.25 ? 525  GLU A CD    1 
ATOM   3002 O  OE1   . GLU A 1 422 ? 18.065  24.500  15.106  1.00 188.92 ? 525  GLU A OE1   1 
ATOM   3003 O  OE2   . GLU A 1 422 ? 17.142  23.829  13.230  1.00 188.69 ? 525  GLU A OE2   1 
ATOM   3004 N  N     . ASN A 1 423 ? 14.333  22.908  16.074  1.00 187.23 ? 526  ASN A N     1 
ATOM   3005 C  CA    . ASN A 1 423 ? 13.182  22.039  15.855  1.00 188.50 ? 526  ASN A CA    1 
ATOM   3006 C  C     . ASN A 1 423 ? 13.556  20.600  15.547  1.00 187.32 ? 526  ASN A C     1 
ATOM   3007 O  O     . ASN A 1 423 ? 12.727  19.713  15.775  1.00 181.67 ? 526  ASN A O     1 
ATOM   3008 C  CB    . ASN A 1 423 ? 12.303  22.576  14.717  1.00 190.18 ? 526  ASN A CB    1 
ATOM   3009 C  CG    . ASN A 1 423 ? 12.968  22.461  13.359  1.00 191.92 ? 526  ASN A CG    1 
ATOM   3010 O  OD1   . ASN A 1 423 ? 13.718  23.345  12.946  1.00 198.50 ? 526  ASN A OD1   1 
ATOM   3011 N  ND2   . ASN A 1 423 ? 12.692  21.369  12.654  1.00 187.53 ? 526  ASN A ND2   1 
ATOM   3012 N  N     . ASP A 1 424 ? 14.764  20.329  15.046  1.00 180.26 ? 527  ASP A N     1 
ATOM   3013 C  CA    . ASP A 1 424 ? 15.168  18.954  14.776  1.00 173.82 ? 527  ASP A CA    1 
ATOM   3014 C  C     . ASP A 1 424 ? 15.143  18.105  16.040  1.00 175.82 ? 527  ASP A C     1 
ATOM   3015 O  O     . ASP A 1 424 ? 14.835  16.910  15.978  1.00 173.97 ? 527  ASP A O     1 
ATOM   3016 C  CB    . ASP A 1 424 ? 16.561  18.931  14.148  1.00 170.45 ? 527  ASP A CB    1 
ATOM   3017 C  CG    . ASP A 1 424 ? 16.637  19.746  12.871  1.00 177.18 ? 527  ASP A CG    1 
ATOM   3018 O  OD1   . ASP A 1 424 ? 15.619  19.822  12.151  1.00 180.38 ? 527  ASP A OD1   1 
ATOM   3019 O  OD2   . ASP A 1 424 ? 17.715  20.311  12.589  1.00 175.27 ? 527  ASP A OD2   1 
ATOM   3020 N  N     . LYS A 1 425 ? 15.455  18.701  17.191  1.00 170.66 ? 528  LYS A N     1 
ATOM   3021 C  CA    . LYS A 1 425 ? 15.393  17.958  18.444  1.00 166.24 ? 528  LYS A CA    1 
ATOM   3022 C  C     . LYS A 1 425 ? 13.949  17.742  18.882  1.00 161.57 ? 528  LYS A C     1 
ATOM   3023 O  O     . LYS A 1 425 ? 13.555  16.621  19.223  1.00 155.73 ? 528  LYS A O     1 
ATOM   3024 C  CB    . LYS A 1 425 ? 16.182  18.690  19.530  1.00 168.12 ? 528  LYS A CB    1 
ATOM   3025 C  CG    . LYS A 1 425 ? 16.155  17.997  20.884  1.00 160.20 ? 528  LYS A CG    1 
ATOM   3026 C  CD    . LYS A 1 425 ? 16.922  18.792  21.927  1.00 157.59 ? 528  LYS A CD    1 
ATOM   3027 C  CE    . LYS A 1 425 ? 16.326  20.178  22.109  1.00 163.97 ? 528  LYS A CE    1 
ATOM   3028 N  NZ    . LYS A 1 425 ? 17.064  20.968  23.132  1.00 170.41 ? 528  LYS A NZ    1 
ATOM   3029 N  N     . GLU A 1 426 ? 13.142  18.806  18.868  1.00 163.22 ? 529  GLU A N     1 
ATOM   3030 C  CA    . GLU A 1 426 ? 11.762  18.696  19.333  1.00 159.10 ? 529  GLU A CA    1 
ATOM   3031 C  C     . GLU A 1 426 ? 10.944  17.771  18.441  1.00 157.90 ? 529  GLU A C     1 
ATOM   3032 O  O     . GLU A 1 426 ? 10.105  17.007  18.933  1.00 152.69 ? 529  GLU A O     1 
ATOM   3033 C  CB    . GLU A 1 426 ? 11.114  20.080  19.403  1.00 162.40 ? 529  GLU A CB    1 
ATOM   3034 C  CG    . GLU A 1 426 ? 11.589  20.945  20.564  1.00 159.48 ? 529  GLU A CG    1 
ATOM   3035 C  CD    . GLU A 1 426 ? 12.980  21.511  20.351  1.00 169.53 ? 529  GLU A CD    1 
ATOM   3036 O  OE1   . GLU A 1 426 ? 13.520  21.369  19.233  1.00 173.50 ? 529  GLU A OE1   1 
ATOM   3037 O  OE2   . GLU A 1 426 ? 13.533  22.102  21.302  1.00 168.06 ? 529  GLU A OE2   1 
ATOM   3038 N  N     . GLN A 1 427 ? 11.168  17.828  17.125  1.00 165.21 ? 530  GLN A N     1 
ATOM   3039 C  CA    . GLN A 1 427 ? 10.433  16.947  16.223  1.00 162.51 ? 530  GLN A CA    1 
ATOM   3040 C  C     . GLN A 1 427 ? 10.772  15.486  16.487  1.00 156.15 ? 530  GLN A C     1 
ATOM   3041 O  O     . GLN A 1 427 ? 9.887   14.623  16.458  1.00 151.37 ? 530  GLN A O     1 
ATOM   3042 C  CB    . GLN A 1 427 ? 10.719  17.314  14.767  1.00 164.81 ? 530  GLN A CB    1 
ATOM   3043 C  CG    . GLN A 1 427 ? 10.168  18.670  14.350  1.00 174.78 ? 530  GLN A CG    1 
ATOM   3044 C  CD    . GLN A 1 427 ? 8.700   18.839  14.691  1.00 186.03 ? 530  GLN A CD    1 
ATOM   3045 O  OE1   . GLN A 1 427 ? 7.897   17.922  14.515  1.00 190.62 ? 530  GLN A OE1   1 
ATOM   3046 N  NE2   . GLN A 1 427 ? 8.342   20.017  15.189  1.00 191.61 ? 530  GLN A NE2   1 
ATOM   3047 N  N     . LEU A 1 428 ? 12.046  15.189  16.754  1.00 148.92 ? 531  LEU A N     1 
ATOM   3048 C  CA    . LEU A 1 428 ? 12.413  13.829  17.133  1.00 141.46 ? 531  LEU A CA    1 
ATOM   3049 C  C     . LEU A 1 428 ? 11.790  13.436  18.465  1.00 138.90 ? 531  LEU A C     1 
ATOM   3050 O  O     . LEU A 1 428 ? 11.453  12.264  18.671  1.00 134.62 ? 531  LEU A O     1 
ATOM   3051 C  CB    . LEU A 1 428 ? 13.934  13.686  17.193  1.00 138.43 ? 531  LEU A CB    1 
ATOM   3052 C  CG    . LEU A 1 428 ? 14.677  13.729  15.856  1.00 134.01 ? 531  LEU A CG    1 
ATOM   3053 C  CD1   . LEU A 1 428 ? 16.161  13.467  16.059  1.00 124.96 ? 531  LEU A CD1   1 
ATOM   3054 C  CD2   . LEU A 1 428 ? 14.080  12.734  14.873  1.00 130.83 ? 531  LEU A CD2   1 
ATOM   3055 N  N     . LYS A 1 429 ? 11.628  14.396  19.379  1.00 140.19 ? 532  LYS A N     1 
ATOM   3056 C  CA    . LYS A 1 429 ? 10.933  14.109  20.630  1.00 138.08 ? 532  LYS A CA    1 
ATOM   3057 C  C     . LYS A 1 429 ? 9.442   13.899  20.391  1.00 134.59 ? 532  LYS A C     1 
ATOM   3058 O  O     . LYS A 1 429 ? 8.825   13.026  21.012  1.00 130.77 ? 532  LYS A O     1 
ATOM   3059 C  CB    . LYS A 1 429 ? 11.164  15.240  21.633  1.00 140.10 ? 532  LYS A CB    1 
ATOM   3060 C  CG    . LYS A 1 429 ? 12.627  15.492  21.964  1.00 142.12 ? 532  LYS A CG    1 
ATOM   3061 C  CD    . LYS A 1 429 ? 13.247  14.325  22.715  1.00 139.24 ? 532  LYS A CD    1 
ATOM   3062 C  CE    . LYS A 1 429 ? 13.129  14.511  24.218  1.00 143.05 ? 532  LYS A CE    1 
ATOM   3063 N  NZ    . LYS A 1 429 ? 13.887  15.708  24.681  1.00 141.35 ? 532  LYS A NZ    1 
ATOM   3064 N  N     . ALA A 1 430 ? 8.849   14.687  19.490  1.00 135.14 ? 533  ALA A N     1 
ATOM   3065 C  CA    . ALA A 1 430 ? 7.428   14.537  19.196  1.00 132.11 ? 533  ALA A CA    1 
ATOM   3066 C  C     . ALA A 1 430 ? 7.150   13.279  18.385  1.00 131.44 ? 533  ALA A C     1 
ATOM   3067 O  O     . ALA A 1 430 ? 6.085   12.669  18.538  1.00 131.87 ? 533  ALA A O     1 
ATOM   3068 C  CB    . ALA A 1 430 ? 6.909   15.771  18.460  1.00 135.50 ? 533  ALA A CB    1 
ATOM   3069 N  N     . ILE A 1 431 ? 8.083   12.879  17.517  1.00 128.20 ? 534  ILE A N     1 
ATOM   3070 C  CA    . ILE A 1 431 ? 7.910   11.645  16.755  1.00 125.56 ? 534  ILE A CA    1 
ATOM   3071 C  C     . ILE A 1 431 ? 7.884   10.442  17.690  1.00 124.66 ? 534  ILE A C     1 
ATOM   3072 O  O     . ILE A 1 431 ? 7.095   9.507   17.504  1.00 125.51 ? 534  ILE A O     1 
ATOM   3073 C  CB    . ILE A 1 431 ? 9.016   11.514  15.689  1.00 123.76 ? 534  ILE A CB    1 
ATOM   3074 C  CG1   . ILE A 1 431 ? 8.748   12.456  14.513  1.00 127.92 ? 534  ILE A CG1   1 
ATOM   3075 C  CG2   . ILE A 1 431 ? 9.140   10.077  15.202  1.00 112.00 ? 534  ILE A CG2   1 
ATOM   3076 C  CD1   . ILE A 1 431 ? 7.470   12.152  13.767  1.00 136.39 ? 534  ILE A CD1   1 
ATOM   3077 N  N     . SER A 1 432 ? 8.733   10.456  18.721  1.00 122.79 ? 535  SER A N     1 
ATOM   3078 C  CA    . SER A 1 432 ? 8.835   9.305   19.611  1.00 119.91 ? 535  SER A CA    1 
ATOM   3079 C  C     . SER A 1 432 ? 7.612   9.164   20.509  1.00 123.29 ? 535  SER A C     1 
ATOM   3080 O  O     . SER A 1 432 ? 7.202   8.040   20.821  1.00 120.53 ? 535  SER A O     1 
ATOM   3081 C  CB    . SER A 1 432 ? 10.103  9.411   20.457  1.00 119.40 ? 535  SER A CB    1 
ATOM   3082 O  OG    . SER A 1 432 ? 10.226  8.300   21.327  1.00 122.38 ? 535  SER A OG    1 
ATOM   3083 N  N     . THR A 1 433 ? 7.016   10.280  20.933  1.00 125.89 ? 536  THR A N     1 
ATOM   3084 C  CA    . THR A 1 433 ? 5.881   10.218  21.846  1.00 123.44 ? 536  THR A CA    1 
ATOM   3085 C  C     . THR A 1 433 ? 4.593   9.765   21.170  1.00 127.09 ? 536  THR A C     1 
ATOM   3086 O  O     . THR A 1 433 ? 3.632   9.437   21.876  1.00 126.29 ? 536  THR A O     1 
ATOM   3087 C  CB    . THR A 1 433 ? 5.656   11.580  22.508  1.00 129.88 ? 536  THR A CB    1 
ATOM   3088 O  OG1   . THR A 1 433 ? 5.521   12.589  21.500  1.00 130.99 ? 536  THR A OG1   1 
ATOM   3089 C  CG2   . THR A 1 433 ? 6.823   11.930  23.421  1.00 130.75 ? 536  THR A CG2   1 
ATOM   3090 N  N     . ARG A 1 434 ? 4.545   9.734   19.840  1.00 121.24 ? 537  ARG A N     1 
ATOM   3091 C  CA    . ARG A 1 434 ? 3.329   9.327   19.151  1.00 118.97 ? 537  ARG A CA    1 
ATOM   3092 C  C     . ARG A 1 434 ? 3.092   7.828   19.308  1.00 112.98 ? 537  ARG A C     1 
ATOM   3093 O  O     . ARG A 1 434 ? 4.025   7.042   19.494  1.00 110.87 ? 537  ARG A O     1 
ATOM   3094 C  CB    . ARG A 1 434 ? 3.399   9.694   17.667  1.00 117.41 ? 537  ARG A CB    1 
ATOM   3095 C  CG    . ARG A 1 434 ? 3.351   11.189  17.387  1.00 118.21 ? 537  ARG A CG    1 
ATOM   3096 C  CD    . ARG A 1 434 ? 2.585   11.482  16.104  1.00 118.65 ? 537  ARG A CD    1 
ATOM   3097 N  NE    . ARG A 1 434 ? 3.162   10.805  14.948  1.00 124.30 ? 537  ARG A NE    1 
ATOM   3098 C  CZ    . ARG A 1 434 ? 3.907   11.399  14.025  1.00 121.56 ? 537  ARG A CZ    1 
ATOM   3099 N  NH1   . ARG A 1 434 ? 4.176   12.693  14.081  1.00 120.04 ? 537  ARG A NH1   1 
ATOM   3100 N  NH2   . ARG A 1 434 ? 4.390   10.676  13.018  1.00 121.66 ? 537  ARG A NH2   1 
ATOM   3101 N  N     . ASP A 1 435 ? 1.821   7.438   19.231  1.00 108.19 ? 538  ASP A N     1 
ATOM   3102 C  CA    . ASP A 1 435 ? 1.449   6.046   19.419  1.00 107.42 ? 538  ASP A CA    1 
ATOM   3103 C  C     . ASP A 1 435 ? 1.934   5.194   18.245  1.00 105.27 ? 538  ASP A C     1 
ATOM   3104 O  O     . ASP A 1 435 ? 2.137   5.703   17.139  1.00 111.49 ? 538  ASP A O     1 
ATOM   3105 C  CB    . ASP A 1 435 ? -0.065  5.919   19.568  1.00 106.18 ? 538  ASP A CB    1 
ATOM   3106 C  CG    . ASP A 1 435 ? -0.822  6.812   18.608  1.00 115.09 ? 538  ASP A CG    1 
ATOM   3107 O  OD1   . ASP A 1 435 ? -0.441  7.994   18.473  1.00 118.22 ? 538  ASP A OD1   1 
ATOM   3108 O  OD2   . ASP A 1 435 ? -1.794  6.333   17.987  1.00 115.75 ? 538  ASP A OD2   1 
ATOM   3109 N  N     . PRO A 1 436 ? 2.136   3.889   18.462  1.00 104.17 ? 539  PRO A N     1 
ATOM   3110 C  CA    . PRO A 1 436 ? 2.597   3.029   17.360  1.00 104.70 ? 539  PRO A CA    1 
ATOM   3111 C  C     . PRO A 1 436 ? 1.582   2.862   16.241  1.00 107.59 ? 539  PRO A C     1 
ATOM   3112 O  O     . PRO A 1 436 ? 1.961   2.403   15.156  1.00 108.62 ? 539  PRO A O     1 
ATOM   3113 C  CB    . PRO A 1 436 ? 2.889   1.691   18.053  1.00 103.48 ? 539  PRO A CB    1 
ATOM   3114 C  CG    . PRO A 1 436 ? 2.075   1.721   19.298  1.00 104.39 ? 539  PRO A CG    1 
ATOM   3115 C  CD    . PRO A 1 436 ? 2.057   3.154   19.736  1.00 104.36 ? 539  PRO A CD    1 
ATOM   3116 N  N     . LEU A 1 437 ? 0.315   3.209   16.460  1.00 107.70 ? 540  LEU A N     1 
ATOM   3117 C  CA    . LEU A 1 437 ? -0.675  3.178   15.392  1.00 108.09 ? 540  LEU A CA    1 
ATOM   3118 C  C     . LEU A 1 437 ? -0.748  4.481   14.609  1.00 110.44 ? 540  LEU A C     1 
ATOM   3119 O  O     . LEU A 1 437 ? -1.374  4.511   13.544  1.00 112.82 ? 540  LEU A O     1 
ATOM   3120 C  CB    . LEU A 1 437 ? -2.064  2.850   15.953  1.00 102.72 ? 540  LEU A CB    1 
ATOM   3121 C  CG    . LEU A 1 437 ? -2.317  1.407   16.391  1.00 95.56  ? 540  LEU A CG    1 
ATOM   3122 C  CD1   . LEU A 1 437 ? -3.804  1.176   16.611  1.00 96.96  ? 540  LEU A CD1   1 
ATOM   3123 C  CD2   . LEU A 1 437 ? -1.760  0.422   15.376  1.00 100.42 ? 540  LEU A CD2   1 
ATOM   3124 N  N     . SER A 1 438 ? -0.133  5.551   15.105  1.00 114.75 ? 541  SER A N     1 
ATOM   3125 C  CA    . SER A 1 438 ? -0.153  6.820   14.393  1.00 124.69 ? 541  SER A CA    1 
ATOM   3126 C  C     . SER A 1 438 ? 0.698   6.735   13.134  1.00 135.42 ? 541  SER A C     1 
ATOM   3127 O  O     . SER A 1 438 ? 1.769   6.122   13.128  1.00 131.59 ? 541  SER A O     1 
ATOM   3128 C  CB    . SER A 1 438 ? 0.353   7.945   15.294  1.00 121.03 ? 541  SER A CB    1 
ATOM   3129 O  OG    . SER A 1 438 ? 0.352   9.185   14.608  1.00 128.29 ? 541  SER A OG    1 
ATOM   3130 N  N     . GLU A 1 439 ? 0.213   7.354   12.062  1.00 164.61 ? 542  GLU A N     1 
ATOM   3131 C  CA    . GLU A 1 439 ? 0.929   7.328   10.797  1.00 159.49 ? 542  GLU A CA    1 
ATOM   3132 C  C     . GLU A 1 439 ? 2.174   8.206   10.864  1.00 160.26 ? 542  GLU A C     1 
ATOM   3133 O  O     . GLU A 1 439 ? 2.226   9.200   11.594  1.00 161.90 ? 542  GLU A O     1 
ATOM   3134 C  CB    . GLU A 1 439 ? 0.021   7.791   9.655   1.00 167.65 ? 542  GLU A CB    1 
ATOM   3135 C  CG    . GLU A 1 439 ? -0.280  9.286   9.638   1.00 167.12 ? 542  GLU A CG    1 
ATOM   3136 C  CD    . GLU A 1 439 ? -1.212  9.719   10.756  1.00 182.27 ? 542  GLU A CD    1 
ATOM   3137 O  OE1   . GLU A 1 439 ? -1.860  8.845   11.369  1.00 178.81 ? 542  GLU A OE1   1 
ATOM   3138 O  OE2   . GLU A 1 439 ? -1.294  10.937  11.022  1.00 195.34 ? 542  GLU A OE2   1 
ATOM   3139 N  N     . ILE A 1 440 ? 3.189   7.818   10.099  1.00 133.39 ? 543  ILE A N     1 
ATOM   3140 C  CA    . ILE A 1 440 ? 4.435   8.566   9.988   1.00 126.69 ? 543  ILE A CA    1 
ATOM   3141 C  C     . ILE A 1 440 ? 4.606   8.925   8.520   1.00 127.56 ? 543  ILE A C     1 
ATOM   3142 O  O     . ILE A 1 440 ? 4.828   8.043   7.680   1.00 126.31 ? 543  ILE A O     1 
ATOM   3143 C  CB    . ILE A 1 440 ? 5.637   7.768   10.508  1.00 119.75 ? 543  ILE A CB    1 
ATOM   3144 C  CG1   . ILE A 1 440 ? 5.353   7.227   11.910  1.00 116.91 ? 543  ILE A CG1   1 
ATOM   3145 C  CG2   . ILE A 1 440 ? 6.885   8.636   10.520  1.00 120.66 ? 543  ILE A CG2   1 
ATOM   3146 N  N     . THR A 1 441 ? 4.497   10.215  8.206   1.00 121.67 ? 544  THR A N     1 
ATOM   3147 C  CA    . THR A 1 441 ? 4.572   10.661  6.823   1.00 122.63 ? 544  THR A CA    1 
ATOM   3148 C  C     . THR A 1 441 ? 5.957   10.387  6.242   1.00 123.36 ? 544  THR A C     1 
ATOM   3149 O  O     . THR A 1 441 ? 6.949   10.241  6.963   1.00 121.24 ? 544  THR A O     1 
ATOM   3150 C  CB    . THR A 1 441 ? 4.249   12.151  6.717   1.00 119.71 ? 544  THR A CB    1 
ATOM   3151 O  OG1   . THR A 1 441 ? 5.275   12.913  7.365   1.00 118.70 ? 544  THR A OG1   1 
ATOM   3152 C  CG2   . THR A 1 441 ? 2.910   12.452  7.375   1.00 119.88 ? 544  THR A CG2   1 
ATOM   3153 N  N     . GLU A 1 442 ? 6.012   10.320  4.908   1.00 120.54 ? 545  GLU A N     1 
ATOM   3154 C  CA    . GLU A 1 442 ? 7.268   10.014  4.230   1.00 122.86 ? 545  GLU A CA    1 
ATOM   3155 C  C     . GLU A 1 442 ? 8.329   11.070  4.510   1.00 119.71 ? 545  GLU A C     1 
ATOM   3156 O  O     . GLU A 1 442 ? 9.521   10.747  4.583   1.00 116.12 ? 545  GLU A O     1 
ATOM   3157 C  CB    . GLU A 1 442 ? 7.030   9.883   2.725   1.00 129.35 ? 545  GLU A CB    1 
ATOM   3158 C  CG    . GLU A 1 442 ? 8.085   9.068   1.991   1.00 135.73 ? 545  GLU A CG    1 
ATOM   3159 C  CD    . GLU A 1 442 ? 7.964   7.578   2.256   1.00 137.34 ? 545  GLU A CD    1 
ATOM   3160 O  OE1   . GLU A 1 442 ? 6.926   7.148   2.804   1.00 140.80 ? 545  GLU A OE1   1 
ATOM   3161 O  OE2   . GLU A 1 442 ? 8.907   6.834   1.915   1.00 141.16 ? 545  GLU A OE2   1 
ATOM   3162 N  N     . GLN A 1 443 ? 7.919   12.331  4.669   1.00 117.99 ? 546  GLN A N     1 
ATOM   3163 C  CA    . GLN A 1 443 ? 8.870   13.379  5.027   1.00 118.74 ? 546  GLN A CA    1 
ATOM   3164 C  C     . GLN A 1 443 ? 9.507   13.100  6.383   1.00 124.96 ? 546  GLN A C     1 
ATOM   3165 O  O     . GLN A 1 443 ? 10.721  13.263  6.553   1.00 123.27 ? 546  GLN A O     1 
ATOM   3166 C  CB    . GLN A 1 443 ? 8.171   14.740  5.019   1.00 117.19 ? 546  GLN A CB    1 
ATOM   3167 C  CG    . GLN A 1 443 ? 8.997   15.888  5.588   1.00 123.03 ? 546  GLN A CG    1 
ATOM   3168 C  CD    . GLN A 1 443 ? 8.756   16.107  7.074   1.00 141.77 ? 546  GLN A CD    1 
ATOM   3169 O  OE1   . GLN A 1 443 ? 7.772   15.623  7.635   1.00 132.89 ? 546  GLN A OE1   1 
ATOM   3170 N  NE2   . GLN A 1 443 ? 9.659   16.839  7.718   1.00 139.43 ? 546  GLN A NE2   1 
ATOM   3171 N  N     . GLU A 1 444 ? 8.702   12.674  7.360   1.00 123.68 ? 547  GLU A N     1 
ATOM   3172 C  CA    . GLU A 1 444 ? 9.241   12.339  8.673   1.00 122.38 ? 547  GLU A CA    1 
ATOM   3173 C  C     . GLU A 1 444 ? 10.133  11.106  8.618   1.00 119.57 ? 547  GLU A C     1 
ATOM   3174 O  O     . GLU A 1 444 ? 11.110  11.016  9.369   1.00 118.80 ? 547  GLU A O     1 
ATOM   3175 C  CB    . GLU A 1 444 ? 8.101   12.125  9.669   1.00 129.82 ? 547  GLU A CB    1 
ATOM   3176 C  CG    . GLU A 1 444 ? 7.254   13.361  9.915   1.00 128.55 ? 547  GLU A CG    1 
ATOM   3177 C  CD    . GLU A 1 444 ? 5.964   13.045  10.643  1.00 124.11 ? 547  GLU A CD    1 
ATOM   3178 O  OE1   . GLU A 1 444 ? 5.666   11.847  10.832  1.00 122.06 ? 547  GLU A OE1   1 
ATOM   3179 O  OE2   . GLU A 1 444 ? 5.247   13.994  11.024  1.00 129.94 ? 547  GLU A OE2   1 
ATOM   3180 N  N     . LYS A 1 445 ? 9.815   10.149  7.741   1.00 124.19 ? 548  LYS A N     1 
ATOM   3181 C  CA    . LYS A 1 445 ? 10.650  8.960   7.611   1.00 121.03 ? 548  LYS A CA    1 
ATOM   3182 C  C     . LYS A 1 445 ? 12.054  9.322   7.144   1.00 125.01 ? 548  LYS A C     1 
ATOM   3183 O  O     . LYS A 1 445 ? 13.045  8.802   7.672   1.00 124.55 ? 548  LYS A O     1 
ATOM   3184 C  CB    . LYS A 1 445 ? 9.997   7.963   6.653   1.00 118.35 ? 548  LYS A CB    1 
ATOM   3185 C  CG    . LYS A 1 445 ? 8.603   7.520   7.081   1.00 117.99 ? 548  LYS A CG    1 
ATOM   3186 C  CD    . LYS A 1 445 ? 7.906   6.718   5.992   1.00 124.70 ? 548  LYS A CD    1 
ATOM   3187 C  CE    . LYS A 1 445 ? 8.415   5.288   5.932   1.00 121.77 ? 548  LYS A CE    1 
ATOM   3188 N  NZ    . LYS A 1 445 ? 8.002   4.507   7.130   1.00 111.88 ? 548  LYS A NZ    1 
ATOM   3189 N  N     . ASP A 1 446 ? 12.162  10.219  6.160   1.00 121.36 ? 549  ASP A N     1 
ATOM   3190 C  CA    . ASP A 1 446 ? 13.476  10.697  5.744   1.00 123.62 ? 549  ASP A CA    1 
ATOM   3191 C  C     . ASP A 1 446 ? 14.115  11.577  6.811   1.00 125.13 ? 549  ASP A C     1 
ATOM   3192 O  O     . ASP A 1 446 ? 15.343  11.578  6.958   1.00 122.07 ? 549  ASP A O     1 
ATOM   3193 C  CB    . ASP A 1 446 ? 13.372  11.462  4.424   1.00 128.29 ? 549  ASP A CB    1 
ATOM   3194 C  CG    . ASP A 1 446 ? 13.016  10.566  3.254   1.00 125.76 ? 549  ASP A CG    1 
ATOM   3195 O  OD1   . ASP A 1 446 ? 13.279  9.347   3.333   1.00 125.48 ? 549  ASP A OD1   1 
ATOM   3196 O  OD2   . ASP A 1 446 ? 12.479  11.083  2.252   1.00 116.12 ? 549  ASP A OD2   1 
ATOM   3197 N  N     . PHE A 1 447 ? 13.305  12.329  7.560   1.00 124.81 ? 550  PHE A N     1 
ATOM   3198 C  CA    . PHE A 1 447 ? 13.849  13.195  8.602   1.00 126.57 ? 550  PHE A CA    1 
ATOM   3199 C  C     . PHE A 1 447 ? 14.450  12.379  9.740   1.00 126.08 ? 550  PHE A C     1 
ATOM   3200 O  O     . PHE A 1 447 ? 15.506  12.736  10.276  1.00 129.19 ? 550  PHE A O     1 
ATOM   3201 C  CB    . PHE A 1 447 ? 12.760  14.132  9.126   1.00 128.31 ? 550  PHE A CB    1 
ATOM   3202 C  CG    . PHE A 1 447 ? 13.200  14.988  10.278  1.00 134.45 ? 550  PHE A CG    1 
ATOM   3203 C  CD1   . PHE A 1 447 ? 14.095  16.027  10.084  1.00 136.94 ? 550  PHE A CD1   1 
ATOM   3204 C  CD2   . PHE A 1 447 ? 12.713  14.759  11.555  1.00 137.87 ? 550  PHE A CD2   1 
ATOM   3205 C  CE1   . PHE A 1 447 ? 14.501  16.818  11.142  1.00 144.82 ? 550  PHE A CE1   1 
ATOM   3206 C  CE2   . PHE A 1 447 ? 13.114  15.547  12.617  1.00 142.13 ? 550  PHE A CE2   1 
ATOM   3207 C  CZ    . PHE A 1 447 ? 14.009  16.577  12.410  1.00 147.55 ? 550  PHE A CZ    1 
ATOM   3208 N  N     . LEU A 1 448 ? 13.790  11.285  10.125  1.00 123.47 ? 551  LEU A N     1 
ATOM   3209 C  CA    . LEU A 1 448 ? 14.360  10.390  11.126  1.00 121.96 ? 551  LEU A CA    1 
ATOM   3210 C  C     . LEU A 1 448 ? 15.650  9.761   10.619  1.00 120.19 ? 551  LEU A C     1 
ATOM   3211 O  O     . LEU A 1 448 ? 16.659  9.716   11.333  1.00 120.34 ? 551  LEU A O     1 
ATOM   3212 C  CB    . LEU A 1 448 ? 13.349  9.304   11.496  1.00 118.91 ? 551  LEU A CB    1 
ATOM   3213 C  CG    . LEU A 1 448 ? 12.410  9.528   12.681  1.00 106.38 ? 551  LEU A CG    1 
ATOM   3214 C  CD1   . LEU A 1 448 ? 11.646  10.835  12.553  1.00 115.95 ? 551  LEU A CD1   1 
ATOM   3215 C  CD2   . LEU A 1 448 ? 11.452  8.355   12.796  1.00 102.39 ? 551  LEU A CD2   1 
ATOM   3216 N  N     . TRP A 1 449 ? 15.634  9.273   9.377   1.00 120.51 ? 552  TRP A N     1 
ATOM   3217 C  CA    . TRP A 1 449 ? 16.800  8.591   8.828   1.00 119.77 ? 552  TRP A CA    1 
ATOM   3218 C  C     . TRP A 1 449 ? 17.989  9.535   8.703   1.00 121.01 ? 552  TRP A C     1 
ATOM   3219 O  O     . TRP A 1 449 ? 19.138  9.129   8.915   1.00 119.43 ? 552  TRP A O     1 
ATOM   3220 C  CB    . TRP A 1 449 ? 16.448  7.978   7.473   1.00 123.82 ? 552  TRP A CB    1 
ATOM   3221 C  CG    . TRP A 1 449 ? 17.576  7.236   6.837   1.00 124.10 ? 552  TRP A CG    1 
ATOM   3222 C  CD1   . TRP A 1 449 ? 18.230  7.567   5.688   1.00 116.76 ? 552  TRP A CD1   1 
ATOM   3223 C  CD2   . TRP A 1 449 ? 18.192  6.037   7.320   1.00 121.98 ? 552  TRP A CD2   1 
ATOM   3224 N  NE1   . TRP A 1 449 ? 19.213  6.645   5.421   1.00 121.22 ? 552  TRP A NE1   1 
ATOM   3225 C  CE2   . TRP A 1 449 ? 19.211  5.696   6.409   1.00 120.19 ? 552  TRP A CE2   1 
ATOM   3226 C  CE3   . TRP A 1 449 ? 17.980  5.217   8.433   1.00 118.94 ? 552  TRP A CE3   1 
ATOM   3227 C  CZ2   . TRP A 1 449 ? 20.016  4.571   6.576   1.00 121.20 ? 552  TRP A CZ2   1 
ATOM   3228 C  CZ3   . TRP A 1 449 ? 18.782  4.102   8.598   1.00 120.38 ? 552  TRP A CZ3   1 
ATOM   3229 C  CH2   . TRP A 1 449 ? 19.786  3.789   7.674   1.00 124.44 ? 552  TRP A CH2   1 
ATOM   3230 N  N     . SER A 1 450 ? 17.735  10.801  8.366   1.00 122.88 ? 553  SER A N     1 
ATOM   3231 C  CA    . SER A 1 450 ? 18.828  11.760  8.234   1.00 124.43 ? 553  SER A CA    1 
ATOM   3232 C  C     . SER A 1 450 ? 19.466  12.062  9.585   1.00 123.05 ? 553  SER A C     1 
ATOM   3233 O  O     . SER A 1 450 ? 20.683  12.263  9.672   1.00 119.14 ? 553  SER A O     1 
ATOM   3234 C  CB    . SER A 1 450 ? 18.324  13.042  7.573   1.00 126.12 ? 553  SER A CB    1 
ATOM   3235 O  OG    . SER A 1 450 ? 17.240  13.598  8.296   1.00 133.85 ? 553  SER A OG    1 
ATOM   3236 N  N     . HIS A 1 451 ? 18.665  12.095  10.650  1.00 124.67 ? 554  HIS A N     1 
ATOM   3237 C  CA    . HIS A 1 451 ? 19.164  12.320  12.002  1.00 127.23 ? 554  HIS A CA    1 
ATOM   3238 C  C     . HIS A 1 451 ? 19.308  11.021  12.788  1.00 121.35 ? 554  HIS A C     1 
ATOM   3239 O  O     . HIS A 1 451 ? 19.169  11.020  14.015  1.00 127.11 ? 554  HIS A O     1 
ATOM   3240 C  CB    . HIS A 1 451 ? 18.255  13.295  12.749  1.00 130.10 ? 554  HIS A CB    1 
ATOM   3241 C  CG    . HIS A 1 451 ? 18.424  14.721  12.328  1.00 137.48 ? 554  HIS A CG    1 
ATOM   3242 N  ND1   . HIS A 1 451 ? 19.174  15.090  11.232  1.00 136.53 ? 554  HIS A ND1   1 
ATOM   3243 C  CD2   . HIS A 1 451 ? 17.944  15.871  12.860  1.00 146.84 ? 554  HIS A CD2   1 
ATOM   3244 C  CE1   . HIS A 1 451 ? 19.146  16.405  11.105  1.00 145.47 ? 554  HIS A CE1   1 
ATOM   3245 N  NE2   . HIS A 1 451 ? 18.407  16.903  12.080  1.00 148.95 ? 554  HIS A NE2   1 
ATOM   3246 N  N     . ARG A 1 452 ? 19.594  9.912   12.101  1.00 121.91 ? 555  ARG A N     1 
ATOM   3247 C  CA    . ARG A 1 452 ? 19.717  8.622   12.771  1.00 118.83 ? 555  ARG A CA    1 
ATOM   3248 C  C     . ARG A 1 452 ? 20.884  8.587   13.749  1.00 120.34 ? 555  ARG A C     1 
ATOM   3249 O  O     . ARG A 1 452 ? 20.885  7.758   14.666  1.00 119.58 ? 555  ARG A O     1 
ATOM   3250 C  CB    . ARG A 1 452 ? 19.871  7.508   11.735  1.00 119.42 ? 555  ARG A CB    1 
ATOM   3251 C  CG    . ARG A 1 452 ? 21.313  7.217   11.359  1.00 123.06 ? 555  ARG A CG    1 
ATOM   3252 C  CD    . ARG A 1 452 ? 21.444  6.704   9.939   1.00 124.75 ? 555  ARG A CD    1 
ATOM   3253 N  NE    . ARG A 1 452 ? 21.188  7.754   8.960   1.00 125.47 ? 555  ARG A NE    1 
ATOM   3254 C  CZ    . ARG A 1 452 ? 21.604  7.719   7.702   1.00 121.32 ? 555  ARG A CZ    1 
ATOM   3255 N  NH1   . ARG A 1 452 ? 22.317  6.706   7.238   1.00 118.83 ? 555  ARG A NH1   1 
ATOM   3256 N  NH2   . ARG A 1 452 ? 21.304  8.729   6.891   1.00 124.65 ? 555  ARG A NH2   1 
ATOM   3257 N  N     . HIS A 1 453 ? 21.879  9.459   13.574  1.00 121.78 ? 556  HIS A N     1 
ATOM   3258 C  CA    . HIS A 1 453 ? 22.991  9.513   14.515  1.00 121.92 ? 556  HIS A CA    1 
ATOM   3259 C  C     . HIS A 1 453 ? 22.633  10.298  15.767  1.00 128.77 ? 556  HIS A C     1 
ATOM   3260 O  O     . HIS A 1 453 ? 23.124  9.980   16.854  1.00 135.30 ? 556  HIS A O     1 
ATOM   3261 C  CB    . HIS A 1 453 ? 24.224  10.119  13.843  1.00 125.75 ? 556  HIS A CB    1 
ATOM   3262 C  CG    . HIS A 1 453 ? 24.791  9.271   12.748  1.00 129.83 ? 556  HIS A CG    1 
ATOM   3263 N  ND1   . HIS A 1 453 ? 24.333  7.999   12.479  1.00 127.34 ? 556  HIS A ND1   1 
ATOM   3264 C  CD2   . HIS A 1 453 ? 25.779  9.512   11.853  1.00 135.22 ? 556  HIS A CD2   1 
ATOM   3265 C  CE1   . HIS A 1 453 ? 25.014  7.493   11.466  1.00 124.58 ? 556  HIS A CE1   1 
ATOM   3266 N  NE2   . HIS A 1 453 ? 25.897  8.391   11.068  1.00 133.49 ? 556  HIS A NE2   1 
ATOM   3267 N  N     . TYR A 1 454 ? 21.787  11.322  15.637  1.00 129.67 ? 557  TYR A N     1 
ATOM   3268 C  CA    . TYR A 1 454 ? 21.278  12.021  16.808  1.00 128.87 ? 557  TYR A CA    1 
ATOM   3269 C  C     . TYR A 1 454 ? 20.187  11.233  17.518  1.00 126.69 ? 557  TYR A C     1 
ATOM   3270 O  O     . TYR A 1 454 ? 19.909  11.503  18.690  1.00 132.45 ? 557  TYR A O     1 
ATOM   3271 C  CB    . TYR A 1 454 ? 20.751  13.404  16.410  1.00 130.65 ? 557  TYR A CB    1 
ATOM   3272 C  CG    . TYR A 1 454 ? 20.336  14.270  17.581  1.00 126.24 ? 557  TYR A CG    1 
ATOM   3273 C  CD1   . TYR A 1 454 ? 21.281  14.970  18.320  1.00 124.21 ? 557  TYR A CD1   1 
ATOM   3274 C  CD2   . TYR A 1 454 ? 19.000  14.394  17.940  1.00 115.70 ? 557  TYR A CD2   1 
ATOM   3275 N  N     . CYS A 1 455 ? 19.574  10.258  16.841  1.00 124.07 ? 558  CYS A N     1 
ATOM   3276 C  CA    . CYS A 1 455 ? 18.535  9.443   17.458  1.00 128.91 ? 558  CYS A CA    1 
ATOM   3277 C  C     . CYS A 1 455 ? 19.057  8.569   18.591  1.00 127.91 ? 558  CYS A C     1 
ATOM   3278 O  O     . CYS A 1 455 ? 18.247  8.031   19.353  1.00 124.86 ? 558  CYS A O     1 
ATOM   3279 C  CB    . CYS A 1 455 ? 17.859  8.563   16.405  1.00 120.89 ? 558  CYS A CB    1 
ATOM   3280 S  SG    . CYS A 1 455 ? 16.748  9.450   15.289  1.00 124.07 ? 558  CYS A SG    1 
ATOM   3281 N  N     . VAL A 1 456 ? 20.377  8.412   18.723  1.00 129.65 ? 559  VAL A N     1 
ATOM   3282 C  CA    . VAL A 1 456 ? 20.915  7.597   19.805  1.00 128.67 ? 559  VAL A CA    1 
ATOM   3283 C  C     . VAL A 1 456 ? 20.815  8.307   21.148  1.00 134.83 ? 559  VAL A C     1 
ATOM   3284 O  O     . VAL A 1 456 ? 20.954  7.664   22.194  1.00 134.98 ? 559  VAL A O     1 
ATOM   3285 C  CB    . VAL A 1 456 ? 22.374  7.197   19.513  1.00 130.29 ? 559  VAL A CB    1 
ATOM   3286 C  CG1   . VAL A 1 456 ? 22.485  6.566   18.132  1.00 125.30 ? 559  VAL A CG1   1 
ATOM   3287 C  CG2   . VAL A 1 456 ? 23.295  8.400   19.641  1.00 137.58 ? 559  VAL A CG2   1 
ATOM   3288 N  N     . THR A 1 457 ? 20.580  9.621   21.152  1.00 145.47 ? 560  THR A N     1 
ATOM   3289 C  CA    . THR A 1 457 ? 20.361  10.338  22.402  1.00 147.93 ? 560  THR A CA    1 
ATOM   3290 C  C     . THR A 1 457 ? 18.954  10.139  22.948  1.00 140.91 ? 560  THR A C     1 
ATOM   3291 O  O     . THR A 1 457 ? 18.696  10.500  24.102  1.00 142.99 ? 560  THR A O     1 
ATOM   3292 C  CB    . THR A 1 457 ? 20.631  11.836  22.217  1.00 152.07 ? 560  THR A CB    1 
ATOM   3293 O  OG1   . THR A 1 457 ? 20.913  12.431  23.489  1.00 166.89 ? 560  THR A OG1   1 
ATOM   3294 C  CG2   . THR A 1 457 ? 19.421  12.530  21.609  1.00 144.66 ? 560  THR A CG2   1 
ATOM   3295 N  N     . ILE A 1 458 ? 18.048  9.579   22.152  1.00 133.36 ? 561  ILE A N     1 
ATOM   3296 C  CA    . ILE A 1 458 ? 16.687  9.273   22.583  1.00 125.75 ? 561  ILE A CA    1 
ATOM   3297 C  C     . ILE A 1 458 ? 16.340  7.874   22.088  1.00 117.33 ? 561  ILE A C     1 
ATOM   3298 O  O     . ILE A 1 458 ? 15.591  7.728   21.111  1.00 115.57 ? 561  ILE A O     1 
ATOM   3299 C  CB    . ILE A 1 458 ? 15.690  10.324  22.072  1.00 127.59 ? 561  ILE A CB    1 
ATOM   3300 C  CG1   . ILE A 1 458 ? 16.091  10.810  20.676  1.00 129.22 ? 561  ILE A CG1   1 
ATOM   3301 C  CG2   . ILE A 1 458 ? 15.603  11.491  23.044  1.00 133.44 ? 561  ILE A CG2   1 
ATOM   3302 N  N     . PRO A 1 459 ? 16.852  6.820   22.732  1.00 114.69 ? 562  PRO A N     1 
ATOM   3303 C  CA    . PRO A 1 459 ? 16.684  5.462   22.186  1.00 109.85 ? 562  PRO A CA    1 
ATOM   3304 C  C     . PRO A 1 459 ? 15.240  4.993   22.112  1.00 106.69 ? 562  PRO A C     1 
ATOM   3305 O  O     . PRO A 1 459 ? 14.979  3.972   21.463  1.00 109.90 ? 562  PRO A O     1 
ATOM   3306 C  CB    . PRO A 1 459 ? 17.497  4.590   23.154  1.00 106.92 ? 562  PRO A CB    1 
ATOM   3307 C  CG    . PRO A 1 459 ? 18.419  5.541   23.854  1.00 112.90 ? 562  PRO A CG    1 
ATOM   3308 C  CD    . PRO A 1 459 ? 17.666  6.826   23.957  1.00 117.67 ? 562  PRO A CD    1 
ATOM   3309 N  N     . GLU A 1 460 ? 14.300  5.692   22.748  1.00 107.34 ? 563  GLU A N     1 
ATOM   3310 C  CA    . GLU A 1 460 ? 12.896  5.313   22.654  1.00 106.30 ? 563  GLU A CA    1 
ATOM   3311 C  C     . GLU A 1 460 ? 12.309  5.565   21.271  1.00 102.15 ? 563  GLU A C     1 
ATOM   3312 O  O     . GLU A 1 460 ? 11.215  5.069   20.983  1.00 100.05 ? 563  GLU A O     1 
ATOM   3313 C  CB    . GLU A 1 460 ? 12.074  6.056   23.713  1.00 106.01 ? 563  GLU A CB    1 
ATOM   3314 C  CG    . GLU A 1 460 ? 12.293  7.565   23.752  1.00 112.57 ? 563  GLU A CG    1 
ATOM   3315 C  CD    . GLU A 1 460 ? 13.477  7.969   24.613  1.00 119.06 ? 563  GLU A CD    1 
ATOM   3316 O  OE1   . GLU A 1 460 ? 14.135  7.073   25.183  1.00 117.75 ? 563  GLU A OE1   1 
ATOM   3317 O  OE2   . GLU A 1 460 ? 13.749  9.184   24.722  1.00 119.54 ? 563  GLU A OE2   1 
ATOM   3318 N  N     . ILE A 1 461 ? 13.007  6.317   20.412  1.00 103.83 ? 564  ILE A N     1 
ATOM   3319 C  CA    . ILE A 1 461 ? 12.535  6.563   19.049  1.00 105.08 ? 564  ILE A CA    1 
ATOM   3320 C  C     . ILE A 1 461 ? 12.886  5.429   18.101  1.00 101.75 ? 564  ILE A C     1 
ATOM   3321 O  O     . ILE A 1 461 ? 12.518  5.486   16.919  1.00 98.95  ? 564  ILE A O     1 
ATOM   3322 C  CB    . ILE A 1 461 ? 13.110  7.895   18.523  1.00 104.49 ? 564  ILE A CB    1 
ATOM   3323 C  CG1   . ILE A 1 461 ? 12.209  8.488   17.437  1.00 104.27 ? 564  ILE A CG1   1 
ATOM   3324 C  CG2   . ILE A 1 461 ? 14.533  7.703   18.005  1.00 102.23 ? 564  ILE A CG2   1 
ATOM   3325 C  CD1   . ILE A 1 461 ? 12.728  9.783   16.856  1.00 110.71 ? 564  ILE A CD1   1 
ATOM   3326 N  N     . LEU A 1 462 ? 13.572  4.393   18.585  1.00 98.85  ? 565  LEU A N     1 
ATOM   3327 C  CA    . LEU A 1 462 ? 14.005  3.309   17.706  1.00 103.99 ? 565  LEU A CA    1 
ATOM   3328 C  C     . LEU A 1 462 ? 12.866  2.641   16.939  1.00 100.27 ? 565  LEU A C     1 
ATOM   3329 O  O     . LEU A 1 462 ? 13.055  2.366   15.741  1.00 88.10  ? 565  LEU A O     1 
ATOM   3330 C  CB    . LEU A 1 462 ? 14.794  2.270   18.515  1.00 99.37  ? 565  LEU A CB    1 
ATOM   3331 C  CG    . LEU A 1 462 ? 15.375  1.112   17.699  1.00 101.92 ? 565  LEU A CG    1 
ATOM   3332 C  CD1   . LEU A 1 462 ? 16.348  1.629   16.645  1.00 98.42  ? 565  LEU A CD1   1 
ATOM   3333 C  CD2   . LEU A 1 462 ? 16.045  0.090   18.604  1.00 95.24  ? 565  LEU A CD2   1 
ATOM   3334 N  N     . PRO A 1 463 ? 11.700  2.343   17.530  1.00 102.22 ? 566  PRO A N     1 
ATOM   3335 C  CA    . PRO A 1 463 ? 10.611  1.779   16.711  1.00 100.33 ? 566  PRO A CA    1 
ATOM   3336 C  C     . PRO A 1 463 ? 10.205  2.676   15.554  1.00 95.87  ? 566  PRO A C     1 
ATOM   3337 O  O     . PRO A 1 463 ? 9.891   2.177   14.466  1.00 92.10  ? 566  PRO A O     1 
ATOM   3338 C  CB    . PRO A 1 463 ? 9.471   1.601   17.723  1.00 95.96  ? 566  PRO A CB    1 
ATOM   3339 C  CG    . PRO A 1 463 ? 10.154  1.444   19.027  1.00 97.09  ? 566  PRO A CG    1 
ATOM   3340 C  CD    . PRO A 1 463 ? 11.348  2.348   18.963  1.00 93.03  ? 566  PRO A CD    1 
ATOM   3341 N  N     . LYS A 1 464 ? 10.205  3.995   15.759  1.00 95.48  ? 567  LYS A N     1 
ATOM   3342 C  CA    . LYS A 1 464 ? 9.882   4.908   14.670  1.00 100.07 ? 567  LYS A CA    1 
ATOM   3343 C  C     . LYS A 1 464 ? 10.976  4.924   13.610  1.00 100.66 ? 567  LYS A C     1 
ATOM   3344 O  O     . LYS A 1 464 ? 10.683  5.084   12.419  1.00 93.52  ? 567  LYS A O     1 
ATOM   3345 C  CB    . LYS A 1 464 ? 9.656   6.317   15.217  1.00 98.38  ? 567  LYS A CB    1 
ATOM   3346 C  CG    . LYS A 1 464 ? 8.691   6.387   16.386  1.00 101.49 ? 567  LYS A CG    1 
ATOM   3347 C  CD    . LYS A 1 464 ? 7.302   5.917   15.995  1.00 100.39 ? 567  LYS A CD    1 
ATOM   3348 C  CE    . LYS A 1 464 ? 6.340   6.031   17.166  1.00 109.35 ? 567  LYS A CE    1 
ATOM   3349 N  NZ    . LYS A 1 464 ? 4.962   5.603   16.800  1.00 124.64 ? 567  LYS A NZ    1 
ATOM   3350 N  N     . LEU A 1 465 ? 12.236  4.760   14.019  1.00 100.53 ? 568  LEU A N     1 
ATOM   3351 C  CA    . LEU A 1 465 ? 13.335  4.776   13.060  1.00 96.41  ? 568  LEU A CA    1 
ATOM   3352 C  C     . LEU A 1 465 ? 13.348  3.510   12.211  1.00 95.63  ? 568  LEU A C     1 
ATOM   3353 O  O     . LEU A 1 465 ? 13.629  3.569   11.008  1.00 102.61 ? 568  LEU A O     1 
ATOM   3354 C  CB    . LEU A 1 465 ? 14.666  4.948   13.793  1.00 98.48  ? 568  LEU A CB    1 
ATOM   3355 C  CG    . LEU A 1 465 ? 15.931  4.916   12.933  1.00 101.23 ? 568  LEU A CG    1 
ATOM   3356 C  CD1   . LEU A 1 465 ? 15.872  5.983   11.850  1.00 109.15 ? 568  LEU A CD1   1 
ATOM   3357 C  CD2   . LEU A 1 465 ? 17.168  5.094   13.796  1.00 104.73 ? 568  LEU A CD2   1 
ATOM   3358 N  N     . LEU A 1 466 ? 13.047  2.358   12.817  1.00 92.68  ? 569  LEU A N     1 
ATOM   3359 C  CA    . LEU A 1 466 ? 13.032  1.109   12.062  1.00 94.12  ? 569  LEU A CA    1 
ATOM   3360 C  C     . LEU A 1 466 ? 11.971  1.125   10.970  1.00 99.34  ? 569  LEU A C     1 
ATOM   3361 O  O     . LEU A 1 466 ? 12.169  0.531   9.904   1.00 104.16 ? 569  LEU A O     1 
ATOM   3362 C  CB    . LEU A 1 466 ? 12.803  -0.074  13.004  1.00 87.18  ? 569  LEU A CB    1 
ATOM   3363 C  CG    . LEU A 1 466 ? 13.852  -0.311  14.092  1.00 96.73  ? 569  LEU A CG    1 
ATOM   3364 C  CD1   . LEU A 1 466 ? 13.423  -1.447  15.009  1.00 100.77 ? 569  LEU A CD1   1 
ATOM   3365 C  CD2   . LEU A 1 466 ? 15.217  -0.593  13.486  1.00 79.94  ? 569  LEU A CD2   1 
ATOM   3366 N  N     . LEU A 1 467 ? 10.841  1.793   11.212  1.00 97.54  ? 570  LEU A N     1 
ATOM   3367 C  CA    . LEU A 1 467 ? 9.810   1.914   10.190  1.00 100.23 ? 570  LEU A CA    1 
ATOM   3368 C  C     . LEU A 1 467 ? 10.179  2.916   9.107   1.00 102.51 ? 570  LEU A C     1 
ATOM   3369 O  O     . LEU A 1 467 ? 9.611   2.862   8.010   1.00 107.70 ? 570  LEU A O     1 
ATOM   3370 C  CB    . LEU A 1 467 ? 8.477   2.314   10.826  1.00 101.52 ? 570  LEU A CB    1 
ATOM   3371 C  CG    . LEU A 1 467 ? 7.888   1.341   11.847  1.00 96.17  ? 570  LEU A CG    1 
ATOM   3372 C  CD1   . LEU A 1 467 ? 6.518   1.816   12.300  1.00 94.40  ? 570  LEU A CD1   1 
ATOM   3373 C  CD2   . LEU A 1 467 ? 7.812   -0.065  11.271  1.00 96.41  ? 570  LEU A CD2   1 
ATOM   3374 N  N     . SER A 1 468 ? 11.113  3.826   9.388   1.00 100.76 ? 571  SER A N     1 
ATOM   3375 C  CA    . SER A 1 468 ? 11.555  4.794   8.393   1.00 109.38 ? 571  SER A CA    1 
ATOM   3376 C  C     . SER A 1 468 ? 12.582  4.219   7.428   1.00 106.72 ? 571  SER A C     1 
ATOM   3377 O  O     . SER A 1 468 ? 12.715  4.727   6.310   1.00 102.15 ? 571  SER A O     1 
ATOM   3378 C  CB    . SER A 1 468 ? 12.138  6.027   9.086   1.00 105.80 ? 571  SER A CB    1 
ATOM   3379 O  OG    . SER A 1 468 ? 11.157  6.677   9.874   1.00 107.79 ? 571  SER A OG    1 
ATOM   3380 N  N     . VAL A 1 469 ? 13.307  3.177   7.833   1.00 106.55 ? 572  VAL A N     1 
ATOM   3381 C  CA    . VAL A 1 469 ? 14.324  2.585   6.974   1.00 103.59 ? 572  VAL A CA    1 
ATOM   3382 C  C     . VAL A 1 469 ? 13.654  1.855   5.821   1.00 107.13 ? 572  VAL A C     1 
ATOM   3383 O  O     . VAL A 1 469 ? 12.756  1.028   6.026   1.00 106.99 ? 572  VAL A O     1 
ATOM   3384 C  CB    . VAL A 1 469 ? 15.221  1.634   7.779   1.00 104.64 ? 572  VAL A CB    1 
ATOM   3385 C  CG1   . VAL A 1 469 ? 16.309  1.049   6.890   1.00 105.80 ? 572  VAL A CG1   1 
ATOM   3386 C  CG2   . VAL A 1 469 ? 15.823  2.358   8.963   1.00 107.32 ? 572  VAL A CG2   1 
ATOM   3387 N  N     . LYS A 1 470 ? 14.086  2.159   4.601   1.00 108.75 ? 573  LYS A N     1 
ATOM   3388 C  CA    . LYS A 1 470 ? 13.623  1.428   3.426   1.00 110.46 ? 573  LYS A CA    1 
ATOM   3389 C  C     . LYS A 1 470 ? 14.293  0.061   3.422   1.00 103.76 ? 573  LYS A C     1 
ATOM   3390 O  O     . LYS A 1 470 ? 15.463  -0.073  3.057   1.00 103.97 ? 573  LYS A O     1 
ATOM   3391 C  CB    . LYS A 1 470 ? 13.930  2.204   2.150   1.00 112.76 ? 573  LYS A CB    1 
ATOM   3392 C  CG    . LYS A 1 470 ? 13.358  3.613   2.124   1.00 112.62 ? 573  LYS A CG    1 
ATOM   3393 C  CD    . LYS A 1 470 ? 13.502  4.245   0.749   1.00 112.33 ? 573  LYS A CD    1 
ATOM   3394 C  CE    . LYS A 1 470 ? 14.962  4.375   0.341   1.00 121.96 ? 573  LYS A CE    1 
ATOM   3395 N  NZ    . LYS A 1 470 ? 15.699  5.351   1.189   1.00 117.31 ? 573  LYS A NZ    1 
ATOM   3396 N  N     . TRP A 1 471 ? 13.553  -0.964  3.845   1.00 105.96 ? 574  TRP A N     1 
ATOM   3397 C  CA    . TRP A 1 471 ? 14.100  -2.313  3.903   1.00 106.42 ? 574  TRP A CA    1 
ATOM   3398 C  C     . TRP A 1 471 ? 14.312  -2.919  2.525   1.00 100.38 ? 574  TRP A C     1 
ATOM   3399 O  O     . TRP A 1 471 ? 14.961  -3.966  2.423   1.00 95.73  ? 574  TRP A O     1 
ATOM   3400 C  CB    . TRP A 1 471 ? 13.182  -3.210  4.734   1.00 107.58 ? 574  TRP A CB    1 
ATOM   3401 C  CG    . TRP A 1 471 ? 12.997  -2.706  6.124   1.00 106.39 ? 574  TRP A CG    1 
ATOM   3402 C  CD1   . TRP A 1 471 ? 12.013  -1.875  6.571   1.00 112.75 ? 574  TRP A CD1   1 
ATOM   3403 C  CD2   . TRP A 1 471 ? 13.830  -2.986  7.254   1.00 107.93 ? 574  TRP A CD2   1 
ATOM   3404 N  NE1   . TRP A 1 471 ? 12.178  -1.624  7.911   1.00 109.37 ? 574  TRP A NE1   1 
ATOM   3405 C  CE2   . TRP A 1 471 ? 13.287  -2.295  8.354   1.00 106.43 ? 574  TRP A CE2   1 
ATOM   3406 C  CE3   . TRP A 1 471 ? 14.981  -3.756  7.443   1.00 110.37 ? 574  TRP A CE3   1 
ATOM   3407 C  CZ2   . TRP A 1 471 ? 13.855  -2.352  9.625   1.00 110.83 ? 574  TRP A CZ2   1 
ATOM   3408 C  CZ3   . TRP A 1 471 ? 15.544  -3.811  8.705   1.00 102.77 ? 574  TRP A CZ3   1 
ATOM   3409 C  CH2   . TRP A 1 471 ? 14.981  -3.113  9.779   1.00 100.14 ? 574  TRP A CH2   1 
ATOM   3410 N  N     . ASN A 1 472 ? 13.782  -2.290  1.472   1.00 115.79 ? 575  ASN A N     1 
ATOM   3411 C  CA    . ASN A 1 472 ? 14.001  -2.783  0.117   1.00 100.90 ? 575  ASN A CA    1 
ATOM   3412 C  C     . ASN A 1 472 ? 15.470  -2.714  -0.275  1.00 100.87 ? 575  ASN A C     1 
ATOM   3413 O  O     . ASN A 1 472 ? 15.955  -3.578  -1.012  1.00 112.95 ? 575  ASN A O     1 
ATOM   3414 C  CB    . ASN A 1 472 ? 13.149  -1.986  -0.871  1.00 93.78  ? 575  ASN A CB    1 
ATOM   3415 C  CG    . ASN A 1 472 ? 13.301  -0.487  -0.694  1.00 102.06 ? 575  ASN A CG    1 
ATOM   3416 O  OD1   . ASN A 1 472 ? 12.514  0.150   0.006   1.00 118.33 ? 575  ASN A OD1   1 
ATOM   3417 N  ND2   . ASN A 1 472 ? 14.320  0.084   -1.325  1.00 112.20 ? 575  ASN A ND2   1 
ATOM   3418 N  N     . SER A 1 473 ? 16.189  -1.703  0.201   1.00 103.02 ? 576  SER A N     1 
ATOM   3419 C  CA    . SER A 1 473 ? 17.601  -1.557  -0.112  1.00 108.60 ? 576  SER A CA    1 
ATOM   3420 C  C     . SER A 1 473 ? 18.454  -2.343  0.881   1.00 106.71 ? 576  SER A C     1 
ATOM   3421 O  O     . SER A 1 473 ? 17.981  -2.814  1.917   1.00 107.67 ? 576  SER A O     1 
ATOM   3422 C  CB    . SER A 1 473 ? 18.002  -0.081  -0.108  1.00 109.95 ? 576  SER A CB    1 
ATOM   3423 O  OG    . SER A 1 473 ? 17.882  0.477   1.189   1.00 114.72 ? 576  SER A OG    1 
ATOM   3424 N  N     . ARG A 1 474 ? 19.735  -2.489  0.542   1.00 110.51 ? 577  ARG A N     1 
ATOM   3425 C  CA    . ARG A 1 474 ? 20.692  -3.151  1.415   1.00 108.90 ? 577  ARG A CA    1 
ATOM   3426 C  C     . ARG A 1 474 ? 21.709  -2.200  2.024   1.00 115.64 ? 577  ARG A C     1 
ATOM   3427 O  O     . ARG A 1 474 ? 22.301  -2.535  3.053   1.00 118.60 ? 577  ARG A O     1 
ATOM   3428 C  CB    . ARG A 1 474 ? 21.443  -4.254  0.653   1.00 115.10 ? 577  ARG A CB    1 
ATOM   3429 C  CG    . ARG A 1 474 ? 22.601  -3.739  -0.184  1.00 124.45 ? 577  ARG A CG    1 
ATOM   3430 C  CD    . ARG A 1 474 ? 23.268  -4.844  -0.981  1.00 125.93 ? 577  ARG A CD    1 
ATOM   3431 N  NE    . ARG A 1 474 ? 24.559  -4.414  -1.505  1.00 134.67 ? 577  ARG A NE    1 
ATOM   3432 C  CZ    . ARG A 1 474 ? 25.279  -5.099  -2.382  1.00 137.21 ? 577  ARG A CZ    1 
ATOM   3433 N  NH1   . ARG A 1 474 ? 24.852  -6.248  -2.879  1.00 137.45 ? 577  ARG A NH1   1 
ATOM   3434 N  NH2   . ARG A 1 474 ? 26.455  -4.617  -2.774  1.00 139.60 ? 577  ARG A NH2   1 
ATOM   3435 N  N     . ASP A 1 475 ? 21.928  -1.030  1.417   1.00 119.17 ? 578  ASP A N     1 
ATOM   3436 C  CA    . ASP A 1 475 ? 22.868  -0.069  1.983   1.00 123.32 ? 578  ASP A CA    1 
ATOM   3437 C  C     . ASP A 1 475 ? 22.333  0.519   3.281   1.00 119.96 ? 578  ASP A C     1 
ATOM   3438 O  O     . ASP A 1 475 ? 23.100  0.780   4.214   1.00 120.60 ? 578  ASP A O     1 
ATOM   3439 C  CB    . ASP A 1 475 ? 23.160  1.041   0.974   1.00 130.03 ? 578  ASP A CB    1 
ATOM   3440 C  CG    . ASP A 1 475 ? 23.704  0.510   -0.337  1.00 135.89 ? 578  ASP A CG    1 
ATOM   3441 O  OD1   . ASP A 1 475 ? 23.829  -0.725  -0.474  1.00 134.34 ? 578  ASP A OD1   1 
ATOM   3442 O  OD2   . ASP A 1 475 ? 24.006  1.328   -1.231  1.00 151.31 ? 578  ASP A OD2   1 
ATOM   3443 N  N     . GLU A 1 476 ? 21.018  0.731   3.358   1.00 120.99 ? 579  GLU A N     1 
ATOM   3444 C  CA    . GLU A 1 476 ? 20.422  1.276   4.571   1.00 118.40 ? 579  GLU A CA    1 
ATOM   3445 C  C     . GLU A 1 476 ? 20.269  0.210   5.649   1.00 114.90 ? 579  GLU A C     1 
ATOM   3446 O  O     . GLU A 1 476 ? 20.541  0.472   6.826   1.00 113.65 ? 579  GLU A O     1 
ATOM   3447 C  CB    . GLU A 1 476 ? 19.070  1.911   4.247   1.00 115.47 ? 579  GLU A CB    1 
ATOM   3448 C  CG    . GLU A 1 476 ? 19.165  3.131   3.347   1.00 114.76 ? 579  GLU A CG    1 
ATOM   3449 C  CD    . GLU A 1 476 ? 17.808  3.705   3.005   1.00 124.87 ? 579  GLU A CD    1 
ATOM   3450 O  OE1   . GLU A 1 476 ? 16.807  2.969   3.125   1.00 119.19 ? 579  GLU A OE1   1 
ATOM   3451 O  OE2   . GLU A 1 476 ? 17.740  4.892   2.620   1.00 134.25 ? 579  GLU A OE2   1 
ATOM   3452 N  N     . VAL A 1 477 ? 19.838  -0.995  5.268   1.00 111.51 ? 580  VAL A N     1 
ATOM   3453 C  CA    . VAL A 1 477 ? 19.693  -2.070  6.244   1.00 113.68 ? 580  VAL A CA    1 
ATOM   3454 C  C     . VAL A 1 477 ? 21.052  -2.474  6.804   1.00 114.90 ? 580  VAL A C     1 
ATOM   3455 O  O     . VAL A 1 477 ? 21.154  -2.889  7.966   1.00 116.55 ? 580  VAL A O     1 
ATOM   3456 C  CB    . VAL A 1 477 ? 18.951  -3.264  5.613   1.00 107.54 ? 580  VAL A CB    1 
ATOM   3457 C  CG1   . VAL A 1 477 ? 18.805  -4.403  6.612   1.00 107.36 ? 580  VAL A CG1   1 
ATOM   3458 C  CG2   . VAL A 1 477 ? 17.586  -2.825  5.116   1.00 106.22 ? 580  VAL A CG2   1 
ATOM   3459 N  N     . ALA A 1 478 ? 22.116  -2.349  6.006   1.00 114.79 ? 581  ALA A N     1 
ATOM   3460 C  CA    . ALA A 1 478 ? 23.453  -2.623  6.520   1.00 116.39 ? 581  ALA A CA    1 
ATOM   3461 C  C     . ALA A 1 478 ? 23.858  -1.597  7.571   1.00 119.48 ? 581  ALA A C     1 
ATOM   3462 O  O     . ALA A 1 478 ? 24.498  -1.944  8.571   1.00 123.18 ? 581  ALA A O     1 
ATOM   3463 C  CB    . ALA A 1 478 ? 24.467  -2.650  5.377   1.00 119.63 ? 581  ALA A CB    1 
ATOM   3464 N  N     . GLN A 1 479 ? 23.494  -0.330  7.363   1.00 116.59 ? 582  GLN A N     1 
ATOM   3465 C  CA    . GLN A 1 479 ? 23.776  0.690   8.368   1.00 118.49 ? 582  GLN A CA    1 
ATOM   3466 C  C     . GLN A 1 479 ? 22.911  0.497   9.606   1.00 114.56 ? 582  GLN A C     1 
ATOM   3467 O  O     . GLN A 1 479 ? 23.371  0.716   10.732  1.00 113.33 ? 582  GLN A O     1 
ATOM   3468 C  CB    . GLN A 1 479 ? 23.559  2.084   7.780   1.00 122.65 ? 582  GLN A CB    1 
ATOM   3469 C  CG    . GLN A 1 479 ? 24.470  2.425   6.616   1.00 123.55 ? 582  GLN A CG    1 
ATOM   3470 C  CD    . GLN A 1 479 ? 24.179  3.797   6.043   1.00 127.83 ? 582  GLN A CD    1 
ATOM   3471 O  OE1   . GLN A 1 479 ? 23.358  4.543   6.578   1.00 125.51 ? 582  GLN A OE1   1 
ATOM   3472 N  NE2   . GLN A 1 479 ? 24.850  4.137   4.949   1.00 138.75 ? 582  GLN A NE2   1 
ATOM   3473 N  N     . MET A 1 480 ? 21.654  0.089   9.415   1.00 116.13 ? 583  MET A N     1 
ATOM   3474 C  CA    . MET A 1 480 ? 20.756  -0.109  10.547  1.00 112.17 ? 583  MET A CA    1 
ATOM   3475 C  C     . MET A 1 480 ? 21.245  -1.225  11.461  1.00 113.50 ? 583  MET A C     1 
ATOM   3476 O  O     . MET A 1 480 ? 21.043  -1.160  12.679  1.00 112.91 ? 583  MET A O     1 
ATOM   3477 C  CB    . MET A 1 480 ? 19.342  -0.408  10.046  1.00 110.79 ? 583  MET A CB    1 
ATOM   3478 C  CG    . MET A 1 480 ? 18.261  -0.370  11.120  1.00 113.68 ? 583  MET A CG    1 
ATOM   3479 S  SD    . MET A 1 480 ? 17.849  1.298   11.678  1.00 135.61 ? 583  MET A SD    1 
ATOM   3480 C  CE    . MET A 1 480 ? 18.827  1.432   13.170  1.00 113.59 ? 583  MET A CE    1 
ATOM   3481 N  N     . TYR A 1 481 ? 21.888  -2.252  10.898  1.00 113.50 ? 584  TYR A N     1 
ATOM   3482 C  CA    . TYR A 1 481 ? 22.456  -3.307  11.731  1.00 117.17 ? 584  TYR A CA    1 
ATOM   3483 C  C     . TYR A 1 481 ? 23.581  -2.780  12.613  1.00 121.50 ? 584  TYR A C     1 
ATOM   3484 O  O     . TYR A 1 481 ? 23.779  -3.280  13.726  1.00 117.27 ? 584  TYR A O     1 
ATOM   3485 C  CB    . TYR A 1 481 ? 22.968  -4.459  10.864  1.00 116.82 ? 584  TYR A CB    1 
ATOM   3486 C  CG    . TYR A 1 481 ? 21.891  -5.403  10.375  1.00 116.21 ? 584  TYR A CG    1 
ATOM   3487 C  CD1   . TYR A 1 481 ? 20.555  -5.188  10.685  1.00 113.35 ? 584  TYR A CD1   1 
ATOM   3488 C  CD2   . TYR A 1 481 ? 22.215  -6.518  9.613   1.00 125.24 ? 584  TYR A CD2   1 
ATOM   3489 C  CE1   . TYR A 1 481 ? 19.572  -6.050  10.240  1.00 116.71 ? 584  TYR A CE1   1 
ATOM   3490 C  CE2   . TYR A 1 481 ? 21.238  -7.388  9.164   1.00 120.44 ? 584  TYR A CE2   1 
ATOM   3491 C  CZ    . TYR A 1 481 ? 19.918  -7.150  9.481   1.00 120.38 ? 584  TYR A CZ    1 
ATOM   3492 O  OH    . TYR A 1 481 ? 18.941  -8.013  9.037   1.00 103.26 ? 584  TYR A OH    1 
ATOM   3493 N  N     . CYS A 1 482 ? 24.322  -1.776  12.140  1.00 118.77 ? 585  CYS A N     1 
ATOM   3494 C  CA    . CYS A 1 482 ? 25.407  -1.221  12.942  1.00 128.17 ? 585  CYS A CA    1 
ATOM   3495 C  C     . CYS A 1 482 ? 24.872  -0.403  14.110  1.00 119.12 ? 585  CYS A C     1 
ATOM   3496 O  O     . CYS A 1 482 ? 25.449  -0.423  15.204  1.00 112.23 ? 585  CYS A O     1 
ATOM   3497 C  CB    . CYS A 1 482 ? 26.326  -0.371  12.067  1.00 119.91 ? 585  CYS A CB    1 
ATOM   3498 S  SG    . CYS A 1 482 ? 27.212  -1.311  10.809  1.00 150.09 ? 585  CYS A SG    1 
ATOM   3499 N  N     . LEU A 1 483 ? 23.774  0.327   13.900  1.00 115.10 ? 586  LEU A N     1 
ATOM   3500 C  CA    . LEU A 1 483 ? 23.179  1.092   14.990  1.00 111.32 ? 586  LEU A CA    1 
ATOM   3501 C  C     . LEU A 1 483 ? 22.561  0.167   16.031  1.00 111.59 ? 586  LEU A C     1 
ATOM   3502 O  O     . LEU A 1 483 ? 22.790  0.329   17.234  1.00 111.28 ? 586  LEU A O     1 
ATOM   3503 C  CB    . LEU A 1 483 ? 22.133  2.063   14.446  1.00 110.52 ? 586  LEU A CB    1 
ATOM   3504 C  CG    . LEU A 1 483 ? 22.621  3.199   13.548  1.00 109.33 ? 586  LEU A CG    1 
ATOM   3505 C  CD1   . LEU A 1 483 ? 21.454  4.084   13.144  1.00 109.58 ? 586  LEU A CD1   1 
ATOM   3506 C  CD2   . LEU A 1 483 ? 23.698  4.014   14.248  1.00 113.11 ? 586  LEU A CD2   1 
ATOM   3507 N  N     . VAL A 1 484 ? 21.776  -0.816  15.580  1.00 111.08 ? 587  VAL A N     1 
ATOM   3508 C  CA    . VAL A 1 484 ? 21.151  -1.762  16.500  1.00 105.80 ? 587  VAL A CA    1 
ATOM   3509 C  C     . VAL A 1 484 ? 22.206  -2.583  17.232  1.00 108.80 ? 587  VAL A C     1 
ATOM   3510 O  O     . VAL A 1 484 ? 21.984  -3.025  18.367  1.00 112.13 ? 587  VAL A O     1 
ATOM   3511 C  CB    . VAL A 1 484 ? 20.152  -2.651  15.729  1.00 101.82 ? 587  VAL A CB    1 
ATOM   3512 C  CG1   . VAL A 1 484 ? 19.608  -3.765  16.609  1.00 96.97  ? 587  VAL A CG1   1 
ATOM   3513 C  CG2   . VAL A 1 484 ? 19.010  -1.804  15.190  1.00 101.22 ? 587  VAL A CG2   1 
ATOM   3514 N  N     . LYS A 1 485 ? 23.374  -2.780  16.615  1.00 112.25 ? 588  LYS A N     1 
ATOM   3515 C  CA    . LYS A 1 485 ? 24.447  -3.507  17.287  1.00 113.99 ? 588  LYS A CA    1 
ATOM   3516 C  C     . LYS A 1 485 ? 24.935  -2.768  18.527  1.00 111.95 ? 588  LYS A C     1 
ATOM   3517 O  O     . LYS A 1 485 ? 25.348  -3.402  19.504  1.00 113.38 ? 588  LYS A O     1 
ATOM   3518 C  CB    . LYS A 1 485 ? 25.608  -3.744  16.320  1.00 118.01 ? 588  LYS A CB    1 
ATOM   3519 C  CG    . LYS A 1 485 ? 26.671  -4.685  16.858  1.00 121.28 ? 588  LYS A CG    1 
ATOM   3520 C  CD    . LYS A 1 485 ? 26.116  -6.090  17.025  1.00 125.34 ? 588  LYS A CD    1 
ATOM   3521 C  CE    . LYS A 1 485 ? 26.721  -6.785  18.234  1.00 129.61 ? 588  LYS A CE    1 
ATOM   3522 N  NZ    . LYS A 1 485 ? 26.297  -6.134  19.506  1.00 124.64 ? 588  LYS A NZ    1 
ATOM   3523 N  N     . ASP A 1 486 ? 24.895  -1.434  18.510  1.00 108.59 ? 589  ASP A N     1 
ATOM   3524 C  CA    . ASP A 1 486 ? 25.339  -0.623  19.639  1.00 111.82 ? 589  ASP A CA    1 
ATOM   3525 C  C     . ASP A 1 486 ? 24.267  0.377   20.059  1.00 114.30 ? 589  ASP A C     1 
ATOM   3526 O  O     . ASP A 1 486 ? 24.582  1.479   20.515  1.00 118.83 ? 589  ASP A O     1 
ATOM   3527 C  CB    . ASP A 1 486 ? 26.646  0.100   19.313  1.00 114.84 ? 589  ASP A CB    1 
ATOM   3528 C  CG    . ASP A 1 486 ? 27.812  -0.854  19.135  1.00 123.85 ? 589  ASP A CG    1 
ATOM   3529 O  OD1   . ASP A 1 486 ? 27.804  -1.631  18.157  1.00 133.34 ? 589  ASP A OD1   1 
ATOM   3530 O  OD2   . ASP A 1 486 ? 28.740  -0.825  19.971  1.00 124.22 ? 589  ASP A OD2   1 
ATOM   3531 N  N     . TRP A 1 487 ? 22.996  0.007   19.910  1.00 110.26 ? 590  TRP A N     1 
ATOM   3532 C  CA    . TRP A 1 487 ? 21.906  0.884   20.317  1.00 107.59 ? 590  TRP A CA    1 
ATOM   3533 C  C     . TRP A 1 487 ? 21.681  0.768   21.823  1.00 110.66 ? 590  TRP A C     1 
ATOM   3534 O  O     . TRP A 1 487 ? 21.690  -0.339  22.367  1.00 116.42 ? 590  TRP A O     1 
ATOM   3535 C  CB    . TRP A 1 487 ? 20.622  0.527   19.567  1.00 104.86 ? 590  TRP A CB    1 
ATOM   3536 C  CG    . TRP A 1 487 ? 19.549  1.575   19.640  1.00 102.70 ? 590  TRP A CG    1 
ATOM   3537 C  CD1   . TRP A 1 487 ? 18.517  1.629   20.529  1.00 104.13 ? 590  TRP A CD1   1 
ATOM   3538 C  CD2   . TRP A 1 487 ? 19.400  2.714   18.782  1.00 104.43 ? 590  TRP A CD2   1 
ATOM   3539 N  NE1   . TRP A 1 487 ? 17.735  2.731   20.280  1.00 103.61 ? 590  TRP A NE1   1 
ATOM   3540 C  CE2   . TRP A 1 487 ? 18.256  3.414   19.213  1.00 103.34 ? 590  TRP A CE2   1 
ATOM   3541 C  CE3   . TRP A 1 487 ? 20.123  3.210   17.693  1.00 109.37 ? 590  TRP A CE3   1 
ATOM   3542 C  CZ2   . TRP A 1 487 ? 17.818  4.584   18.594  1.00 108.31 ? 590  TRP A CZ2   1 
ATOM   3543 C  CZ3   . TRP A 1 487 ? 19.687  4.371   17.079  1.00 112.33 ? 590  TRP A CZ3   1 
ATOM   3544 C  CH2   . TRP A 1 487 ? 18.546  5.045   17.532  1.00 112.00 ? 590  TRP A CH2   1 
ATOM   3545 N  N     . PRO A 1 488 ? 21.490  1.887   22.517  1.00 109.56 ? 591  PRO A N     1 
ATOM   3546 C  CA    . PRO A 1 488 ? 21.299  1.840   23.971  1.00 110.09 ? 591  PRO A CA    1 
ATOM   3547 C  C     . PRO A 1 488 ? 20.031  1.087   24.328  1.00 110.81 ? 591  PRO A C     1 
ATOM   3548 O  O     . PRO A 1 488 ? 18.995  1.249   23.666  1.00 109.45 ? 591  PRO A O     1 
ATOM   3549 C  CB    . PRO A 1 488 ? 21.198  3.322   24.366  1.00 108.85 ? 591  PRO A CB    1 
ATOM   3550 C  CG    . PRO A 1 488 ? 21.818  4.070   23.230  1.00 111.82 ? 591  PRO A CG    1 
ATOM   3551 C  CD    . PRO A 1 488 ? 21.507  3.267   22.006  1.00 108.61 ? 591  PRO A CD    1 
ATOM   3552 N  N     . PRO A 1 489 ? 20.076  0.245   25.360  1.00 111.64 ? 592  PRO A N     1 
ATOM   3553 C  CA    . PRO A 1 489 ? 18.885  -0.523  25.737  1.00 111.22 ? 592  PRO A CA    1 
ATOM   3554 C  C     . PRO A 1 489 ? 17.738  0.385   26.154  1.00 113.82 ? 592  PRO A C     1 
ATOM   3555 O  O     . PRO A 1 489 ? 17.941  1.491   26.660  1.00 106.66 ? 592  PRO A O     1 
ATOM   3556 C  CB    . PRO A 1 489 ? 19.373  -1.384  26.908  1.00 113.20 ? 592  PRO A CB    1 
ATOM   3557 C  CG    . PRO A 1 489 ? 20.855  -1.465  26.727  1.00 119.11 ? 592  PRO A CG    1 
ATOM   3558 C  CD    . PRO A 1 489 ? 21.256  -0.139  26.153  1.00 119.26 ? 592  PRO A CD    1 
ATOM   3559 N  N     . ILE A 1 490 ? 16.519  -0.100  25.929  1.00 106.32 ? 593  ILE A N     1 
ATOM   3560 C  CA    . ILE A 1 490 ? 15.304  0.641   26.229  1.00 102.34 ? 593  ILE A CA    1 
ATOM   3561 C  C     . ILE A 1 490 ? 14.520  -0.111  27.299  1.00 97.07  ? 593  ILE A C     1 
ATOM   3562 O  O     . ILE A 1 490 ? 14.882  -1.215  27.708  1.00 96.21  ? 593  ILE A O     1 
ATOM   3563 C  CB    . ILE A 1 490 ? 14.438  0.869   24.976  1.00 97.80  ? 593  ILE A CB    1 
ATOM   3564 C  CG1   . ILE A 1 490 ? 14.160  -0.461  24.272  1.00 93.72  ? 593  ILE A CG1   1 
ATOM   3565 C  CG2   . ILE A 1 490 ? 15.116  1.849   24.032  1.00 101.01 ? 593  ILE A CG2   1 
ATOM   3566 C  CD1   . ILE A 1 490 ? 13.226  -0.342  23.084  1.00 89.86  ? 593  ILE A CD1   1 
ATOM   3567 N  N     . LYS A 1 491 ? 13.430  0.508   27.748  1.00 95.02  ? 594  LYS A N     1 
ATOM   3568 C  CA    . LYS A 1 491 ? 12.588  -0.104  28.762  1.00 98.07  ? 594  LYS A CA    1 
ATOM   3569 C  C     . LYS A 1 491 ? 11.953  -1.383  28.216  1.00 97.30  ? 594  LYS A C     1 
ATOM   3570 O  O     . LYS A 1 491 ? 11.682  -1.488  27.016  1.00 93.92  ? 594  LYS A O     1 
ATOM   3571 C  CB    . LYS A 1 491 ? 11.503  0.871   29.217  1.00 95.07  ? 594  LYS A CB    1 
ATOM   3572 C  CG    . LYS A 1 491 ? 12.038  2.146   29.848  1.00 92.61  ? 594  LYS A CG    1 
ATOM   3573 N  N     . PRO A 1 492 ? 11.711  -2.377  29.076  1.00 97.94  ? 595  PRO A N     1 
ATOM   3574 C  CA    . PRO A 1 492 ? 11.151  -3.646  28.578  1.00 97.70  ? 595  PRO A CA    1 
ATOM   3575 C  C     . PRO A 1 492 ? 9.762   -3.503  27.982  1.00 98.02  ? 595  PRO A C     1 
ATOM   3576 O  O     . PRO A 1 492 ? 9.439   -4.202  27.015  1.00 97.43  ? 595  PRO A O     1 
ATOM   3577 C  CB    . PRO A 1 492 ? 11.152  -4.541  29.826  1.00 91.95  ? 595  PRO A CB    1 
ATOM   3578 C  CG    . PRO A 1 492 ? 11.153  -3.591  30.975  1.00 94.79  ? 595  PRO A CG    1 
ATOM   3579 C  CD    . PRO A 1 492 ? 11.961  -2.413  30.526  1.00 94.04  ? 595  PRO A CD    1 
ATOM   3580 N  N     . GLU A 1 493 ? 8.925   -2.618  28.532  1.00 102.06 ? 596  GLU A N     1 
ATOM   3581 C  CA    . GLU A 1 493 ? 7.612   -2.387  27.939  1.00 95.95  ? 596  GLU A CA    1 
ATOM   3582 C  C     . GLU A 1 493 ? 7.730   -1.820  26.531  1.00 106.51 ? 596  GLU A C     1 
ATOM   3583 O  O     . GLU A 1 493 ? 6.858   -2.060  25.689  1.00 120.74 ? 596  GLU A O     1 
ATOM   3584 C  CB    . GLU A 1 493 ? 6.786   -1.446  28.818  1.00 105.64 ? 596  GLU A CB    1 
ATOM   3585 C  CG    . GLU A 1 493 ? 6.245   -2.076  30.096  1.00 108.03 ? 596  GLU A CG    1 
ATOM   3586 C  CD    . GLU A 1 493 ? 7.269   -2.123  31.215  1.00 123.15 ? 596  GLU A CD    1 
ATOM   3587 O  OE1   . GLU A 1 493 ? 8.396   -1.618  31.020  1.00 113.89 ? 596  GLU A OE1   1 
ATOM   3588 O  OE2   . GLU A 1 493 ? 6.943   -2.662  32.295  1.00 119.09 ? 596  GLU A OE2   1 
ATOM   3589 N  N     . GLN A 1 494 ? 8.800   -1.070  26.257  1.00 99.48  ? 597  GLN A N     1 
ATOM   3590 C  CA    . GLN A 1 494 ? 9.011   -0.526  24.921  1.00 98.60  ? 597  GLN A CA    1 
ATOM   3591 C  C     . GLN A 1 494 ? 9.607   -1.568  23.982  1.00 95.99  ? 597  GLN A C     1 
ATOM   3592 O  O     . GLN A 1 494 ? 9.263   -1.606  22.796  1.00 100.73 ? 597  GLN A O     1 
ATOM   3593 C  CB    . GLN A 1 494 ? 9.913   0.705   24.998  1.00 95.47  ? 597  GLN A CB    1 
ATOM   3594 C  CG    . GLN A 1 494 ? 9.353   1.827   25.858  1.00 92.46  ? 597  GLN A CG    1 
ATOM   3595 C  CD    . GLN A 1 494 ? 10.330  2.973   26.034  1.00 96.74  ? 597  GLN A CD    1 
ATOM   3596 O  OE1   . GLN A 1 494 ? 11.540  2.802   25.888  1.00 99.27  ? 597  GLN A OE1   1 
ATOM   3597 N  NE2   . GLN A 1 494 ? 9.806   4.152   26.349  1.00 97.31  ? 597  GLN A NE2   1 
ATOM   3598 N  N     . ALA A 1 495 ? 10.499  -2.419  24.495  1.00 95.02  ? 598  ALA A N     1 
ATOM   3599 C  CA    . ALA A 1 495 ? 11.105  -3.458  23.672  1.00 91.48  ? 598  ALA A CA    1 
ATOM   3600 C  C     . ALA A 1 495 ? 10.098  -4.512  23.231  1.00 95.49  ? 598  ALA A C     1 
ATOM   3601 O  O     . ALA A 1 495 ? 10.322  -5.175  22.212  1.00 94.55  ? 598  ALA A O     1 
ATOM   3602 C  CB    . ALA A 1 495 ? 12.257  -4.124  24.426  1.00 90.81  ? 598  ALA A CB    1 
ATOM   3603 N  N     . MET A 1 496 ? 8.999   -4.685  23.971  1.00 96.62  ? 599  MET A N     1 
ATOM   3604 C  CA    . MET A 1 496 ? 7.966   -5.621  23.541  1.00 99.13  ? 599  MET A CA    1 
ATOM   3605 C  C     . MET A 1 496 ? 7.328   -5.183  22.231  1.00 99.63  ? 599  MET A C     1 
ATOM   3606 O  O     . MET A 1 496 ? 6.814   -6.020  21.481  1.00 96.80  ? 599  MET A O     1 
ATOM   3607 C  CB    . MET A 1 496 ? 6.895   -5.769  24.621  1.00 97.28  ? 599  MET A CB    1 
ATOM   3608 C  CG    . MET A 1 496 ? 7.377   -6.425  25.900  1.00 96.57  ? 599  MET A CG    1 
ATOM   3609 S  SD    . MET A 1 496 ? 6.007   -6.784  27.013  1.00 97.00  ? 599  MET A SD    1 
ATOM   3610 C  CE    . MET A 1 496 ? 5.200   -5.185  27.083  1.00 89.64  ? 599  MET A CE    1 
ATOM   3611 N  N     . GLU A 1 497 ? 7.343   -3.879  21.944  1.00 104.94 ? 600  GLU A N     1 
ATOM   3612 C  CA    . GLU A 1 497 ? 6.836   -3.395  20.666  1.00 107.86 ? 600  GLU A CA    1 
ATOM   3613 C  C     . GLU A 1 497 ? 7.666   -3.927  19.504  1.00 108.34 ? 600  GLU A C     1 
ATOM   3614 O  O     . GLU A 1 497 ? 7.132   -4.163  18.415  1.00 104.80 ? 600  GLU A O     1 
ATOM   3615 C  CB    . GLU A 1 497 ? 6.817   -1.865  20.660  1.00 112.29 ? 600  GLU A CB    1 
ATOM   3616 C  CG    . GLU A 1 497 ? 6.279   -1.241  19.381  1.00 129.45 ? 600  GLU A CG    1 
ATOM   3617 C  CD    . GLU A 1 497 ? 6.299   0.276   19.420  1.00 129.78 ? 600  GLU A CD    1 
ATOM   3618 O  OE1   . GLU A 1 497 ? 6.541   0.840   20.508  1.00 132.16 ? 600  GLU A OE1   1 
ATOM   3619 O  OE2   . GLU A 1 497 ? 6.077   0.904   18.364  1.00 113.31 ? 600  GLU A OE2   1 
ATOM   3620 N  N     . LEU A 1 498 ? 8.963   -4.137  19.720  1.00 99.78  ? 601  LEU A N     1 
ATOM   3621 C  CA    . LEU A 1 498 ? 9.857   -4.667  18.699  1.00 91.50  ? 601  LEU A CA    1 
ATOM   3622 C  C     . LEU A 1 498 ? 9.711   -6.171  18.503  1.00 89.39  ? 601  LEU A C     1 
ATOM   3623 O  O     . LEU A 1 498 ? 10.566  -6.780  17.852  1.00 86.56  ? 601  LEU A O     1 
ATOM   3624 C  CB    . LEU A 1 498 ? 11.310  -4.335  19.052  1.00 89.30  ? 601  LEU A CB    1 
ATOM   3625 C  CG    . LEU A 1 498 ? 11.603  -2.868  19.364  1.00 89.62  ? 601  LEU A CG    1 
ATOM   3626 C  CD1   . LEU A 1 498 ? 13.062  -2.680  19.751  1.00 75.98  ? 601  LEU A CD1   1 
ATOM   3627 C  CD2   . LEU A 1 498 ? 11.240  -1.990  18.177  1.00 102.23 ? 601  LEU A CD2   1 
ATOM   3628 N  N     . LEU A 1 499 ? 8.658   -6.781  19.047  1.00 91.72  ? 602  LEU A N     1 
ATOM   3629 C  CA    . LEU A 1 499 ? 8.457   -8.217  18.940  1.00 88.50  ? 602  LEU A CA    1 
ATOM   3630 C  C     . LEU A 1 499 ? 7.121   -8.597  18.318  1.00 88.80  ? 602  LEU A C     1 
ATOM   3631 O  O     . LEU A 1 499 ? 6.831   -9.793  18.200  1.00 91.59  ? 602  LEU A O     1 
ATOM   3632 C  CB    . LEU A 1 499 ? 8.586   -8.878  20.320  1.00 93.34  ? 602  LEU A CB    1 
ATOM   3633 C  CG    . LEU A 1 499 ? 10.010  -8.944  20.876  1.00 92.37  ? 602  LEU A CG    1 
ATOM   3634 C  CD1   . LEU A 1 499 ? 10.025  -9.529  22.280  1.00 74.91  ? 602  LEU A CD1   1 
ATOM   3635 C  CD2   . LEU A 1 499 ? 10.903  -9.752  19.945  1.00 83.12  ? 602  LEU A CD2   1 
ATOM   3636 N  N     . ASP A 1 500 ? 6.304   -7.628  17.914  1.00 86.42  ? 603  ASP A N     1 
ATOM   3637 C  CA    . ASP A 1 500 ? 5.053   -7.930  17.233  1.00 96.68  ? 603  ASP A CA    1 
ATOM   3638 C  C     . ASP A 1 500 ? 5.337   -8.221  15.758  1.00 99.37  ? 603  ASP A C     1 
ATOM   3639 O  O     . ASP A 1 500 ? 6.483   -8.421  15.345  1.00 97.59  ? 603  ASP A O     1 
ATOM   3640 C  CB    . ASP A 1 500 ? 4.050   -6.794  17.427  1.00 95.06  ? 603  ASP A CB    1 
ATOM   3641 C  CG    . ASP A 1 500 ? 4.581   -5.448  16.961  1.00 102.77 ? 603  ASP A CG    1 
ATOM   3642 O  OD1   . ASP A 1 500 ? 5.690   -5.397  16.392  1.00 106.62 ? 603  ASP A OD1   1 
ATOM   3643 O  OD2   . ASP A 1 500 ? 3.881   -4.434  17.169  1.00 104.10 ? 603  ASP A OD2   1 
ATOM   3644 N  N     . CYS A 1 501 ? 4.288   -8.236  14.937  1.00 99.02  ? 604  CYS A N     1 
ATOM   3645 C  CA    . CYS A 1 501 ? 4.431   -8.630  13.540  1.00 99.88  ? 604  CYS A CA    1 
ATOM   3646 C  C     . CYS A 1 501 ? 5.078   -7.559  12.669  1.00 95.96  ? 604  CYS A C     1 
ATOM   3647 O  O     . CYS A 1 501 ? 5.474   -7.867  11.540  1.00 93.43  ? 604  CYS A O     1 
ATOM   3648 C  CB    . CYS A 1 501 ? 3.062   -9.004  12.970  1.00 100.95 ? 604  CYS A CB    1 
ATOM   3649 S  SG    . CYS A 1 501 ? 1.749   -7.828  13.369  1.00 121.71 ? 604  CYS A SG    1 
ATOM   3650 N  N     . ASN A 1 502 ? 5.204   -6.324  13.154  1.00 96.77  ? 605  ASN A N     1 
ATOM   3651 C  CA    . ASN A 1 502 ? 5.737   -5.233  12.346  1.00 90.43  ? 605  ASN A CA    1 
ATOM   3652 C  C     . ASN A 1 502 ? 7.256   -5.164  12.350  1.00 89.90  ? 605  ASN A C     1 
ATOM   3653 O  O     . ASN A 1 502 ? 7.821   -4.322  11.642  1.00 94.35  ? 605  ASN A O     1 
ATOM   3654 C  CB    . ASN A 1 502 ? 5.171   -3.896  12.828  1.00 92.05  ? 605  ASN A CB    1 
ATOM   3655 C  CG    . ASN A 1 502 ? 3.684   -3.779  12.594  1.00 112.33 ? 605  ASN A CG    1 
ATOM   3656 O  OD1   . ASN A 1 502 ? 2.996   -4.779  12.388  1.00 123.91 ? 605  ASN A OD1   1 
ATOM   3657 N  ND2   . ASN A 1 502 ? 3.177   -2.553  12.622  1.00 121.06 ? 605  ASN A ND2   1 
ATOM   3658 N  N     . TYR A 1 503 ? 7.923   -6.016  13.128  1.00 88.34  ? 606  TYR A N     1 
ATOM   3659 C  CA    . TYR A 1 503 ? 9.383   -6.030  13.208  1.00 87.63  ? 606  TYR A CA    1 
ATOM   3660 C  C     . TYR A 1 503 ? 9.864   -7.473  13.143  1.00 87.79  ? 606  TYR A C     1 
ATOM   3661 O  O     . TYR A 1 503 ? 10.007  -8.149  14.170  1.00 91.86  ? 606  TYR A O     1 
ATOM   3662 C  CB    . TYR A 1 503 ? 9.882   -5.345  14.479  1.00 82.42  ? 606  TYR A CB    1 
ATOM   3663 C  CG    . TYR A 1 503 ? 9.380   -3.927  14.662  1.00 79.25  ? 606  TYR A CG    1 
ATOM   3664 C  CD1   . TYR A 1 503 ? 8.126   -3.675  15.209  1.00 88.61  ? 606  TYR A CD1   1 
ATOM   3665 C  CD2   . TYR A 1 503 ? 10.162  -2.840  14.297  1.00 77.05  ? 606  TYR A CD2   1 
ATOM   3666 C  CE1   . TYR A 1 503 ? 7.665   -2.386  15.375  1.00 91.25  ? 606  TYR A CE1   1 
ATOM   3667 C  CE2   . TYR A 1 503 ? 9.709   -1.546  14.462  1.00 84.26  ? 606  TYR A CE2   1 
ATOM   3668 C  CZ    . TYR A 1 503 ? 8.460   -1.326  15.002  1.00 89.39  ? 606  TYR A CZ    1 
ATOM   3669 O  OH    . TYR A 1 503 ? 8.002   -0.041  15.169  1.00 93.07  ? 606  TYR A OH    1 
ATOM   3670 N  N     . PRO A 1 504 ? 10.122  -7.982  11.938  1.00 93.98  ? 607  PRO A N     1 
ATOM   3671 C  CA    . PRO A 1 504 ? 10.604  -9.364  11.771  1.00 87.16  ? 607  PRO A CA    1 
ATOM   3672 C  C     . PRO A 1 504 ? 12.118  -9.517  11.680  1.00 88.70  ? 607  PRO A C     1 
ATOM   3673 O  O     . PRO A 1 504 ? 12.593  -10.654 11.638  1.00 89.55  ? 607  PRO A O     1 
ATOM   3674 C  CB    . PRO A 1 504 ? 9.956   -9.757  10.441  1.00 85.93  ? 607  PRO A CB    1 
ATOM   3675 C  CG    . PRO A 1 504 ? 10.001  -8.469  9.646   1.00 91.14  ? 607  PRO A CG    1 
ATOM   3676 C  CD    . PRO A 1 504 ? 9.873   -7.331  10.639  1.00 88.93  ? 607  PRO A CD    1 
ATOM   3677 N  N     . ASP A 1 505 ? 12.875  -8.424  11.638  1.00 90.85  ? 608  ASP A N     1 
ATOM   3678 C  CA    . ASP A 1 505 ? 14.317  -8.529  11.425  1.00 86.81  ? 608  ASP A CA    1 
ATOM   3679 C  C     . ASP A 1 505 ? 14.985  -9.220  12.611  1.00 93.92  ? 608  ASP A C     1 
ATOM   3680 O  O     . ASP A 1 505 ? 14.820  -8.772  13.752  1.00 87.49  ? 608  ASP A O     1 
ATOM   3681 C  CB    . ASP A 1 505 ? 14.921  -7.141  11.211  1.00 86.41  ? 608  ASP A CB    1 
ATOM   3682 C  CG    . ASP A 1 505 ? 16.339  -7.193  10.669  1.00 108.03 ? 608  ASP A CG    1 
ATOM   3683 O  OD1   . ASP A 1 505 ? 17.225  -7.768  11.340  1.00 104.57 ? 608  ASP A OD1   1 
ATOM   3684 O  OD2   . ASP A 1 505 ? 16.568  -6.662  9.560   1.00 113.52 ? 608  ASP A OD2   1 
ATOM   3685 N  N     . PRO A 1 506 ? 15.760  -10.289 12.385  1.00 93.95  ? 609  PRO A N     1 
ATOM   3686 C  CA    . PRO A 1 506 ? 16.350  -11.023 13.523  1.00 87.72  ? 609  PRO A CA    1 
ATOM   3687 C  C     . PRO A 1 506 ? 17.235  -10.169 14.417  1.00 89.94  ? 609  PRO A C     1 
ATOM   3688 O  O     . PRO A 1 506 ? 17.192  -10.321 15.645  1.00 93.64  ? 609  PRO A O     1 
ATOM   3689 C  CB    . PRO A 1 506 ? 17.148  -12.142 12.838  1.00 88.66  ? 609  PRO A CB    1 
ATOM   3690 C  CG    . PRO A 1 506 ? 16.505  -12.302 11.495  1.00 100.54 ? 609  PRO A CG    1 
ATOM   3691 C  CD    . PRO A 1 506 ? 16.068  -10.926 11.093  1.00 93.72  ? 609  PRO A CD    1 
ATOM   3692 N  N     . MET A 1 507 ? 18.042  -9.276  13.839  1.00 92.73  ? 610  MET A N     1 
ATOM   3693 C  CA    . MET A 1 507 ? 18.860  -8.389  14.659  1.00 91.67  ? 610  MET A CA    1 
ATOM   3694 C  C     . MET A 1 507 ? 17.998  -7.453  15.497  1.00 93.76  ? 610  MET A C     1 
ATOM   3695 O  O     . MET A 1 507 ? 18.408  -7.043  16.589  1.00 94.44  ? 610  MET A O     1 
ATOM   3696 C  CB    . MET A 1 507 ? 19.816  -7.586  13.778  1.00 93.20  ? 610  MET A CB    1 
ATOM   3697 C  CG    . MET A 1 507 ? 20.781  -8.428  12.949  1.00 106.34 ? 610  MET A CG    1 
ATOM   3698 S  SD    . MET A 1 507 ? 22.170  -9.110  13.882  1.00 106.27 ? 610  MET A SD    1 
ATOM   3699 C  CE    . MET A 1 507 ? 21.540  -10.727 14.334  1.00 99.47  ? 610  MET A CE    1 
ATOM   3700 N  N     . VAL A 1 508 ? 16.805  -7.109  15.008  1.00 91.14  ? 611  VAL A N     1 
ATOM   3701 C  CA    . VAL A 1 508 ? 15.888  -6.296  15.800  1.00 90.61  ? 611  VAL A CA    1 
ATOM   3702 C  C     . VAL A 1 508 ? 15.304  -7.114  16.945  1.00 86.82  ? 611  VAL A C     1 
ATOM   3703 O  O     . VAL A 1 508 ? 15.207  -6.633  18.081  1.00 85.22  ? 611  VAL A O     1 
ATOM   3704 C  CB    . VAL A 1 508 ? 14.788  -5.705  14.899  1.00 90.93  ? 611  VAL A CB    1 
ATOM   3705 C  CG1   . VAL A 1 508 ? 13.709  -5.040  15.739  1.00 82.31  ? 611  VAL A CG1   1 
ATOM   3706 C  CG2   . VAL A 1 508 ? 15.390  -4.709  13.916  1.00 88.37  ? 611  VAL A CG2   1 
ATOM   3707 N  N     . ARG A 1 509 ? 14.910  -8.362  16.670  1.00 86.06  ? 612  ARG A N     1 
ATOM   3708 C  CA    . ARG A 1 509 ? 14.421  -9.236  17.733  1.00 83.69  ? 612  ARG A CA    1 
ATOM   3709 C  C     . ARG A 1 509 ? 15.487  -9.445  18.801  1.00 90.37  ? 612  ARG A C     1 
ATOM   3710 O  O     . ARG A 1 509 ? 15.188  -9.421  20.001  1.00 82.10  ? 612  ARG A O     1 
ATOM   3711 C  CB    . ARG A 1 509 ? 13.987  -10.586 17.158  1.00 83.34  ? 612  ARG A CB    1 
ATOM   3712 C  CG    . ARG A 1 509 ? 13.338  -10.526 15.788  1.00 88.36  ? 612  ARG A CG    1 
ATOM   3713 C  CD    . ARG A 1 509 ? 11.907  -10.036 15.851  1.00 81.82  ? 612  ARG A CD    1 
ATOM   3714 N  NE    . ARG A 1 509 ? 11.005  -11.046 16.390  1.00 75.06  ? 612  ARG A NE    1 
ATOM   3715 C  CZ    . ARG A 1 509 ? 9.692   -10.898 16.489  1.00 83.02  ? 612  ARG A CZ    1 
ATOM   3716 N  NH1   . ARG A 1 509 ? 9.089   -9.794  16.079  1.00 83.26  ? 612  ARG A NH1   1 
ATOM   3717 N  NH2   . ARG A 1 509 ? 8.965   -11.881 17.011  1.00 89.47  ? 612  ARG A NH2   1 
ATOM   3718 N  N     . GLY A 1 510 ? 16.737  -9.653  18.379  1.00 84.04  ? 613  GLY A N     1 
ATOM   3719 C  CA    . GLY A 1 510 ? 17.812  -9.860  19.334  1.00 86.34  ? 613  GLY A CA    1 
ATOM   3720 C  C     . GLY A 1 510 ? 18.018  -8.683  20.266  1.00 87.64  ? 613  GLY A C     1 
ATOM   3721 O  O     . GLY A 1 510 ? 18.413  -8.863  21.420  1.00 84.47  ? 613  GLY A O     1 
ATOM   3722 N  N     . PHE A 1 511 ? 17.756  -7.467  19.784  1.00 88.73  ? 614  PHE A N     1 
ATOM   3723 C  CA    . PHE A 1 511 ? 17.854  -6.298  20.652  1.00 84.51  ? 614  PHE A CA    1 
ATOM   3724 C  C     . PHE A 1 511 ? 16.733  -6.283  21.683  1.00 86.60  ? 614  PHE A C     1 
ATOM   3725 O  O     . PHE A 1 511 ? 16.965  -5.967  22.855  1.00 92.78  ? 614  PHE A O     1 
ATOM   3726 C  CB    . PHE A 1 511 ? 17.833  -5.019  19.817  1.00 85.99  ? 614  PHE A CB    1 
ATOM   3727 C  CG    . PHE A 1 511 ? 17.765  -3.763  20.637  1.00 86.03  ? 614  PHE A CG    1 
ATOM   3728 C  CD1   . PHE A 1 511 ? 18.904  -3.249  21.235  1.00 93.43  ? 614  PHE A CD1   1 
ATOM   3729 C  CD2   . PHE A 1 511 ? 16.564  -3.094  20.808  1.00 80.00  ? 614  PHE A CD2   1 
ATOM   3730 C  CE1   . PHE A 1 511 ? 18.845  -2.094  21.991  1.00 94.97  ? 614  PHE A CE1   1 
ATOM   3731 C  CE2   . PHE A 1 511 ? 16.499  -1.939  21.561  1.00 85.19  ? 614  PHE A CE2   1 
ATOM   3732 C  CZ    . PHE A 1 511 ? 17.641  -1.437  22.153  1.00 92.19  ? 614  PHE A CZ    1 
ATOM   3733 N  N     . ALA A 1 512 ? 15.511  -6.619  21.265  1.00 83.71  ? 615  ALA A N     1 
ATOM   3734 C  CA    . ALA A 1 512 ? 14.388  -6.625  22.198  1.00 85.70  ? 615  ALA A CA    1 
ATOM   3735 C  C     . ALA A 1 512 ? 14.552  -7.710  23.255  1.00 81.20  ? 615  ALA A C     1 
ATOM   3736 O  O     . ALA A 1 512 ? 14.323  -7.464  24.444  1.00 89.68  ? 615  ALA A O     1 
ATOM   3737 C  CB    . ALA A 1 512 ? 13.076  -6.809  21.437  1.00 89.56  ? 615  ALA A CB    1 
ATOM   3738 N  N     . VAL A 1 513 ? 14.949  -8.916  22.841  1.00 81.97  ? 616  VAL A N     1 
ATOM   3739 C  CA    . VAL A 1 513 ? 15.130  -10.008 23.792  1.00 75.97  ? 616  VAL A CA    1 
ATOM   3740 C  C     . VAL A 1 513 ? 16.286  -9.715  24.740  1.00 87.40  ? 616  VAL A C     1 
ATOM   3741 O  O     . VAL A 1 513 ? 16.237  -10.082 25.922  1.00 92.83  ? 616  VAL A O     1 
ATOM   3742 C  CB    . VAL A 1 513 ? 15.324  -11.335 23.034  1.00 75.62  ? 616  VAL A CB    1 
ATOM   3743 C  CG1   . VAL A 1 513 ? 15.730  -12.450 23.983  1.00 78.94  ? 616  VAL A CG1   1 
ATOM   3744 C  CG2   . VAL A 1 513 ? 14.047  -11.705 22.302  1.00 77.08  ? 616  VAL A CG2   1 
ATOM   3745 N  N     . ARG A 1 514 ? 17.334  -9.043  24.258  1.00 84.43  ? 617  ARG A N     1 
ATOM   3746 C  CA    . ARG A 1 514 ? 18.416  -8.644  25.154  1.00 90.01  ? 617  ARG A CA    1 
ATOM   3747 C  C     . ARG A 1 514 ? 17.951  -7.575  26.136  1.00 96.77  ? 617  ARG A C     1 
ATOM   3748 O  O     . ARG A 1 514 ? 18.372  -7.569  27.299  1.00 93.85  ? 617  ARG A O     1 
ATOM   3749 C  CB    . ARG A 1 514 ? 19.622  -8.159  24.349  1.00 82.43  ? 617  ARG A CB    1 
ATOM   3750 C  CG    . ARG A 1 514 ? 20.606  -9.268  24.005  1.00 87.18  ? 617  ARG A CG    1 
ATOM   3751 C  CD    . ARG A 1 514 ? 21.798  -8.758  23.206  1.00 90.43  ? 617  ARG A CD    1 
ATOM   3752 N  NE    . ARG A 1 514 ? 21.558  -8.792  21.768  1.00 97.59  ? 617  ARG A NE    1 
ATOM   3753 C  CZ    . ARG A 1 514 ? 21.252  -7.732  21.032  1.00 98.35  ? 617  ARG A CZ    1 
ATOM   3754 N  NH1   . ARG A 1 514 ? 21.146  -6.526  21.565  1.00 100.44 ? 617  ARG A NH1   1 
ATOM   3755 N  NH2   . ARG A 1 514 ? 21.049  -7.887  19.726  1.00 93.28  ? 617  ARG A NH2   1 
ATOM   3756 N  N     . CYS A 1 515 ? 17.077  -6.668  25.691  1.00 92.17  ? 618  CYS A N     1 
ATOM   3757 C  CA    . CYS A 1 515 ? 16.508  -5.685  26.607  1.00 90.24  ? 618  CYS A CA    1 
ATOM   3758 C  C     . CYS A 1 515 ? 15.664  -6.351  27.686  1.00 88.36  ? 618  CYS A C     1 
ATOM   3759 O  O     . CYS A 1 515 ? 15.525  -5.809  28.788  1.00 95.97  ? 618  CYS A O     1 
ATOM   3760 C  CB    . CYS A 1 515 ? 15.673  -4.662  25.836  1.00 89.90  ? 618  CYS A CB    1 
ATOM   3761 S  SG    . CYS A 1 515 ? 16.637  -3.452  24.898  1.00 96.32  ? 618  CYS A SG    1 
ATOM   3762 N  N     . LEU A 1 516 ? 15.094  -7.520  27.391  1.00 85.35  ? 619  LEU A N     1 
ATOM   3763 C  CA    . LEU A 1 516 ? 14.315  -8.238  28.391  1.00 88.04  ? 619  LEU A CA    1 
ATOM   3764 C  C     . LEU A 1 516 ? 15.203  -8.984  29.377  1.00 91.84  ? 619  LEU A C     1 
ATOM   3765 O  O     . LEU A 1 516 ? 14.854  -9.094  30.557  1.00 87.75  ? 619  LEU A O     1 
ATOM   3766 C  CB    . LEU A 1 516 ? 13.352  -9.213  27.713  1.00 81.84  ? 619  LEU A CB    1 
ATOM   3767 C  CG    . LEU A 1 516 ? 12.312  -8.593  26.780  1.00 76.08  ? 619  LEU A CG    1 
ATOM   3768 C  CD1   . LEU A 1 516 ? 11.252  -9.616  26.399  1.00 79.56  ? 619  LEU A CD1   1 
ATOM   3769 C  CD2   . LEU A 1 516 ? 11.679  -7.365  27.415  1.00 79.20  ? 619  LEU A CD2   1 
ATOM   3770 N  N     . GLU A 1 517 ? 16.349  -9.494  28.920  1.00 108.01 ? 620  GLU A N     1 
ATOM   3771 C  CA    . GLU A 1 517 ? 17.250  -10.221 29.806  1.00 100.96 ? 620  GLU A CA    1 
ATOM   3772 C  C     . GLU A 1 517 ? 17.881  -9.322  30.861  1.00 103.49 ? 620  GLU A C     1 
ATOM   3773 O  O     . GLU A 1 517 ? 18.373  -9.829  31.874  1.00 115.74 ? 620  GLU A O     1 
ATOM   3774 C  CB    . GLU A 1 517 ? 18.345  -10.911 28.991  1.00 97.65  ? 620  GLU A CB    1 
ATOM   3775 C  CG    . GLU A 1 517 ? 17.831  -12.000 28.068  1.00 101.60 ? 620  GLU A CG    1 
ATOM   3776 C  CD    . GLU A 1 517 ? 18.916  -12.577 27.180  1.00 127.88 ? 620  GLU A CD    1 
ATOM   3777 O  OE1   . GLU A 1 517 ? 20.046  -12.043 27.192  1.00 119.44 ? 620  GLU A OE1   1 
ATOM   3778 O  OE2   . GLU A 1 517 ? 18.637  -13.566 26.469  1.00 136.75 ? 620  GLU A OE2   1 
ATOM   3779 N  N     . LYS A 1 518 ? 17.876  -8.007  30.651  1.00 95.94  ? 621  LYS A N     1 
ATOM   3780 C  CA    . LYS A 1 518 ? 18.467  -7.065  31.592  1.00 97.13  ? 621  LYS A CA    1 
ATOM   3781 C  C     . LYS A 1 518 ? 17.439  -6.399  32.496  1.00 100.14 ? 621  LYS A C     1 
ATOM   3782 O  O     . LYS A 1 518 ? 17.688  -6.241  33.695  1.00 103.00 ? 621  LYS A O     1 
ATOM   3783 C  CB    . LYS A 1 518 ? 19.243  -5.979  30.840  1.00 99.37  ? 621  LYS A CB    1 
ATOM   3784 C  CG    . LYS A 1 518 ? 20.212  -6.501  29.792  1.00 118.90 ? 621  LYS A CG    1 
ATOM   3785 C  CD    . LYS A 1 518 ? 20.700  -5.369  28.896  1.00 136.82 ? 621  LYS A CD    1 
ATOM   3786 C  CE    . LYS A 1 518 ? 21.498  -5.890  27.709  1.00 123.15 ? 621  LYS A CE    1 
ATOM   3787 N  NZ    . LYS A 1 518 ? 22.773  -6.533  28.129  1.00 125.21 ? 621  LYS A NZ    1 
ATOM   3788 N  N     . TYR A 1 519 ? 16.284  -6.007  31.953  1.00 95.96  ? 622  TYR A N     1 
ATOM   3789 C  CA    . TYR A 1 519 ? 15.358  -5.144  32.672  1.00 91.77  ? 622  TYR A CA    1 
ATOM   3790 C  C     . TYR A 1 519 ? 14.039  -5.802  33.051  1.00 85.95  ? 622  TYR A C     1 
ATOM   3791 O  O     . TYR A 1 519 ? 13.387  -5.331  33.987  1.00 89.00  ? 622  TYR A O     1 
ATOM   3792 C  CB    . TYR A 1 519 ? 15.058  -3.884  31.844  1.00 96.66  ? 622  TYR A CB    1 
ATOM   3793 C  CG    . TYR A 1 519 ? 16.269  -3.014  31.580  1.00 98.84  ? 622  TYR A CG    1 
ATOM   3794 C  CD1   . TYR A 1 519 ? 17.402  -3.103  32.380  1.00 99.85  ? 622  TYR A CD1   1 
ATOM   3795 C  CD2   . TYR A 1 519 ? 16.278  -2.100  30.535  1.00 103.08 ? 622  TYR A CD2   1 
ATOM   3796 C  CE1   . TYR A 1 519 ? 18.509  -2.312  32.143  1.00 104.66 ? 622  TYR A CE1   1 
ATOM   3797 C  CE2   . TYR A 1 519 ? 17.382  -1.302  30.292  1.00 108.86 ? 622  TYR A CE2   1 
ATOM   3798 C  CZ    . TYR A 1 519 ? 18.494  -1.413  31.100  1.00 109.17 ? 622  TYR A CZ    1 
ATOM   3799 O  OH    . TYR A 1 519 ? 19.597  -0.625  30.865  1.00 111.54 ? 622  TYR A OH    1 
ATOM   3800 N  N     . LEU A 1 520 ? 13.626  -6.863  32.361  1.00 87.94  ? 623  LEU A N     1 
ATOM   3801 C  CA    . LEU A 1 520 ? 12.329  -7.480  32.623  1.00 85.75  ? 623  LEU A CA    1 
ATOM   3802 C  C     . LEU A 1 520 ? 12.419  -8.334  33.882  1.00 82.94  ? 623  LEU A C     1 
ATOM   3803 O  O     . LEU A 1 520 ? 13.084  -9.375  33.890  1.00 88.43  ? 623  LEU A O     1 
ATOM   3804 C  CB    . LEU A 1 520 ? 11.875  -8.315  31.430  1.00 76.34  ? 623  LEU A CB    1 
ATOM   3805 C  CG    . LEU A 1 520 ? 10.455  -8.876  31.550  1.00 75.22  ? 623  LEU A CG    1 
ATOM   3806 C  CD1   . LEU A 1 520 ? 9.436   -7.749  31.512  1.00 74.28  ? 623  LEU A CD1   1 
ATOM   3807 C  CD2   . LEU A 1 520 ? 10.171  -9.896  30.461  1.00 77.00  ? 623  LEU A CD2   1 
ATOM   3808 N  N     . THR A 1 521 ? 11.746  -7.899  34.943  1.00 76.14  ? 624  THR A N     1 
ATOM   3809 C  CA    . THR A 1 521 ? 11.695  -8.667  36.175  1.00 84.17  ? 624  THR A CA    1 
ATOM   3810 C  C     . THR A 1 521 ? 10.711  -9.824  36.037  1.00 83.38  ? 624  THR A C     1 
ATOM   3811 O  O     . THR A 1 521 ? 9.823   -9.820  35.180  1.00 91.29  ? 624  THR A O     1 
ATOM   3812 C  CB    . THR A 1 521 ? 11.285  -7.780  37.350  1.00 78.27  ? 624  THR A CB    1 
ATOM   3813 O  OG1   . THR A 1 521 ? 9.933   -7.340  37.167  1.00 74.86  ? 624  THR A OG1   1 
ATOM   3814 C  CG2   . THR A 1 521 ? 12.195  -6.566  37.443  1.00 75.39  ? 624  THR A CG2   1 
ATOM   3815 N  N     . ASP A 1 522 ? 10.877  -10.828 36.903  1.00 78.13  ? 625  ASP A N     1 
ATOM   3816 C  CA    . ASP A 1 522 ? 9.953   -11.956 36.910  1.00 73.67  ? 625  ASP A CA    1 
ATOM   3817 C  C     . ASP A 1 522 ? 8.541   -11.532 37.285  1.00 75.33  ? 625  ASP A C     1 
ATOM   3818 O  O     . ASP A 1 522 ? 7.581   -12.235 36.949  1.00 75.43  ? 625  ASP A O     1 
ATOM   3819 C  CB    . ASP A 1 522 ? 10.445  -13.042 37.868  1.00 79.46  ? 625  ASP A CB    1 
ATOM   3820 C  CG    . ASP A 1 522 ? 11.788  -13.615 37.461  1.00 87.33  ? 625  ASP A CG    1 
ATOM   3821 O  OD1   . ASP A 1 522 ? 12.420  -13.056 36.539  1.00 102.85 ? 625  ASP A OD1   1 
ATOM   3822 O  OD2   . ASP A 1 522 ? 12.210  -14.628 38.059  1.00 93.14  ? 625  ASP A OD2   1 
ATOM   3823 N  N     . ASP A 1 523 ? 8.394   -10.401 37.976  1.00 88.33  ? 626  ASP A N     1 
ATOM   3824 C  CA    . ASP A 1 523 ? 7.066   -9.874  38.267  1.00 85.14  ? 626  ASP A CA    1 
ATOM   3825 C  C     . ASP A 1 523 ? 6.379   -9.402  36.992  1.00 87.70  ? 626  ASP A C     1 
ATOM   3826 O  O     . ASP A 1 523 ? 5.227   -9.764  36.725  1.00 93.09  ? 626  ASP A O     1 
ATOM   3827 C  CB    . ASP A 1 523 ? 7.171   -8.737  39.285  1.00 88.59  ? 626  ASP A CB    1 
ATOM   3828 C  CG    . ASP A 1 523 ? 5.897   -7.924  39.387  1.00 95.03  ? 626  ASP A CG    1 
ATOM   3829 O  OD1   . ASP A 1 523 ? 4.809   -8.529  39.484  1.00 94.90  ? 626  ASP A OD1   1 
ATOM   3830 O  OD2   . ASP A 1 523 ? 5.986   -6.677  39.382  1.00 87.65  ? 626  ASP A OD2   1 
ATOM   3831 N  N     . LYS A 1 524 ? 7.077   -8.600  36.185  1.00 87.72  ? 627  LYS A N     1 
ATOM   3832 C  CA    . LYS A 1 524 ? 6.496   -8.117  34.937  1.00 78.11  ? 627  LYS A CA    1 
ATOM   3833 C  C     . LYS A 1 524 ? 6.430   -9.213  33.882  1.00 75.48  ? 627  LYS A C     1 
ATOM   3834 O  O     . LYS A 1 524 ? 5.538   -9.190  33.026  1.00 80.79  ? 627  LYS A O     1 
ATOM   3835 C  CB    . LYS A 1 524 ? 7.293   -6.925  34.411  1.00 83.09  ? 627  LYS A CB    1 
ATOM   3836 C  CG    . LYS A 1 524 ? 7.113   -5.650  35.216  1.00 86.29  ? 627  LYS A CG    1 
ATOM   3837 C  CD    . LYS A 1 524 ? 5.677   -5.162  35.154  1.00 93.16  ? 627  LYS A CD    1 
ATOM   3838 C  CE    . LYS A 1 524 ? 5.536   -3.788  35.786  1.00 117.34 ? 627  LYS A CE    1 
ATOM   3839 N  NZ    . LYS A 1 524 ? 6.386   -2.778  35.095  1.00 121.87 ? 627  LYS A NZ    1 
ATOM   3840 N  N     . LEU A 1 525 ? 7.360   -10.172 33.919  1.00 69.67  ? 628  LEU A N     1 
ATOM   3841 C  CA    . LEU A 1 525 ? 7.331   -11.260 32.947  1.00 71.84  ? 628  LEU A CA    1 
ATOM   3842 C  C     . LEU A 1 525 ? 6.048   -12.070 33.071  1.00 72.06  ? 628  LEU A C     1 
ATOM   3843 O  O     . LEU A 1 525 ? 5.430   -12.427 32.061  1.00 76.00  ? 628  LEU A O     1 
ATOM   3844 C  CB    . LEU A 1 525 ? 8.559   -12.157 33.120  1.00 70.06  ? 628  LEU A CB    1 
ATOM   3845 C  CG    . LEU A 1 525 ? 8.970   -13.048 31.940  1.00 77.60  ? 628  LEU A CG    1 
ATOM   3846 C  CD1   . LEU A 1 525 ? 10.446  -13.392 32.034  1.00 84.37  ? 628  LEU A CD1   1 
ATOM   3847 C  CD2   . LEU A 1 525 ? 8.142   -14.325 31.865  1.00 74.37  ? 628  LEU A CD2   1 
ATOM   3848 N  N     . SER A 1 526 ? 5.627   -12.367 34.302  1.00 74.27  ? 629  SER A N     1 
ATOM   3849 C  CA    . SER A 1 526 ? 4.370   -13.079 34.498  1.00 70.90  ? 629  SER A CA    1 
ATOM   3850 C  C     . SER A 1 526 ? 3.162   -12.214 34.168  1.00 62.86  ? 629  SER A C     1 
ATOM   3851 O  O     . SER A 1 526 ? 2.076   -12.753 33.932  1.00 57.52  ? 629  SER A O     1 
ATOM   3852 C  CB    . SER A 1 526 ? 4.270   -13.591 35.935  1.00 66.98  ? 629  SER A CB    1 
ATOM   3853 O  OG    . SER A 1 526 ? 4.410   -12.531 36.864  1.00 90.43  ? 629  SER A OG    1 
ATOM   3854 N  N     . GLN A 1 527 ? 3.323   -10.890 34.147  1.00 62.71  ? 630  GLN A N     1 
ATOM   3855 C  CA    . GLN A 1 527 ? 2.211   -10.014 33.800  1.00 69.82  ? 630  GLN A CA    1 
ATOM   3856 C  C     . GLN A 1 527 ? 1.975   -9.984  32.294  1.00 74.65  ? 630  GLN A C     1 
ATOM   3857 O  O     . GLN A 1 527 ? 0.824   -9.976  31.843  1.00 67.30  ? 630  GLN A O     1 
ATOM   3858 C  CB    . GLN A 1 527 ? 2.470   -8.602  34.329  1.00 72.49  ? 630  GLN A CB    1 
ATOM   3859 C  CG    . GLN A 1 527 ? 1.327   -7.627  34.094  1.00 74.31  ? 630  GLN A CG    1 
ATOM   3860 C  CD    . GLN A 1 527 ? 0.051   -8.040  34.808  1.00 89.35  ? 630  GLN A CD    1 
ATOM   3861 O  OE1   . GLN A 1 527 ? -0.098  -7.825  36.012  1.00 96.98  ? 630  GLN A OE1   1 
ATOM   3862 N  NE2   . GLN A 1 527 ? -0.876  -8.637  34.068  1.00 84.03  ? 630  GLN A NE2   1 
ATOM   3863 N  N     . TYR A 1 528 ? 3.051   -9.973  31.506  1.00 76.71  ? 631  TYR A N     1 
ATOM   3864 C  CA    . TYR A 1 528 ? 2.971   -9.938  30.052  1.00 81.32  ? 631  TYR A CA    1 
ATOM   3865 C  C     . TYR A 1 528 ? 3.221   -11.303 29.420  1.00 72.96  ? 631  TYR A C     1 
ATOM   3866 O  O     . TYR A 1 528 ? 3.476   -11.379 28.214  1.00 82.90  ? 631  TYR A O     1 
ATOM   3867 C  CB    . TYR A 1 528 ? 3.967   -8.919  29.495  1.00 77.15  ? 631  TYR A CB    1 
ATOM   3868 C  CG    . TYR A 1 528 ? 3.833   -7.530  30.073  1.00 76.32  ? 631  TYR A CG    1 
ATOM   3869 C  CD1   . TYR A 1 528 ? 2.592   -6.919  30.187  1.00 77.26  ? 631  TYR A CD1   1 
ATOM   3870 C  CD2   . TYR A 1 528 ? 4.951   -6.830  30.511  1.00 77.95  ? 631  TYR A CD2   1 
ATOM   3871 C  CE1   . TYR A 1 528 ? 2.469   -5.648  30.715  1.00 79.41  ? 631  TYR A CE1   1 
ATOM   3872 C  CE2   . TYR A 1 528 ? 4.838   -5.560  31.041  1.00 81.72  ? 631  TYR A CE2   1 
ATOM   3873 C  CZ    . TYR A 1 528 ? 3.594   -4.973  31.141  1.00 88.88  ? 631  TYR A CZ    1 
ATOM   3874 O  OH    . TYR A 1 528 ? 3.474   -3.708  31.669  1.00 96.63  ? 631  TYR A OH    1 
ATOM   3875 N  N     . LEU A 1 529 ? 3.155   -12.380 30.208  1.00 72.34  ? 632  LEU A N     1 
ATOM   3876 C  CA    . LEU A 1 529 ? 3.505   -13.699 29.690  1.00 73.98  ? 632  LEU A CA    1 
ATOM   3877 C  C     . LEU A 1 529 ? 2.586   -14.129 28.554  1.00 80.71  ? 632  LEU A C     1 
ATOM   3878 O  O     . LEU A 1 529 ? 3.034   -14.800 27.617  1.00 84.76  ? 632  LEU A O     1 
ATOM   3879 C  CB    . LEU A 1 529 ? 3.470   -14.735 30.815  1.00 67.66  ? 632  LEU A CB    1 
ATOM   3880 C  CG    . LEU A 1 529 ? 3.925   -16.147 30.435  1.00 63.83  ? 632  LEU A CG    1 
ATOM   3881 C  CD1   . LEU A 1 529 ? 5.415   -16.168 30.148  1.00 64.80  ? 632  LEU A CD1   1 
ATOM   3882 C  CD2   . LEU A 1 529 ? 3.570   -17.151 31.521  1.00 79.30  ? 632  LEU A CD2   1 
ATOM   3883 N  N     . ILE A 1 530 ? 1.307   -13.752 28.611  1.00 81.69  ? 633  ILE A N     1 
ATOM   3884 C  CA    . ILE A 1 530 ? 0.377   -14.165 27.564  1.00 78.18  ? 633  ILE A CA    1 
ATOM   3885 C  C     . ILE A 1 530 ? 0.738   -13.513 26.233  1.00 84.68  ? 633  ILE A C     1 
ATOM   3886 O  O     . ILE A 1 530 ? 0.570   -14.125 25.171  1.00 94.03  ? 633  ILE A O     1 
ATOM   3887 C  CB    . ILE A 1 530 ? -1.073  -13.857 27.986  1.00 78.30  ? 633  ILE A CB    1 
ATOM   3888 C  CG1   . ILE A 1 530 ? -2.062  -14.370 26.937  1.00 87.79  ? 633  ILE A CG1   1 
ATOM   3889 C  CG2   . ILE A 1 530 ? -1.265  -12.370 28.225  1.00 79.94  ? 633  ILE A CG2   1 
ATOM   3890 C  CD1   . ILE A 1 530 ? -2.032  -15.872 26.755  1.00 100.97 ? 633  ILE A CD1   1 
ATOM   3891 N  N     . GLN A 1 531 ? 1.255   -12.282 26.260  1.00 82.04  ? 634  GLN A N     1 
ATOM   3892 C  CA    . GLN A 1 531 ? 1.695   -11.643 25.023  1.00 80.05  ? 634  GLN A CA    1 
ATOM   3893 C  C     . GLN A 1 531 ? 3.012   -12.232 24.534  1.00 84.28  ? 634  GLN A C     1 
ATOM   3894 O  O     . GLN A 1 531 ? 3.185   -12.463 23.332  1.00 89.83  ? 634  GLN A O     1 
ATOM   3895 C  CB    . GLN A 1 531 ? 1.833   -10.134 25.219  1.00 77.43  ? 634  GLN A CB    1 
ATOM   3896 C  CG    . GLN A 1 531 ? 0.522   -9.372  25.167  1.00 83.59  ? 634  GLN A CG    1 
ATOM   3897 C  CD    . GLN A 1 531 ? -0.220  -9.401  26.485  1.00 84.06  ? 634  GLN A CD    1 
ATOM   3898 O  OE1   . GLN A 1 531 ? 0.363   -9.681  27.533  1.00 83.75  ? 634  GLN A OE1   1 
ATOM   3899 N  NE2   . GLN A 1 531 ? -1.515  -9.108  26.440  1.00 80.60  ? 634  GLN A NE2   1 
ATOM   3900 N  N     . LEU A 1 532 ? 3.954   -12.475 25.450  1.00 77.77  ? 635  LEU A N     1 
ATOM   3901 C  CA    . LEU A 1 532 ? 5.254   -13.005 25.054  1.00 84.35  ? 635  LEU A CA    1 
ATOM   3902 C  C     . LEU A 1 532 ? 5.140   -14.400 24.454  1.00 86.61  ? 635  LEU A C     1 
ATOM   3903 O  O     . LEU A 1 532 ? 5.998   -14.807 23.662  1.00 92.80  ? 635  LEU A O     1 
ATOM   3904 C  CB    . LEU A 1 532 ? 6.200   -13.018 26.254  1.00 82.84  ? 635  LEU A CB    1 
ATOM   3905 C  CG    . LEU A 1 532 ? 6.610   -11.644 26.783  1.00 82.61  ? 635  LEU A CG    1 
ATOM   3906 C  CD1   . LEU A 1 532 ? 7.367   -11.781 28.091  1.00 86.68  ? 635  LEU A CD1   1 
ATOM   3907 C  CD2   . LEU A 1 532 ? 7.449   -10.906 25.749  1.00 91.59  ? 635  LEU A CD2   1 
ATOM   3908 N  N     . VAL A 1 533 ? 4.097   -15.147 24.817  1.00 89.08  ? 636  VAL A N     1 
ATOM   3909 C  CA    . VAL A 1 533 ? 3.895   -16.465 24.228  1.00 84.01  ? 636  VAL A CA    1 
ATOM   3910 C  C     . VAL A 1 533 ? 3.210   -16.352 22.870  1.00 88.45  ? 636  VAL A C     1 
ATOM   3911 O  O     . VAL A 1 533 ? 3.453   -17.173 21.976  1.00 98.07  ? 636  VAL A O     1 
ATOM   3912 C  CB    . VAL A 1 533 ? 3.106   -17.357 25.203  1.00 81.67  ? 636  VAL A CB    1 
ATOM   3913 C  CG1   . VAL A 1 533 ? 2.675   -18.652 24.535  1.00 77.65  ? 636  VAL A CG1   1 
ATOM   3914 C  CG2   . VAL A 1 533 ? 3.948   -17.654 26.431  1.00 77.22  ? 636  VAL A CG2   1 
ATOM   3915 N  N     . GLN A 1 534 ? 2.373   -15.330 22.676  1.00 85.54  ? 637  GLN A N     1 
ATOM   3916 C  CA    . GLN A 1 534 ? 1.698   -15.169 21.392  1.00 85.66  ? 637  GLN A CA    1 
ATOM   3917 C  C     . GLN A 1 534 ? 2.671   -14.741 20.298  1.00 89.73  ? 637  GLN A C     1 
ATOM   3918 O  O     . GLN A 1 534 ? 2.591   -15.232 19.166  1.00 87.76  ? 637  GLN A O     1 
ATOM   3919 C  CB    . GLN A 1 534 ? 0.553   -14.167 21.523  1.00 80.97  ? 637  GLN A CB    1 
ATOM   3920 C  CG    . GLN A 1 534 ? -0.646  -14.719 22.269  1.00 88.83  ? 637  GLN A CG    1 
ATOM   3921 C  CD    . GLN A 1 534 ? -1.160  -16.008 21.658  1.00 93.79  ? 637  GLN A CD    1 
ATOM   3922 O  OE1   . GLN A 1 534 ? -1.588  -16.035 20.505  1.00 102.44 ? 637  GLN A OE1   1 
ATOM   3923 N  NE2   . GLN A 1 534 ? -1.115  -17.087 22.429  1.00 91.29  ? 637  GLN A NE2   1 
ATOM   3924 N  N     . VAL A 1 535 ? 3.602   -13.836 20.614  1.00 87.04  ? 638  VAL A N     1 
ATOM   3925 C  CA    . VAL A 1 535 ? 4.581   -13.397 19.624  1.00 83.21  ? 638  VAL A CA    1 
ATOM   3926 C  C     . VAL A 1 535 ? 5.585   -14.481 19.275  1.00 85.63  ? 638  VAL A C     1 
ATOM   3927 O  O     . VAL A 1 535 ? 6.413   -14.278 18.380  1.00 89.37  ? 638  VAL A O     1 
ATOM   3928 C  CB    . VAL A 1 535 ? 5.332   -12.136 20.094  1.00 83.21  ? 638  VAL A CB    1 
ATOM   3929 C  CG1   . VAL A 1 535 ? 4.392   -10.947 20.116  1.00 84.43  ? 638  VAL A CG1   1 
ATOM   3930 C  CG2   . VAL A 1 535 ? 5.957   -12.362 21.459  1.00 88.41  ? 638  VAL A CG2   1 
ATOM   3931 N  N     . LEU A 1 536 ? 5.543   -15.623 19.964  1.00 81.53  ? 639  LEU A N     1 
ATOM   3932 C  CA    . LEU A 1 536 ? 6.306   -16.779 19.512  1.00 84.57  ? 639  LEU A CA    1 
ATOM   3933 C  C     . LEU A 1 536 ? 5.791   -17.307 18.180  1.00 90.22  ? 639  LEU A C     1 
ATOM   3934 O  O     . LEU A 1 536 ? 6.540   -17.971 17.457  1.00 87.56  ? 639  LEU A O     1 
ATOM   3935 C  CB    . LEU A 1 536 ? 6.268   -17.885 20.567  1.00 85.68  ? 639  LEU A CB    1 
ATOM   3936 C  CG    . LEU A 1 536 ? 6.993   -17.602 21.883  1.00 87.36  ? 639  LEU A CG    1 
ATOM   3937 C  CD1   . LEU A 1 536 ? 6.890   -18.802 22.805  1.00 81.85  ? 639  LEU A CD1   1 
ATOM   3938 C  CD2   . LEU A 1 536 ? 8.449   -17.243 21.628  1.00 84.83  ? 639  LEU A CD2   1 
ATOM   3939 N  N     . LYS A 1 537 ? 4.532   -17.019 17.841  1.00 90.04  ? 640  LYS A N     1 
ATOM   3940 C  CA    . LYS A 1 537 ? 4.006   -17.397 16.534  1.00 90.74  ? 640  LYS A CA    1 
ATOM   3941 C  C     . LYS A 1 537 ? 4.566   -16.512 15.427  1.00 89.06  ? 640  LYS A C     1 
ATOM   3942 O  O     . LYS A 1 537 ? 4.704   -16.965 14.285  1.00 92.92  ? 640  LYS A O     1 
ATOM   3943 C  CB    . LYS A 1 537 ? 2.481   -17.326 16.547  1.00 91.32  ? 640  LYS A CB    1 
ATOM   3944 C  CG    . LYS A 1 537 ? 1.829   -18.071 17.698  1.00 86.87  ? 640  LYS A CG    1 
ATOM   3945 C  CD    . LYS A 1 537 ? 0.326   -17.855 17.691  1.00 95.69  ? 640  LYS A CD    1 
ATOM   3946 C  CE    . LYS A 1 537 ? -0.361  -18.632 18.797  1.00 87.24  ? 640  LYS A CE    1 
ATOM   3947 N  NZ    . LYS A 1 537 ? -1.839  -18.483 18.714  1.00 92.75  ? 640  LYS A NZ    1 
ATOM   3948 N  N     . TYR A 1 538 ? 4.887   -15.255 15.741  1.00 86.82  ? 641  TYR A N     1 
ATOM   3949 C  CA    . TYR A 1 538 ? 5.456   -14.342 14.757  1.00 89.35  ? 641  TYR A CA    1 
ATOM   3950 C  C     . TYR A 1 538 ? 6.897   -14.681 14.398  1.00 87.47  ? 641  TYR A C     1 
ATOM   3951 O  O     . TYR A 1 538 ? 7.437   -14.084 13.461  1.00 88.45  ? 641  TYR A O     1 
ATOM   3952 C  CB    . TYR A 1 538 ? 5.400   -12.900 15.268  1.00 91.88  ? 641  TYR A CB    1 
ATOM   3953 C  CG    . TYR A 1 538 ? 4.009   -12.356 15.510  1.00 98.05  ? 641  TYR A CG    1 
ATOM   3954 C  CD1   . TYR A 1 538 ? 2.914   -12.837 14.803  1.00 102.88 ? 641  TYR A CD1   1 
ATOM   3955 C  CD2   . TYR A 1 538 ? 3.795   -11.352 16.447  1.00 101.29 ? 641  TYR A CD2   1 
ATOM   3956 C  CE1   . TYR A 1 538 ? 1.643   -12.332 15.026  1.00 114.98 ? 641  TYR A CE1   1 
ATOM   3957 C  CE2   . TYR A 1 538 ? 2.531   -10.843 16.676  1.00 97.74  ? 641  TYR A CE2   1 
ATOM   3958 C  CZ    . TYR A 1 538 ? 1.460   -11.336 15.965  1.00 107.62 ? 641  TYR A CZ    1 
ATOM   3959 O  OH    . TYR A 1 538 ? 0.203   -10.827 16.197  1.00 109.20 ? 641  TYR A OH    1 
ATOM   3960 N  N     . GLU A 1 539 ? 7.531   -15.604 15.117  1.00 86.61  ? 642  GLU A N     1 
ATOM   3961 C  CA    . GLU A 1 539 ? 8.924   -15.933 14.847  1.00 92.89  ? 642  GLU A CA    1 
ATOM   3962 C  C     . GLU A 1 539 ? 9.045   -16.718 13.547  1.00 82.99  ? 642  GLU A C     1 
ATOM   3963 O  O     . GLU A 1 539 ? 8.278   -17.652 13.296  1.00 76.72  ? 642  GLU A O     1 
ATOM   3964 C  CB    . GLU A 1 539 ? 9.517   -16.729 16.010  1.00 88.21  ? 642  GLU A CB    1 
ATOM   3965 C  CG    . GLU A 1 539 ? 9.730   -15.910 17.272  1.00 87.97  ? 642  GLU A CG    1 
ATOM   3966 C  CD    . GLU A 1 539 ? 10.742  -14.796 17.079  1.00 89.97  ? 642  GLU A CD    1 
ATOM   3967 O  OE1   . GLU A 1 539 ? 11.676  -14.969 16.268  1.00 92.10  ? 642  GLU A OE1   1 
ATOM   3968 O  OE2   . GLU A 1 539 ? 10.601  -13.743 17.737  1.00 97.94  ? 642  GLU A OE2   1 
ATOM   3969 N  N     . GLN A 1 540 ? 10.020  -16.334 12.719  1.00 84.01  ? 643  GLN A N     1 
ATOM   3970 C  CA    . GLN A 1 540 ? 10.186  -16.969 11.416  1.00 86.08  ? 643  GLN A CA    1 
ATOM   3971 C  C     . GLN A 1 540 ? 10.639  -18.418 11.537  1.00 84.96  ? 643  GLN A C     1 
ATOM   3972 O  O     . GLN A 1 540 ? 10.322  -19.236 10.667  1.00 77.60  ? 643  GLN A O     1 
ATOM   3973 C  CB    . GLN A 1 540 ? 11.186  -16.179 10.570  1.00 81.80  ? 643  GLN A CB    1 
ATOM   3974 C  CG    . GLN A 1 540 ? 10.574  -15.485 9.365   1.00 97.52  ? 643  GLN A CG    1 
ATOM   3975 C  CD    . GLN A 1 540 ? 11.619  -14.861 8.459   1.00 95.05  ? 643  GLN A CD    1 
ATOM   3976 O  OE1   . GLN A 1 540 ? 12.687  -14.447 8.915   1.00 89.04  ? 643  GLN A OE1   1 
ATOM   3977 N  NE2   . GLN A 1 540 ? 11.320  -14.797 7.166   1.00 92.41  ? 643  GLN A NE2   1 
ATOM   3978 N  N     . TYR A 1 541 ? 11.373  -18.756 12.594  1.00 91.26  ? 644  TYR A N     1 
ATOM   3979 C  CA    . TYR A 1 541 ? 11.941  -20.086 12.752  1.00 87.76  ? 644  TYR A CA    1 
ATOM   3980 C  C     . TYR A 1 541 ? 11.690  -20.592 14.167  1.00 85.46  ? 644  TYR A C     1 
ATOM   3981 O  O     . TYR A 1 541 ? 11.272  -19.846 15.057  1.00 90.36  ? 644  TYR A O     1 
ATOM   3982 C  CB    . TYR A 1 541 ? 13.445  -20.089 12.445  1.00 87.94  ? 644  TYR A CB    1 
ATOM   3983 C  CG    . TYR A 1 541 ? 13.811  -19.334 11.188  1.00 89.53  ? 644  TYR A CG    1 
ATOM   3984 C  CD1   . TYR A 1 541 ? 13.465  -19.824 9.935   1.00 95.14  ? 644  TYR A CD1   1 
ATOM   3985 C  CD2   . TYR A 1 541 ? 14.505  -18.133 11.253  1.00 83.27  ? 644  TYR A CD2   1 
ATOM   3986 C  CE1   . TYR A 1 541 ? 13.795  -19.138 8.784   1.00 89.73  ? 644  TYR A CE1   1 
ATOM   3987 C  CE2   . TYR A 1 541 ? 14.842  -17.440 10.108  1.00 91.46  ? 644  TYR A CE2   1 
ATOM   3988 C  CZ    . TYR A 1 541 ? 14.485  -17.948 8.875   1.00 92.10  ? 644  TYR A CZ    1 
ATOM   3989 O  OH    . TYR A 1 541 ? 14.818  -17.262 7.729   1.00 77.73  ? 644  TYR A OH    1 
ATOM   3990 N  N     . LEU A 1 542 ? 11.955  -21.884 14.366  1.00 80.97  ? 645  LEU A N     1 
ATOM   3991 C  CA    . LEU A 1 542 ? 11.763  -22.487 15.681  1.00 84.90  ? 645  LEU A CA    1 
ATOM   3992 C  C     . LEU A 1 542 ? 12.817  -22.001 16.669  1.00 91.95  ? 645  LEU A C     1 
ATOM   3993 O  O     . LEU A 1 542 ? 12.496  -21.631 17.805  1.00 86.66  ? 645  LEU A O     1 
ATOM   3994 C  CB    . LEU A 1 542 ? 11.797  -24.012 15.570  1.00 80.94  ? 645  LEU A CB    1 
ATOM   3995 C  CG    . LEU A 1 542 ? 10.679  -24.686 14.775  1.00 80.94  ? 645  LEU A CG    1 
ATOM   3996 C  CD1   . LEU A 1 542 ? 10.825  -26.199 14.838  1.00 78.80  ? 645  LEU A CD1   1 
ATOM   3997 C  CD2   . LEU A 1 542 ? 9.317   -24.251 15.290  1.00 79.68  ? 645  LEU A CD2   1 
ATOM   3998 N  N     . ASP A 1 543 ? 14.081  -21.998 16.256  1.00 93.02  ? 646  ASP A N     1 
ATOM   3999 C  CA    . ASP A 1 543 ? 15.190  -21.617 17.128  1.00 84.05  ? 646  ASP A CA    1 
ATOM   4000 C  C     . ASP A 1 543 ? 15.430  -20.120 16.974  1.00 87.26  ? 646  ASP A C     1 
ATOM   4001 O  O     . ASP A 1 543 ? 15.996  -19.666 15.976  1.00 87.94  ? 646  ASP A O     1 
ATOM   4002 C  CB    . ASP A 1 543 ? 16.439  -22.424 16.790  1.00 83.55  ? 646  ASP A CB    1 
ATOM   4003 C  CG    . ASP A 1 543 ? 17.529  -22.292 17.840  1.00 86.85  ? 646  ASP A CG    1 
ATOM   4004 O  OD1   . ASP A 1 543 ? 17.520  -21.305 18.606  1.00 84.09  ? 646  ASP A OD1   1 
ATOM   4005 O  OD2   . ASP A 1 543 ? 18.403  -23.182 17.895  1.00 97.05  ? 646  ASP A OD2   1 
ATOM   4006 N  N     . ASN A 1 544 ? 14.998  -19.350 17.969  1.00 88.54  ? 647  ASN A N     1 
ATOM   4007 C  CA    . ASN A 1 544 ? 15.260  -17.921 18.028  1.00 84.76  ? 647  ASN A CA    1 
ATOM   4008 C  C     . ASN A 1 544 ? 15.638  -17.563 19.459  1.00 90.10  ? 647  ASN A C     1 
ATOM   4009 O  O     . ASN A 1 544 ? 15.645  -18.415 20.354  1.00 92.96  ? 647  ASN A O     1 
ATOM   4010 C  CB    . ASN A 1 544 ? 14.052  -17.112 17.543  1.00 81.33  ? 647  ASN A CB    1 
ATOM   4011 C  CG    . ASN A 1 544 ? 12.785  -17.456 18.291  1.00 85.21  ? 647  ASN A CG    1 
ATOM   4012 O  OD1   . ASN A 1 544 ? 12.500  -16.889 19.345  1.00 93.97  ? 647  ASN A OD1   1 
ATOM   4013 N  ND2   . ASN A 1 544 ? 12.012  -18.391 17.749  1.00 90.76  ? 647  ASN A ND2   1 
ATOM   4014 N  N     . LEU A 1 545 ? 15.959  -16.288 19.678  1.00 89.57  ? 648  LEU A N     1 
ATOM   4015 C  CA    . LEU A 1 545 ? 16.388  -15.847 20.998  1.00 75.02  ? 648  LEU A CA    1 
ATOM   4016 C  C     . LEU A 1 545 ? 15.225  -15.627 21.956  1.00 81.62  ? 648  LEU A C     1 
ATOM   4017 O  O     . LEU A 1 545 ? 15.429  -15.676 23.174  1.00 84.63  ? 648  LEU A O     1 
ATOM   4018 C  CB    . LEU A 1 545 ? 17.212  -14.565 20.880  1.00 74.27  ? 648  LEU A CB    1 
ATOM   4019 C  CG    . LEU A 1 545 ? 18.519  -14.702 20.098  1.00 75.80  ? 648  LEU A CG    1 
ATOM   4020 C  CD1   . LEU A 1 545 ? 19.310  -13.405 20.134  1.00 80.52  ? 648  LEU A CD1   1 
ATOM   4021 C  CD2   . LEU A 1 545 ? 19.350  -15.859 20.634  1.00 70.83  ? 648  LEU A CD2   1 
ATOM   4022 N  N     . LEU A 1 546 ? 14.017  -15.388 21.444  1.00 81.55  ? 649  LEU A N     1 
ATOM   4023 C  CA    . LEU A 1 546 ? 12.876  -15.185 22.331  1.00 84.20  ? 649  LEU A CA    1 
ATOM   4024 C  C     . LEU A 1 546 ? 12.422  -16.497 22.960  1.00 84.59  ? 649  LEU A C     1 
ATOM   4025 O  O     . LEU A 1 546 ? 12.004  -16.520 24.123  1.00 92.19  ? 649  LEU A O     1 
ATOM   4026 C  CB    . LEU A 1 546 ? 11.724  -14.529 21.570  1.00 82.54  ? 649  LEU A CB    1 
ATOM   4027 C  CG    . LEU A 1 546 ? 10.454  -14.269 22.383  1.00 91.72  ? 649  LEU A CG    1 
ATOM   4028 C  CD1   . LEU A 1 546 ? 10.759  -13.410 23.602  1.00 84.28  ? 649  LEU A CD1   1 
ATOM   4029 C  CD2   . LEU A 1 546 ? 9.386   -13.620 21.521  1.00 89.70  ? 649  LEU A CD2   1 
ATOM   4030 N  N     . VAL A 1 547 ? 12.499  -17.599 22.211  1.00 81.36  ? 650  VAL A N     1 
ATOM   4031 C  CA    . VAL A 1 547 ? 12.065  -18.880 22.756  1.00 79.16  ? 650  VAL A CA    1 
ATOM   4032 C  C     . VAL A 1 547 ? 13.079  -19.409 23.764  1.00 79.43  ? 650  VAL A C     1 
ATOM   4033 O  O     . VAL A 1 547 ? 12.708  -20.092 24.727  1.00 79.40  ? 650  VAL A O     1 
ATOM   4034 C  CB    . VAL A 1 547 ? 11.804  -19.887 21.618  1.00 67.03  ? 650  VAL A CB    1 
ATOM   4035 C  CG1   . VAL A 1 547 ? 13.107  -20.341 20.971  1.00 78.04  ? 650  VAL A CG1   1 
ATOM   4036 C  CG2   . VAL A 1 547 ? 11.012  -21.074 22.129  1.00 64.25  ? 650  VAL A CG2   1 
ATOM   4037 N  N     . ARG A 1 548 ? 14.364  -19.097 23.579  1.00 73.68  ? 651  ARG A N     1 
ATOM   4038 C  CA    . ARG A 1 548 ? 15.366  -19.507 24.556  1.00 77.56  ? 651  ARG A CA    1 
ATOM   4039 C  C     . ARG A 1 548 ? 15.298  -18.649 25.812  1.00 82.87  ? 651  ARG A C     1 
ATOM   4040 O  O     . ARG A 1 548 ? 15.687  -19.102 26.895  1.00 80.42  ? 651  ARG A O     1 
ATOM   4041 C  CB    . ARG A 1 548 ? 16.764  -19.442 23.940  1.00 77.60  ? 651  ARG A CB    1 
ATOM   4042 C  CG    . ARG A 1 548 ? 17.000  -20.458 22.834  1.00 84.17  ? 651  ARG A CG    1 
ATOM   4043 C  CD    . ARG A 1 548 ? 18.394  -20.325 22.245  1.00 86.72  ? 651  ARG A CD    1 
ATOM   4044 N  NE    . ARG A 1 548 ? 18.639  -21.309 21.198  1.00 88.97  ? 651  ARG A NE    1 
ATOM   4045 C  CZ    . ARG A 1 548 ? 19.226  -22.482 21.392  1.00 89.46  ? 651  ARG A CZ    1 
ATOM   4046 N  NH1   . ARG A 1 548 ? 19.659  -22.849 22.587  1.00 92.10  ? 651  ARG A NH1   1 
ATOM   4047 N  NH2   . ARG A 1 548 ? 19.385  -23.308 20.362  1.00 100.92 ? 651  ARG A NH2   1 
ATOM   4048 N  N     . PHE A 1 549 ? 14.808  -17.415 25.686  1.00 81.89  ? 652  PHE A N     1 
ATOM   4049 C  CA    . PHE A 1 549 ? 14.658  -16.545 26.847  1.00 76.41  ? 652  PHE A CA    1 
ATOM   4050 C  C     . PHE A 1 549 ? 13.475  -16.976 27.704  1.00 84.18  ? 652  PHE A C     1 
ATOM   4051 O  O     . PHE A 1 549 ? 13.585  -17.061 28.933  1.00 84.32  ? 652  PHE A O     1 
ATOM   4052 C  CB    . PHE A 1 549 ? 14.501  -15.096 26.386  1.00 79.67  ? 652  PHE A CB    1 
ATOM   4053 C  CG    . PHE A 1 549 ? 14.003  -14.166 27.452  1.00 80.62  ? 652  PHE A CG    1 
ATOM   4054 C  CD1   . PHE A 1 549 ? 14.847  -13.731 28.458  1.00 82.40  ? 652  PHE A CD1   1 
ATOM   4055 C  CD2   . PHE A 1 549 ? 12.694  -13.712 27.436  1.00 80.88  ? 652  PHE A CD2   1 
ATOM   4056 C  CE1   . PHE A 1 549 ? 14.394  -12.868 29.436  1.00 81.76  ? 652  PHE A CE1   1 
ATOM   4057 C  CE2   . PHE A 1 549 ? 12.234  -12.850 28.410  1.00 82.06  ? 652  PHE A CE2   1 
ATOM   4058 C  CZ    . PHE A 1 549 ? 13.085  -12.427 29.413  1.00 85.64  ? 652  PHE A CZ    1 
ATOM   4059 N  N     . LEU A 1 550 ? 12.335  -17.262 27.070  1.00 81.88  ? 653  LEU A N     1 
ATOM   4060 C  CA    . LEU A 1 550 ? 11.155  -17.682 27.819  1.00 76.63  ? 653  LEU A CA    1 
ATOM   4061 C  C     . LEU A 1 550 ? 11.349  -19.061 28.438  1.00 76.04  ? 653  LEU A C     1 
ATOM   4062 O  O     . LEU A 1 550 ? 10.900  -19.310 29.562  1.00 78.89  ? 653  LEU A O     1 
ATOM   4063 C  CB    . LEU A 1 550 ? 9.926   -17.672 26.911  1.00 81.71  ? 653  LEU A CB    1 
ATOM   4064 C  CG    . LEU A 1 550 ? 9.558   -16.322 26.294  1.00 85.52  ? 653  LEU A CG    1 
ATOM   4065 C  CD1   . LEU A 1 550 ? 8.314   -16.444 25.429  1.00 76.03  ? 653  LEU A CD1   1 
ATOM   4066 C  CD2   . LEU A 1 550 ? 9.365   -15.276 27.380  1.00 84.03  ? 653  LEU A CD2   1 
ATOM   4067 N  N     . LEU A 1 551 ? 12.016  -19.969 27.723  1.00 78.83  ? 654  LEU A N     1 
ATOM   4068 C  CA    . LEU A 1 551 ? 12.202  -21.319 28.243  1.00 76.52  ? 654  LEU A CA    1 
ATOM   4069 C  C     . LEU A 1 551 ? 13.125  -21.325 29.456  1.00 86.82  ? 654  LEU A C     1 
ATOM   4070 O  O     . LEU A 1 551 ? 12.858  -22.024 30.441  1.00 82.84  ? 654  LEU A O     1 
ATOM   4071 C  CB    . LEU A 1 551 ? 12.748  -22.236 27.148  1.00 66.15  ? 654  LEU A CB    1 
ATOM   4072 C  CG    . LEU A 1 551 ? 12.873  -23.716 27.518  1.00 68.50  ? 654  LEU A CG    1 
ATOM   4073 C  CD1   . LEU A 1 551 ? 11.510  -24.311 27.841  1.00 76.16  ? 654  LEU A CD1   1 
ATOM   4074 C  CD2   . LEU A 1 551 ? 13.552  -24.496 26.407  1.00 72.44  ? 654  LEU A CD2   1 
ATOM   4075 N  N     . LYS A 1 552 ? 14.215  -20.552 29.407  1.00 81.11  ? 655  LYS A N     1 
ATOM   4076 C  CA    . LYS A 1 552 ? 15.132  -20.506 30.542  1.00 84.90  ? 655  LYS A CA    1 
ATOM   4077 C  C     . LYS A 1 552 ? 14.463  -19.903 31.772  1.00 79.60  ? 655  LYS A C     1 
ATOM   4078 O  O     . LYS A 1 552 ? 14.697  -20.358 32.898  1.00 76.84  ? 655  LYS A O     1 
ATOM   4079 C  CB    . LYS A 1 552 ? 16.394  -19.722 30.174  1.00 78.23  ? 655  LYS A CB    1 
ATOM   4080 C  CG    . LYS A 1 552 ? 17.273  -19.377 31.368  1.00 80.54  ? 655  LYS A CG    1 
ATOM   4081 C  CD    . LYS A 1 552 ? 18.618  -18.802 30.953  1.00 77.83  ? 655  LYS A CD    1 
ATOM   4082 C  CE    . LYS A 1 552 ? 19.627  -19.901 30.670  1.00 87.55  ? 655  LYS A CE    1 
ATOM   4083 N  NZ    . LYS A 1 552 ? 21.007  -19.358 30.513  1.00 85.79  ? 655  LYS A NZ    1 
ATOM   4084 N  N     . LYS A 1 553 ? 13.621  -18.886 31.579  1.00 81.39  ? 656  LYS A N     1 
ATOM   4085 C  CA    . LYS A 1 553 ? 12.909  -18.297 32.709  1.00 77.58  ? 656  LYS A CA    1 
ATOM   4086 C  C     . LYS A 1 553 ? 11.859  -19.253 33.260  1.00 74.56  ? 656  LYS A C     1 
ATOM   4087 O  O     . LYS A 1 553 ? 11.696  -19.367 34.480  1.00 80.24  ? 656  LYS A O     1 
ATOM   4088 C  CB    . LYS A 1 553 ? 12.271  -16.971 32.294  1.00 77.00  ? 656  LYS A CB    1 
ATOM   4089 C  CG    . LYS A 1 553 ? 13.243  -15.804 32.300  1.00 82.14  ? 656  LYS A CG    1 
ATOM   4090 C  CD    . LYS A 1 553 ? 13.614  -15.419 33.724  1.00 88.81  ? 656  LYS A CD    1 
ATOM   4091 C  CE    . LYS A 1 553 ? 14.964  -14.725 33.784  1.00 98.69  ? 656  LYS A CE    1 
ATOM   4092 N  NZ    . LYS A 1 553 ? 16.079  -15.665 33.477  1.00 110.02 ? 656  LYS A NZ    1 
ATOM   4093 N  N     . ALA A 1 554 ? 11.140  -19.952 32.378  1.00 76.79  ? 657  ALA A N     1 
ATOM   4094 C  CA    . ALA A 1 554 ? 10.145  -20.915 32.837  1.00 75.56  ? 657  ALA A CA    1 
ATOM   4095 C  C     . ALA A 1 554 ? 10.789  -22.066 33.599  1.00 77.68  ? 657  ALA A C     1 
ATOM   4096 O  O     . ALA A 1 554 ? 10.163  -22.645 34.494  1.00 77.31  ? 657  ALA A O     1 
ATOM   4097 C  CB    . ALA A 1 554 ? 9.343   -21.447 31.649  1.00 68.59  ? 657  ALA A CB    1 
ATOM   4098 N  N     . LEU A 1 555 ? 12.031  -22.407 33.266  1.00 77.03  ? 658  LEU A N     1 
ATOM   4099 C  CA    . LEU A 1 555 ? 12.747  -23.487 33.927  1.00 77.06  ? 658  LEU A CA    1 
ATOM   4100 C  C     . LEU A 1 555 ? 13.551  -23.021 35.135  1.00 79.00  ? 658  LEU A C     1 
ATOM   4101 O  O     . LEU A 1 555 ? 14.234  -23.839 35.756  1.00 87.94  ? 658  LEU A O     1 
ATOM   4102 C  CB    . LEU A 1 555 ? 13.677  -24.191 32.933  1.00 83.71  ? 658  LEU A CB    1 
ATOM   4103 C  CG    . LEU A 1 555 ? 13.024  -24.982 31.798  1.00 85.50  ? 658  LEU A CG    1 
ATOM   4104 C  CD1   . LEU A 1 555 ? 14.084  -25.545 30.863  1.00 83.59  ? 658  LEU A CD1   1 
ATOM   4105 C  CD2   . LEU A 1 555 ? 12.149  -26.095 32.348  1.00 84.87  ? 658  LEU A CD2   1 
ATOM   4106 N  N     . THR A 1 556 ? 13.499  -21.731 35.476  1.00 76.22  ? 659  THR A N     1 
ATOM   4107 C  CA    . THR A 1 556 ? 14.108  -21.221 36.701  1.00 79.24  ? 659  THR A CA    1 
ATOM   4108 C  C     . THR A 1 556 ? 13.082  -20.538 37.597  1.00 79.05  ? 659  THR A C     1 
ATOM   4109 O  O     . THR A 1 556 ? 13.456  -19.799 38.514  1.00 77.69  ? 659  THR A O     1 
ATOM   4110 C  CB    . THR A 1 556 ? 15.256  -20.259 36.384  1.00 72.25  ? 659  THR A CB    1 
ATOM   4111 O  OG1   . THR A 1 556 ? 14.766  -19.169 35.592  1.00 68.85  ? 659  THR A OG1   1 
ATOM   4112 C  CG2   . THR A 1 556 ? 16.366  -20.976 35.632  1.00 78.20  ? 659  THR A CG2   1 
ATOM   4113 N  N     . ASN A 1 557 ? 11.794  -20.774 37.347  1.00 74.05  ? 660  ASN A N     1 
ATOM   4114 C  CA    . ASN A 1 557 ? 10.722  -20.147 38.115  1.00 75.97  ? 660  ASN A CA    1 
ATOM   4115 C  C     . ASN A 1 557 ? 9.460   -20.960 37.864  1.00 75.60  ? 660  ASN A C     1 
ATOM   4116 O  O     . ASN A 1 557 ? 8.873   -20.865 36.782  1.00 80.38  ? 660  ASN A O     1 
ATOM   4117 C  CB    . ASN A 1 557 ? 10.540  -18.690 37.701  1.00 73.02  ? 660  ASN A CB    1 
ATOM   4118 C  CG    . ASN A 1 557 ? 9.565   -17.938 38.595  1.00 76.49  ? 660  ASN A CG    1 
ATOM   4119 O  OD1   . ASN A 1 557 ? 8.529   -18.467 39.000  1.00 72.83  ? 660  ASN A OD1   1 
ATOM   4120 N  ND2   . ASN A 1 557 ? 9.895   -16.688 38.900  1.00 68.70  ? 660  ASN A ND2   1 
ATOM   4121 N  N     . GLN A 1 558 ? 9.046   -21.754 38.857  1.00 71.66  ? 661  GLN A N     1 
ATOM   4122 C  CA    . GLN A 1 558 ? 7.890   -22.623 38.665  1.00 72.61  ? 661  GLN A CA    1 
ATOM   4123 C  C     . GLN A 1 558 ? 6.599   -21.832 38.505  1.00 70.09  ? 661  GLN A C     1 
ATOM   4124 O  O     . GLN A 1 558 ? 5.674   -22.299 37.832  1.00 73.47  ? 661  GLN A O     1 
ATOM   4125 C  CB    . GLN A 1 558 ? 7.759   -23.610 39.825  1.00 82.53  ? 661  GLN A CB    1 
ATOM   4126 C  CG    . GLN A 1 558 ? 8.501   -24.914 39.605  1.00 82.69  ? 661  GLN A CG    1 
ATOM   4127 C  CD    . GLN A 1 558 ? 8.053   -26.006 40.553  1.00 89.17  ? 661  GLN A CD    1 
ATOM   4128 O  OE1   . GLN A 1 558 ? 7.105   -25.828 41.318  1.00 99.85  ? 661  GLN A OE1   1 
ATOM   4129 N  NE2   . GLN A 1 558 ? 8.734   -27.146 40.508  1.00 84.39  ? 661  GLN A NE2   1 
ATOM   4130 N  N     . ARG A 1 559 ? 6.507   -20.648 39.115  1.00 70.15  ? 662  ARG A N     1 
ATOM   4131 C  CA    . ARG A 1 559 ? 5.326   -19.819 38.897  1.00 76.64  ? 662  ARG A CA    1 
ATOM   4132 C  C     . ARG A 1 559 ? 5.272   -19.320 37.458  1.00 79.57  ? 662  ARG A C     1 
ATOM   4133 O  O     . ARG A 1 559 ? 4.187   -19.194 36.878  1.00 79.34  ? 662  ARG A O     1 
ATOM   4134 C  CB    . ARG A 1 559 ? 5.304   -18.647 39.877  1.00 74.55  ? 662  ARG A CB    1 
ATOM   4135 C  CG    . ARG A 1 559 ? 3.965   -17.923 39.929  1.00 73.53  ? 662  ARG A CG    1 
ATOM   4136 C  CD    . ARG A 1 559 ? 4.051   -16.613 40.700  1.00 86.01  ? 662  ARG A CD    1 
ATOM   4137 N  NE    . ARG A 1 559 ? 4.932   -15.653 40.045  1.00 101.99 ? 662  ARG A NE    1 
ATOM   4138 C  CZ    . ARG A 1 559 ? 6.164   -15.371 40.446  1.00 111.44 ? 662  ARG A CZ    1 
ATOM   4139 N  NH1   . ARG A 1 559 ? 6.684   -15.931 41.527  1.00 88.43  ? 662  ARG A NH1   1 
ATOM   4140 N  NH2   . ARG A 1 559 ? 6.891   -14.504 39.746  1.00 89.72  ? 662  ARG A NH2   1 
ATOM   4141 N  N     . ILE A 1 560 ? 6.434   -19.032 36.868  1.00 87.33  ? 663  ILE A N     1 
ATOM   4142 C  CA    . ILE A 1 560 ? 6.494   -18.724 35.443  1.00 74.78  ? 663  ILE A CA    1 
ATOM   4143 C  C     . ILE A 1 560 ? 6.236   -19.980 34.622  1.00 72.81  ? 663  ILE A C     1 
ATOM   4144 O  O     . ILE A 1 560 ? 5.442   -19.972 33.674  1.00 77.15  ? 663  ILE A O     1 
ATOM   4145 C  CB    . ILE A 1 560 ? 7.851   -18.092 35.084  1.00 75.76  ? 663  ILE A CB    1 
ATOM   4146 C  CG1   . ILE A 1 560 ? 8.019   -16.736 35.770  1.00 76.23  ? 663  ILE A CG1   1 
ATOM   4147 C  CG2   . ILE A 1 560 ? 7.989   -17.949 33.577  1.00 73.72  ? 663  ILE A CG2   1 
ATOM   4148 C  CD1   . ILE A 1 560 ? 7.082   -15.676 35.255  1.00 86.77  ? 663  ILE A CD1   1 
ATOM   4149 N  N     . GLY A 1 561 ? 6.898   -21.082 34.981  1.00 67.83  ? 664  GLY A N     1 
ATOM   4150 C  CA    . GLY A 1 561 ? 6.760   -22.308 34.216  1.00 73.79  ? 664  GLY A CA    1 
ATOM   4151 C  C     . GLY A 1 561 ? 5.362   -22.892 34.247  1.00 78.22  ? 664  GLY A C     1 
ATOM   4152 O  O     . GLY A 1 561 ? 4.949   -23.567 33.300  1.00 85.52  ? 664  GLY A O     1 
ATOM   4153 N  N     . HIS A 1 562 ? 4.616   -22.649 35.327  1.00 77.45  ? 665  HIS A N     1 
ATOM   4154 C  CA    . HIS A 1 562 ? 3.262   -23.185 35.432  1.00 78.86  ? 665  HIS A CA    1 
ATOM   4155 C  C     . HIS A 1 562 ? 2.359   -22.609 34.347  1.00 73.93  ? 665  HIS A C     1 
ATOM   4156 O  O     . HIS A 1 562 ? 1.765   -23.349 33.554  1.00 66.94  ? 665  HIS A O     1 
ATOM   4157 C  CB    . HIS A 1 562 ? 2.685   -22.902 36.821  1.00 67.45  ? 665  HIS A CB    1 
ATOM   4158 C  CG    . HIS A 1 562 ? 1.209   -23.138 36.917  1.00 65.97  ? 665  HIS A CG    1 
ATOM   4159 N  ND1   . HIS A 1 562 ? 0.660   -24.400 36.998  1.00 66.40  ? 665  HIS A ND1   1 
ATOM   4160 C  CD2   . HIS A 1 562 ? 0.167   -22.274 36.927  1.00 65.08  ? 665  HIS A CD2   1 
ATOM   4161 C  CE1   . HIS A 1 562 ? -0.656  -24.302 37.063  1.00 69.45  ? 665  HIS A CE1   1 
ATOM   4162 N  NE2   . HIS A 1 562 ? -0.981  -23.023 37.020  1.00 66.93  ? 665  HIS A NE2   1 
ATOM   4163 N  N     . PHE A 1 563 ? 2.238   -21.279 34.301  1.00 74.84  ? 666  PHE A N     1 
ATOM   4164 C  CA    . PHE A 1 563 ? 1.406   -20.644 33.287  1.00 75.63  ? 666  PHE A CA    1 
ATOM   4165 C  C     . PHE A 1 563 ? 2.039   -20.708 31.904  1.00 82.80  ? 666  PHE A C     1 
ATOM   4166 O  O     . PHE A 1 563 ? 1.320   -20.635 30.902  1.00 86.64  ? 666  PHE A O     1 
ATOM   4167 C  CB    . PHE A 1 563 ? 1.122   -19.196 33.681  1.00 71.63  ? 666  PHE A CB    1 
ATOM   4168 C  CG    . PHE A 1 563 ? 0.301   -19.066 34.930  1.00 75.46  ? 666  PHE A CG    1 
ATOM   4169 C  CD1   . PHE A 1 563 ? -1.083  -19.090 34.869  1.00 75.07  ? 666  PHE A CD1   1 
ATOM   4170 C  CD2   . PHE A 1 563 ? 0.911   -18.931 36.166  1.00 76.00  ? 666  PHE A CD2   1 
ATOM   4171 C  CE1   . PHE A 1 563 ? -1.843  -18.977 36.013  1.00 66.56  ? 666  PHE A CE1   1 
ATOM   4172 C  CE2   . PHE A 1 563 ? 0.158   -18.818 37.314  1.00 77.07  ? 666  PHE A CE2   1 
ATOM   4173 C  CZ    . PHE A 1 563 ? -1.222  -18.841 37.238  1.00 89.02  ? 666  PHE A CZ    1 
ATOM   4174 N  N     . PHE A 1 564 ? 3.364   -20.835 31.831  1.00 78.40  ? 667  PHE A N     1 
ATOM   4175 C  CA    . PHE A 1 564 ? 4.019   -21.102 30.555  1.00 73.10  ? 667  PHE A CA    1 
ATOM   4176 C  C     . PHE A 1 564 ? 3.478   -22.381 29.930  1.00 73.44  ? 667  PHE A C     1 
ATOM   4177 O  O     . PHE A 1 564 ? 3.099   -22.402 28.754  1.00 76.96  ? 667  PHE A O     1 
ATOM   4178 C  CB    . PHE A 1 564 ? 5.532   -21.195 30.768  1.00 71.95  ? 667  PHE A CB    1 
ATOM   4179 C  CG    . PHE A 1 564 ? 6.325   -21.357 29.504  1.00 73.49  ? 667  PHE A CG    1 
ATOM   4180 C  CD1   . PHE A 1 564 ? 6.481   -20.297 28.626  1.00 75.82  ? 667  PHE A CD1   1 
ATOM   4181 C  CD2   . PHE A 1 564 ? 6.942   -22.563 29.208  1.00 71.71  ? 667  PHE A CD2   1 
ATOM   4182 C  CE1   . PHE A 1 564 ? 7.221   -20.440 27.469  1.00 75.49  ? 667  PHE A CE1   1 
ATOM   4183 C  CE2   . PHE A 1 564 ? 7.686   -22.712 28.053  1.00 73.76  ? 667  PHE A CE2   1 
ATOM   4184 C  CZ    . PHE A 1 564 ? 7.825   -21.648 27.183  1.00 76.26  ? 667  PHE A CZ    1 
ATOM   4185 N  N     . PHE A 1 565 ? 3.420   -23.458 30.717  1.00 74.45  ? 668  PHE A N     1 
ATOM   4186 C  CA    . PHE A 1 565 ? 2.902   -24.730 30.224  1.00 73.53  ? 668  PHE A CA    1 
ATOM   4187 C  C     . PHE A 1 565 ? 1.451   -24.608 29.775  1.00 76.85  ? 668  PHE A C     1 
ATOM   4188 O  O     . PHE A 1 565 ? 1.078   -25.125 28.715  1.00 85.18  ? 668  PHE A O     1 
ATOM   4189 C  CB    . PHE A 1 565 ? 3.045   -25.796 31.315  1.00 75.83  ? 668  PHE A CB    1 
ATOM   4190 C  CG    . PHE A 1 565 ? 2.304   -27.077 31.032  1.00 75.39  ? 668  PHE A CG    1 
ATOM   4191 C  CD1   . PHE A 1 565 ? 0.976   -27.230 31.411  1.00 76.68  ? 668  PHE A CD1   1 
ATOM   4192 C  CD2   . PHE A 1 565 ? 2.944   -28.140 30.417  1.00 77.15  ? 668  PHE A CD2   1 
ATOM   4193 C  CE1   . PHE A 1 565 ? 0.297   -28.407 31.157  1.00 78.76  ? 668  PHE A CE1   1 
ATOM   4194 C  CE2   . PHE A 1 565 ? 2.270   -29.322 30.165  1.00 78.98  ? 668  PHE A CE2   1 
ATOM   4195 C  CZ    . PHE A 1 565 ? 0.945   -29.455 30.535  1.00 75.40  ? 668  PHE A CZ    1 
ATOM   4196 N  N     . TRP A 1 566 ? 0.615   -23.935 30.568  1.00 69.70  ? 669  TRP A N     1 
ATOM   4197 C  CA    . TRP A 1 566 ? -0.820  -23.955 30.298  1.00 81.17  ? 669  TRP A CA    1 
ATOM   4198 C  C     . TRP A 1 566 ? -1.185  -23.082 29.104  1.00 76.81  ? 669  TRP A C     1 
ATOM   4199 O  O     . TRP A 1 566 ? -2.099  -23.420 28.343  1.00 87.17  ? 669  TRP A O     1 
ATOM   4200 C  CB    . TRP A 1 566 ? -1.599  -23.532 31.543  1.00 80.83  ? 669  TRP A CB    1 
ATOM   4201 C  CG    . TRP A 1 566 ? -1.805  -24.663 32.498  1.00 76.39  ? 669  TRP A CG    1 
ATOM   4202 C  CD1   . TRP A 1 566 ? -1.223  -24.822 33.719  1.00 78.51  ? 669  TRP A CD1   1 
ATOM   4203 C  CD2   . TRP A 1 566 ? -2.637  -25.812 32.296  1.00 78.03  ? 669  TRP A CD2   1 
ATOM   4204 N  NE1   . TRP A 1 566 ? -1.650  -25.993 34.298  1.00 85.85  ? 669  TRP A NE1   1 
ATOM   4205 C  CE2   . TRP A 1 566 ? -2.518  -26.620 33.443  1.00 77.51  ? 669  TRP A CE2   1 
ATOM   4206 C  CE3   . TRP A 1 566 ? -3.475  -26.232 31.259  1.00 79.43  ? 669  TRP A CE3   1 
ATOM   4207 C  CZ2   . TRP A 1 566 ? -3.205  -27.824 33.583  1.00 79.49  ? 669  TRP A CZ2   1 
ATOM   4208 C  CZ3   . TRP A 1 566 ? -4.156  -27.428 31.400  1.00 81.97  ? 669  TRP A CZ3   1 
ATOM   4209 C  CH2   . TRP A 1 566 ? -4.016  -28.210 32.553  1.00 81.79  ? 669  TRP A CH2   1 
ATOM   4210 N  N     . HIS A 1 567 ? -0.491  -21.957 28.921  1.00 76.13  ? 670  HIS A N     1 
ATOM   4211 C  CA    . HIS A 1 567 ? -0.722  -21.148 27.729  1.00 77.64  ? 670  HIS A CA    1 
ATOM   4212 C  C     . HIS A 1 567 ? -0.365  -21.922 26.466  1.00 79.83  ? 670  HIS A C     1 
ATOM   4213 O  O     . HIS A 1 567 ? -1.064  -21.826 25.451  1.00 78.00  ? 670  HIS A O     1 
ATOM   4214 C  CB    . HIS A 1 567 ? 0.079   -19.849 27.810  1.00 78.86  ? 670  HIS A CB    1 
ATOM   4215 C  CG    . HIS A 1 567 ? -0.391  -18.913 28.879  1.00 83.20  ? 670  HIS A CG    1 
ATOM   4216 N  ND1   . HIS A 1 567 ? -1.620  -19.038 29.491  1.00 81.68  ? 670  HIS A ND1   1 
ATOM   4217 C  CD2   . HIS A 1 567 ? 0.204   -17.837 29.446  1.00 80.65  ? 670  HIS A CD2   1 
ATOM   4218 C  CE1   . HIS A 1 567 ? -1.762  -18.079 30.388  1.00 82.71  ? 670  HIS A CE1   1 
ATOM   4219 N  NE2   . HIS A 1 567 ? -0.669  -17.336 30.381  1.00 80.49  ? 670  HIS A NE2   1 
ATOM   4220 N  N     . LEU A 1 568 ? 0.715   -22.705 26.514  1.00 77.34  ? 671  LEU A N     1 
ATOM   4221 C  CA    . LEU A 1 568 ? 1.097   -23.514 25.362  1.00 77.24  ? 671  LEU A CA    1 
ATOM   4222 C  C     . LEU A 1 568 ? 0.150   -24.692 25.175  1.00 80.96  ? 671  LEU A C     1 
ATOM   4223 O  O     . LEU A 1 568 ? -0.256  -24.996 24.048  1.00 84.21  ? 671  LEU A O     1 
ATOM   4224 C  CB    . LEU A 1 568 ? 2.536   -24.002 25.522  1.00 77.03  ? 671  LEU A CB    1 
ATOM   4225 C  CG    . LEU A 1 568 ? 3.606   -22.914 25.617  1.00 77.52  ? 671  LEU A CG    1 
ATOM   4226 C  CD1   . LEU A 1 568 ? 4.967   -23.519 25.917  1.00 72.97  ? 671  LEU A CD1   1 
ATOM   4227 C  CD2   . LEU A 1 568 ? 3.652   -22.101 24.336  1.00 70.54  ? 671  LEU A CD2   1 
ATOM   4228 N  N     . LYS A 1 569 ? -0.214  -25.367 26.269  1.00 80.34  ? 672  LYS A N     1 
ATOM   4229 C  CA    . LYS A 1 569 ? -1.118  -26.508 26.170  1.00 80.04  ? 672  LYS A CA    1 
ATOM   4230 C  C     . LYS A 1 569 ? -2.500  -26.086 25.690  1.00 77.95  ? 672  LYS A C     1 
ATOM   4231 O  O     . LYS A 1 569 ? -3.192  -26.868 25.026  1.00 78.21  ? 672  LYS A O     1 
ATOM   4232 C  CB    . LYS A 1 569 ? -1.216  -27.216 27.523  1.00 81.20  ? 672  LYS A CB    1 
ATOM   4233 C  CG    . LYS A 1 569 ? -2.051  -28.490 27.512  1.00 79.03  ? 672  LYS A CG    1 
ATOM   4234 C  CD    . LYS A 1 569 ? -1.427  -29.551 26.621  1.00 81.73  ? 672  LYS A CD    1 
ATOM   4235 C  CE    . LYS A 1 569 ? -2.312  -30.783 26.522  1.00 84.32  ? 672  LYS A CE    1 
ATOM   4236 N  NZ    . LYS A 1 569 ? -2.526  -31.432 27.843  1.00 80.04  ? 672  LYS A NZ    1 
ATOM   4237 N  N     . SER A 1 570 ? -2.917  -24.858 26.008  1.00 78.84  ? 673  SER A N     1 
ATOM   4238 C  CA    . SER A 1 570 ? -4.242  -24.399 25.605  1.00 84.28  ? 673  SER A CA    1 
ATOM   4239 C  C     . SER A 1 570 ? -4.361  -24.309 24.089  1.00 82.33  ? 673  SER A C     1 
ATOM   4240 O  O     . SER A 1 570 ? -5.401  -24.664 23.521  1.00 83.37  ? 673  SER A O     1 
ATOM   4241 C  CB    . SER A 1 570 ? -4.548  -23.046 26.246  1.00 78.33  ? 673  SER A CB    1 
ATOM   4242 O  OG    . SER A 1 570 ? -3.597  -22.071 25.856  1.00 69.96  ? 673  SER A OG    1 
ATOM   4243 N  N     . GLU A 1 571 ? -3.310  -23.843 23.417  1.00 83.26  ? 674  GLU A N     1 
ATOM   4244 C  CA    . GLU A 1 571 ? -3.309  -23.691 21.968  1.00 87.89  ? 674  GLU A CA    1 
ATOM   4245 C  C     . GLU A 1 571 ? -2.820  -24.938 21.241  1.00 91.66  ? 674  GLU A C     1 
ATOM   4246 O  O     . GLU A 1 571 ? -2.600  -24.885 20.027  1.00 88.72  ? 674  GLU A O     1 
ATOM   4247 C  CB    . GLU A 1 571 ? -2.450  -22.490 21.566  1.00 84.35  ? 674  GLU A CB    1 
ATOM   4248 C  CG    . GLU A 1 571 ? -2.882  -21.179 22.193  1.00 81.62  ? 674  GLU A CG    1 
ATOM   4249 C  CD    . GLU A 1 571 ? -2.959  -20.054 21.182  1.00 94.58  ? 674  GLU A CD    1 
ATOM   4250 O  OE1   . GLU A 1 571 ? -2.950  -20.347 19.968  1.00 101.22 ? 674  GLU A OE1   1 
ATOM   4251 O  OE2   . GLU A 1 571 ? -3.030  -18.878 21.597  1.00 99.68  ? 674  GLU A OE2   1 
ATOM   4252 N  N     . MET A 1 572 ? -2.649  -26.054 21.954  1.00 86.65  ? 675  MET A N     1 
ATOM   4253 C  CA    . MET A 1 572 ? -2.135  -27.272 21.337  1.00 87.68  ? 675  MET A CA    1 
ATOM   4254 C  C     . MET A 1 572 ? -3.123  -27.885 20.353  1.00 96.79  ? 675  MET A C     1 
ATOM   4255 O  O     . MET A 1 572 ? -2.706  -28.622 19.453  1.00 95.75  ? 675  MET A O     1 
ATOM   4256 C  CB    . MET A 1 572 ? -1.768  -28.284 22.425  1.00 84.11  ? 675  MET A CB    1 
ATOM   4257 C  CG    . MET A 1 572 ? -0.849  -29.412 21.978  1.00 86.31  ? 675  MET A CG    1 
ATOM   4258 S  SD    . MET A 1 572 ? 0.757   -28.853 21.371  1.00 86.57  ? 675  MET A SD    1 
ATOM   4259 C  CE    . MET A 1 572 ? 1.167   -27.584 22.558  1.00 86.11  ? 675  MET A CE    1 
ATOM   4260 N  N     . HIS A 1 573 ? -4.418  -27.599 20.502  1.00 98.69  ? 676  HIS A N     1 
ATOM   4261 C  CA    . HIS A 1 573 ? -5.395  -28.074 19.528  1.00 96.71  ? 676  HIS A CA    1 
ATOM   4262 C  C     . HIS A 1 573 ? -5.205  -27.398 18.177  1.00 94.80  ? 676  HIS A C     1 
ATOM   4263 O  O     . HIS A 1 573 ? -5.421  -28.025 17.134  1.00 98.53  ? 676  HIS A O     1 
ATOM   4264 C  CB    . HIS A 1 573 ? -6.812  -27.830 20.046  1.00 98.88  ? 676  HIS A CB    1 
ATOM   4265 C  CG    . HIS A 1 573 ? -7.173  -26.381 20.149  1.00 98.98  ? 676  HIS A CG    1 
ATOM   4266 N  ND1   . HIS A 1 573 ? -6.833  -25.603 21.235  1.00 87.08  ? 676  HIS A ND1   1 
ATOM   4267 C  CD2   . HIS A 1 573 ? -7.837  -25.565 19.296  1.00 106.56 ? 676  HIS A CD2   1 
ATOM   4268 C  CE1   . HIS A 1 573 ? -7.276  -24.372 21.049  1.00 88.30  ? 676  HIS A CE1   1 
ATOM   4269 N  NE2   . HIS A 1 573 ? -7.889  -24.323 19.881  1.00 106.06 ? 676  HIS A NE2   1 
ATOM   4270 N  N     . ASN A 1 574 ? -4.801  -26.131 18.180  1.00 94.33  ? 677  ASN A N     1 
ATOM   4271 C  CA    . ASN A 1 574 ? -4.581  -25.377 16.951  1.00 95.51  ? 677  ASN A CA    1 
ATOM   4272 C  C     . ASN A 1 574 ? -3.400  -25.976 16.197  1.00 95.58  ? 677  ASN A C     1 
ATOM   4273 O  O     . ASN A 1 574 ? -2.248  -25.840 16.622  1.00 95.74  ? 677  ASN A O     1 
ATOM   4274 C  CB    . ASN A 1 574 ? -4.341  -23.908 17.289  1.00 95.24  ? 677  ASN A CB    1 
ATOM   4275 C  CG    . ASN A 1 574 ? -4.220  -23.032 16.058  1.00 94.26  ? 677  ASN A CG    1 
ATOM   4276 O  OD1   . ASN A 1 574 ? -4.502  -23.464 14.940  1.00 105.95 ? 677  ASN A OD1   1 
ATOM   4277 N  ND2   . ASN A 1 574 ? -3.806  -21.786 16.261  1.00 85.07  ? 677  ASN A ND2   1 
ATOM   4278 N  N     . LYS A 1 575 ? -3.683  -26.642 15.073  1.00 96.92  ? 678  LYS A N     1 
ATOM   4279 C  CA    . LYS A 1 575 ? -2.630  -27.296 14.304  1.00 98.32  ? 678  LYS A CA    1 
ATOM   4280 C  C     . LYS A 1 575 ? -1.691  -26.300 13.636  1.00 97.18  ? 678  LYS A C     1 
ATOM   4281 O  O     . LYS A 1 575 ? -0.610  -26.694 13.188  1.00 100.61 ? 678  LYS A O     1 
ATOM   4282 C  CB    . LYS A 1 575 ? -3.242  -28.224 13.253  1.00 98.17  ? 678  LYS A CB    1 
ATOM   4283 C  CG    . LYS A 1 575 ? -3.962  -29.424 13.846  1.00 96.01  ? 678  LYS A CG    1 
ATOM   4284 C  CD    . LYS A 1 575 ? -3.051  -30.183 14.798  1.00 107.46 ? 678  LYS A CD    1 
ATOM   4285 C  CE    . LYS A 1 575 ? -3.823  -31.200 15.622  1.00 109.80 ? 678  LYS A CE    1 
ATOM   4286 N  NZ    . LYS A 1 575 ? -2.972  -31.793 16.692  1.00 102.85 ? 678  LYS A NZ    1 
ATOM   4287 N  N     . THR A 1 576 ? -2.079  -25.026 13.558  1.00 96.47  ? 679  THR A N     1 
ATOM   4288 C  CA    . THR A 1 576 ? -1.175  -24.007 13.034  1.00 96.55  ? 679  THR A CA    1 
ATOM   4289 C  C     . THR A 1 576 ? 0.069   -23.877 13.906  1.00 102.57 ? 679  THR A C     1 
ATOM   4290 O  O     . THR A 1 576 ? 1.177   -23.671 13.395  1.00 106.15 ? 679  THR A O     1 
ATOM   4291 C  CB    . THR A 1 576 ? -1.907  -22.667 12.932  1.00 96.76  ? 679  THR A CB    1 
ATOM   4292 O  OG1   . THR A 1 576 ? -2.954  -22.768 11.959  1.00 102.34 ? 679  THR A OG1   1 
ATOM   4293 C  CG2   . THR A 1 576 ? -0.951  -21.554 12.530  1.00 96.98  ? 679  THR A CG2   1 
ATOM   4294 N  N     . VAL A 1 577 ? -0.091  -24.014 15.222  1.00 98.04  ? 680  VAL A N     1 
ATOM   4295 C  CA    . VAL A 1 577 ? 1.005   -23.861 16.170  1.00 91.46  ? 680  VAL A CA    1 
ATOM   4296 C  C     . VAL A 1 577 ? 1.268   -25.123 16.975  1.00 83.80  ? 680  VAL A C     1 
ATOM   4297 O  O     . VAL A 1 577 ? 2.154   -25.117 17.836  1.00 79.68  ? 680  VAL A O     1 
ATOM   4298 C  CB    . VAL A 1 577 ? 0.759   -22.671 17.119  1.00 87.89  ? 680  VAL A CB    1 
ATOM   4299 C  CG1   . VAL A 1 577 ? 0.797   -21.362 16.348  1.00 92.06  ? 680  VAL A CG1   1 
ATOM   4300 C  CG2   . VAL A 1 577 ? -0.574  -22.833 17.832  1.00 89.73  ? 680  VAL A CG2   1 
ATOM   4301 N  N     . SER A 1 578 ? 0.538   -26.211 16.716  1.00 85.66  ? 681  SER A N     1 
ATOM   4302 C  CA    . SER A 1 578 ? 0.664   -27.416 17.531  1.00 85.90  ? 681  SER A CA    1 
ATOM   4303 C  C     . SER A 1 578 ? 2.059   -28.027 17.473  1.00 82.81  ? 681  SER A C     1 
ATOM   4304 O  O     . SER A 1 578 ? 2.427   -28.783 18.378  1.00 81.01  ? 681  SER A O     1 
ATOM   4305 C  CB    . SER A 1 578 ? -0.370  -28.457 17.098  1.00 92.43  ? 681  SER A CB    1 
ATOM   4306 O  OG    . SER A 1 578 ? -0.119  -28.903 15.777  1.00 98.69  ? 681  SER A OG    1 
ATOM   4307 N  N     . GLN A 1 579 ? 2.841   -27.732 16.435  1.00 96.62  ? 682  GLN A N     1 
ATOM   4308 C  CA    . GLN A 1 579 ? 4.196   -28.265 16.361  1.00 85.79  ? 682  GLN A CA    1 
ATOM   4309 C  C     . GLN A 1 579 ? 5.220   -27.324 16.982  1.00 83.01  ? 682  GLN A C     1 
ATOM   4310 O  O     . GLN A 1 579 ? 6.154   -27.782 17.650  1.00 81.07  ? 682  GLN A O     1 
ATOM   4311 C  CB    . GLN A 1 579 ? 4.577   -28.559 14.909  1.00 80.40  ? 682  GLN A CB    1 
ATOM   4312 C  CG    . GLN A 1 579 ? 5.898   -29.295 14.772  1.00 83.39  ? 682  GLN A CG    1 
ATOM   4313 C  CD    . GLN A 1 579 ? 6.266   -29.581 13.332  1.00 85.84  ? 682  GLN A CD    1 
ATOM   4314 O  OE1   . GLN A 1 579 ? 6.432   -28.665 12.527  1.00 91.88  ? 682  GLN A OE1   1 
ATOM   4315 N  NE2   . GLN A 1 579 ? 6.395   -30.860 12.997  1.00 76.35  ? 682  GLN A NE2   1 
ATOM   4316 N  N     . ARG A 1 580 ? 5.067   -26.015 16.769  1.00 80.52  ? 683  ARG A N     1 
ATOM   4317 C  CA    . ARG A 1 580 ? 5.964   -25.053 17.401  1.00 76.28  ? 683  ARG A CA    1 
ATOM   4318 C  C     . ARG A 1 580 ? 5.835   -25.098 18.919  1.00 83.05  ? 683  ARG A C     1 
ATOM   4319 O  O     . ARG A 1 580 ? 6.839   -25.038 19.638  1.00 82.50  ? 683  ARG A O     1 
ATOM   4320 C  CB    . ARG A 1 580 ? 5.675   -23.646 16.877  1.00 75.76  ? 683  ARG A CB    1 
ATOM   4321 C  CG    . ARG A 1 580 ? 6.190   -22.529 17.772  1.00 80.21  ? 683  ARG A CG    1 
ATOM   4322 C  CD    . ARG A 1 580 ? 7.228   -21.676 17.066  1.00 79.86  ? 683  ARG A CD    1 
ATOM   4323 N  NE    . ARG A 1 580 ? 6.661   -20.944 15.941  1.00 90.78  ? 683  ARG A NE    1 
ATOM   4324 C  CZ    . ARG A 1 580 ? 7.352   -20.133 15.152  1.00 96.13  ? 683  ARG A CZ    1 
ATOM   4325 N  NH1   . ARG A 1 580 ? 8.646   -19.926 15.336  1.00 89.59  ? 683  ARG A NH1   1 
ATOM   4326 N  NH2   . ARG A 1 580 ? 6.729   -19.514 14.153  1.00 89.08  ? 683  ARG A NH2   1 
ATOM   4327 N  N     . PHE A 1 581 ? 4.607   -25.211 19.425  1.00 77.55  ? 684  PHE A N     1 
ATOM   4328 C  CA    . PHE A 1 581 ? 4.408   -25.259 20.869  1.00 79.68  ? 684  PHE A CA    1 
ATOM   4329 C  C     . PHE A 1 581 ? 4.664   -26.655 21.424  1.00 82.21  ? 684  PHE A C     1 
ATOM   4330 O  O     . PHE A 1 581 ? 5.185   -26.796 22.537  1.00 91.48  ? 684  PHE A O     1 
ATOM   4331 C  CB    . PHE A 1 581 ? 2.995   -24.793 21.225  1.00 78.70  ? 684  PHE A CB    1 
ATOM   4332 C  CG    . PHE A 1 581 ? 2.788   -23.309 21.083  1.00 78.46  ? 684  PHE A CG    1 
ATOM   4333 C  CD1   . PHE A 1 581 ? 3.849   -22.469 20.775  1.00 72.42  ? 684  PHE A CD1   1 
ATOM   4334 C  CD2   . PHE A 1 581 ? 1.532   -22.752 21.268  1.00 72.79  ? 684  PHE A CD2   1 
ATOM   4335 C  CE1   . PHE A 1 581 ? 3.660   -21.104 20.648  1.00 63.92  ? 684  PHE A CE1   1 
ATOM   4336 C  CE2   . PHE A 1 581 ? 1.337   -21.388 21.143  1.00 73.60  ? 684  PHE A CE2   1 
ATOM   4337 C  CZ    . PHE A 1 581 ? 2.402   -20.563 20.832  1.00 65.91  ? 684  PHE A CZ    1 
ATOM   4338 N  N     . GLY A 1 582 ? 4.307   -27.695 20.668  1.00 80.13  ? 685  GLY A N     1 
ATOM   4339 C  CA    . GLY A 1 582 ? 4.543   -29.052 21.137  1.00 82.81  ? 685  GLY A CA    1 
ATOM   4340 C  C     . GLY A 1 582 ? 6.015   -29.351 21.347  1.00 83.54  ? 685  GLY A C     1 
ATOM   4341 O  O     . GLY A 1 582 ? 6.393   -30.004 22.322  1.00 83.39  ? 685  GLY A O     1 
ATOM   4342 N  N     . LEU A 1 583 ? 6.866   -28.880 20.433  1.00 85.59  ? 686  LEU A N     1 
ATOM   4343 C  CA    . LEU A 1 583 ? 8.304   -29.031 20.624  1.00 86.72  ? 686  LEU A CA    1 
ATOM   4344 C  C     . LEU A 1 583 ? 8.804   -28.183 21.784  1.00 79.34  ? 686  LEU A C     1 
ATOM   4345 O  O     . LEU A 1 583 ? 9.784   -28.549 22.443  1.00 89.04  ? 686  LEU A O     1 
ATOM   4346 C  CB    . LEU A 1 583 ? 9.052   -28.660 19.344  1.00 83.64  ? 686  LEU A CB    1 
ATOM   4347 C  CG    . LEU A 1 583 ? 8.914   -29.605 18.152  1.00 83.06  ? 686  LEU A CG    1 
ATOM   4348 C  CD1   . LEU A 1 583 ? 9.634   -29.023 16.952  1.00 86.22  ? 686  LEU A CD1   1 
ATOM   4349 C  CD2   . LEU A 1 583 ? 9.461   -30.982 18.492  1.00 85.99  ? 686  LEU A CD2   1 
ATOM   4350 N  N     . LEU A 1 584 ? 8.152   -27.049 22.045  1.00 71.19  ? 687  LEU A N     1 
ATOM   4351 C  CA    . LEU A 1 584 ? 8.558   -26.213 23.168  1.00 80.00  ? 687  LEU A CA    1 
ATOM   4352 C  C     . LEU A 1 584 ? 8.182   -26.859 24.495  1.00 84.18  ? 687  LEU A C     1 
ATOM   4353 O  O     . LEU A 1 584 ? 8.945   -26.788 25.466  1.00 89.30  ? 687  LEU A O     1 
ATOM   4354 C  CB    . LEU A 1 584 ? 7.930   -24.826 23.040  1.00 76.03  ? 687  LEU A CB    1 
ATOM   4355 C  CG    . LEU A 1 584 ? 8.394   -23.791 24.064  1.00 75.48  ? 687  LEU A CG    1 
ATOM   4356 C  CD1   . LEU A 1 584 ? 9.912   -23.786 24.146  1.00 70.72  ? 687  LEU A CD1   1 
ATOM   4357 C  CD2   . LEU A 1 584 ? 7.865   -22.410 23.707  1.00 66.03  ? 687  LEU A CD2   1 
ATOM   4358 N  N     . LEU A 1 585 ? 7.014   -27.503 24.554  1.00 80.88  ? 688  LEU A N     1 
ATOM   4359 C  CA    . LEU A 1 585 ? 6.604   -28.181 25.778  1.00 80.79  ? 688  LEU A CA    1 
ATOM   4360 C  C     . LEU A 1 585 ? 7.477   -29.394 26.076  1.00 83.03  ? 688  LEU A C     1 
ATOM   4361 O  O     . LEU A 1 585 ? 7.722   -29.704 27.247  1.00 88.75  ? 688  LEU A O     1 
ATOM   4362 C  CB    . LEU A 1 585 ? 5.139   -28.601 25.679  1.00 82.09  ? 688  LEU A CB    1 
ATOM   4363 C  CG    . LEU A 1 585 ? 4.104   -27.491 25.834  1.00 85.28  ? 688  LEU A CG    1 
ATOM   4364 C  CD1   . LEU A 1 585 ? 2.709   -28.058 25.676  1.00 83.39  ? 688  LEU A CD1   1 
ATOM   4365 C  CD2   . LEU A 1 585 ? 4.258   -26.822 27.188  1.00 83.12  ? 688  LEU A CD2   1 
ATOM   4366 N  N     . GLU A 1 586 ? 7.947   -30.093 25.041  1.00 84.35  ? 689  GLU A N     1 
ATOM   4367 C  CA    . GLU A 1 586 ? 8.790   -31.264 25.263  1.00 88.12  ? 689  GLU A CA    1 
ATOM   4368 C  C     . GLU A 1 586 ? 10.072  -30.883 25.991  1.00 85.00  ? 689  GLU A C     1 
ATOM   4369 O  O     . GLU A 1 586 ? 10.482  -31.555 26.944  1.00 87.72  ? 689  GLU A O     1 
ATOM   4370 C  CB    . GLU A 1 586 ? 9.112   -31.945 23.932  1.00 84.04  ? 689  GLU A CB    1 
ATOM   4371 C  CG    . GLU A 1 586 ? 9.957   -33.202 24.078  1.00 86.04  ? 689  GLU A CG    1 
ATOM   4372 C  CD    . GLU A 1 586 ? 10.605  -33.628 22.776  1.00 98.68  ? 689  GLU A CD    1 
ATOM   4373 O  OE1   . GLU A 1 586 ? 10.613  -32.822 21.821  1.00 95.48  ? 689  GLU A OE1   1 
ATOM   4374 O  OE2   . GLU A 1 586 ? 11.109  -34.769 22.709  1.00 102.13 ? 689  GLU A OE2   1 
ATOM   4375 N  N     . SER A 1 587 ? 10.720  -29.802 25.552  1.00 81.82  ? 690  SER A N     1 
ATOM   4376 C  CA    . SER A 1 587 ? 11.931  -29.347 26.225  1.00 83.74  ? 690  SER A CA    1 
ATOM   4377 C  C     . SER A 1 587 ? 11.628  -28.873 27.641  1.00 89.90  ? 690  SER A C     1 
ATOM   4378 O  O     . SER A 1 587 ? 12.421  -29.102 28.562  1.00 98.02  ? 690  SER A O     1 
ATOM   4379 C  CB    . SER A 1 587 ? 12.594  -28.233 25.416  1.00 79.60  ? 690  SER A CB    1 
ATOM   4380 O  OG    . SER A 1 587 ? 11.738  -27.109 25.306  1.00 83.58  ? 690  SER A OG    1 
ATOM   4381 N  N     . TYR A 1 588 ? 10.483  -28.215 27.835  1.00 85.03  ? 691  TYR A N     1 
ATOM   4382 C  CA    . TYR A 1 588 ? 10.102  -27.778 29.174  1.00 83.37  ? 691  TYR A CA    1 
ATOM   4383 C  C     . TYR A 1 588 ? 9.822   -28.969 30.081  1.00 85.55  ? 691  TYR A C     1 
ATOM   4384 O  O     . TYR A 1 588 ? 10.343  -29.045 31.200  1.00 88.26  ? 691  TYR A O     1 
ATOM   4385 C  CB    . TYR A 1 588 ? 8.880   -26.860 29.103  1.00 79.24  ? 691  TYR A CB    1 
ATOM   4386 C  CG    . TYR A 1 588 ? 8.268   -26.574 30.454  1.00 83.02  ? 691  TYR A CG    1 
ATOM   4387 C  CD1   . TYR A 1 588 ? 8.796   -25.593 31.284  1.00 81.07  ? 691  TYR A CD1   1 
ATOM   4388 C  CD2   . TYR A 1 588 ? 7.165   -27.291 30.906  1.00 87.45  ? 691  TYR A CD2   1 
ATOM   4389 C  CE1   . TYR A 1 588 ? 8.243   -25.331 32.524  1.00 81.78  ? 691  TYR A CE1   1 
ATOM   4390 C  CE2   . TYR A 1 588 ? 6.607   -27.037 32.145  1.00 93.13  ? 691  TYR A CE2   1 
ATOM   4391 C  CZ    . TYR A 1 588 ? 7.149   -26.056 32.948  1.00 84.55  ? 691  TYR A CZ    1 
ATOM   4392 O  OH    . TYR A 1 588 ? 6.594   -25.801 34.181  1.00 86.36  ? 691  TYR A OH    1 
ATOM   4393 N  N     . CYS A 1 589 ? 8.997   -29.911 29.615  1.00 82.97  ? 692  CYS A N     1 
ATOM   4394 C  CA    . CYS A 1 589 ? 8.633   -31.055 30.443  1.00 84.62  ? 692  CYS A CA    1 
ATOM   4395 C  C     . CYS A 1 589 ? 9.839   -31.921 30.774  1.00 87.77  ? 692  CYS A C     1 
ATOM   4396 O  O     . CYS A 1 589 ? 9.878   -32.549 31.839  1.00 90.06  ? 692  CYS A O     1 
ATOM   4397 C  CB    . CYS A 1 589 ? 7.560   -31.891 29.747  1.00 78.18  ? 692  CYS A CB    1 
ATOM   4398 S  SG    . CYS A 1 589 ? 5.940   -31.102 29.680  1.00 84.14  ? 692  CYS A SG    1 
ATOM   4399 N  N     . ARG A 1 590 ? 10.832  -31.967 29.885  1.00 87.33  ? 693  ARG A N     1 
ATOM   4400 C  CA    . ARG A 1 590 ? 12.012  -32.783 30.135  1.00 95.49  ? 693  ARG A CA    1 
ATOM   4401 C  C     . ARG A 1 590 ? 12.949  -32.166 31.166  1.00 90.88  ? 693  ARG A C     1 
ATOM   4402 O  O     . ARG A 1 590 ? 13.828  -32.869 31.677  1.00 91.86  ? 693  ARG A O     1 
ATOM   4403 C  CB    . ARG A 1 590 ? 12.759  -33.027 28.821  1.00 89.74  ? 693  ARG A CB    1 
ATOM   4404 C  CG    . ARG A 1 590 ? 13.715  -34.211 28.849  1.00 99.77  ? 693  ARG A CG    1 
ATOM   4405 C  CD    . ARG A 1 590 ? 14.212  -34.553 27.453  1.00 105.39 ? 693  ARG A CD    1 
ATOM   4406 N  NE    . ARG A 1 590 ? 13.118  -34.921 26.562  1.00 96.09  ? 693  ARG A NE    1 
ATOM   4407 C  CZ    . ARG A 1 590 ? 12.642  -36.152 26.428  1.00 98.26  ? 693  ARG A CZ    1 
ATOM   4408 N  NH1   . ARG A 1 590 ? 13.143  -37.166 27.114  1.00 102.12 ? 693  ARG A NH1   1 
ATOM   4409 N  NH2   . ARG A 1 590 ? 11.638  -36.371 25.584  1.00 97.86  ? 693  ARG A NH2   1 
ATOM   4410 N  N     . ALA A 1 591 ? 12.776  -30.885 31.502  1.00 89.21  ? 694  ALA A N     1 
ATOM   4411 C  CA    . ALA A 1 591 ? 13.688  -30.206 32.410  1.00 90.63  ? 694  ALA A CA    1 
ATOM   4412 C  C     . ALA A 1 591 ? 13.003  -29.453 33.543  1.00 89.73  ? 694  ALA A C     1 
ATOM   4413 O  O     . ALA A 1 591 ? 13.702  -28.876 34.383  1.00 85.52  ? 694  ALA A O     1 
ATOM   4414 C  CB    . ALA A 1 591 ? 14.581  -29.227 31.632  1.00 91.85  ? 694  ALA A CB    1 
ATOM   4415 N  N     . CYS A 1 592 ? 11.669  -29.435 33.599  1.00 87.38  ? 695  CYS A N     1 
ATOM   4416 C  CA    . CYS A 1 592 ? 10.994  -28.723 34.679  1.00 85.61  ? 695  CYS A CA    1 
ATOM   4417 C  C     . CYS A 1 592 ? 11.156  -29.425 36.021  1.00 90.32  ? 695  CYS A C     1 
ATOM   4418 O  O     . CYS A 1 592 ? 10.927  -28.803 37.064  1.00 84.31  ? 695  CYS A O     1 
ATOM   4419 C  CB    . CYS A 1 592 ? 9.510   -28.544 34.355  1.00 82.57  ? 695  CYS A CB    1 
ATOM   4420 S  SG    . CYS A 1 592 ? 8.587   -30.082 34.159  1.00 89.26  ? 695  CYS A SG    1 
ATOM   4421 N  N     . GLY A 1 593 ? 11.546  -30.697 36.020  1.00 88.02  ? 696  GLY A N     1 
ATOM   4422 C  CA    . GLY A 1 593 ? 11.810  -31.408 37.254  1.00 87.16  ? 696  GLY A CA    1 
ATOM   4423 C  C     . GLY A 1 593 ? 10.605  -32.132 37.816  1.00 92.75  ? 696  GLY A C     1 
ATOM   4424 O  O     . GLY A 1 593 ? 9.852   -32.774 37.077  1.00 107.51 ? 696  GLY A O     1 
ATOM   4425 N  N     . MET A 1 594 ? 10.414  -32.030 39.132  1.00 89.26  ? 697  MET A N     1 
ATOM   4426 C  CA    . MET A 1 594 ? 9.327   -32.739 39.794  1.00 92.69  ? 697  MET A CA    1 
ATOM   4427 C  C     . MET A 1 594 ? 7.961   -32.156 39.455  1.00 84.37  ? 697  MET A C     1 
ATOM   4428 O  O     . MET A 1 594 ? 6.951   -32.855 39.599  1.00 83.29  ? 697  MET A O     1 
ATOM   4429 C  CB    . MET A 1 594 ? 9.547   -32.723 41.310  1.00 99.61  ? 697  MET A CB    1 
ATOM   4430 C  CG    . MET A 1 594 ? 8.641   -33.659 42.096  1.00 96.10  ? 697  MET A CG    1 
ATOM   4431 S  SD    . MET A 1 594 ? 8.752   -35.368 41.530  1.00 129.67 ? 697  MET A SD    1 
ATOM   4432 C  CE    . MET A 1 594 ? 10.509  -35.675 41.704  1.00 107.35 ? 697  MET A CE    1 
ATOM   4433 N  N     . TYR A 1 595 ? 7.905   -30.903 38.996  1.00 81.97  ? 698  TYR A N     1 
ATOM   4434 C  CA    . TYR A 1 595 ? 6.620   -30.267 38.728  1.00 82.62  ? 698  TYR A CA    1 
ATOM   4435 C  C     . TYR A 1 595 ? 5.853   -30.959 37.609  1.00 83.93  ? 698  TYR A C     1 
ATOM   4436 O  O     . TYR A 1 595 ? 4.632   -30.787 37.514  1.00 81.33  ? 698  TYR A O     1 
ATOM   4437 C  CB    . TYR A 1 595 ? 6.822   -28.789 38.388  1.00 80.52  ? 698  TYR A CB    1 
ATOM   4438 C  CG    . TYR A 1 595 ? 5.549   -27.978 38.448  1.00 80.10  ? 698  TYR A CG    1 
ATOM   4439 C  CD1   . TYR A 1 595 ? 4.809   -27.904 39.620  1.00 81.89  ? 698  TYR A CD1   1 
ATOM   4440 C  CD2   . TYR A 1 595 ? 5.089   -27.284 37.338  1.00 83.40  ? 698  TYR A CD2   1 
ATOM   4441 C  CE1   . TYR A 1 595 ? 3.643   -27.166 39.684  1.00 82.41  ? 698  TYR A CE1   1 
ATOM   4442 C  CE2   . TYR A 1 595 ? 3.924   -26.540 37.393  1.00 81.37  ? 698  TYR A CE2   1 
ATOM   4443 C  CZ    . TYR A 1 595 ? 3.205   -26.485 38.568  1.00 79.86  ? 698  TYR A CZ    1 
ATOM   4444 O  OH    . TYR A 1 595 ? 2.044   -25.748 38.631  1.00 77.11  ? 698  TYR A OH    1 
ATOM   4445 N  N     . LEU A 1 596 ? 6.538   -31.734 36.763  1.00 83.13  ? 699  LEU A N     1 
ATOM   4446 C  CA    . LEU A 1 596 ? 5.848   -32.481 35.717  1.00 82.09  ? 699  LEU A CA    1 
ATOM   4447 C  C     . LEU A 1 596 ? 4.838   -33.453 36.312  1.00 82.02  ? 699  LEU A C     1 
ATOM   4448 O  O     . LEU A 1 596 ? 3.733   -33.617 35.779  1.00 81.67  ? 699  LEU A O     1 
ATOM   4449 C  CB    . LEU A 1 596 ? 6.862   -33.227 34.851  1.00 86.53  ? 699  LEU A CB    1 
ATOM   4450 C  CG    . LEU A 1 596 ? 6.277   -34.163 33.794  1.00 84.70  ? 699  LEU A CG    1 
ATOM   4451 C  CD1   . LEU A 1 596 ? 5.441   -33.381 32.793  1.00 83.92  ? 699  LEU A CD1   1 
ATOM   4452 C  CD2   . LEU A 1 596 ? 7.379   -34.943 33.092  1.00 84.16  ? 699  LEU A CD2   1 
ATOM   4453 N  N     . LYS A 1 597 ? 5.200   -34.106 37.419  1.00 83.87  ? 700  LYS A N     1 
ATOM   4454 C  CA    . LYS A 1 597 ? 4.266   -35.003 38.090  1.00 83.25  ? 700  LYS A CA    1 
ATOM   4455 C  C     . LYS A 1 597 ? 3.042   -34.246 38.587  1.00 79.69  ? 700  LYS A C     1 
ATOM   4456 O  O     . LYS A 1 597 ? 1.918   -34.761 38.535  1.00 78.03  ? 700  LYS A O     1 
ATOM   4457 C  CB    . LYS A 1 597 ? 4.970   -35.718 39.243  1.00 88.21  ? 700  LYS A CB    1 
ATOM   4458 C  CG    . LYS A 1 597 ? 4.103   -36.722 39.986  1.00 95.71  ? 700  LYS A CG    1 
ATOM   4459 C  CD    . LYS A 1 597 ? 4.890   -37.415 41.087  1.00 110.84 ? 700  LYS A CD    1 
ATOM   4460 C  CE    . LYS A 1 597 ? 4.029   -38.412 41.844  1.00 118.29 ? 700  LYS A CE    1 
ATOM   4461 N  NZ    . LYS A 1 597 ? 4.798   -39.100 42.919  1.00 111.36 ? 700  LYS A NZ    1 
ATOM   4462 N  N     . HIS A 1 598 ? 3.238   -33.014 39.065  1.00 74.15  ? 701  HIS A N     1 
ATOM   4463 C  CA    . HIS A 1 598 ? 2.106   -32.192 39.474  1.00 77.11  ? 701  HIS A CA    1 
ATOM   4464 C  C     . HIS A 1 598 ? 1.270   -31.770 38.273  1.00 84.46  ? 701  HIS A C     1 
ATOM   4465 O  O     . HIS A 1 598 ? 0.036   -31.745 38.347  1.00 83.65  ? 701  HIS A O     1 
ATOM   4466 C  CB    . HIS A 1 598 ? 2.595   -30.965 40.244  1.00 79.85  ? 701  HIS A CB    1 
ATOM   4467 C  CG    . HIS A 1 598 ? 3.238   -31.291 41.556  1.00 85.68  ? 701  HIS A CG    1 
ATOM   4468 N  ND1   . HIS A 1 598 ? 2.527   -31.772 42.634  1.00 79.58  ? 701  HIS A ND1   1 
ATOM   4469 C  CD2   . HIS A 1 598 ? 4.526   -31.200 41.965  1.00 82.99  ? 701  HIS A CD2   1 
ATOM   4470 C  CE1   . HIS A 1 598 ? 3.349   -31.965 43.650  1.00 76.35  ? 701  HIS A CE1   1 
ATOM   4471 N  NE2   . HIS A 1 598 ? 4.568   -31.626 43.270  1.00 78.45  ? 701  HIS A NE2   1 
ATOM   4472 N  N     . LEU A 1 599 ? 1.926   -31.435 37.158  1.00 87.40  ? 702  LEU A N     1 
ATOM   4473 C  CA    . LEU A 1 599 ? 1.196   -31.035 35.959  1.00 81.44  ? 702  LEU A CA    1 
ATOM   4474 C  C     . LEU A 1 599 ? 0.356   -32.183 35.414  1.00 81.66  ? 702  LEU A C     1 
ATOM   4475 O  O     . LEU A 1 599 ? -0.792  -31.979 35.004  1.00 83.07  ? 702  LEU A O     1 
ATOM   4476 C  CB    . LEU A 1 599 ? 2.171   -30.529 34.896  1.00 79.69  ? 702  LEU A CB    1 
ATOM   4477 C  CG    . LEU A 1 599 ? 2.795   -29.160 35.165  1.00 80.35  ? 702  LEU A CG    1 
ATOM   4478 C  CD1   . LEU A 1 599 ? 3.970   -28.908 34.235  1.00 78.17  ? 702  LEU A CD1   1 
ATOM   4479 C  CD2   . LEU A 1 599 ? 1.750   -28.065 35.017  1.00 79.21  ? 702  LEU A CD2   1 
ATOM   4480 N  N     . ASN A 1 600 ? 0.912   -33.398 35.401  1.00 75.99  ? 703  ASN A N     1 
ATOM   4481 C  CA    . ASN A 1 600 ? 0.151   -34.554 34.936  1.00 84.08  ? 703  ASN A CA    1 
ATOM   4482 C  C     . ASN A 1 600 ? -1.099  -34.768 35.780  1.00 87.55  ? 703  ASN A C     1 
ATOM   4483 O  O     . ASN A 1 600 ? -2.155  -35.140 35.254  1.00 96.10  ? 703  ASN A O     1 
ATOM   4484 C  CB    . ASN A 1 600 ? 1.027   -35.807 34.954  1.00 87.63  ? 703  ASN A CB    1 
ATOM   4485 C  CG    . ASN A 1 600 ? 1.943   -35.894 33.752  1.00 93.83  ? 703  ASN A CG    1 
ATOM   4486 O  OD1   . ASN A 1 600 ? 1.608   -35.421 32.666  1.00 94.97  ? 703  ASN A OD1   1 
ATOM   4487 N  ND2   . ASN A 1 600 ? 3.107   -36.506 33.939  1.00 100.14 ? 703  ASN A ND2   1 
ATOM   4488 N  N     . ARG A 1 601 ? -1.001  -34.536 37.090  1.00 87.04  ? 704  ARG A N     1 
ATOM   4489 C  CA    . ARG A 1 601 ? -2.173  -34.677 37.946  1.00 86.67  ? 704  ARG A CA    1 
ATOM   4490 C  C     . ARG A 1 601 ? -3.178  -33.559 37.699  1.00 84.22  ? 704  ARG A C     1 
ATOM   4491 O  O     . ARG A 1 601 ? -4.377  -33.741 37.937  1.00 85.98  ? 704  ARG A O     1 
ATOM   4492 C  CB    . ARG A 1 601 ? -1.748  -34.717 39.413  1.00 86.93  ? 704  ARG A CB    1 
ATOM   4493 C  CG    . ARG A 1 601 ? -2.839  -35.181 40.362  1.00 94.45  ? 704  ARG A CG    1 
ATOM   4494 C  CD    . ARG A 1 601 ? -2.265  -35.582 41.708  1.00 99.33  ? 704  ARG A CD    1 
ATOM   4495 N  NE    . ARG A 1 601 ? -3.314  -35.904 42.668  1.00 115.21 ? 704  ARG A NE    1 
ATOM   4496 C  CZ    . ARG A 1 601 ? -3.907  -37.087 42.764  1.00 118.32 ? 704  ARG A CZ    1 
ATOM   4497 N  NH1   . ARG A 1 601 ? -3.582  -38.090 41.964  1.00 103.69 ? 704  ARG A NH1   1 
ATOM   4498 N  NH2   . ARG A 1 601 ? -4.851  -37.267 43.684  1.00 121.42 ? 704  ARG A NH2   1 
ATOM   4499 N  N     . GLN A 1 602 ? -2.713  -32.402 37.220  1.00 87.84  ? 705  GLN A N     1 
ATOM   4500 C  CA    . GLN A 1 602 ? -3.629  -31.337 36.827  1.00 86.11  ? 705  GLN A CA    1 
ATOM   4501 C  C     . GLN A 1 602 ? -4.235  -31.605 35.456  1.00 89.42  ? 705  GLN A C     1 
ATOM   4502 O  O     . GLN A 1 602 ? -5.413  -31.308 35.226  1.00 96.95  ? 705  GLN A O     1 
ATOM   4503 C  CB    . GLN A 1 602 ? -2.908  -29.990 36.826  1.00 83.41  ? 705  GLN A CB    1 
ATOM   4504 C  CG    . GLN A 1 602 ? -2.324  -29.589 38.166  1.00 90.51  ? 705  GLN A CG    1 
ATOM   4505 C  CD    . GLN A 1 602 ? -1.505  -28.319 38.077  1.00 93.65  ? 705  GLN A CD    1 
ATOM   4506 O  OE1   . GLN A 1 602 ? -1.758  -27.462 37.229  1.00 83.13  ? 705  GLN A OE1   1 
ATOM   4507 N  NE2   . GLN A 1 602 ? -0.510  -28.193 38.948  1.00 96.74  ? 705  GLN A NE2   1 
ATOM   4508 N  N     . VAL A 1 603 ? -3.443  -32.155 34.533  1.00 87.67  ? 706  VAL A N     1 
ATOM   4509 C  CA    . VAL A 1 603 ? -3.956  -32.468 33.201  1.00 87.35  ? 706  VAL A CA    1 
ATOM   4510 C  C     . VAL A 1 603 ? -5.057  -33.516 33.293  1.00 88.73  ? 706  VAL A C     1 
ATOM   4511 O  O     . VAL A 1 603 ? -6.131  -33.370 32.697  1.00 89.84  ? 706  VAL A O     1 
ATOM   4512 C  CB    . VAL A 1 603 ? -2.812  -32.927 32.278  1.00 91.12  ? 706  VAL A CB    1 
ATOM   4513 C  CG1   . VAL A 1 603 ? -3.369  -33.516 30.991  1.00 86.97  ? 706  VAL A CG1   1 
ATOM   4514 C  CG2   . VAL A 1 603 ? -1.880  -31.765 31.970  1.00 87.26  ? 706  VAL A CG2   1 
ATOM   4515 N  N     . GLU A 1 604 ? -4.810  -34.588 34.052  1.00 87.74  ? 707  GLU A N     1 
ATOM   4516 C  CA    . GLU A 1 604 ? -5.823  -35.626 34.204  1.00 89.14  ? 707  GLU A CA    1 
ATOM   4517 C  C     . GLU A 1 604 ? -7.055  -35.101 34.927  1.00 89.62  ? 707  GLU A C     1 
ATOM   4518 O  O     . GLU A 1 604 ? -8.173  -35.554 34.656  1.00 90.40  ? 707  GLU A O     1 
ATOM   4519 C  CB    . GLU A 1 604 ? -5.237  -36.829 34.943  1.00 84.26  ? 707  GLU A CB    1 
ATOM   4520 C  CG    . GLU A 1 604 ? -6.135  -38.055 34.940  1.00 95.61  ? 707  GLU A CG    1 
ATOM   4521 C  CD    . GLU A 1 604 ? -5.435  -39.294 35.463  1.00 111.51 ? 707  GLU A CD    1 
ATOM   4522 O  OE1   . GLU A 1 604 ? -4.232  -39.207 35.790  1.00 120.23 ? 707  GLU A OE1   1 
ATOM   4523 O  OE2   . GLU A 1 604 ? -6.087  -40.357 35.546  1.00 120.27 ? 707  GLU A OE2   1 
ATOM   4524 N  N     . ALA A 1 605 ? -6.874  -34.144 35.839  1.00 90.02  ? 708  ALA A N     1 
ATOM   4525 C  CA    . ALA A 1 605 ? -8.017  -33.545 36.523  1.00 89.37  ? 708  ALA A CA    1 
ATOM   4526 C  C     . ALA A 1 605 ? -8.892  -32.769 35.546  1.00 87.52  ? 708  ALA A C     1 
ATOM   4527 O  O     . ALA A 1 605 ? -10.112 -32.966 35.498  1.00 85.94  ? 708  ALA A O     1 
ATOM   4528 C  CB    . ALA A 1 605 ? -7.535  -32.640 37.656  1.00 87.36  ? 708  ALA A CB    1 
ATOM   4529 N  N     . MET A 1 606 ? -8.283  -31.880 34.757  1.00 88.14  ? 709  MET A N     1 
ATOM   4530 C  CA    . MET A 1 606 ? -9.045  -31.139 33.758  1.00 88.89  ? 709  MET A CA    1 
ATOM   4531 C  C     . MET A 1 606 ? -9.616  -32.064 32.693  1.00 90.15  ? 709  MET A C     1 
ATOM   4532 O  O     . MET A 1 606 ? -10.707 -31.808 32.169  1.00 86.80  ? 709  MET A O     1 
ATOM   4533 C  CB    . MET A 1 606 ? -8.167  -30.066 33.113  1.00 82.07  ? 709  MET A CB    1 
ATOM   4534 C  CG    . MET A 1 606 ? -7.614  -29.029 34.081  1.00 84.60  ? 709  MET A CG    1 
ATOM   4535 S  SD    . MET A 1 606 ? -8.890  -28.102 34.958  1.00 95.07  ? 709  MET A SD    1 
ATOM   4536 C  CE    . MET A 1 606 ? -8.903  -28.935 36.547  1.00 80.25  ? 709  MET A CE    1 
ATOM   4537 N  N     . GLU A 1 607 ? -8.901  -33.142 32.365  1.00 92.21  ? 710  GLU A N     1 
ATOM   4538 C  CA    . GLU A 1 607 ? -9.389  -34.073 31.353  1.00 92.09  ? 710  GLU A CA    1 
ATOM   4539 C  C     . GLU A 1 607 ? -10.678 -34.749 31.802  1.00 97.79  ? 710  GLU A C     1 
ATOM   4540 O  O     . GLU A 1 607 ? -11.592 -34.958 30.995  1.00 99.49  ? 710  GLU A O     1 
ATOM   4541 C  CB    . GLU A 1 607 ? -8.312  -35.113 31.041  1.00 96.33  ? 710  GLU A CB    1 
ATOM   4542 C  CG    . GLU A 1 607 ? -8.029  -35.292 29.559  1.00 113.67 ? 710  GLU A CG    1 
ATOM   4543 C  CD    . GLU A 1 607 ? -9.180  -35.943 28.818  1.00 131.94 ? 710  GLU A CD    1 
ATOM   4544 O  OE1   . GLU A 1 607 ? -9.939  -36.706 29.452  1.00 126.86 ? 710  GLU A OE1   1 
ATOM   4545 O  OE2   . GLU A 1 607 ? -9.325  -35.691 27.603  1.00 131.76 ? 710  GLU A OE2   1 
ATOM   4546 N  N     . LYS A 1 608 ? -10.776 -35.093 33.088  1.00 94.50  ? 711  LYS A N     1 
ATOM   4547 C  CA    . LYS A 1 608 ? -11.995 -35.720 33.588  1.00 92.89  ? 711  LYS A CA    1 
ATOM   4548 C  C     . LYS A 1 608 ? -13.155 -34.733 33.637  1.00 89.08  ? 711  LYS A C     1 
ATOM   4549 O  O     . LYS A 1 608 ? -14.308 -35.124 33.420  1.00 88.16  ? 711  LYS A O     1 
ATOM   4550 C  CB    . LYS A 1 608 ? -11.750 -36.327 34.969  1.00 92.12  ? 711  LYS A CB    1 
ATOM   4551 C  CG    . LYS A 1 608 ? -10.786 -37.504 34.965  1.00 95.26  ? 711  LYS A CG    1 
ATOM   4552 C  CD    . LYS A 1 608 ? -11.280 -38.619 34.055  1.00 98.35  ? 711  LYS A CD    1 
ATOM   4553 C  CE    . LYS A 1 608 ? -10.278 -39.762 33.971  1.00 100.15 ? 711  LYS A CE    1 
ATOM   4554 N  NZ    . LYS A 1 608 ? -10.090 -40.447 35.279  1.00 108.60 ? 711  LYS A NZ    1 
ATOM   4555 N  N     . LEU A 1 609 ? -12.875 -33.457 33.916  1.00 89.34  ? 712  LEU A N     1 
ATOM   4556 C  CA    . LEU A 1 609 ? -13.935 -32.454 33.904  1.00 89.41  ? 712  LEU A CA    1 
ATOM   4557 C  C     . LEU A 1 609 ? -14.456 -32.208 32.495  1.00 90.78  ? 712  LEU A C     1 
ATOM   4558 O  O     . LEU A 1 609 ? -15.651 -31.947 32.315  1.00 90.08  ? 712  LEU A O     1 
ATOM   4559 C  CB    . LEU A 1 609 ? -13.435 -31.147 34.516  1.00 89.57  ? 712  LEU A CB    1 
ATOM   4560 C  CG    . LEU A 1 609 ? -13.090 -31.184 36.005  1.00 87.89  ? 712  LEU A CG    1 
ATOM   4561 C  CD1   . LEU A 1 609 ? -12.659 -29.808 36.481  1.00 86.57  ? 712  LEU A CD1   1 
ATOM   4562 C  CD2   . LEU A 1 609 ? -14.272 -31.694 36.815  1.00 82.40  ? 712  LEU A CD2   1 
ATOM   4563 N  N     . ILE A 1 610 ? -13.581 -32.285 31.491  1.00 95.79  ? 713  ILE A N     1 
ATOM   4564 C  CA    . ILE A 1 610 ? -14.015 -32.101 30.110  1.00 90.23  ? 713  ILE A CA    1 
ATOM   4565 C  C     . ILE A 1 610 ? -14.882 -33.272 29.666  1.00 90.92  ? 713  ILE A C     1 
ATOM   4566 O  O     . ILE A 1 610 ? -15.959 -33.083 29.089  1.00 90.46  ? 713  ILE A O     1 
ATOM   4567 C  CB    . ILE A 1 610 ? -12.798 -31.917 29.186  1.00 87.82  ? 713  ILE A CB    1 
ATOM   4568 C  CG1   . ILE A 1 610 ? -12.073 -30.611 29.515  1.00 84.10  ? 713  ILE A CG1   1 
ATOM   4569 C  CG2   . ILE A 1 610 ? -13.227 -31.937 27.730  1.00 94.60  ? 713  ILE A CG2   1 
ATOM   4570 C  CD1   . ILE A 1 610 ? -10.779 -30.427 28.764  1.00 72.39  ? 713  ILE A CD1   1 
ATOM   4571 N  N     . ASN A 1 611 ? -14.427 -34.500 29.933  1.00 90.82  ? 714  ASN A N     1 
ATOM   4572 C  CA    . ASN A 1 611 ? -15.199 -35.681 29.556  1.00 93.75  ? 714  ASN A CA    1 
ATOM   4573 C  C     . ASN A 1 611 ? -16.580 -35.669 30.197  1.00 96.15  ? 714  ASN A C     1 
ATOM   4574 O  O     . ASN A 1 611 ? -17.574 -36.028 29.556  1.00 100.47 ? 714  ASN A O     1 
ATOM   4575 C  CB    . ASN A 1 611 ? -14.446 -36.952 29.951  1.00 97.51  ? 714  ASN A CB    1 
ATOM   4576 C  CG    . ASN A 1 611 ? -13.081 -37.049 29.302  1.00 109.07 ? 714  ASN A CG    1 
ATOM   4577 O  OD1   . ASN A 1 611 ? -12.903 -36.675 28.143  1.00 108.48 ? 714  ASN A OD1   1 
ATOM   4578 N  ND2   . ASN A 1 611 ? -12.107 -37.554 30.051  1.00 115.12 ? 714  ASN A ND2   1 
ATOM   4579 N  N     . LEU A 1 612 ? -16.660 -35.256 31.463  1.00 96.13  ? 715  LEU A N     1 
ATOM   4580 C  CA    . LEU A 1 612 ? -17.946 -35.214 32.151  1.00 94.93  ? 715  LEU A CA    1 
ATOM   4581 C  C     . LEU A 1 612 ? -18.867 -34.171 31.530  1.00 94.41  ? 715  LEU A C     1 
ATOM   4582 O  O     . LEU A 1 612 ? -20.045 -34.444 31.270  1.00 94.57  ? 715  LEU A O     1 
ATOM   4583 C  CB    . LEU A 1 612 ? -17.727 -34.934 33.638  1.00 92.65  ? 715  LEU A CB    1 
ATOM   4584 C  CG    . LEU A 1 612 ? -18.960 -34.874 34.537  1.00 91.93  ? 715  LEU A CG    1 
ATOM   4585 C  CD1   . LEU A 1 612 ? -19.799 -36.130 34.386  1.00 99.52  ? 715  LEU A CD1   1 
ATOM   4586 C  CD2   . LEU A 1 612 ? -18.535 -34.685 35.981  1.00 92.74  ? 715  LEU A CD2   1 
ATOM   4587 N  N     . THR A 1 613 ? -18.344 -32.969 31.276  1.00 92.93  ? 716  THR A N     1 
ATOM   4588 C  CA    . THR A 1 613 ? -19.159 -31.924 30.666  1.00 93.83  ? 716  THR A CA    1 
ATOM   4589 C  C     . THR A 1 613 ? -19.537 -32.269 29.231  1.00 99.94  ? 716  THR A C     1 
ATOM   4590 O  O     . THR A 1 613 ? -20.562 -31.790 28.731  1.00 103.91 ? 716  THR A O     1 
ATOM   4591 C  CB    . THR A 1 613 ? -18.424 -30.585 30.711  1.00 91.36  ? 716  THR A CB    1 
ATOM   4592 O  OG1   . THR A 1 613 ? -17.094 -30.749 30.202  1.00 94.78  ? 716  THR A OG1   1 
ATOM   4593 C  CG2   . THR A 1 613 ? -18.360 -30.062 32.138  1.00 86.88  ? 716  THR A CG2   1 
ATOM   4594 N  N     . ASP A 1 614 ? -18.731 -33.089 28.553  1.00 99.13  ? 717  ASP A N     1 
ATOM   4595 C  CA    . ASP A 1 614 ? -19.081 -33.517 27.203  1.00 97.76  ? 717  ASP A CA    1 
ATOM   4596 C  C     . ASP A 1 614 ? -20.259 -34.483 27.226  1.00 100.80 ? 717  ASP A C     1 
ATOM   4597 O  O     . ASP A 1 614 ? -21.206 -34.342 26.442  1.00 103.19 ? 717  ASP A O     1 
ATOM   4598 C  CB    . ASP A 1 614 ? -17.871 -34.156 26.519  1.00 97.69  ? 717  ASP A CB    1 
ATOM   4599 C  CG    . ASP A 1 614 ? -16.775 -33.152 26.213  1.00 105.27 ? 717  ASP A CG    1 
ATOM   4600 O  OD1   . ASP A 1 614 ? -16.934 -31.966 26.574  1.00 106.17 ? 717  ASP A OD1   1 
ATOM   4601 O  OD2   . ASP A 1 614 ? -15.753 -33.549 25.612  1.00 102.74 ? 717  ASP A OD2   1 
ATOM   4602 N  N     . ILE A 1 615 ? -20.219 -35.473 28.121  1.00 100.41 ? 718  ILE A N     1 
ATOM   4603 C  CA    . ILE A 1 615 ? -21.336 -36.404 28.244  1.00 102.56 ? 718  ILE A CA    1 
ATOM   4604 C  C     . ILE A 1 615 ? -22.576 -35.687 28.761  1.00 106.28 ? 718  ILE A C     1 
ATOM   4605 O  O     . ILE A 1 615 ? -23.706 -36.068 28.434  1.00 112.14 ? 718  ILE A O     1 
ATOM   4606 C  CB    . ILE A 1 615 ? -20.948 -37.587 29.151  1.00 101.49 ? 718  ILE A CB    1 
ATOM   4607 C  CG1   . ILE A 1 615 ? -19.671 -38.254 28.641  1.00 105.24 ? 718  ILE A CG1   1 
ATOM   4608 C  CG2   . ILE A 1 615 ? -22.072 -38.608 29.214  1.00 103.41 ? 718  ILE A CG2   1 
ATOM   4609 C  CD1   . ILE A 1 615 ? -19.251 -39.465 29.449  1.00 110.93 ? 718  ILE A CD1   1 
ATOM   4610 N  N     . LEU A 1 616 ? -22.391 -34.634 29.559  1.00 103.00 ? 719  LEU A N     1 
ATOM   4611 C  CA    . LEU A 1 616 ? -23.532 -33.904 30.097  1.00 103.38 ? 719  LEU A CA    1 
ATOM   4612 C  C     . LEU A 1 616 ? -24.287 -33.152 29.007  1.00 111.33 ? 719  LEU A C     1 
ATOM   4613 O  O     . LEU A 1 616 ? -25.514 -33.023 29.082  1.00 114.87 ? 719  LEU A O     1 
ATOM   4614 C  CB    . LEU A 1 616 ? -23.063 -32.938 31.185  1.00 103.27 ? 719  LEU A CB    1 
ATOM   4615 C  CG    . LEU A 1 616 ? -24.130 -32.356 32.111  1.00 97.93  ? 719  LEU A CG    1 
ATOM   4616 C  CD1   . LEU A 1 616 ? -24.839 -33.465 32.874  1.00 97.68  ? 719  LEU A CD1   1 
ATOM   4617 C  CD2   . LEU A 1 616 ? -23.505 -31.357 33.068  1.00 75.99  ? 719  LEU A CD2   1 
ATOM   4618 N  N     . LYS A 1 617 ? -23.581 -32.660 27.988  1.00 112.83 ? 720  LYS A N     1 
ATOM   4619 C  CA    . LYS A 1 617 ? -24.209 -31.891 26.922  1.00 112.85 ? 720  LYS A CA    1 
ATOM   4620 C  C     . LYS A 1 617 ? -24.759 -32.761 25.799  1.00 120.74 ? 720  LYS A C     1 
ATOM   4621 O  O     . LYS A 1 617 ? -25.614 -32.297 25.037  1.00 132.90 ? 720  LYS A O     1 
ATOM   4622 C  CB    . LYS A 1 617 ? -23.210 -30.881 26.342  1.00 106.71 ? 720  LYS A CB    1 
ATOM   4623 C  CG    . LYS A 1 617 ? -23.842 -29.812 25.460  1.00 125.64 ? 720  LYS A CG    1 
ATOM   4624 C  CD    . LYS A 1 617 ? -22.796 -28.895 24.846  1.00 144.64 ? 720  LYS A CD    1 
ATOM   4625 C  CE    . LYS A 1 617 ? -23.437 -27.884 23.906  1.00 131.44 ? 720  LYS A CE    1 
ATOM   4626 N  NZ    . LYS A 1 617 ? -22.434 -26.966 23.300  1.00 121.49 ? 720  LYS A NZ    1 
ATOM   4627 N  N     . GLN A 1 618 ? -24.302 -34.005 25.679  1.00 120.21 ? 721  GLN A N     1 
ATOM   4628 C  CA    . GLN A 1 618 ? -24.773 -34.890 24.621  1.00 125.11 ? 721  GLN A CA    1 
ATOM   4629 C  C     . GLN A 1 618 ? -25.828 -35.880 25.091  1.00 127.55 ? 721  GLN A C     1 
ATOM   4630 O  O     . GLN A 1 618 ? -26.677 -36.289 24.292  1.00 130.32 ? 721  GLN A O     1 
ATOM   4631 C  CB    . GLN A 1 618 ? -23.593 -35.657 24.009  1.00 126.55 ? 721  GLN A CB    1 
ATOM   4632 C  CG    . GLN A 1 618 ? -23.955 -36.508 22.799  1.00 137.72 ? 721  GLN A CG    1 
ATOM   4633 C  CD    . GLN A 1 618 ? -24.649 -35.711 21.710  1.00 140.08 ? 721  GLN A CD    1 
ATOM   4634 O  OE1   . GLN A 1 618 ? -24.202 -34.626 21.338  1.00 141.25 ? 721  GLN A OE1   1 
ATOM   4635 N  NE2   . GLN A 1 618 ? -25.752 -36.245 21.198  1.00 136.71 ? 721  GLN A NE2   1 
ATOM   4636 N  N     . GLU A 1 619 ? -25.812 -36.261 26.367  1.00 132.30 ? 722  GLU A N     1 
ATOM   4637 C  CA    . GLU A 1 619 ? -26.734 -37.262 26.889  1.00 139.59 ? 722  GLU A CA    1 
ATOM   4638 C  C     . GLU A 1 619 ? -27.886 -36.664 27.687  1.00 139.42 ? 722  GLU A C     1 
ATOM   4639 O  O     . GLU A 1 619 ? -29.021 -37.139 27.571  1.00 137.87 ? 722  GLU A O     1 
ATOM   4640 C  CB    . GLU A 1 619 ? -25.977 -38.267 27.766  1.00 140.34 ? 722  GLU A CB    1 
ATOM   4641 C  CG    . GLU A 1 619 ? -26.780 -39.503 28.144  1.00 146.28 ? 722  GLU A CG    1 
ATOM   4642 C  CD    . GLU A 1 619 ? -26.972 -40.457 26.979  1.00 160.97 ? 722  GLU A CD    1 
ATOM   4643 O  OE1   . GLU A 1 619 ? -26.227 -40.343 25.983  1.00 157.44 ? 722  GLU A OE1   1 
ATOM   4644 O  OE2   . GLU A 1 619 ? -27.869 -41.323 27.061  1.00 162.49 ? 722  GLU A OE2   1 
ATOM   4645 N  N     . LYS A 1 620 ? -27.630 -35.637 28.496  1.00 125.32 ? 723  LYS A N     1 
ATOM   4646 C  CA    . LYS A 1 620 ? -28.636 -35.063 29.387  1.00 122.95 ? 723  LYS A CA    1 
ATOM   4647 C  C     . LYS A 1 620 ? -28.731 -33.554 29.193  1.00 121.91 ? 723  LYS A C     1 
ATOM   4648 O  O     . LYS A 1 620 ? -28.774 -32.781 30.152  1.00 121.75 ? 723  LYS A O     1 
ATOM   4649 C  CB    . LYS A 1 620 ? -28.319 -35.392 30.847  1.00 119.29 ? 723  LYS A CB    1 
ATOM   4650 C  CG    . LYS A 1 620 ? -27.755 -36.789 31.077  1.00 116.64 ? 723  LYS A CG    1 
ATOM   4651 C  CD    . LYS A 1 620 ? -28.666 -37.639 31.951  1.00 110.47 ? 723  LYS A CD    1 
ATOM   4652 C  CE    . LYS A 1 620 ? -29.956 -37.995 31.232  1.00 116.08 ? 723  LYS A CE    1 
ATOM   4653 N  NZ    . LYS A 1 620 ? -30.783 -38.953 32.016  1.00 109.50 ? 723  LYS A NZ    1 
ATOM   4654 N  N     . LYS A 1 621 ? -28.774 -33.111 27.935  1.00 123.09 ? 724  LYS A N     1 
ATOM   4655 C  CA    . LYS A 1 621 ? -28.833 -31.678 27.656  1.00 122.05 ? 724  LYS A CA    1 
ATOM   4656 C  C     . LYS A 1 621 ? -30.238 -31.126 27.870  1.00 122.31 ? 724  LYS A C     1 
ATOM   4657 O  O     . LYS A 1 621 ? -30.453 -30.255 28.720  1.00 122.17 ? 724  LYS A O     1 
ATOM   4658 C  CB    . LYS A 1 621 ? -28.363 -31.396 26.228  1.00 124.90 ? 724  LYS A CB    1 
ATOM   4659 C  CG    . LYS A 1 621 ? -28.378 -29.920 25.864  1.00 128.19 ? 724  LYS A CG    1 
ATOM   4660 C  CD    . LYS A 1 621 ? -28.005 -29.697 24.409  1.00 134.72 ? 724  LYS A CD    1 
ATOM   4661 C  CE    . LYS A 1 621 ? -28.070 -28.222 24.046  1.00 141.39 ? 724  LYS A CE    1 
ATOM   4662 N  NZ    . LYS A 1 621 ? -27.794 -27.992 22.601  1.00 145.03 ? 724  LYS A NZ    1 
ATOM   4663 N  N     . ASP A 1 622 ? -31.208 -31.620 27.099  1.00 123.82 ? 725  ASP A N     1 
ATOM   4664 C  CA    . ASP A 1 622 ? -32.578 -31.136 27.205  1.00 125.29 ? 725  ASP A CA    1 
ATOM   4665 C  C     . ASP A 1 622 ? -33.281 -31.616 28.468  1.00 132.00 ? 725  ASP A C     1 
ATOM   4666 O  O     . ASP A 1 622 ? -34.408 -31.182 28.728  1.00 130.93 ? 725  ASP A O     1 
ATOM   4667 C  CB    . ASP A 1 622 ? -33.378 -31.560 25.972  1.00 134.44 ? 725  ASP A CB    1 
ATOM   4668 C  CG    . ASP A 1 622 ? -33.229 -33.036 25.658  1.00 149.30 ? 725  ASP A CG    1 
ATOM   4669 O  OD1   . ASP A 1 622 ? -32.467 -33.722 26.372  1.00 148.11 ? 725  ASP A OD1   1 
ATOM   4670 O  OD2   . ASP A 1 622 ? -33.871 -33.510 24.697  1.00 150.24 ? 725  ASP A OD2   1 
ATOM   4671 N  N     . GLU A 1 623 ? -32.654 -32.493 29.248  1.00 130.96 ? 726  GLU A N     1 
ATOM   4672 C  CA    . GLU A 1 623 ? -33.241 -32.948 30.498  1.00 121.99 ? 726  GLU A CA    1 
ATOM   4673 C  C     . GLU A 1 623 ? -33.277 -31.812 31.516  1.00 111.19 ? 726  GLU A C     1 
ATOM   4674 O  O     . GLU A 1 623 ? -32.508 -30.849 31.443  1.00 104.57 ? 726  GLU A O     1 
ATOM   4675 C  CB    . GLU A 1 623 ? -32.450 -34.127 31.065  1.00 120.68 ? 726  GLU A CB    1 
ATOM   4676 C  CG    . GLU A 1 623 ? -32.362 -35.337 30.146  1.00 125.09 ? 726  GLU A CG    1 
ATOM   4677 C  CD    . GLU A 1 623 ? -33.589 -36.229 30.220  1.00 135.38 ? 726  GLU A CD    1 
ATOM   4678 O  OE1   . GLU A 1 623 ? -34.605 -35.809 30.814  1.00 129.22 ? 726  GLU A OE1   1 
ATOM   4679 O  OE2   . GLU A 1 623 ? -33.533 -37.357 29.686  1.00 148.18 ? 726  GLU A OE2   1 
ATOM   4680 N  N     . THR A 1 624 ? -34.186 -31.936 32.481  1.00 111.94 ? 727  THR A N     1 
ATOM   4681 C  CA    . THR A 1 624 ? -34.292 -30.934 33.529  1.00 106.90 ? 727  THR A CA    1 
ATOM   4682 C  C     . THR A 1 624 ? -33.025 -30.920 34.381  1.00 102.17 ? 727  THR A C     1 
ATOM   4683 O  O     . THR A 1 624 ? -32.246 -31.877 34.404  1.00 101.04 ? 727  THR A O     1 
ATOM   4684 C  CB    . THR A 1 624 ? -35.516 -31.195 34.409  1.00 103.57 ? 727  THR A CB    1 
ATOM   4685 O  OG1   . THR A 1 624 ? -35.729 -30.076 35.276  1.00 116.45 ? 727  THR A OG1   1 
ATOM   4686 C  CG2   . THR A 1 624 ? -35.312 -32.442 35.252  1.00 100.51 ? 727  THR A CG2   1 
ATOM   4687 N  N     . GLN A 1 625 ? -32.823 -29.804 35.086  1.00 100.15 ? 728  GLN A N     1 
ATOM   4688 C  CA    . GLN A 1 625 ? -31.605 -29.641 35.873  1.00 99.94  ? 728  GLN A CA    1 
ATOM   4689 C  C     . GLN A 1 625 ? -31.521 -30.664 36.999  1.00 100.27 ? 728  GLN A C     1 
ATOM   4690 O  O     . GLN A 1 625 ? -30.418 -31.041 37.411  1.00 98.56  ? 728  GLN A O     1 
ATOM   4691 C  CB    . GLN A 1 625 ? -31.529 -28.217 36.427  1.00 98.26  ? 728  GLN A CB    1 
ATOM   4692 C  CG    . GLN A 1 625 ? -30.128 -27.762 36.813  1.00 98.47  ? 728  GLN A CG    1 
ATOM   4693 C  CD    . GLN A 1 625 ? -29.854 -27.885 38.300  1.00 104.39 ? 728  GLN A CD    1 
ATOM   4694 O  OE1   . GLN A 1 625 ? -30.564 -28.585 39.021  1.00 114.37 ? 728  GLN A OE1   1 
ATOM   4695 N  NE2   . GLN A 1 625 ? -28.820 -27.194 38.768  1.00 99.97  ? 728  GLN A NE2   1 
ATOM   4696 N  N     . LYS A 1 626 ? -32.668 -31.127 37.505  1.00 101.64 ? 729  LYS A N     1 
ATOM   4697 C  CA    . LYS A 1 626 ? -32.659 -32.186 38.510  1.00 100.58 ? 729  LYS A CA    1 
ATOM   4698 C  C     . LYS A 1 626 ? -32.077 -33.475 37.943  1.00 103.71 ? 729  LYS A C     1 
ATOM   4699 O  O     . LYS A 1 626 ? -31.223 -34.113 38.570  1.00 107.21 ? 729  LYS A O     1 
ATOM   4700 C  CB    . LYS A 1 626 ? -34.074 -32.429 39.037  1.00 105.94 ? 729  LYS A CB    1 
ATOM   4701 C  CG    . LYS A 1 626 ? -34.610 -31.336 39.940  1.00 114.90 ? 729  LYS A CG    1 
ATOM   4702 C  CD    . LYS A 1 626 ? -35.949 -31.740 40.538  1.00 119.92 ? 729  LYS A CD    1 
ATOM   4703 C  CE    . LYS A 1 626 ? -35.836 -33.044 41.314  1.00 122.37 ? 729  LYS A CE    1 
ATOM   4704 N  NZ    . LYS A 1 626 ? -37.136 -33.449 41.919  1.00 124.03 ? 729  LYS A NZ    1 
ATOM   4705 N  N     . VAL A 1 627 ? -32.534 -33.875 36.753  1.00 106.16 ? 730  VAL A N     1 
ATOM   4706 C  CA    . VAL A 1 627 ? -32.033 -35.098 36.131  1.00 102.44 ? 730  VAL A CA    1 
ATOM   4707 C  C     . VAL A 1 627 ? -30.542 -34.979 35.843  1.00 101.60 ? 730  VAL A C     1 
ATOM   4708 O  O     . VAL A 1 627 ? -29.784 -35.943 36.007  1.00 102.82 ? 730  VAL A O     1 
ATOM   4709 C  CB    . VAL A 1 627 ? -32.840 -35.415 34.856  1.00 104.48 ? 730  VAL A CB    1 
ATOM   4710 C  CG1   . VAL A 1 627 ? -32.145 -36.486 34.030  1.00 111.01 ? 730  VAL A CG1   1 
ATOM   4711 C  CG2   . VAL A 1 627 ? -34.244 -35.863 35.222  1.00 100.48 ? 730  VAL A CG2   1 
ATOM   4712 N  N     . GLN A 1 628 ? -30.095 -33.792 35.421  1.00 101.58 ? 731  GLN A N     1 
ATOM   4713 C  CA    . GLN A 1 628 ? -28.670 -33.584 35.182  1.00 100.42 ? 731  GLN A CA    1 
ATOM   4714 C  C     . GLN A 1 628 ? -27.868 -33.736 36.467  1.00 101.70 ? 731  GLN A C     1 
ATOM   4715 O  O     . GLN A 1 628 ? -26.740 -34.242 36.448  1.00 105.61 ? 731  GLN A O     1 
ATOM   4716 C  CB    . GLN A 1 628 ? -28.432 -32.204 34.569  1.00 99.34  ? 731  GLN A CB    1 
ATOM   4717 C  CG    . GLN A 1 628 ? -29.143 -31.969 33.249  1.00 104.08 ? 731  GLN A CG    1 
ATOM   4718 C  CD    . GLN A 1 628 ? -28.857 -30.595 32.676  1.00 106.83 ? 731  GLN A CD    1 
ATOM   4719 O  OE1   . GLN A 1 628 ? -28.076 -29.826 33.237  1.00 102.79 ? 731  GLN A OE1   1 
ATOM   4720 N  NE2   . GLN A 1 628 ? -29.491 -30.277 31.552  1.00 111.37 ? 731  GLN A NE2   1 
ATOM   4721 N  N     . MET A 1 629 ? -28.434 -33.304 37.597  1.00 100.36 ? 732  MET A N     1 
ATOM   4722 C  CA    . MET A 1 629 ? -27.717 -33.397 38.864  1.00 98.47  ? 732  MET A CA    1 
ATOM   4723 C  C     . MET A 1 629 ? -27.547 -34.846 39.302  1.00 101.99 ? 732  MET A C     1 
ATOM   4724 O  O     . MET A 1 629 ? -26.482 -35.225 39.803  1.00 103.17 ? 732  MET A O     1 
ATOM   4725 C  CB    . MET A 1 629 ? -28.441 -32.587 39.938  1.00 102.76 ? 732  MET A CB    1 
ATOM   4726 C  CG    . MET A 1 629 ? -28.282 -31.085 39.781  1.00 99.38  ? 732  MET A CG    1 
ATOM   4727 S  SD    . MET A 1 629 ? -26.550 -30.580 39.800  1.00 96.87  ? 732  MET A SD    1 
ATOM   4728 C  CE    . MET A 1 629 ? -26.065 -31.103 41.443  1.00 94.43  ? 732  MET A CE    1 
ATOM   4729 N  N     . LYS A 1 630 ? -28.585 -35.669 39.127  1.00 101.43 ? 733  LYS A N     1 
ATOM   4730 C  CA    . LYS A 1 630 ? -28.465 -37.085 39.457  1.00 106.17 ? 733  LYS A CA    1 
ATOM   4731 C  C     . LYS A 1 630 ? -27.386 -37.749 38.612  1.00 108.39 ? 733  LYS A C     1 
ATOM   4732 O  O     . LYS A 1 630 ? -26.620 -38.584 39.109  1.00 113.69 ? 733  LYS A O     1 
ATOM   4733 C  CB    . LYS A 1 630 ? -29.809 -37.787 39.263  1.00 103.15 ? 733  LYS A CB    1 
ATOM   4734 C  CG    . LYS A 1 630 ? -30.974 -37.069 39.919  1.00 113.33 ? 733  LYS A CG    1 
ATOM   4735 C  CD    . LYS A 1 630 ? -30.747 -36.898 41.411  1.00 141.47 ? 733  LYS A CD    1 
ATOM   4736 C  CE    . LYS A 1 630 ? -31.638 -35.806 41.981  1.00 137.60 ? 733  LYS A CE    1 
ATOM   4737 N  NZ    . LYS A 1 630 ? -31.294 -34.469 41.416  1.00 114.28 ? 733  LYS A NZ    1 
ATOM   4738 N  N     . PHE A 1 631 ? -27.308 -37.384 37.332  1.00 106.94 ? 734  PHE A N     1 
ATOM   4739 C  CA    . PHE A 1 631 ? -26.228 -37.873 36.485  1.00 109.15 ? 734  PHE A CA    1 
ATOM   4740 C  C     . PHE A 1 631 ? -24.879 -37.325 36.933  1.00 103.55 ? 734  PHE A C     1 
ATOM   4741 O  O     . PHE A 1 631 ? -23.864 -38.023 36.838  1.00 104.56 ? 734  PHE A O     1 
ATOM   4742 C  CB    . PHE A 1 631 ? -26.500 -37.497 35.028  1.00 107.35 ? 734  PHE A CB    1 
ATOM   4743 C  CG    . PHE A 1 631 ? -25.533 -38.102 34.054  1.00 109.16 ? 734  PHE A CG    1 
ATOM   4744 C  CD1   . PHE A 1 631 ? -25.729 -39.387 33.574  1.00 117.25 ? 734  PHE A CD1   1 
ATOM   4745 C  CD2   . PHE A 1 631 ? -24.434 -37.386 33.610  1.00 107.16 ? 734  PHE A CD2   1 
ATOM   4746 C  CE1   . PHE A 1 631 ? -24.844 -39.949 32.676  1.00 115.85 ? 734  PHE A CE1   1 
ATOM   4747 C  CE2   . PHE A 1 631 ? -23.544 -37.942 32.712  1.00 110.33 ? 734  PHE A CE2   1 
ATOM   4748 C  CZ    . PHE A 1 631 ? -23.751 -39.226 32.245  1.00 119.51 ? 734  PHE A CZ    1 
ATOM   4749 N  N     . LEU A 1 632 ? -24.848 -36.087 37.430  1.00 102.82 ? 735  LEU A N     1 
ATOM   4750 C  CA    . LEU A 1 632 ? -23.587 -35.485 37.853  1.00 102.20 ? 735  LEU A CA    1 
ATOM   4751 C  C     . LEU A 1 632 ? -23.057 -36.146 39.120  1.00 102.49 ? 735  LEU A C     1 
ATOM   4752 O  O     . LEU A 1 632 ? -21.873 -36.494 39.200  1.00 102.55 ? 735  LEU A O     1 
ATOM   4753 C  CB    . LEU A 1 632 ? -23.769 -33.983 38.070  1.00 99.72  ? 735  LEU A CB    1 
ATOM   4754 C  CG    . LEU A 1 632 ? -22.510 -33.195 38.437  1.00 98.45  ? 735  LEU A CG    1 
ATOM   4755 C  CD1   . LEU A 1 632 ? -21.574 -33.107 37.245  1.00 97.11  ? 735  LEU A CD1   1 
ATOM   4756 C  CD2   . LEU A 1 632 ? -22.862 -31.807 38.950  1.00 97.69  ? 735  LEU A CD2   1 
ATOM   4757 N  N     . VAL A 1 633 ? -23.921 -36.330 40.122  1.00 102.93 ? 736  VAL A N     1 
ATOM   4758 C  CA    . VAL A 1 633 ? -23.462 -36.873 41.397  1.00 103.67 ? 736  VAL A CA    1 
ATOM   4759 C  C     . VAL A 1 633 ? -23.028 -38.326 41.251  1.00 106.46 ? 736  VAL A C     1 
ATOM   4760 O  O     . VAL A 1 633 ? -22.172 -38.802 42.007  1.00 109.25 ? 736  VAL A O     1 
ATOM   4761 C  CB    . VAL A 1 633 ? -24.551 -36.716 42.476  1.00 97.45  ? 736  VAL A CB    1 
ATOM   4762 C  CG1   . VAL A 1 633 ? -24.867 -35.245 42.703  1.00 90.43  ? 736  VAL A CG1   1 
ATOM   4763 C  CG2   . VAL A 1 633 ? -25.807 -37.486 42.092  1.00 100.47 ? 736  VAL A CG2   1 
ATOM   4764 N  N     . GLU A 1 634 ? -23.594 -39.052 40.285  1.00 107.76 ? 737  GLU A N     1 
ATOM   4765 C  CA    . GLU A 1 634 ? -23.206 -40.445 40.090  1.00 111.44 ? 737  GLU A CA    1 
ATOM   4766 C  C     . GLU A 1 634 ? -21.838 -40.547 39.429  1.00 112.78 ? 737  GLU A C     1 
ATOM   4767 O  O     . GLU A 1 634 ? -20.982 -41.326 39.865  1.00 117.15 ? 737  GLU A O     1 
ATOM   4768 C  CB    . GLU A 1 634 ? -24.261 -41.177 39.261  1.00 113.18 ? 737  GLU A CB    1 
ATOM   4769 C  CG    . GLU A 1 634 ? -25.517 -41.539 40.030  1.00 115.80 ? 737  GLU A CG    1 
ATOM   4770 C  CD    . GLU A 1 634 ? -26.482 -42.366 39.204  1.00 121.15 ? 737  GLU A CD    1 
ATOM   4771 O  OE1   . GLU A 1 634 ? -26.355 -42.360 37.960  1.00 122.62 ? 737  GLU A OE1   1 
ATOM   4772 O  OE2   . GLU A 1 634 ? -27.361 -43.028 39.796  1.00 120.65 ? 737  GLU A OE2   1 
ATOM   4773 N  N     . GLN A 1 635 ? -21.611 -39.767 38.371  1.00 109.03 ? 738  GLN A N     1 
ATOM   4774 C  CA    . GLN A 1 635 ? -20.338 -39.819 37.666  1.00 112.99 ? 738  GLN A CA    1 
ATOM   4775 C  C     . GLN A 1 635 ? -19.198 -39.195 38.458  1.00 108.77 ? 738  GLN A C     1 
ATOM   4776 O  O     . GLN A 1 635 ? -18.036 -39.375 38.080  1.00 111.77 ? 738  GLN A O     1 
ATOM   4777 C  CB    . GLN A 1 635 ? -20.460 -39.129 36.307  1.00 109.83 ? 738  GLN A CB    1 
ATOM   4778 C  CG    . GLN A 1 635 ? -21.576 -39.678 35.437  1.00 113.30 ? 738  GLN A CG    1 
ATOM   4779 C  CD    . GLN A 1 635 ? -21.534 -41.187 35.319  1.00 128.52 ? 738  GLN A CD    1 
ATOM   4780 O  OE1   . GLN A 1 635 ? -20.499 -41.767 34.988  1.00 135.45 ? 738  GLN A OE1   1 
ATOM   4781 N  NE2   . GLN A 1 635 ? -22.660 -41.835 35.597  1.00 128.29 ? 738  GLN A NE2   1 
ATOM   4782 N  N     . MET A 1 636 ? -19.494 -38.470 39.535  1.00 108.68 ? 739  MET A N     1 
ATOM   4783 C  CA    . MET A 1 636 ? -18.457 -37.871 40.364  1.00 107.18 ? 739  MET A CA    1 
ATOM   4784 C  C     . MET A 1 636 ? -18.117 -38.697 41.594  1.00 112.03 ? 739  MET A C     1 
ATOM   4785 O  O     . MET A 1 636 ? -16.975 -38.646 42.061  1.00 110.57 ? 739  MET A O     1 
ATOM   4786 C  CB    . MET A 1 636 ? -18.872 -36.463 40.805  1.00 105.03 ? 739  MET A CB    1 
ATOM   4787 C  CG    . MET A 1 636 ? -18.942 -35.451 39.673  1.00 102.88 ? 739  MET A CG    1 
ATOM   4788 S  SD    . MET A 1 636 ? -19.319 -33.784 40.248  1.00 107.34 ? 739  MET A SD    1 
ATOM   4789 C  CE    . MET A 1 636 ? -17.859 -33.419 41.220  1.00 95.93  ? 739  MET A CE    1 
ATOM   4790 N  N     . ARG A 1 637 ? -19.073 -39.458 42.129  1.00 122.80 ? 740  ARG A N     1 
ATOM   4791 C  CA    . ARG A 1 637 ? -18.821 -40.275 43.308  1.00 116.10 ? 740  ARG A CA    1 
ATOM   4792 C  C     . ARG A 1 637 ? -18.040 -41.545 42.997  1.00 121.31 ? 740  ARG A C     1 
ATOM   4793 O  O     . ARG A 1 637 ? -17.622 -42.237 43.932  1.00 123.54 ? 740  ARG A O     1 
ATOM   4794 C  CB    . ARG A 1 637 ? -20.143 -40.641 43.990  1.00 114.30 ? 740  ARG A CB    1 
ATOM   4795 C  CG    . ARG A 1 637 ? -21.027 -41.572 43.177  1.00 116.63 ? 740  ARG A CG    1 
ATOM   4796 C  CD    . ARG A 1 637 ? -22.339 -41.848 43.895  1.00 125.24 ? 740  ARG A CD    1 
ATOM   4797 N  NE    . ARG A 1 637 ? -23.223 -42.702 43.111  1.00 139.46 ? 740  ARG A NE    1 
ATOM   4798 C  CZ    . ARG A 1 637 ? -24.443 -43.063 43.486  1.00 143.50 ? 740  ARG A CZ    1 
ATOM   4799 N  NH1   . ARG A 1 637 ? -24.960 -42.661 44.636  1.00 144.66 ? 740  ARG A NH1   1 
ATOM   4800 N  NH2   . ARG A 1 637 ? -25.163 -43.846 42.687  1.00 139.51 ? 740  ARG A NH2   1 
ATOM   4801 N  N     . ARG A 1 638 ? -17.839 -41.870 41.722  1.00 116.40 ? 741  ARG A N     1 
ATOM   4802 C  CA    . ARG A 1 638 ? -17.052 -43.039 41.369  1.00 118.93 ? 741  ARG A CA    1 
ATOM   4803 C  C     . ARG A 1 638 ? -15.603 -42.844 41.816  1.00 116.77 ? 741  ARG A C     1 
ATOM   4804 O  O     . ARG A 1 638 ? -15.117 -41.712 41.896  1.00 118.53 ? 741  ARG A O     1 
ATOM   4805 C  CB    . ARG A 1 638 ? -17.116 -43.293 39.863  1.00 126.66 ? 741  ARG A CB    1 
ATOM   4806 C  CG    . ARG A 1 638 ? -16.749 -42.093 39.011  1.00 130.26 ? 741  ARG A CG    1 
ATOM   4807 C  CD    . ARG A 1 638 ? -16.742 -42.449 37.533  1.00 132.48 ? 741  ARG A CD    1 
ATOM   4808 N  NE    . ARG A 1 638 ? -17.964 -43.134 37.131  1.00 132.38 ? 741  ARG A NE    1 
ATOM   4809 C  CZ    . ARG A 1 638 ? -18.191 -43.606 35.913  1.00 139.26 ? 741  ARG A CZ    1 
ATOM   4810 N  NH1   . ARG A 1 638 ? -17.298 -43.481 34.945  1.00 143.52 ? 741  ARG A NH1   1 
ATOM   4811 N  NH2   . ARG A 1 638 ? -19.343 -44.222 35.660  1.00 143.33 ? 741  ARG A NH2   1 
ATOM   4812 N  N     . PRO A 1 639 ? -14.889 -43.933 42.119  1.00 121.33 ? 742  PRO A N     1 
ATOM   4813 C  CA    . PRO A 1 639 ? -13.542 -43.771 42.693  1.00 121.30 ? 742  PRO A CA    1 
ATOM   4814 C  C     . PRO A 1 639 ? -12.534 -43.175 41.727  1.00 122.32 ? 742  PRO A C     1 
ATOM   4815 O  O     . PRO A 1 639 ? -11.686 -42.376 42.148  1.00 119.63 ? 742  PRO A O     1 
ATOM   4816 C  CB    . PRO A 1 639 ? -13.167 -45.202 43.100  1.00 123.92 ? 742  PRO A CB    1 
ATOM   4817 C  CG    . PRO A 1 639 ? -13.967 -46.066 42.191  1.00 131.55 ? 742  PRO A CG    1 
ATOM   4818 C  CD    . PRO A 1 639 ? -15.270 -45.351 41.999  1.00 126.76 ? 742  PRO A CD    1 
ATOM   4819 N  N     . ASP A 1 640 ? -12.594 -43.539 40.443  1.00 124.88 ? 743  ASP A N     1 
ATOM   4820 C  CA    . ASP A 1 640 ? -11.610 -43.034 39.490  1.00 119.11 ? 743  ASP A CA    1 
ATOM   4821 C  C     . ASP A 1 640 ? -11.736 -41.530 39.289  1.00 116.02 ? 743  ASP A C     1 
ATOM   4822 O  O     . ASP A 1 640 ? -10.740 -40.862 38.985  1.00 115.04 ? 743  ASP A O     1 
ATOM   4823 C  CB    . ASP A 1 640 ? -11.745 -43.765 38.154  1.00 132.27 ? 743  ASP A CB    1 
ATOM   4824 C  CG    . ASP A 1 640 ? -13.176 -43.815 37.660  1.00 142.61 ? 743  ASP A CG    1 
ATOM   4825 O  OD1   . ASP A 1 640 ? -14.088 -43.979 38.498  1.00 139.19 ? 743  ASP A OD1   1 
ATOM   4826 O  OD2   . ASP A 1 640 ? -13.389 -43.689 36.436  1.00 139.43 ? 743  ASP A OD2   1 
ATOM   4827 N  N     . PHE A 1 641 ? -12.940 -40.978 39.452  1.00 113.21 ? 744  PHE A N     1 
ATOM   4828 C  CA    . PHE A 1 641 ? -13.111 -39.533 39.352  1.00 108.09 ? 744  PHE A CA    1 
ATOM   4829 C  C     . PHE A 1 641 ? -12.699 -38.834 40.641  1.00 104.83 ? 744  PHE A C     1 
ATOM   4830 O  O     . PHE A 1 641 ? -12.138 -37.734 40.601  1.00 100.00 ? 744  PHE A O     1 
ATOM   4831 C  CB    . PHE A 1 641 ? -14.563 -39.199 39.004  1.00 105.49 ? 744  PHE A CB    1 
ATOM   4832 C  CG    . PHE A 1 641 ? -14.809 -37.737 38.753  1.00 99.89  ? 744  PHE A CG    1 
ATOM   4833 C  CD1   . PHE A 1 641 ? -15.145 -36.885 39.794  1.00 99.95  ? 744  PHE A CD1   1 
ATOM   4834 C  CD2   . PHE A 1 641 ? -14.710 -37.215 37.475  1.00 96.15  ? 744  PHE A CD2   1 
ATOM   4835 C  CE1   . PHE A 1 641 ? -15.373 -35.541 39.565  1.00 96.02  ? 744  PHE A CE1   1 
ATOM   4836 C  CE2   . PHE A 1 641 ? -14.938 -35.872 37.238  1.00 93.17  ? 744  PHE A CE2   1 
ATOM   4837 C  CZ    . PHE A 1 641 ? -15.270 -35.034 38.285  1.00 95.65  ? 744  PHE A CZ    1 
ATOM   4838 N  N     . MET A 1 642 ? -12.975 -39.455 41.790  1.00 108.87 ? 745  MET A N     1 
ATOM   4839 C  CA    . MET A 1 642 ? -12.608 -38.850 43.066  1.00 102.10 ? 745  MET A CA    1 
ATOM   4840 C  C     . MET A 1 642 ? -11.095 -38.789 43.238  1.00 102.81 ? 745  MET A C     1 
ATOM   4841 O  O     . MET A 1 642 ? -10.571 -37.842 43.831  1.00 99.17  ? 745  MET A O     1 
ATOM   4842 C  CB    . MET A 1 642 ? -13.246 -39.627 44.217  1.00 111.39 ? 745  MET A CB    1 
ATOM   4843 C  CG    . MET A 1 642 ? -14.765 -39.566 44.250  1.00 112.67 ? 745  MET A CG    1 
ATOM   4844 S  SD    . MET A 1 642 ? -15.402 -37.972 44.801  1.00 124.40 ? 745  MET A SD    1 
ATOM   4845 C  CE    . MET A 1 642 ? -14.886 -37.979 46.516  1.00 106.90 ? 745  MET A CE    1 
ATOM   4846 N  N     . ASP A 1 643 ? -10.376 -39.789 42.726  1.00 107.07 ? 746  ASP A N     1 
ATOM   4847 C  CA    . ASP A 1 643 ? -8.927  -39.808 42.889  1.00 107.76 ? 746  ASP A CA    1 
ATOM   4848 C  C     . ASP A 1 643 ? -8.239  -38.827 41.952  1.00 99.92  ? 746  ASP A C     1 
ATOM   4849 O  O     . ASP A 1 643 ? -7.125  -38.374 42.243  1.00 101.12 ? 746  ASP A O     1 
ATOM   4850 C  CB    . ASP A 1 643 ? -8.385  -41.221 42.665  1.00 113.42 ? 746  ASP A CB    1 
ATOM   4851 C  CG    . ASP A 1 643 ? -8.915  -42.217 43.681  1.00 125.24 ? 746  ASP A CG    1 
ATOM   4852 O  OD1   . ASP A 1 643 ? -9.824  -41.859 44.457  1.00 124.09 ? 746  ASP A OD1   1 
ATOM   4853 O  OD2   . ASP A 1 643 ? -8.417  -43.361 43.700  1.00 122.80 ? 746  ASP A OD2   1 
ATOM   4854 N  N     . ALA A 1 644 ? -8.875  -38.488 40.834  1.00 97.84  ? 747  ALA A N     1 
ATOM   4855 C  CA    . ALA A 1 644 ? -8.282  -37.572 39.871  1.00 98.67  ? 747  ALA A CA    1 
ATOM   4856 C  C     . ALA A 1 644 ? -8.607  -36.113 40.157  1.00 95.49  ? 747  ALA A C     1 
ATOM   4857 O  O     . ALA A 1 644 ? -7.865  -35.229 39.713  1.00 93.92  ? 747  ALA A O     1 
ATOM   4858 C  CB    . ALA A 1 644 ? -8.741  -37.927 38.453  1.00 99.21  ? 747  ALA A CB    1 
ATOM   4859 N  N     . LEU A 1 645 ? -9.685  -35.840 40.888  1.00 92.45  ? 748  LEU A N     1 
ATOM   4860 C  CA    . LEU A 1 645 ? -10.116 -34.478 41.170  1.00 91.95  ? 748  LEU A CA    1 
ATOM   4861 C  C     . LEU A 1 645 ? -9.790  -34.035 42.590  1.00 91.45  ? 748  LEU A C     1 
ATOM   4862 O  O     . LEU A 1 645 ? -10.236 -32.962 43.008  1.00 90.67  ? 748  LEU A O     1 
ATOM   4863 C  CB    . LEU A 1 645 ? -11.618 -34.335 40.913  1.00 93.01  ? 748  LEU A CB    1 
ATOM   4864 C  CG    . LEU A 1 645 ? -12.033 -33.853 39.521  1.00 90.76  ? 748  LEU A CG    1 
ATOM   4865 C  CD1   . LEU A 1 645 ? -11.444 -32.480 39.241  1.00 88.18  ? 748  LEU A CD1   1 
ATOM   4866 C  CD2   . LEU A 1 645 ? -11.624 -34.846 38.441  1.00 91.64  ? 748  LEU A CD2   1 
ATOM   4867 N  N     . GLN A 1 646 ? -9.022  -34.826 43.336  1.00 95.83  ? 749  GLN A N     1 
ATOM   4868 C  CA    . GLN A 1 646 ? -8.659  -34.499 44.709  1.00 92.70  ? 749  GLN A CA    1 
ATOM   4869 C  C     . GLN A 1 646 ? -7.164  -34.702 44.899  1.00 92.04  ? 749  GLN A C     1 
ATOM   4870 O  O     . GLN A 1 646 ? -6.629  -35.760 44.555  1.00 94.47  ? 749  GLN A O     1 
ATOM   4871 C  CB    . GLN A 1 646 ? -9.440  -35.356 45.711  1.00 90.27  ? 749  GLN A CB    1 
ATOM   4872 C  CG    . GLN A 1 646 ? -10.923 -35.035 45.780  1.00 93.72  ? 749  GLN A CG    1 
ATOM   4873 C  CD    . GLN A 1 646 ? -11.681 -35.972 46.700  1.00 96.84  ? 749  GLN A CD    1 
ATOM   4874 O  OE1   . GLN A 1 646 ? -12.668 -35.583 47.326  1.00 98.13  ? 749  GLN A OE1   1 
ATOM   4875 N  NE2   . GLN A 1 646 ? -11.226 -37.217 46.781  1.00 92.74  ? 749  GLN A NE2   1 
ATOM   4876 N  N     . GLY A 1 647 ? -6.497  -33.688 45.444  1.00 88.11  ? 750  GLY A N     1 
ATOM   4877 C  CA    . GLY A 1 647 ? -5.088  -33.796 45.762  1.00 88.78  ? 750  GLY A CA    1 
ATOM   4878 C  C     . GLY A 1 647 ? -4.165  -33.270 44.683  1.00 92.27  ? 750  GLY A C     1 
ATOM   4879 O  O     . GLY A 1 647 ? -3.080  -33.820 44.468  1.00 97.57  ? 750  GLY A O     1 
ATOM   4880 N  N     . PHE A 1 648 ? -4.579  -32.204 44.000  1.00 88.80  ? 751  PHE A N     1 
ATOM   4881 C  CA    . PHE A 1 648 ? -3.776  -31.585 42.957  1.00 86.27  ? 751  PHE A CA    1 
ATOM   4882 C  C     . PHE A 1 648 ? -3.796  -30.073 43.138  1.00 84.23  ? 751  PHE A C     1 
ATOM   4883 O  O     . PHE A 1 648 ? -4.562  -29.528 43.937  1.00 84.04  ? 751  PHE A O     1 
ATOM   4884 C  CB    . PHE A 1 648 ? -4.275  -31.973 41.555  1.00 87.29  ? 751  PHE A CB    1 
ATOM   4885 C  CG    . PHE A 1 648 ? -5.611  -31.386 41.197  1.00 86.34  ? 751  PHE A CG    1 
ATOM   4886 C  CD1   . PHE A 1 648 ? -6.783  -31.958 41.663  1.00 85.55  ? 751  PHE A CD1   1 
ATOM   4887 C  CD2   . PHE A 1 648 ? -5.694  -30.272 40.380  1.00 84.60  ? 751  PHE A CD2   1 
ATOM   4888 C  CE1   . PHE A 1 648 ? -8.011  -31.420 41.331  1.00 86.64  ? 751  PHE A CE1   1 
ATOM   4889 C  CE2   . PHE A 1 648 ? -6.918  -29.730 40.044  1.00 85.49  ? 751  PHE A CE2   1 
ATOM   4890 C  CZ    . PHE A 1 648 ? -8.079  -30.305 40.520  1.00 86.38  ? 751  PHE A CZ    1 
ATOM   4891 N  N     . LEU A 1 649 ? -2.940  -29.395 42.379  1.00 82.25  ? 752  LEU A N     1 
ATOM   4892 C  CA    . LEU A 1 649 ? -2.760  -27.956 42.512  1.00 84.00  ? 752  LEU A CA    1 
ATOM   4893 C  C     . LEU A 1 649 ? -3.733  -27.209 41.610  1.00 84.78  ? 752  LEU A C     1 
ATOM   4894 O  O     . LEU A 1 649 ? -4.049  -27.658 40.504  1.00 87.01  ? 752  LEU A O     1 
ATOM   4895 C  CB    . LEU A 1 649 ? -1.321  -27.552 42.177  1.00 82.95  ? 752  LEU A CB    1 
ATOM   4896 C  CG    . LEU A 1 649 ? -0.186  -28.117 43.040  1.00 85.34  ? 752  LEU A CG    1 
ATOM   4897 C  CD1   . LEU A 1 649 ? 0.194   -29.528 42.613  1.00 82.41  ? 752  LEU A CD1   1 
ATOM   4898 C  CD2   . LEU A 1 649 ? 1.030   -27.207 43.001  1.00 81.85  ? 752  LEU A CD2   1 
ATOM   4899 N  N     . SER A 1 650 ? -4.201  -26.066 42.090  1.00 87.90  ? 753  SER A N     1 
ATOM   4900 C  CA    . SER A 1 650 ? -5.133  -25.246 41.325  1.00 84.32  ? 753  SER A CA    1 
ATOM   4901 C  C     . SER A 1 650 ? -4.435  -24.650 40.109  1.00 88.73  ? 753  SER A C     1 
ATOM   4902 O  O     . SER A 1 650 ? -3.401  -23.988 40.266  1.00 92.91  ? 753  SER A O     1 
ATOM   4903 C  CB    . SER A 1 650 ? -5.702  -24.138 42.206  1.00 83.89  ? 753  SER A CB    1 
ATOM   4904 O  OG    . SER A 1 650 ? -6.551  -23.277 41.467  1.00 85.46  ? 753  SER A OG    1 
ATOM   4905 N  N     . PRO A 1 651 ? -4.942  -24.864 38.893  1.00 82.54  ? 754  PRO A N     1 
ATOM   4906 C  CA    . PRO A 1 651 ? -4.316  -24.225 37.723  1.00 76.90  ? 754  PRO A CA    1 
ATOM   4907 C  C     . PRO A 1 651 ? -4.411  -22.710 37.740  1.00 73.60  ? 754  PRO A C     1 
ATOM   4908 O  O     . PRO A 1 651 ? -3.545  -22.040 37.164  1.00 73.92  ? 754  PRO A O     1 
ATOM   4909 C  CB    . PRO A 1 651 ? -5.086  -24.830 36.541  1.00 77.09  ? 754  PRO A CB    1 
ATOM   4910 C  CG    . PRO A 1 651 ? -5.636  -26.120 37.068  1.00 78.72  ? 754  PRO A CG    1 
ATOM   4911 C  CD    . PRO A 1 651 ? -5.968  -25.845 38.504  1.00 81.28  ? 754  PRO A CD    1 
ATOM   4912 N  N     . LEU A 1 652 ? -5.436  -22.146 38.386  1.00 74.34  ? 755  LEU A N     1 
ATOM   4913 C  CA    . LEU A 1 652 ? -5.537  -20.693 38.488  1.00 74.09  ? 755  LEU A CA    1 
ATOM   4914 C  C     . LEU A 1 652 ? -4.451  -20.115 39.386  1.00 77.75  ? 755  LEU A C     1 
ATOM   4915 O  O     . LEU A 1 652 ? -4.031  -18.969 39.192  1.00 79.71  ? 755  LEU A O     1 
ATOM   4916 C  CB    . LEU A 1 652 ? -6.917  -20.296 39.012  1.00 73.42  ? 755  LEU A CB    1 
ATOM   4917 C  CG    . LEU A 1 652 ? -8.109  -20.561 38.094  1.00 78.79  ? 755  LEU A CG    1 
ATOM   4918 C  CD1   . LEU A 1 652 ? -9.410  -20.253 38.815  1.00 78.43  ? 755  LEU A CD1   1 
ATOM   4919 C  CD2   . LEU A 1 652 ? -7.992  -19.738 36.821  1.00 72.19  ? 755  LEU A CD2   1 
ATOM   4920 N  N     . ASN A 1 653 ? -3.995  -20.882 40.369  1.00 78.75  ? 756  ASN A N     1 
ATOM   4921 C  CA    . ASN A 1 653 ? -2.931  -20.472 41.275  1.00 73.99  ? 756  ASN A CA    1 
ATOM   4922 C  C     . ASN A 1 653 ? -2.299  -21.722 41.872  1.00 77.09  ? 756  ASN A C     1 
ATOM   4923 O  O     . ASN A 1 653 ? -2.910  -22.379 42.725  1.00 75.68  ? 756  ASN A O     1 
ATOM   4924 C  CB    . ASN A 1 653 ? -3.471  -19.555 42.375  1.00 77.56  ? 756  ASN A CB    1 
ATOM   4925 C  CG    . ASN A 1 653 ? -2.367  -18.892 43.182  1.00 81.19  ? 756  ASN A CG    1 
ATOM   4926 O  OD1   . ASN A 1 653 ? -1.221  -19.345 43.188  1.00 77.96  ? 756  ASN A OD1   1 
ATOM   4927 N  ND2   . ASN A 1 653 ? -2.712  -17.811 43.873  1.00 73.78  ? 756  ASN A ND2   1 
ATOM   4928 N  N     . PRO A 1 654 ? -1.086  -22.089 41.446  1.00 74.73  ? 757  PRO A N     1 
ATOM   4929 C  CA    . PRO A 1 654 ? -0.468  -23.322 41.957  1.00 78.83  ? 757  PRO A CA    1 
ATOM   4930 C  C     . PRO A 1 654 ? -0.115  -23.266 43.435  1.00 78.75  ? 757  PRO A C     1 
ATOM   4931 O  O     . PRO A 1 654 ? 0.161   -24.320 44.023  1.00 80.93  ? 757  PRO A O     1 
ATOM   4932 C  CB    . PRO A 1 654 ? 0.787   -23.472 41.088  1.00 71.81  ? 757  PRO A CB    1 
ATOM   4933 C  CG    . PRO A 1 654 ? 1.101   -22.084 40.643  1.00 69.72  ? 757  PRO A CG    1 
ATOM   4934 C  CD    . PRO A 1 654 ? -0.221  -21.390 40.481  1.00 67.65  ? 757  PRO A CD    1 
ATOM   4935 N  N     . ALA A 1 655 ? -0.114  -22.083 44.054  1.00 77.32  ? 758  ALA A N     1 
ATOM   4936 C  CA    . ALA A 1 655 ? 0.101   -22.013 45.494  1.00 77.04  ? 758  ALA A CA    1 
ATOM   4937 C  C     . ALA A 1 655 ? -1.100  -22.548 46.264  1.00 82.94  ? 758  ALA A C     1 
ATOM   4938 O  O     . ALA A 1 655 ? -0.945  -23.046 47.385  1.00 90.22  ? 758  ALA A O     1 
ATOM   4939 C  CB    . ALA A 1 655 ? 0.405   -20.575 45.915  1.00 72.62  ? 758  ALA A CB    1 
ATOM   4940 N  N     . HIS A 1 656 ? -2.294  -22.459 45.681  1.00 76.76  ? 759  HIS A N     1 
ATOM   4941 C  CA    . HIS A 1 656 ? -3.510  -22.955 46.315  1.00 70.79  ? 759  HIS A CA    1 
ATOM   4942 C  C     . HIS A 1 656 ? -3.653  -24.444 46.022  1.00 75.38  ? 759  HIS A C     1 
ATOM   4943 O  O     . HIS A 1 656 ? -3.874  -24.840 44.874  1.00 86.29  ? 759  HIS A O     1 
ATOM   4944 C  CB    . HIS A 1 656 ? -4.726  -22.184 45.810  1.00 77.80  ? 759  HIS A CB    1 
ATOM   4945 C  CG    . HIS A 1 656 ? -4.673  -20.715 46.092  1.00 81.80  ? 759  HIS A CG    1 
ATOM   4946 N  ND1   . HIS A 1 656 ? -5.456  -19.800 45.420  1.00 86.27  ? 759  HIS A ND1   1 
ATOM   4947 C  CD2   . HIS A 1 656 ? -3.937  -20.002 46.977  1.00 83.64  ? 759  HIS A CD2   1 
ATOM   4948 C  CE1   . HIS A 1 656 ? -5.201  -18.587 45.877  1.00 90.89  ? 759  HIS A CE1   1 
ATOM   4949 N  NE2   . HIS A 1 656 ? -4.284  -18.682 46.822  1.00 89.15  ? 759  HIS A NE2   1 
ATOM   4950 N  N     . GLN A 1 657 ? -3.529  -25.271 47.056  1.00 76.67  ? 760  GLN A N     1 
ATOM   4951 C  CA    . GLN A 1 657 ? -3.744  -26.701 46.900  1.00 82.20  ? 760  GLN A CA    1 
ATOM   4952 C  C     . GLN A 1 657 ? -5.230  -27.026 46.979  1.00 80.85  ? 760  GLN A C     1 
ATOM   4953 O  O     . GLN A 1 657 ? -6.004  -26.344 47.657  1.00 80.65  ? 760  GLN A O     1 
ATOM   4954 C  CB    . GLN A 1 657 ? -2.980  -27.483 47.969  1.00 81.16  ? 760  GLN A CB    1 
ATOM   4955 C  CG    . GLN A 1 657 ? -1.475  -27.277 47.938  1.00 84.06  ? 760  GLN A CG    1 
ATOM   4956 C  CD    . GLN A 1 657 ? -0.742  -28.184 48.909  1.00 99.90  ? 760  GLN A CD    1 
ATOM   4957 O  OE1   . GLN A 1 657 ? -1.342  -29.062 49.530  1.00 103.53 ? 760  GLN A OE1   1 
ATOM   4958 N  NE2   . GLN A 1 657 ? 0.563   -27.977 49.044  1.00 101.76 ? 760  GLN A NE2   1 
ATOM   4959 N  N     . LEU A 1 658 ? -5.626  -28.082 46.273  1.00 79.15  ? 761  LEU A N     1 
ATOM   4960 C  CA    . LEU A 1 658 ? -7.019  -28.521 46.212  1.00 83.72  ? 761  LEU A CA    1 
ATOM   4961 C  C     . LEU A 1 658 ? -7.100  -29.929 46.792  1.00 86.94  ? 761  LEU A C     1 
ATOM   4962 O  O     . LEU A 1 658 ? -6.790  -30.909 46.108  1.00 94.03  ? 761  LEU A O     1 
ATOM   4963 C  CB    . LEU A 1 658 ? -7.543  -28.478 44.779  1.00 86.25  ? 761  LEU A CB    1 
ATOM   4964 C  CG    . LEU A 1 658 ? -7.464  -27.126 44.069  1.00 83.83  ? 761  LEU A CG    1 
ATOM   4965 C  CD1   . LEU A 1 658 ? -7.992  -27.235 42.648  1.00 86.15  ? 761  LEU A CD1   1 
ATOM   4966 C  CD2   . LEU A 1 658 ? -8.228  -26.069 44.849  1.00 82.67  ? 761  LEU A CD2   1 
ATOM   4967 N  N     . GLY A 1 659 ? -7.518  -30.029 48.051  1.00 87.81  ? 762  GLY A N     1 
ATOM   4968 C  CA    . GLY A 1 659 ? -7.648  -31.317 48.702  1.00 90.02  ? 762  GLY A CA    1 
ATOM   4969 C  C     . GLY A 1 659 ? -8.920  -32.045 48.321  1.00 92.63  ? 762  GLY A C     1 
ATOM   4970 O  O     . GLY A 1 659 ? -9.240  -32.171 47.135  1.00 95.22  ? 762  GLY A O     1 
ATOM   4971 N  N     . ASN A 1 660 ? -9.654  -32.534 49.317  1.00 97.65  ? 763  ASN A N     1 
ATOM   4972 C  CA    . ASN A 1 660 ? -10.915 -33.210 49.050  1.00 96.15  ? 763  ASN A CA    1 
ATOM   4973 C  C     . ASN A 1 660 ? -11.991 -32.195 48.689  1.00 95.29  ? 763  ASN A C     1 
ATOM   4974 O  O     . ASN A 1 660 ? -12.024 -31.084 49.223  1.00 95.84  ? 763  ASN A O     1 
ATOM   4975 C  CB    . ASN A 1 660 ? -11.347 -34.032 50.264  1.00 98.96  ? 763  ASN A CB    1 
ATOM   4976 C  CG    . ASN A 1 660 ? -10.445 -35.223 50.511  1.00 97.41  ? 763  ASN A CG    1 
ATOM   4977 O  OD1   . ASN A 1 660 ? -9.370  -35.336 49.920  1.00 101.19 ? 763  ASN A OD1   1 
ATOM   4978 N  ND2   . ASN A 1 660 ? -10.876 -36.120 51.389  1.00 102.09 ? 763  ASN A ND2   1 
ATOM   4979 N  N     . LEU A 1 661 ? -12.872 -32.579 47.771  1.00 95.78  ? 764  LEU A N     1 
ATOM   4980 C  CA    . LEU A 1 661 ? -13.918 -31.691 47.289  1.00 99.21  ? 764  LEU A CA    1 
ATOM   4981 C  C     . LEU A 1 661 ? -15.235 -32.001 47.988  1.00 93.31  ? 764  LEU A C     1 
ATOM   4982 O  O     . LEU A 1 661 ? -15.559 -33.165 48.243  1.00 92.45  ? 764  LEU A O     1 
ATOM   4983 C  CB    . LEU A 1 661 ? -14.078 -31.804 45.769  1.00 101.98 ? 764  LEU A CB    1 
ATOM   4984 C  CG    . LEU A 1 661 ? -14.597 -33.109 45.162  1.00 98.60  ? 764  LEU A CG    1 
ATOM   4985 C  CD1   . LEU A 1 661 ? -16.050 -32.953 44.750  1.00 104.72 ? 764  LEU A CD1   1 
ATOM   4986 C  CD2   . LEU A 1 661 ? -13.747 -33.528 43.975  1.00 99.11  ? 764  LEU A CD2   1 
ATOM   4987 N  N     . ARG A 1 662 ? -15.985 -30.949 48.304  1.00 94.40  ? 765  ARG A N     1 
ATOM   4988 C  CA    . ARG A 1 662 ? -17.275 -31.076 48.978  1.00 99.65  ? 765  ARG A CA    1 
ATOM   4989 C  C     . ARG A 1 662 ? -18.348 -31.247 47.911  1.00 97.57  ? 765  ARG A C     1 
ATOM   4990 O  O     . ARG A 1 662 ? -18.822 -30.269 47.327  1.00 94.38  ? 765  ARG A O     1 
ATOM   4991 C  CB    . ARG A 1 662 ? -17.540 -29.860 49.858  1.00 108.96 ? 765  ARG A CB    1 
ATOM   4992 C  CG    . ARG A 1 662 ? -16.480 -29.623 50.924  1.00 108.74 ? 765  ARG A CG    1 
ATOM   4993 C  CD    . ARG A 1 662 ? -16.832 -28.430 51.797  1.00 118.74 ? 765  ARG A CD    1 
ATOM   4994 N  NE    . ARG A 1 662 ? -15.820 -28.178 52.816  1.00 129.63 ? 765  ARG A NE    1 
ATOM   4995 C  CZ    . ARG A 1 662 ? -15.817 -28.729 54.022  1.00 131.08 ? 765  ARG A CZ    1 
ATOM   4996 N  NH1   . ARG A 1 662 ? -16.760 -29.578 54.396  1.00 128.80 ? 765  ARG A NH1   1 
ATOM   4997 N  NH2   . ARG A 1 662 ? -14.844 -28.420 54.875  1.00 123.61 ? 765  ARG A NH2   1 
ATOM   4998 N  N     . LEU A 1 663 ? -18.739 -32.501 47.662  1.00 97.89  ? 766  LEU A N     1 
ATOM   4999 C  CA    . LEU A 1 663 ? -19.677 -32.792 46.581  1.00 100.46 ? 766  LEU A CA    1 
ATOM   5000 C  C     . LEU A 1 663 ? -21.020 -32.105 46.789  1.00 104.17 ? 766  LEU A C     1 
ATOM   5001 O  O     . LEU A 1 663 ? -21.709 -31.784 45.813  1.00 100.41 ? 766  LEU A O     1 
ATOM   5002 C  CB    . LEU A 1 663 ? -19.879 -34.304 46.443  1.00 98.63  ? 766  LEU A CB    1 
ATOM   5003 C  CG    . LEU A 1 663 ? -18.759 -35.155 45.836  1.00 97.47  ? 766  LEU A CG    1 
ATOM   5004 C  CD1   . LEU A 1 663 ? -17.657 -35.447 46.847  1.00 99.19  ? 766  LEU A CD1   1 
ATOM   5005 C  CD2   . LEU A 1 663 ? -19.321 -36.449 45.264  1.00 105.21 ? 766  LEU A CD2   1 
ATOM   5006 N  N     . GLU A 1 664 ? -21.413 -31.870 48.044  1.00 102.35 ? 767  GLU A N     1 
ATOM   5007 C  CA    . GLU A 1 664 ? -22.686 -31.211 48.309  1.00 101.20 ? 767  GLU A CA    1 
ATOM   5008 C  C     . GLU A 1 664 ? -22.689 -29.757 47.856  1.00 97.63  ? 767  GLU A C     1 
ATOM   5009 O  O     . GLU A 1 664 ? -23.766 -29.196 47.626  1.00 96.38  ? 767  GLU A O     1 
ATOM   5010 C  CB    . GLU A 1 664 ? -23.030 -31.295 49.800  1.00 110.98 ? 767  GLU A CB    1 
ATOM   5011 C  CG    . GLU A 1 664 ? -22.100 -30.511 50.720  1.00 111.15 ? 767  GLU A CG    1 
ATOM   5012 C  CD    . GLU A 1 664 ? -20.811 -31.250 51.033  1.00 115.53 ? 767  GLU A CD    1 
ATOM   5013 O  OE1   . GLU A 1 664 ? -20.644 -32.393 50.559  1.00 116.02 ? 767  GLU A OE1   1 
ATOM   5014 O  OE2   . GLU A 1 664 ? -19.966 -30.685 51.759  1.00 117.43 ? 767  GLU A OE2   1 
ATOM   5015 N  N     . GLU A 1 665 ? -21.517 -29.138 47.721  1.00 98.23  ? 768  GLU A N     1 
ATOM   5016 C  CA    . GLU A 1 665 ? -21.410 -27.769 47.238  1.00 98.76  ? 768  GLU A CA    1 
ATOM   5017 C  C     . GLU A 1 665 ? -21.200 -27.684 45.733  1.00 95.54  ? 768  GLU A C     1 
ATOM   5018 O  O     . GLU A 1 665 ? -21.333 -26.593 45.165  1.00 89.74  ? 768  GLU A O     1 
ATOM   5019 C  CB    . GLU A 1 665 ? -20.264 -27.045 47.954  1.00 104.16 ? 768  GLU A CB    1 
ATOM   5020 C  CG    . GLU A 1 665 ? -20.560 -26.692 49.402  1.00 107.71 ? 768  GLU A CG    1 
ATOM   5021 C  CD    . GLU A 1 665 ? -21.550 -25.551 49.530  1.00 109.86 ? 768  GLU A CD    1 
ATOM   5022 O  OE1   . GLU A 1 665 ? -21.594 -24.697 48.620  1.00 117.24 ? 768  GLU A OE1   1 
ATOM   5023 O  OE2   . GLU A 1 665 ? -22.285 -25.510 50.539  1.00 108.55 ? 768  GLU A OE2   1 
ATOM   5024 N  N     . CYS A 1 666 ? -20.878 -28.796 45.078  1.00 94.37  ? 769  CYS A N     1 
ATOM   5025 C  CA    . CYS A 1 666 ? -20.698 -28.809 43.633  1.00 88.23  ? 769  CYS A CA    1 
ATOM   5026 C  C     . CYS A 1 666 ? -22.055 -28.830 42.944  1.00 87.76  ? 769  CYS A C     1 
ATOM   5027 O  O     . CYS A 1 666 ? -22.908 -29.664 43.263  1.00 89.32  ? 769  CYS A O     1 
ATOM   5028 C  CB    . CYS A 1 666 ? -19.867 -30.019 43.212  1.00 89.41  ? 769  CYS A CB    1 
ATOM   5029 S  SG    . CYS A 1 666 ? -18.250 -30.128 44.016  1.00 88.38  ? 769  CYS A SG    1 
ATOM   5030 N  N     . ARG A 1 667 ? -22.255 -27.915 41.997  1.00 85.64  ? 770  ARG A N     1 
ATOM   5031 C  CA    . ARG A 1 667 ? -23.548 -27.782 41.342  1.00 86.61  ? 770  ARG A CA    1 
ATOM   5032 C  C     . ARG A 1 667 ? -23.360 -27.304 39.910  1.00 89.33  ? 770  ARG A C     1 
ATOM   5033 O  O     . ARG A 1 667 ? -22.328 -26.732 39.549  1.00 79.95  ? 770  ARG A O     1 
ATOM   5034 C  CB    . ARG A 1 667 ? -24.464 -26.815 42.101  1.00 77.07  ? 770  ARG A CB    1 
ATOM   5035 C  CG    . ARG A 1 667 ? -23.876 -25.423 42.267  1.00 83.50  ? 770  ARG A CG    1 
ATOM   5036 C  CD    . ARG A 1 667 ? -24.791 -24.522 43.077  1.00 86.25  ? 770  ARG A CD    1 
ATOM   5037 N  NE    . ARG A 1 667 ? -24.129 -23.279 43.454  1.00 89.38  ? 770  ARG A NE    1 
ATOM   5038 C  CZ    . ARG A 1 667 ? -24.178 -22.158 42.748  1.00 93.47  ? 770  ARG A CZ    1 
ATOM   5039 N  NH1   . ARG A 1 667 ? -24.861 -22.082 41.617  1.00 86.98  ? 770  ARG A NH1   1 
ATOM   5040 N  NH2   . ARG A 1 667 ? -23.526 -21.085 43.189  1.00 93.49  ? 770  ARG A NH2   1 
ATOM   5041 N  N     . ILE A 1 668 ? -24.383 -27.550 39.097  1.00 90.39  ? 771  ILE A N     1 
ATOM   5042 C  CA    . ILE A 1 668 ? -24.451 -27.029 37.737  1.00 89.34  ? 771  ILE A CA    1 
ATOM   5043 C  C     . ILE A 1 668 ? -25.133 -25.669 37.793  1.00 89.82  ? 771  ILE A C     1 
ATOM   5044 O  O     . ILE A 1 668 ? -26.275 -25.557 38.252  1.00 88.50  ? 771  ILE A O     1 
ATOM   5045 C  CB    . ILE A 1 668 ? -25.207 -27.991 36.810  1.00 87.36  ? 771  ILE A CB    1 
ATOM   5046 C  CG1   . ILE A 1 668 ? -24.513 -29.353 36.775  1.00 84.87  ? 771  ILE A CG1   1 
ATOM   5047 C  CG2   . ILE A 1 668 ? -25.321 -27.403 35.413  1.00 89.37  ? 771  ILE A CG2   1 
ATOM   5048 C  CD1   . ILE A 1 668 ? -25.319 -30.429 36.084  1.00 89.39  ? 771  ILE A CD1   1 
ATOM   5049 N  N     . MET A 1 669 ? -24.436 -24.636 37.329  1.00 90.41  ? 772  MET A N     1 
ATOM   5050 C  CA    . MET A 1 669 ? -24.951 -23.280 37.441  1.00 94.66  ? 772  MET A CA    1 
ATOM   5051 C  C     . MET A 1 669 ? -26.127 -23.059 36.496  1.00 109.52 ? 772  MET A C     1 
ATOM   5052 O  O     . MET A 1 669 ? -26.233 -23.686 35.438  1.00 112.48 ? 772  MET A O     1 
ATOM   5053 C  CB    . MET A 1 669 ? -23.848 -22.265 37.147  1.00 93.30  ? 772  MET A CB    1 
ATOM   5054 C  CG    . MET A 1 669 ? -22.628 -22.411 38.036  1.00 87.96  ? 772  MET A CG    1 
ATOM   5055 S  SD    . MET A 1 669 ? -21.412 -21.115 37.756  1.00 86.65  ? 772  MET A SD    1 
ATOM   5056 C  CE    . MET A 1 669 ? -22.362 -19.662 38.196  1.00 84.46  ? 772  MET A CE    1 
ATOM   5057 N  N     . SER A 1 670 ? -27.018 -22.153 36.894  1.00 123.43 ? 773  SER A N     1 
ATOM   5058 C  CA    . SER A 1 670 ? -28.168 -21.773 36.074  1.00 127.49 ? 773  SER A CA    1 
ATOM   5059 C  C     . SER A 1 670 ? -27.822 -20.710 35.038  1.00 123.32 ? 773  SER A C     1 
ATOM   5060 O  O     . SER A 1 670 ? -28.632 -19.826 34.752  1.00 124.90 ? 773  SER A O     1 
ATOM   5061 C  CB    . SER A 1 670 ? -29.302 -21.298 36.980  1.00 130.58 ? 773  SER A CB    1 
ATOM   5062 O  OG    . SER A 1 670 ? -28.921 -20.149 37.717  1.00 140.09 ? 773  SER A OG    1 
ATOM   5063 N  N     . SER A 1 671 ? -26.620 -20.775 34.469  1.00 122.03 ? 774  SER A N     1 
ATOM   5064 C  CA    . SER A 1 671 ? -26.154 -19.831 33.472  1.00 125.27 ? 774  SER A CA    1 
ATOM   5065 C  C     . SER A 1 671 ? -26.120 -20.514 32.102  1.00 132.37 ? 774  SER A C     1 
ATOM   5066 O  O     . SER A 1 671 ? -26.759 -21.556 31.897  1.00 137.33 ? 774  SER A O     1 
ATOM   5067 C  CB    . SER A 1 671 ? -24.790 -19.281 33.898  1.00 124.77 ? 774  SER A CB    1 
ATOM   5068 O  OG    . SER A 1 671 ? -24.869 -18.653 35.166  1.00 119.41 ? 774  SER A OG    1 
ATOM   5069 N  N     . ALA A 1 672 ? -25.372 -19.931 31.170  1.00 131.88 ? 775  ALA A N     1 
ATOM   5070 C  CA    . ALA A 1 672 ? -25.311 -20.452 29.813  1.00 137.26 ? 775  ALA A CA    1 
ATOM   5071 C  C     . ALA A 1 672 ? -24.309 -21.595 29.712  1.00 137.69 ? 775  ALA A C     1 
ATOM   5072 O  O     . ALA A 1 672 ? -23.249 -21.571 30.345  1.00 132.58 ? 775  ALA A O     1 
ATOM   5073 C  CB    . ALA A 1 672 ? -24.937 -19.341 28.832  1.00 137.88 ? 775  ALA A CB    1 
ATOM   5074 N  N     . LYS A 1 673 ? -24.662 -22.603 28.913  1.00 133.02 ? 776  LYS A N     1 
ATOM   5075 C  CA    . LYS A 1 673 ? -23.806 -23.746 28.596  1.00 129.20 ? 776  LYS A CA    1 
ATOM   5076 C  C     . LYS A 1 673 ? -23.428 -24.568 29.826  1.00 118.91 ? 776  LYS A C     1 
ATOM   5077 O  O     . LYS A 1 673 ? -22.429 -25.296 29.801  1.00 112.75 ? 776  LYS A O     1 
ATOM   5078 C  CB    . LYS A 1 673 ? -22.544 -23.304 27.846  1.00 121.82 ? 776  LYS A CB    1 
ATOM   5079 C  CG    . LYS A 1 673 ? -22.823 -22.749 26.458  1.00 123.00 ? 776  LYS A CG    1 
ATOM   5080 C  CD    . LYS A 1 673 ? -21.539 -22.499 25.687  1.00 115.90 ? 776  LYS A CD    1 
ATOM   5081 C  CE    . LYS A 1 673 ? -21.833 -22.013 24.277  1.00 113.50 ? 776  LYS A CE    1 
ATOM   5082 N  NZ    . LYS A 1 673 ? -22.642 -22.998 23.507  1.00 121.30 ? 776  LYS A NZ    1 
ATOM   5083 N  N     . ARG A 1 674 ? -24.214 -24.466 30.901  1.00 116.40 ? 777  ARG A N     1 
ATOM   5084 C  CA    . ARG A 1 674 ? -24.085 -25.294 32.096  1.00 107.38 ? 777  ARG A CA    1 
ATOM   5085 C  C     . ARG A 1 674 ? -22.669 -25.283 32.661  1.00 99.32  ? 777  ARG A C     1 
ATOM   5086 O  O     . ARG A 1 674 ? -21.943 -26.277 32.528  1.00 97.45  ? 777  ARG A O     1 
ATOM   5087 C  CB    . ARG A 1 674 ? -24.507 -26.732 31.786  1.00 106.71 ? 777  ARG A CB    1 
ATOM   5088 C  CG    . ARG A 1 674 ? -25.927 -26.861 31.265  1.00 114.43 ? 777  ARG A CG    1 
ATOM   5089 C  CD    . ARG A 1 674 ? -26.937 -26.417 32.308  1.00 122.33 ? 777  ARG A CD    1 
ATOM   5090 N  NE    . ARG A 1 674 ? -28.289 -26.357 31.766  1.00 134.13 ? 777  ARG A NE    1 
ATOM   5091 C  CZ    . ARG A 1 674 ? -28.833 -25.269 31.238  1.00 137.36 ? 777  ARG A CZ    1 
ATOM   5092 N  NH1   . ARG A 1 674 ? -28.168 -24.127 31.172  1.00 128.58 ? 777  ARG A NH1   1 
ATOM   5093 N  NH2   . ARG A 1 674 ? -30.076 -25.328 30.766  1.00 129.13 ? 777  ARG A NH2   1 
ATOM   5094 N  N     . PRO A 1 675 ? -22.237 -24.194 33.293  1.00 97.21  ? 778  PRO A N     1 
ATOM   5095 C  CA    . PRO A 1 675 ? -20.910 -24.191 33.918  1.00 93.94  ? 778  PRO A CA    1 
ATOM   5096 C  C     . PRO A 1 675 ? -20.898 -25.025 35.189  1.00 90.38  ? 778  PRO A C     1 
ATOM   5097 O  O     . PRO A 1 675 ? -21.891 -25.110 35.917  1.00 87.43  ? 778  PRO A O     1 
ATOM   5098 C  CB    . PRO A 1 675 ? -20.660 -22.708 34.224  1.00 94.10  ? 778  PRO A CB    1 
ATOM   5099 C  CG    . PRO A 1 675 ? -21.704 -21.953 33.447  1.00 100.61 ? 778  PRO A CG    1 
ATOM   5100 C  CD    . PRO A 1 675 ? -22.877 -22.872 33.364  1.00 103.50 ? 778  PRO A CD    1 
ATOM   5101 N  N     . LEU A 1 676 ? -19.752 -25.647 35.452  1.00 87.90  ? 779  LEU A N     1 
ATOM   5102 C  CA    . LEU A 1 676 ? -19.571 -26.465 36.644  1.00 83.53  ? 779  LEU A CA    1 
ATOM   5103 C  C     . LEU A 1 676 ? -19.070 -25.597 37.792  1.00 82.98  ? 779  LEU A C     1 
ATOM   5104 O  O     . LEU A 1 676 ? -17.981 -25.018 37.711  1.00 82.42  ? 779  LEU A O     1 
ATOM   5105 C  CB    . LEU A 1 676 ? -18.593 -27.608 36.380  1.00 82.93  ? 779  LEU A CB    1 
ATOM   5106 C  CG    . LEU A 1 676 ? -19.174 -28.913 35.839  1.00 85.03  ? 779  LEU A CG    1 
ATOM   5107 C  CD1   . LEU A 1 676 ? -18.100 -29.989 35.796  1.00 88.43  ? 779  LEU A CD1   1 
ATOM   5108 C  CD2   . LEU A 1 676 ? -20.350 -29.362 36.687  1.00 87.52  ? 779  LEU A CD2   1 
ATOM   5109 N  N     . TRP A 1 677 ? -19.864 -25.509 38.857  1.00 83.41  ? 780  TRP A N     1 
ATOM   5110 C  CA    . TRP A 1 677 ? -19.448 -24.859 40.095  1.00 82.76  ? 780  TRP A CA    1 
ATOM   5111 C  C     . TRP A 1 677 ? -18.813 -25.920 40.985  1.00 82.47  ? 780  TRP A C     1 
ATOM   5112 O  O     . TRP A 1 677 ? -19.508 -26.795 41.509  1.00 83.57  ? 780  TRP A O     1 
ATOM   5113 C  CB    . TRP A 1 677 ? -20.639 -24.197 40.784  1.00 85.58  ? 780  TRP A CB    1 
ATOM   5114 C  CG    . TRP A 1 677 ? -20.308 -23.507 42.079  1.00 87.10  ? 780  TRP A CG    1 
ATOM   5115 C  CD1   . TRP A 1 677 ? -20.017 -24.099 43.275  1.00 87.58  ? 780  TRP A CD1   1 
ATOM   5116 C  CD2   . TRP A 1 677 ? -20.258 -22.094 42.310  1.00 89.41  ? 780  TRP A CD2   1 
ATOM   5117 N  NE1   . TRP A 1 677 ? -19.776 -23.143 44.232  1.00 88.39  ? 780  TRP A NE1   1 
ATOM   5118 C  CE2   . TRP A 1 677 ? -19.920 -21.904 43.666  1.00 87.86  ? 780  TRP A CE2   1 
ATOM   5119 C  CE3   . TRP A 1 677 ? -20.462 -20.971 41.502  1.00 85.62  ? 780  TRP A CE3   1 
ATOM   5120 C  CZ2   . TRP A 1 677 ? -19.782 -20.638 44.230  1.00 88.31  ? 780  TRP A CZ2   1 
ATOM   5121 C  CZ3   . TRP A 1 677 ? -20.323 -19.715 42.065  1.00 87.66  ? 780  TRP A CZ3   1 
ATOM   5122 C  CH2   . TRP A 1 677 ? -19.988 -19.559 43.416  1.00 92.57  ? 780  TRP A CH2   1 
ATOM   5123 N  N     . LEU A 1 678 ? -17.497 -25.850 41.151  1.00 81.11  ? 781  LEU A N     1 
ATOM   5124 C  CA    . LEU A 1 678 ? -16.753 -26.842 41.913  1.00 83.99  ? 781  LEU A CA    1 
ATOM   5125 C  C     . LEU A 1 678 ? -16.227 -26.230 43.204  1.00 86.84  ? 781  LEU A C     1 
ATOM   5126 O  O     . LEU A 1 678 ? -15.852 -25.054 43.241  1.00 86.67  ? 781  LEU A O     1 
ATOM   5127 C  CB    . LEU A 1 678 ? -15.597 -27.412 41.089  1.00 85.81  ? 781  LEU A CB    1 
ATOM   5128 C  CG    . LEU A 1 678 ? -16.022 -28.181 39.837  1.00 83.43  ? 781  LEU A CG    1 
ATOM   5129 C  CD1   . LEU A 1 678 ? -14.838 -28.911 39.235  1.00 83.89  ? 781  LEU A CD1   1 
ATOM   5130 C  CD2   . LEU A 1 678 ? -17.148 -29.153 40.158  1.00 84.64  ? 781  LEU A CD2   1 
ATOM   5131 N  N     . ASN A 1 679 ? -16.199 -27.040 44.261  1.00 88.26  ? 782  ASN A N     1 
ATOM   5132 C  CA    . ASN A 1 679 ? -15.816 -26.580 45.593  1.00 89.24  ? 782  ASN A CA    1 
ATOM   5133 C  C     . ASN A 1 679 ? -14.876 -27.609 46.206  1.00 91.24  ? 782  ASN A C     1 
ATOM   5134 O  O     . ASN A 1 679 ? -15.297 -28.723 46.530  1.00 93.40  ? 782  ASN A O     1 
ATOM   5135 C  CB    . ASN A 1 679 ? -17.054 -26.372 46.470  1.00 95.68  ? 782  ASN A CB    1 
ATOM   5136 C  CG    . ASN A 1 679 ? -16.738 -25.686 47.789  1.00 99.39  ? 782  ASN A CG    1 
ATOM   5137 O  OD1   . ASN A 1 679 ? -15.823 -26.081 48.512  1.00 98.73  ? 782  ASN A OD1   1 
ATOM   5138 N  ND2   . ASN A 1 679 ? -17.506 -24.651 48.111  1.00 102.17 ? 782  ASN A ND2   1 
ATOM   5139 N  N     . TRP A 1 680 ? -13.608 -27.240 46.357  1.00 92.30  ? 783  TRP A N     1 
ATOM   5140 C  CA    . TRP A 1 680 ? -12.633 -28.045 47.075  1.00 93.61  ? 783  TRP A CA    1 
ATOM   5141 C  C     . TRP A 1 680 ? -12.407 -27.469 48.467  1.00 95.38  ? 783  TRP A C     1 
ATOM   5142 O  O     . TRP A 1 680 ? -12.713 -26.306 48.742  1.00 93.33  ? 783  TRP A O     1 
ATOM   5143 C  CB    . TRP A 1 680 ? -11.299 -28.103 46.325  1.00 90.67  ? 783  TRP A CB    1 
ATOM   5144 C  CG    . TRP A 1 680 ? -11.340 -28.860 45.040  1.00 92.11  ? 783  TRP A CG    1 
ATOM   5145 C  CD1   . TRP A 1 680 ? -11.142 -30.198 44.871  1.00 91.76  ? 783  TRP A CD1   1 
ATOM   5146 C  CD2   . TRP A 1 680 ? -11.578 -28.321 43.736  1.00 92.29  ? 783  TRP A CD2   1 
ATOM   5147 N  NE1   . TRP A 1 680 ? -11.250 -30.528 43.542  1.00 93.01  ? 783  TRP A NE1   1 
ATOM   5148 C  CE2   . TRP A 1 680 ? -11.517 -29.392 42.824  1.00 90.96  ? 783  TRP A CE2   1 
ATOM   5149 C  CE3   . TRP A 1 680 ? -11.841 -27.036 43.251  1.00 89.28  ? 783  TRP A CE3   1 
ATOM   5150 C  CZ2   . TRP A 1 680 ? -11.710 -29.219 41.456  1.00 90.11  ? 783  TRP A CZ2   1 
ATOM   5151 C  CZ3   . TRP A 1 680 ? -12.032 -26.866 41.893  1.00 85.42  ? 783  TRP A CZ3   1 
ATOM   5152 C  CH2   . TRP A 1 680 ? -11.965 -27.951 41.011  1.00 88.62  ? 783  TRP A CH2   1 
ATOM   5153 N  N     . GLU A 1 681 ? -11.863 -28.299 49.349  1.00 104.95 ? 784  GLU A N     1 
ATOM   5154 C  CA    . GLU A 1 681 ? -11.446 -27.849 50.667  1.00 108.77 ? 784  GLU A CA    1 
ATOM   5155 C  C     . GLU A 1 681 ? -9.954  -27.543 50.644  1.00 103.36 ? 784  GLU A C     1 
ATOM   5156 O  O     . GLU A 1 681 ? -9.183  -28.198 49.935  1.00 103.63 ? 784  GLU A O     1 
ATOM   5157 C  CB    . GLU A 1 681 ? -11.765 -28.889 51.747  1.00 109.96 ? 784  GLU A CB    1 
ATOM   5158 C  CG    . GLU A 1 681 ? -10.731 -29.995 51.908  1.00 118.00 ? 784  GLU A CG    1 
ATOM   5159 C  CD    . GLU A 1 681 ? -11.063 -30.948 53.041  1.00 131.66 ? 784  GLU A CD    1 
ATOM   5160 O  OE1   . GLU A 1 681 ? -12.150 -30.804 53.640  1.00 121.04 ? 784  GLU A OE1   1 
ATOM   5161 O  OE2   . GLU A 1 681 ? -10.237 -31.839 53.333  1.00 135.03 ? 784  GLU A OE2   1 
ATOM   5162 N  N     . ASN A 1 682 ? -9.560  -26.527 51.399  1.00 91.84  ? 785  ASN A N     1 
ATOM   5163 C  CA    . ASN A 1 682 ? -8.163  -26.131 51.493  1.00 85.37  ? 785  ASN A CA    1 
ATOM   5164 C  C     . ASN A 1 682 ? -7.454  -27.055 52.477  1.00 87.58  ? 785  ASN A C     1 
ATOM   5165 O  O     . ASN A 1 682 ? -7.742  -27.020 53.680  1.00 94.82  ? 785  ASN A O     1 
ATOM   5166 C  CB    . ASN A 1 682 ? -8.056  -24.667 51.926  1.00 82.42  ? 785  ASN A CB    1 
ATOM   5167 C  CG    . ASN A 1 682 ? -6.633  -24.135 51.874  1.00 78.62  ? 785  ASN A CG    1 
ATOM   5168 O  OD1   . ASN A 1 682 ? -5.664  -24.894 51.888  1.00 77.67  ? 785  ASN A OD1   1 
ATOM   5169 N  ND2   . ASN A 1 682 ? -6.504  -22.813 51.824  1.00 81.55  ? 785  ASN A ND2   1 
ATOM   5170 N  N     . PRO A 1 683 ? -6.524  -27.889 52.010  1.00 85.42  ? 786  PRO A N     1 
ATOM   5171 C  CA    . PRO A 1 683 ? -5.848  -28.838 52.902  1.00 83.73  ? 786  PRO A CA    1 
ATOM   5172 C  C     . PRO A 1 683 ? -4.767  -28.228 53.780  1.00 82.79  ? 786  PRO A C     1 
ATOM   5173 O  O     . PRO A 1 683 ? -4.041  -28.977 54.439  1.00 84.84  ? 786  PRO A O     1 
ATOM   5174 C  CB    . PRO A 1 683 ? -5.240  -29.844 51.913  1.00 84.43  ? 786  PRO A CB    1 
ATOM   5175 C  CG    . PRO A 1 683 ? -4.958  -29.031 50.701  1.00 84.40  ? 786  PRO A CG    1 
ATOM   5176 C  CD    . PRO A 1 683 ? -6.065  -28.012 50.615  1.00 84.66  ? 786  PRO A CD    1 
ATOM   5177 N  N     . ASP A 1 684 ? -4.633  -26.905 53.806  1.00 84.53  ? 787  ASP A N     1 
ATOM   5178 C  CA    . ASP A 1 684 ? -3.653  -26.270 54.676  1.00 91.50  ? 787  ASP A CA    1 
ATOM   5179 C  C     . ASP A 1 684 ? -4.116  -26.344 56.126  1.00 96.78  ? 787  ASP A C     1 
ATOM   5180 O  O     . ASP A 1 684 ? -5.311  -26.234 56.419  1.00 87.03  ? 787  ASP A O     1 
ATOM   5181 C  CB    . ASP A 1 684 ? -3.436  -24.816 54.254  1.00 91.15  ? 787  ASP A CB    1 
ATOM   5182 C  CG    . ASP A 1 684 ? -2.192  -24.201 54.873  1.00 102.39 ? 787  ASP A CG    1 
ATOM   5183 O  OD1   . ASP A 1 684 ? -2.011  -24.306 56.105  1.00 111.98 ? 787  ASP A OD1   1 
ATOM   5184 O  OD2   . ASP A 1 684 ? -1.390  -23.609 54.120  1.00 98.70  ? 787  ASP A OD2   1 
ATOM   5185 N  N     . ILE A 1 685 ? -3.158  -26.535 57.038  1.00 96.30  ? 788  ILE A N     1 
ATOM   5186 C  CA    . ILE A 1 685 ? -3.497  -26.651 58.455  1.00 100.18 ? 788  ILE A CA    1 
ATOM   5187 C  C     . ILE A 1 685 ? -4.107  -25.352 58.966  1.00 96.20  ? 788  ILE A C     1 
ATOM   5188 O  O     . ILE A 1 685 ? -5.046  -25.364 59.771  1.00 101.96 ? 788  ILE A O     1 
ATOM   5189 C  CB    . ILE A 1 685 ? -2.259  -27.062 59.276  1.00 104.79 ? 788  ILE A CB    1 
ATOM   5190 C  CG1   . ILE A 1 685 ? -1.068  -26.155 58.957  1.00 112.16 ? 788  ILE A CG1   1 
ATOM   5191 C  CG2   . ILE A 1 685 ? -1.910  -28.522 59.024  1.00 97.45  ? 788  ILE A CG2   1 
ATOM   5192 N  N     . MET A 1 686 ? -3.593  -24.214 58.504  1.00 90.02  ? 789  MET A N     1 
ATOM   5193 C  CA    . MET A 1 686 ? -4.126  -22.901 58.864  1.00 95.32  ? 789  MET A CA    1 
ATOM   5194 C  C     . MET A 1 686 ? -5.000  -22.330 57.758  1.00 95.81  ? 789  MET A C     1 
ATOM   5195 O  O     . MET A 1 686 ? -4.994  -21.122 57.506  1.00 98.38  ? 789  MET A O     1 
ATOM   5196 C  CB    . MET A 1 686 ? -2.989  -21.943 59.201  1.00 97.72  ? 789  MET A CB    1 
ATOM   5197 C  CG    . MET A 1 686 ? -2.151  -22.381 60.389  1.00 104.96 ? 789  MET A CG    1 
ATOM   5198 S  SD    . MET A 1 686 ? -0.884  -21.180 60.835  1.00 117.31 ? 789  MET A SD    1 
ATOM   5199 C  CE    . MET A 1 686 ? -0.138  -21.988 62.249  1.00 103.65 ? 789  MET A CE    1 
ATOM   5200 N  N     . SER A 1 687 ? -5.769  -23.192 57.086  1.00 97.26  ? 790  SER A N     1 
ATOM   5201 C  CA    . SER A 1 687 ? -6.575  -22.754 55.952  1.00 90.40  ? 790  SER A CA    1 
ATOM   5202 C  C     . SER A 1 687 ? -7.634  -21.740 56.362  1.00 91.90  ? 790  SER A C     1 
ATOM   5203 O  O     . SER A 1 687 ? -8.023  -20.891 55.553  1.00 92.10  ? 790  SER A O     1 
ATOM   5204 C  CB    . SER A 1 687 ? -7.232  -23.960 55.284  1.00 85.14  ? 790  SER A CB    1 
ATOM   5205 O  OG    . SER A 1 687 ? -7.998  -24.709 56.211  1.00 92.08  ? 790  SER A OG    1 
ATOM   5206 N  N     . GLU A 1 688 ? -8.107  -21.808 57.609  1.00 95.95  ? 791  GLU A N     1 
ATOM   5207 C  CA    . GLU A 1 688 ? -9.156  -20.898 58.057  1.00 99.30  ? 791  GLU A CA    1 
ATOM   5208 C  C     . GLU A 1 688 ? -8.704  -19.443 58.013  1.00 97.47  ? 791  GLU A C     1 
ATOM   5209 O  O     . GLU A 1 688 ? -9.531  -18.543 57.829  1.00 87.83  ? 791  GLU A O     1 
ATOM   5210 C  CB    . GLU A 1 688 ? -9.601  -21.273 59.471  1.00 105.13 ? 791  GLU A CB    1 
ATOM   5211 C  CG    . GLU A 1 688 ? -8.469  -21.295 60.486  1.00 110.31 ? 791  GLU A CG    1 
ATOM   5212 C  CD    . GLU A 1 688 ? -8.953  -21.572 61.895  1.00 137.05 ? 791  GLU A CD    1 
ATOM   5213 O  OE1   . GLU A 1 688 ? -10.161 -21.841 62.069  1.00 148.09 ? 791  GLU A OE1   1 
ATOM   5214 O  OE2   . GLU A 1 688 ? -8.125  -21.519 62.829  1.00 134.11 ? 791  GLU A OE2   1 
ATOM   5215 N  N     . LEU A 1 689 ? -7.402  -19.191 58.172  1.00 95.37  ? 792  LEU A N     1 
ATOM   5216 C  CA    . LEU A 1 689 ? -6.887  -17.827 58.188  1.00 95.15  ? 792  LEU A CA    1 
ATOM   5217 C  C     . LEU A 1 689 ? -6.859  -17.187 56.806  1.00 99.25  ? 792  LEU A C     1 
ATOM   5218 O  O     . LEU A 1 689 ? -6.716  -15.963 56.712  1.00 107.60 ? 792  LEU A O     1 
ATOM   5219 C  CB    . LEU A 1 689 ? -5.483  -17.808 58.797  1.00 103.48 ? 792  LEU A CB    1 
ATOM   5220 C  CG    . LEU A 1 689 ? -5.362  -18.349 60.224  1.00 103.38 ? 792  LEU A CG    1 
ATOM   5221 C  CD1   . LEU A 1 689 ? -3.917  -18.295 60.701  1.00 93.70  ? 792  LEU A CD1   1 
ATOM   5222 C  CD2   . LEU A 1 689 ? -6.275  -17.585 61.174  1.00 93.29  ? 792  LEU A CD2   1 
ATOM   5223 N  N     . LEU A 1 690 ? -6.985  -17.975 55.740  1.00 93.79  ? 793  LEU A N     1 
ATOM   5224 C  CA    . LEU A 1 690 ? -7.045  -17.451 54.380  1.00 90.42  ? 793  LEU A CA    1 
ATOM   5225 C  C     . LEU A 1 690 ? -8.414  -17.735 53.773  1.00 89.44  ? 793  LEU A C     1 
ATOM   5226 O  O     . LEU A 1 690 ? -9.230  -16.821 53.632  1.00 91.02  ? 793  LEU A O     1 
ATOM   5227 C  CB    . LEU A 1 690 ? -5.922  -18.052 53.530  1.00 93.21  ? 793  LEU A CB    1 
ATOM   5228 C  CG    . LEU A 1 690 ? -5.608  -17.392 52.187  1.00 84.86  ? 793  LEU A CG    1 
ATOM   5229 C  CD1   . LEU A 1 690 ? -5.083  -15.980 52.397  1.00 74.62  ? 793  LEU A CD1   1 
ATOM   5230 C  CD2   . LEU A 1 690 ? -4.607  -18.233 51.408  1.00 83.23  ? 793  LEU A CD2   1 
ATOM   5231 N  N     . PHE A 1 691 ? -8.688  -18.985 53.407  1.00 84.21  ? 794  PHE A N     1 
ATOM   5232 C  CA    . PHE A 1 691 ? -10.015 -19.413 52.992  1.00 82.98  ? 794  PHE A CA    1 
ATOM   5233 C  C     . PHE A 1 691 ? -10.087 -20.923 53.154  1.00 78.46  ? 794  PHE A C     1 
ATOM   5234 O  O     . PHE A 1 691 ? -9.093  -21.627 52.953  1.00 79.43  ? 794  PHE A O     1 
ATOM   5235 C  CB    . PHE A 1 691 ? -10.333 -18.998 51.549  1.00 94.79  ? 794  PHE A CB    1 
ATOM   5236 C  CG    . PHE A 1 691 ? -9.351  -19.514 50.533  1.00 90.55  ? 794  PHE A CG    1 
ATOM   5237 C  CD1   . PHE A 1 691 ? -8.233  -18.771 50.192  1.00 84.03  ? 794  PHE A CD1   1 
ATOM   5238 C  CD2   . PHE A 1 691 ? -9.555  -20.735 49.908  1.00 87.69  ? 794  PHE A CD2   1 
ATOM   5239 C  CE1   . PHE A 1 691 ? -7.331  -19.239 49.256  1.00 86.68  ? 794  PHE A CE1   1 
ATOM   5240 C  CE2   . PHE A 1 691 ? -8.656  -21.208 48.972  1.00 90.56  ? 794  PHE A CE2   1 
ATOM   5241 C  CZ    . PHE A 1 691 ? -7.543  -20.459 48.645  1.00 91.09  ? 794  PHE A CZ    1 
ATOM   5242 N  N     . GLN A 1 692 ? -11.267 -21.413 53.528  1.00 81.42  ? 795  GLN A N     1 
ATOM   5243 C  CA    . GLN A 1 692 ? -11.439 -22.830 53.819  1.00 95.74  ? 795  GLN A CA    1 
ATOM   5244 C  C     . GLN A 1 692 ? -11.956 -23.632 52.633  1.00 96.42  ? 795  GLN A C     1 
ATOM   5245 O  O     . GLN A 1 692 ? -11.610 -24.811 52.501  1.00 96.91  ? 795  GLN A O     1 
ATOM   5246 C  CB    . GLN A 1 692 ? -12.388 -23.015 55.010  1.00 100.08 ? 795  GLN A CB    1 
ATOM   5247 C  CG    . GLN A 1 692 ? -12.406 -24.428 55.571  1.00 109.23 ? 795  GLN A CG    1 
ATOM   5248 C  CD    . GLN A 1 692 ? -13.064 -24.508 56.934  1.00 134.15 ? 795  GLN A CD    1 
ATOM   5249 O  OE1   . GLN A 1 692 ? -13.402 -23.488 57.534  1.00 135.90 ? 795  GLN A OE1   1 
ATOM   5250 N  NE2   . GLN A 1 692 ? -13.247 -25.726 57.431  1.00 142.33 ? 795  GLN A NE2   1 
ATOM   5251 N  N     . ASN A 1 693 ? -12.765 -23.028 51.767  1.00 93.67  ? 796  ASN A N     1 
ATOM   5252 C  CA    . ASN A 1 693 ? -13.294 -23.691 50.582  1.00 98.83  ? 796  ASN A CA    1 
ATOM   5253 C  C     . ASN A 1 693 ? -12.832 -22.935 49.345  1.00 101.06 ? 796  ASN A C     1 
ATOM   5254 O  O     . ASN A 1 693 ? -13.079 -21.730 49.222  1.00 101.82 ? 796  ASN A O     1 
ATOM   5255 C  CB    . ASN A 1 693 ? -14.822 -23.766 50.625  1.00 103.74 ? 796  ASN A CB    1 
ATOM   5256 C  CG    . ASN A 1 693 ? -15.329 -24.783 51.628  1.00 112.87 ? 796  ASN A CG    1 
ATOM   5257 O  OD1   . ASN A 1 693 ? -14.566 -25.306 52.440  1.00 110.38 ? 796  ASN A OD1   1 
ATOM   5258 N  ND2   . ASN A 1 693 ? -16.626 -25.067 51.578  1.00 119.13 ? 796  ASN A ND2   1 
ATOM   5259 N  N     . ASN A 1 694 ? -12.166 -23.639 48.434  1.00 95.99  ? 797  ASN A N     1 
ATOM   5260 C  CA    . ASN A 1 694 ? -11.733 -23.057 47.171  1.00 93.58  ? 797  ASN A CA    1 
ATOM   5261 C  C     . ASN A 1 694 ? -12.786 -23.352 46.110  1.00 88.25  ? 797  ASN A C     1 
ATOM   5262 O  O     . ASN A 1 694 ? -13.047 -24.518 45.793  1.00 87.31  ? 797  ASN A O     1 
ATOM   5263 C  CB    . ASN A 1 694 ? -10.371 -23.605 46.751  1.00 93.17  ? 797  ASN A CB    1 
ATOM   5264 C  CG    . ASN A 1 694 ? -9.668  -22.712 45.747  1.00 93.42  ? 797  ASN A CG    1 
ATOM   5265 O  OD1   . ASN A 1 694 ? -10.303 -21.907 45.064  1.00 87.50  ? 797  ASN A OD1   1 
ATOM   5266 N  ND2   . ASN A 1 694 ? -8.349  -22.845 45.655  1.00 91.56  ? 797  ASN A ND2   1 
ATOM   5267 N  N     . GLU A 1 695 ? -13.390 -22.300 45.569  1.00 87.12  ? 798  GLU A N     1 
ATOM   5268 C  CA    . GLU A 1 695 ? -14.478 -22.415 44.608  1.00 87.17  ? 798  GLU A CA    1 
ATOM   5269 C  C     . GLU A 1 695 ? -13.989 -21.985 43.232  1.00 83.56  ? 798  GLU A C     1 
ATOM   5270 O  O     . GLU A 1 695 ? -13.444 -20.886 43.077  1.00 80.83  ? 798  GLU A O     1 
ATOM   5271 C  CB    . GLU A 1 695 ? -15.673 -21.567 45.049  1.00 88.30  ? 798  GLU A CB    1 
ATOM   5272 C  CG    . GLU A 1 695 ? -16.280 -22.007 46.372  1.00 93.07  ? 798  GLU A CG    1 
ATOM   5273 C  CD    . GLU A 1 695 ? -17.108 -20.919 47.029  1.00 104.80 ? 798  GLU A CD    1 
ATOM   5274 O  OE1   . GLU A 1 695 ? -16.623 -19.770 47.113  1.00 107.00 ? 798  GLU A OE1   1 
ATOM   5275 O  OE2   . GLU A 1 695 ? -18.244 -21.211 47.459  1.00 105.84 ? 798  GLU A OE2   1 
ATOM   5276 N  N     . ILE A 1 696 ? -14.172 -22.856 42.241  1.00 83.35  ? 799  ILE A N     1 
ATOM   5277 C  CA    . ILE A 1 696 ? -13.725 -22.613 40.875  1.00 82.74  ? 799  ILE A CA    1 
ATOM   5278 C  C     . ILE A 1 696 ? -14.850 -22.988 39.920  1.00 79.67  ? 799  ILE A C     1 
ATOM   5279 O  O     . ILE A 1 696 ? -15.507 -24.020 40.095  1.00 80.37  ? 799  ILE A O     1 
ATOM   5280 C  CB    . ILE A 1 696 ? -12.443 -23.409 40.545  1.00 78.45  ? 799  ILE A CB    1 
ATOM   5281 C  CG1   . ILE A 1 696 ? -11.324 -23.067 41.532  1.00 79.81  ? 799  ILE A CG1   1 
ATOM   5282 C  CG2   . ILE A 1 696 ? -11.989 -23.132 39.120  1.00 78.73  ? 799  ILE A CG2   1 
ATOM   5283 C  CD1   . ILE A 1 696 ? -10.056 -23.874 41.331  1.00 77.63  ? 799  ILE A CD1   1 
ATOM   5284 N  N     . ILE A 1 697 ? -15.073 -22.147 38.913  1.00 77.64  ? 800  ILE A N     1 
ATOM   5285 C  CA    . ILE A 1 697 ? -16.076 -22.393 37.881  1.00 80.79  ? 800  ILE A CA    1 
ATOM   5286 C  C     . ILE A 1 697 ? -15.377 -22.979 36.662  1.00 80.60  ? 800  ILE A C     1 
ATOM   5287 O  O     . ILE A 1 697 ? -14.459 -22.364 36.107  1.00 78.68  ? 800  ILE A O     1 
ATOM   5288 C  CB    . ILE A 1 697 ? -16.834 -21.109 37.512  1.00 79.45  ? 800  ILE A CB    1 
ATOM   5289 C  CG1   . ILE A 1 697 ? -17.682 -20.626 38.690  1.00 82.17  ? 800  ILE A CG1   1 
ATOM   5290 C  CG2   . ILE A 1 697 ? -17.706 -21.341 36.288  1.00 81.96  ? 800  ILE A CG2   1 
ATOM   5291 C  CD1   . ILE A 1 697 ? -18.387 -19.312 38.434  1.00 82.62  ? 800  ILE A CD1   1 
ATOM   5292 N  N     . PHE A 1 698 ? -15.810 -24.166 36.243  1.00 81.16  ? 801  PHE A N     1 
ATOM   5293 C  CA    . PHE A 1 698 ? -15.293 -24.823 35.048  1.00 82.54  ? 801  PHE A CA    1 
ATOM   5294 C  C     . PHE A 1 698 ? -16.295 -24.612 33.918  1.00 90.64  ? 801  PHE A C     1 
ATOM   5295 O  O     . PHE A 1 698 ? -17.395 -25.174 33.941  1.00 84.98  ? 801  PHE A O     1 
ATOM   5296 C  CB    . PHE A 1 698 ? -15.052 -26.309 35.305  1.00 80.27  ? 801  PHE A CB    1 
ATOM   5297 C  CG    . PHE A 1 698 ? -14.631 -27.076 34.084  1.00 85.07  ? 801  PHE A CG    1 
ATOM   5298 C  CD1   . PHE A 1 698 ? -13.307 -27.089 33.681  1.00 86.72  ? 801  PHE A CD1   1 
ATOM   5299 C  CD2   . PHE A 1 698 ? -15.558 -27.791 33.344  1.00 90.83  ? 801  PHE A CD2   1 
ATOM   5300 C  CE1   . PHE A 1 698 ? -12.915 -27.795 32.560  1.00 91.91  ? 801  PHE A CE1   1 
ATOM   5301 C  CE2   . PHE A 1 698 ? -15.172 -28.499 32.222  1.00 93.91  ? 801  PHE A CE2   1 
ATOM   5302 C  CZ    . PHE A 1 698 ? -13.849 -28.501 31.830  1.00 91.75  ? 801  PHE A CZ    1 
ATOM   5303 N  N     . LYS A 1 699 ? -15.914 -23.805 32.930  1.00 82.74  ? 802  LYS A N     1 
ATOM   5304 C  CA    . LYS A 1 699 ? -16.801 -23.411 31.843  1.00 82.90  ? 802  LYS A CA    1 
ATOM   5305 C  C     . LYS A 1 699 ? -16.358 -24.100 30.558  1.00 87.79  ? 802  LYS A C     1 
ATOM   5306 O  O     . LYS A 1 699 ? -15.228 -23.901 30.098  1.00 87.24  ? 802  LYS A O     1 
ATOM   5307 C  CB    . LYS A 1 699 ? -16.805 -21.892 31.672  1.00 84.37  ? 802  LYS A CB    1 
ATOM   5308 C  CG    . LYS A 1 699 ? -18.034 -21.347 30.966  1.00 95.09  ? 802  LYS A CG    1 
ATOM   5309 C  CD    . LYS A 1 699 ? -18.003 -19.829 30.905  1.00 98.91  ? 802  LYS A CD    1 
ATOM   5310 C  CE    . LYS A 1 699 ? -19.304 -19.271 30.350  1.00 110.83 ? 802  LYS A CE    1 
ATOM   5311 N  NZ    . LYS A 1 699 ? -20.464 -19.581 31.233  1.00 111.39 ? 802  LYS A NZ    1 
ATOM   5312 N  N     . ASN A 1 700 ? -17.250 -24.903 29.981  1.00 86.52  ? 803  ASN A N     1 
ATOM   5313 C  CA    . ASN A 1 700 ? -16.972 -25.669 28.772  1.00 86.47  ? 803  ASN A CA    1 
ATOM   5314 C  C     . ASN A 1 700 ? -17.919 -25.207 27.674  1.00 92.37  ? 803  ASN A C     1 
ATOM   5315 O  O     . ASN A 1 700 ? -19.142 -25.246 27.850  1.00 99.05  ? 803  ASN A O     1 
ATOM   5316 C  CB    . ASN A 1 700 ? -17.133 -27.170 29.027  1.00 84.41  ? 803  ASN A CB    1 
ATOM   5317 C  CG    . ASN A 1 700 ? -16.626 -28.024 27.876  1.00 87.73  ? 803  ASN A CG    1 
ATOM   5318 O  OD1   . ASN A 1 700 ? -16.429 -27.541 26.760  1.00 87.57  ? 803  ASN A OD1   1 
ATOM   5319 N  ND2   . ASN A 1 700 ? -16.417 -29.308 28.145  1.00 89.19  ? 803  ASN A ND2   1 
ATOM   5320 N  N     . GLY A 1 701 ? -17.357 -24.777 26.549  1.00 91.23  ? 804  GLY A N     1 
ATOM   5321 C  CA    . GLY A 1 701 ? -18.138 -24.358 25.398  1.00 95.56  ? 804  GLY A CA    1 
ATOM   5322 C  C     . GLY A 1 701 ? -17.952 -22.913 24.984  1.00 102.65 ? 804  GLY A C     1 
ATOM   5323 O  O     . GLY A 1 701 ? -18.358 -22.552 23.869  1.00 107.87 ? 804  GLY A O     1 
ATOM   5324 N  N     . ASP A 1 702 ? -17.363 -22.064 25.820  1.00 97.52  ? 805  ASP A N     1 
ATOM   5325 C  CA    . ASP A 1 702 ? -17.156 -20.659 25.499  1.00 102.45 ? 805  ASP A CA    1 
ATOM   5326 C  C     . ASP A 1 702 ? -15.671 -20.333 25.517  1.00 100.40 ? 805  ASP A C     1 
ATOM   5327 O  O     . ASP A 1 702 ? -14.929 -20.812 26.381  1.00 98.75  ? 805  ASP A O     1 
ATOM   5328 C  CB    . ASP A 1 702 ? -17.900 -19.749 26.481  1.00 110.88 ? 805  ASP A CB    1 
ATOM   5329 C  CG    . ASP A 1 702 ? -19.387 -19.676 26.196  1.00 129.13 ? 805  ASP A CG    1 
ATOM   5330 O  OD1   . ASP A 1 702 ? -19.762 -19.647 25.004  1.00 124.03 ? 805  ASP A OD1   1 
ATOM   5331 O  OD2   . ASP A 1 702 ? -20.179 -19.649 27.162  1.00 133.59 ? 805  ASP A OD2   1 
ATOM   5332 N  N     . ASP A 1 703 ? -15.243 -19.516 24.559  1.00 105.90 ? 806  ASP A N     1 
ATOM   5333 C  CA    . ASP A 1 703 ? -13.851 -19.084 24.485  1.00 102.65 ? 806  ASP A CA    1 
ATOM   5334 C  C     . ASP A 1 703 ? -13.583 -18.073 25.592  1.00 103.64 ? 806  ASP A C     1 
ATOM   5335 O  O     . ASP A 1 703 ? -14.143 -16.972 25.588  1.00 107.75 ? 806  ASP A O     1 
ATOM   5336 C  CB    . ASP A 1 703 ? -13.556 -18.485 23.114  1.00 98.04  ? 806  ASP A CB    1 
ATOM   5337 C  CG    . ASP A 1 703 ? -12.085 -18.180 22.916  1.00 104.68 ? 806  ASP A CG    1 
ATOM   5338 O  OD1   . ASP A 1 703 ? -11.251 -18.765 23.640  1.00 114.55 ? 806  ASP A OD1   1 
ATOM   5339 O  OD2   . ASP A 1 703 ? -11.761 -17.349 22.042  1.00 104.61 ? 806  ASP A OD2   1 
ATOM   5340 N  N     . LEU A 1 704 ? -12.728 -18.441 26.545  1.00 102.51 ? 807  LEU A N     1 
ATOM   5341 C  CA    . LEU A 1 704 ? -12.400 -17.580 27.672  1.00 97.87  ? 807  LEU A CA    1 
ATOM   5342 C  C     . LEU A 1 704 ? -11.116 -16.789 27.456  1.00 95.22  ? 807  LEU A C     1 
ATOM   5343 O  O     . LEU A 1 704 ? -10.604 -16.188 28.405  1.00 93.56  ? 807  LEU A O     1 
ATOM   5344 C  CB    . LEU A 1 704 ? -12.298 -18.409 28.953  1.00 92.36  ? 807  LEU A CB    1 
ATOM   5345 C  CG    . LEU A 1 704 ? -13.615 -19.010 29.450  1.00 95.99  ? 807  LEU A CG    1 
ATOM   5346 C  CD1   . LEU A 1 704 ? -13.396 -19.850 30.696  1.00 91.59  ? 807  LEU A CD1   1 
ATOM   5347 C  CD2   . LEU A 1 704 ? -14.633 -17.913 29.719  1.00 98.18  ? 807  LEU A CD2   1 
ATOM   5348 N  N     . ARG A 1 705 ? -10.584 -16.773 26.231  1.00 95.02  ? 808  ARG A N     1 
ATOM   5349 C  CA    . ARG A 1 705 ? -9.390  -15.979 25.961  1.00 95.07  ? 808  ARG A CA    1 
ATOM   5350 C  C     . ARG A 1 705 ? -9.696  -14.488 26.018  1.00 91.91  ? 808  ARG A C     1 
ATOM   5351 O  O     . ARG A 1 705 ? -8.857  -13.693 26.458  1.00 88.36  ? 808  ARG A O     1 
ATOM   5352 C  CB    . ARG A 1 705 ? -8.802  -16.353 24.601  1.00 97.40  ? 808  ARG A CB    1 
ATOM   5353 C  CG    . ARG A 1 705 ? -8.215  -17.752 24.535  1.00 96.73  ? 808  ARG A CG    1 
ATOM   5354 C  CD    . ARG A 1 705 ? -7.567  -18.002 23.183  1.00 106.16 ? 808  ARG A CD    1 
ATOM   5355 N  NE    . ARG A 1 705 ? -8.527  -17.877 22.093  1.00 108.69 ? 808  ARG A NE    1 
ATOM   5356 C  CZ    . ARG A 1 705 ? -8.205  -17.879 20.807  1.00 106.05 ? 808  ARG A CZ    1 
ATOM   5357 N  NH1   . ARG A 1 705 ? -6.947  -17.987 20.410  1.00 111.68 ? 808  ARG A NH1   1 
ATOM   5358 N  NH2   . ARG A 1 705 ? -9.168  -17.767 19.897  1.00 105.63 ? 808  ARG A NH2   1 
ATOM   5359 N  N     . GLN A 1 706 ? -10.890 -14.091 25.574  1.00 97.44  ? 809  GLN A N     1 
ATOM   5360 C  CA    . GLN A 1 706 ? -11.274 -12.685 25.634  1.00 98.29  ? 809  GLN A CA    1 
ATOM   5361 C  C     . GLN A 1 706 ? -11.380 -12.207 27.076  1.00 100.18 ? 809  GLN A C     1 
ATOM   5362 O  O     . GLN A 1 706 ? -11.050 -11.054 27.381  1.00 97.60  ? 809  GLN A O     1 
ATOM   5363 C  CB    . GLN A 1 706 ? -12.598 -12.466 24.902  1.00 104.43 ? 809  GLN A CB    1 
ATOM   5364 C  CG    . GLN A 1 706 ? -12.528 -12.659 23.395  1.00 107.61 ? 809  GLN A CG    1 
ATOM   5365 C  CD    . GLN A 1 706 ? -12.397 -14.114 22.985  1.00 108.54 ? 809  GLN A CD    1 
ATOM   5366 O  OE1   . GLN A 1 706 ? -12.691 -15.021 23.765  1.00 103.15 ? 809  GLN A OE1   1 
ATOM   5367 N  NE2   . GLN A 1 706 ? -11.948 -14.345 21.757  1.00 115.39 ? 809  GLN A NE2   1 
ATOM   5368 N  N     . ASP A 1 707 ? -11.839 -13.078 27.976  1.00 100.86 ? 810  ASP A N     1 
ATOM   5369 C  CA    . ASP A 1 707 ? -11.906 -12.714 29.387  1.00 91.19  ? 810  ASP A CA    1 
ATOM   5370 C  C     . ASP A 1 707 ? -10.513 -12.598 29.993  1.00 88.47  ? 810  ASP A C     1 
ATOM   5371 O  O     . ASP A 1 707 ? -10.253 -11.686 30.786  1.00 93.71  ? 810  ASP A O     1 
ATOM   5372 C  CB    . ASP A 1 707 ? -12.748 -13.735 30.151  1.00 98.79  ? 810  ASP A CB    1 
ATOM   5373 C  CG    . ASP A 1 707 ? -14.217 -13.668 29.782  1.00 120.02 ? 810  ASP A CG    1 
ATOM   5374 O  OD1   . ASP A 1 707 ? -14.543 -13.859 28.591  1.00 120.63 ? 810  ASP A OD1   1 
ATOM   5375 O  OD2   . ASP A 1 707 ? -15.045 -13.425 30.684  1.00 113.00 ? 810  ASP A OD2   1 
ATOM   5376 N  N     . MET A 1 708 ? -9.606  -13.510 29.631  1.00 81.45  ? 811  MET A N     1 
ATOM   5377 C  CA    . MET A 1 708 ? -8.227  -13.420 30.102  1.00 77.94  ? 811  MET A CA    1 
ATOM   5378 C  C     . MET A 1 708 ? -7.612  -12.072 29.751  1.00 84.92  ? 811  MET A C     1 
ATOM   5379 O  O     . MET A 1 708 ? -7.020  -11.403 30.606  1.00 88.71  ? 811  MET A O     1 
ATOM   5380 C  CB    . MET A 1 708 ? -7.387  -14.549 29.503  1.00 76.12  ? 811  MET A CB    1 
ATOM   5381 C  CG    . MET A 1 708 ? -7.601  -15.912 30.123  1.00 79.65  ? 811  MET A CG    1 
ATOM   5382 S  SD    . MET A 1 708 ? -6.425  -17.109 29.460  1.00 85.87  ? 811  MET A SD    1 
ATOM   5383 C  CE    . MET A 1 708 ? -4.880  -16.254 29.753  1.00 78.83  ? 811  MET A CE    1 
ATOM   5384 N  N     . LEU A 1 709 ? -7.744  -11.658 28.488  1.00 84.37  ? 812  LEU A N     1 
ATOM   5385 C  CA    . LEU A 1 709 ? -7.121  -10.416 28.045  1.00 81.75  ? 812  LEU A CA    1 
ATOM   5386 C  C     . LEU A 1 709 ? -7.739  -9.207  28.737  1.00 79.99  ? 812  LEU A C     1 
ATOM   5387 O  O     . LEU A 1 709 ? -7.018  -8.312  29.192  1.00 78.93  ? 812  LEU A O     1 
ATOM   5388 C  CB    . LEU A 1 709 ? -7.236  -10.287 26.526  1.00 87.86  ? 812  LEU A CB    1 
ATOM   5389 C  CG    . LEU A 1 709 ? -6.541  -9.086  25.883  1.00 80.63  ? 812  LEU A CG    1 
ATOM   5390 C  CD1   . LEU A 1 709 ? -5.034  -9.171  26.061  1.00 80.72  ? 812  LEU A CD1   1 
ATOM   5391 C  CD2   . LEU A 1 709 ? -6.901  -8.990  24.415  1.00 85.01  ? 812  LEU A CD2   1 
ATOM   5392 N  N     . THR A 1 710 ? -9.071  -9.161  28.829  1.00 81.54  ? 813  THR A N     1 
ATOM   5393 C  CA    . THR A 1 710 ? -9.720  -8.039  29.500  1.00 83.60  ? 813  THR A CA    1 
ATOM   5394 C  C     . THR A 1 710 ? -9.368  -8.003  30.981  1.00 81.25  ? 813  THR A C     1 
ATOM   5395 O  O     . THR A 1 710 ? -9.124  -6.928  31.541  1.00 80.72  ? 813  THR A O     1 
ATOM   5396 C  CB    . THR A 1 710 ? -11.237 -8.111  29.311  1.00 87.17  ? 813  THR A CB    1 
ATOM   5397 O  OG1   . THR A 1 710 ? -11.709 -9.409  29.693  1.00 102.51 ? 813  THR A OG1   1 
ATOM   5398 C  CG2   . THR A 1 710 ? -11.607 -7.848  27.863  1.00 88.08  ? 813  THR A CG2   1 
ATOM   5399 N  N     . LEU A 1 711 ? -9.330  -9.167  31.632  1.00 80.39  ? 814  LEU A N     1 
ATOM   5400 C  CA    . LEU A 1 711 ? -8.940  -9.211  33.037  1.00 79.39  ? 814  LEU A CA    1 
ATOM   5401 C  C     . LEU A 1 711 ? -7.475  -8.835  33.215  1.00 78.54  ? 814  LEU A C     1 
ATOM   5402 O  O     . LEU A 1 711 ? -7.109  -8.197  34.209  1.00 82.77  ? 814  LEU A O     1 
ATOM   5403 C  CB    . LEU A 1 711 ? -9.223  -10.597 33.615  1.00 80.69  ? 814  LEU A CB    1 
ATOM   5404 C  CG    . LEU A 1 711 ? -10.704 -10.895 33.863  1.00 79.37  ? 814  LEU A CG    1 
ATOM   5405 C  CD1   . LEU A 1 711 ? -10.958 -12.389 33.901  1.00 77.76  ? 814  LEU A CD1   1 
ATOM   5406 C  CD2   . LEU A 1 711 ? -11.166 -10.242 35.156  1.00 78.54  ? 814  LEU A CD2   1 
ATOM   5407 N  N     . GLN A 1 712 ? -6.621  -9.217  32.262  1.00 74.14  ? 815  GLN A N     1 
ATOM   5408 C  CA    . GLN A 1 712 ? -5.221  -8.812  32.327  1.00 76.07  ? 815  GLN A CA    1 
ATOM   5409 C  C     . GLN A 1 712 ? -5.074  -7.304  32.161  1.00 74.93  ? 815  GLN A C     1 
ATOM   5410 O  O     . GLN A 1 712 ? -4.233  -6.680  32.818  1.00 76.74  ? 815  GLN A O     1 
ATOM   5411 C  CB    . GLN A 1 712 ? -4.409  -9.545  31.261  1.00 73.85  ? 815  GLN A CB    1 
ATOM   5412 C  CG    . GLN A 1 712 ? -2.936  -9.171  31.249  1.00 78.81  ? 815  GLN A CG    1 
ATOM   5413 C  CD    . GLN A 1 712 ? -2.288  -9.393  29.897  1.00 81.97  ? 815  GLN A CD    1 
ATOM   5414 O  OE1   . GLN A 1 712 ? -2.962  -9.715  28.919  1.00 88.27  ? 815  GLN A OE1   1 
ATOM   5415 N  NE2   . GLN A 1 712 ? -0.972  -9.218  29.833  1.00 76.75  ? 815  GLN A NE2   1 
ATOM   5416 N  N     . ILE A 1 713 ? -5.880  -6.702  31.285  1.00 77.44  ? 816  ILE A N     1 
ATOM   5417 C  CA    . ILE A 1 713 ? -5.813  -5.257  31.089  1.00 79.02  ? 816  ILE A CA    1 
ATOM   5418 C  C     . ILE A 1 713 ? -6.342  -4.530  32.317  1.00 71.71  ? 816  ILE A C     1 
ATOM   5419 O  O     . ILE A 1 713 ? -5.796  -3.498  32.727  1.00 69.68  ? 816  ILE A O     1 
ATOM   5420 C  CB    . ILE A 1 713 ? -6.576  -4.859  29.812  1.00 75.52  ? 816  ILE A CB    1 
ATOM   5421 C  CG1   . ILE A 1 713 ? -5.894  -5.462  28.585  1.00 73.01  ? 816  ILE A CG1   1 
ATOM   5422 C  CG2   . ILE A 1 713 ? -6.659  -3.344  29.675  1.00 69.64  ? 816  ILE A CG2   1 
ATOM   5423 C  CD1   . ILE A 1 713 ? -6.766  -5.485  27.363  1.00 87.24  ? 816  ILE A CD1   1 
ATOM   5424 N  N     . ILE A 1 714 ? -7.403  -5.060  32.930  1.00 74.81  ? 817  ILE A N     1 
ATOM   5425 C  CA    . ILE A 1 714 ? -7.946  -4.453  34.143  1.00 79.38  ? 817  ILE A CA    1 
ATOM   5426 C  C     . ILE A 1 714 ? -6.900  -4.450  35.251  1.00 75.43  ? 817  ILE A C     1 
ATOM   5427 O  O     . ILE A 1 714 ? -6.731  -3.452  35.963  1.00 85.36  ? 817  ILE A O     1 
ATOM   5428 C  CB    . ILE A 1 714 ? -9.233  -5.182  34.575  1.00 81.59  ? 817  ILE A CB    1 
ATOM   5429 C  CG1   . ILE A 1 714 ? -10.381 -4.836  33.625  1.00 74.43  ? 817  ILE A CG1   1 
ATOM   5430 C  CG2   . ILE A 1 714 ? -9.594  -4.834  36.012  1.00 77.12  ? 817  ILE A CG2   1 
ATOM   5431 C  CD1   . ILE A 1 714 ? -11.702 -5.458  34.011  1.00 78.07  ? 817  ILE A CD1   1 
ATOM   5432 N  N     . ARG A 1 715 ? -6.174  -5.559  35.407  1.00 67.77  ? 818  ARG A N     1 
ATOM   5433 C  CA    . ARG A 1 715 ? -5.112  -5.610  36.406  1.00 73.80  ? 818  ARG A CA    1 
ATOM   5434 C  C     . ARG A 1 715 ? -4.028  -4.581  36.109  1.00 75.47  ? 818  ARG A C     1 
ATOM   5435 O  O     . ARG A 1 715 ? -3.521  -3.921  37.023  1.00 86.28  ? 818  ARG A O     1 
ATOM   5436 C  CB    . ARG A 1 715 ? -4.517  -7.017  36.470  1.00 79.01  ? 818  ARG A CB    1 
ATOM   5437 C  CG    . ARG A 1 715 ? -3.384  -7.167  37.477  1.00 76.54  ? 818  ARG A CG    1 
ATOM   5438 C  CD    . ARG A 1 715 ? -2.909  -8.608  37.573  1.00 80.97  ? 818  ARG A CD    1 
ATOM   5439 N  NE    . ARG A 1 715 ? -3.961  -9.502  38.041  1.00 92.94  ? 818  ARG A NE    1 
ATOM   5440 N  N     . ILE A 1 716 ? -3.669  -4.424  34.834  1.00 76.92  ? 819  ILE A N     1 
ATOM   5441 C  CA    . ILE A 1 716 ? -2.624  -3.474  34.466  1.00 76.31  ? 819  ILE A CA    1 
ATOM   5442 C  C     . ILE A 1 716 ? -3.099  -2.042  34.681  1.00 74.51  ? 819  ILE A C     1 
ATOM   5443 O  O     . ILE A 1 716 ? -2.347  -1.190  35.171  1.00 67.40  ? 819  ILE A O     1 
ATOM   5444 C  CB    . ILE A 1 716 ? -2.176  -3.724  33.014  1.00 72.89  ? 819  ILE A CB    1 
ATOM   5445 C  CG1   . ILE A 1 716 ? -1.500  -5.092  32.909  1.00 72.31  ? 819  ILE A CG1   1 
ATOM   5446 C  CG2   . ILE A 1 716 ? -1.241  -2.621  32.531  1.00 62.29  ? 819  ILE A CG2   1 
ATOM   5447 C  CD1   . ILE A 1 716 ? -1.047  -5.449  31.521  1.00 78.41  ? 819  ILE A CD1   1 
ATOM   5448 N  N     . MET A 1 717 ? -4.354  -1.753  34.326  1.00 78.34  ? 820  MET A N     1 
ATOM   5449 C  CA    . MET A 1 717 ? -4.892  -0.413  34.543  1.00 79.89  ? 820  MET A CA    1 
ATOM   5450 C  C     . MET A 1 717 ? -4.927  -0.066  36.025  1.00 83.59  ? 820  MET A C     1 
ATOM   5451 O  O     . MET A 1 717 ? -4.647  1.075   36.410  1.00 83.15  ? 820  MET A O     1 
ATOM   5452 C  CB    . MET A 1 717 ? -6.292  -0.304  33.939  1.00 79.54  ? 820  MET A CB    1 
ATOM   5453 C  CG    . MET A 1 717 ? -6.337  -0.446  32.434  1.00 77.96  ? 820  MET A CG    1 
ATOM   5454 S  SD    . MET A 1 717 ? -8.024  -0.426  31.809  1.00 91.60  ? 820  MET A SD    1 
ATOM   5455 C  CE    . MET A 1 717 ? -8.535  1.214   32.305  1.00 83.61  ? 820  MET A CE    1 
ATOM   5456 N  N     . GLU A 1 718 ? -5.273  -1.040  36.872  1.00 87.43  ? 821  GLU A N     1 
ATOM   5457 C  CA    . GLU A 1 718 ? -5.305  -0.798  38.310  1.00 87.61  ? 821  GLU A CA    1 
ATOM   5458 C  C     . GLU A 1 718 ? -3.916  -0.475  38.845  1.00 89.53  ? 821  GLU A C     1 
ATOM   5459 O  O     . GLU A 1 718 ? -3.758  0.409   39.695  1.00 90.44  ? 821  GLU A O     1 
ATOM   5460 C  CB    . GLU A 1 718 ? -5.890  -2.012  39.031  1.00 94.79  ? 821  GLU A CB    1 
ATOM   5461 C  CG    . GLU A 1 718 ? -5.990  -1.858  40.540  1.00 96.64  ? 821  GLU A CG    1 
ATOM   5462 C  CD    . GLU A 1 718 ? -6.479  -3.121  41.221  1.00 99.39  ? 821  GLU A CD    1 
ATOM   5463 O  OE1   . GLU A 1 718 ? -6.383  -4.204  40.605  1.00 98.68  ? 821  GLU A OE1   1 
ATOM   5464 O  OE2   . GLU A 1 718 ? -6.963  -3.030  42.370  1.00 100.19 ? 821  GLU A OE2   1 
ATOM   5465 N  N     . ASN A 1 719 ? -2.893  -1.182  38.356  1.00 82.44  ? 822  ASN A N     1 
ATOM   5466 C  CA    . ASN A 1 719 ? -1.527  -0.890  38.772  1.00 80.33  ? 822  ASN A CA    1 
ATOM   5467 C  C     . ASN A 1 719 ? -1.076  0.483   38.287  1.00 86.55  ? 822  ASN A C     1 
ATOM   5468 O  O     . ASN A 1 719 ? -0.253  1.130   38.943  1.00 98.07  ? 822  ASN A O     1 
ATOM   5469 C  CB    . ASN A 1 719 ? -0.581  -1.977  38.263  1.00 85.28  ? 822  ASN A CB    1 
ATOM   5470 C  CG    . ASN A 1 719 ? 0.831   -1.815  38.788  1.00 98.86  ? 822  ASN A CG    1 
ATOM   5471 O  OD1   . ASN A 1 719 ? 1.157   -2.287  39.878  1.00 115.99 ? 822  ASN A OD1   1 
ATOM   5472 N  ND2   . ASN A 1 719 ? 1.680   -1.148  38.013  1.00 106.89 ? 822  ASN A ND2   1 
ATOM   5473 N  N     . ILE A 1 720 ? -1.599  0.940   37.147  1.00 89.86  ? 823  ILE A N     1 
ATOM   5474 C  CA    . ILE A 1 720 ? -1.307  2.294   36.685  1.00 90.61  ? 823  ILE A CA    1 
ATOM   5475 C  C     . ILE A 1 720 ? -1.910  3.318   37.637  1.00 90.11  ? 823  ILE A C     1 
ATOM   5476 O  O     . ILE A 1 720 ? -1.230  4.245   38.092  1.00 93.96  ? 823  ILE A O     1 
ATOM   5477 C  CB    . ILE A 1 720 ? -1.820  2.495   35.247  1.00 90.53  ? 823  ILE A CB    1 
ATOM   5478 C  CG1   . ILE A 1 720 ? -0.997  1.667   34.258  1.00 87.46  ? 823  ILE A CG1   1 
ATOM   5479 C  CG2   . ILE A 1 720 ? -1.792  3.972   34.872  1.00 79.58  ? 823  ILE A CG2   1 
ATOM   5480 C  CD1   . ILE A 1 720 ? 0.439   2.124   34.125  1.00 89.23  ? 823  ILE A CD1   1 
ATOM   5481 N  N     . TRP A 1 721 ? -3.199  3.164   37.951  1.00 90.36  ? 824  TRP A N     1 
ATOM   5482 C  CA    . TRP A 1 721 ? -3.871  4.109   38.837  1.00 90.41  ? 824  TRP A CA    1 
ATOM   5483 C  C     . TRP A 1 721 ? -3.272  4.082   40.236  1.00 94.04  ? 824  TRP A C     1 
ATOM   5484 O  O     . TRP A 1 721 ? -3.131  5.129   40.879  1.00 97.51  ? 824  TRP A O     1 
ATOM   5485 C  CB    . TRP A 1 721 ? -5.365  3.796   38.900  1.00 89.68  ? 824  TRP A CB    1 
ATOM   5486 C  CG    . TRP A 1 721 ? -6.088  4.005   37.611  1.00 89.18  ? 824  TRP A CG    1 
ATOM   5487 C  CD1   . TRP A 1 721 ? -5.778  4.903   36.631  1.00 86.73  ? 824  TRP A CD1   1 
ATOM   5488 C  CD2   . TRP A 1 721 ? -7.246  3.296   37.156  1.00 86.87  ? 824  TRP A CD2   1 
ATOM   5489 N  NE1   . TRP A 1 721 ? -6.676  4.801   35.596  1.00 84.87  ? 824  TRP A NE1   1 
ATOM   5490 C  CE2   . TRP A 1 721 ? -7.585  3.820   35.893  1.00 83.47  ? 824  TRP A CE2   1 
ATOM   5491 C  CE3   . TRP A 1 721 ? -8.028  2.270   37.694  1.00 87.25  ? 824  TRP A CE3   1 
ATOM   5492 C  CZ2   . TRP A 1 721 ? -8.674  3.354   35.160  1.00 82.01  ? 824  TRP A CZ2   1 
ATOM   5493 C  CZ3   . TRP A 1 721 ? -9.108  1.808   36.964  1.00 89.04  ? 824  TRP A CZ3   1 
ATOM   5494 C  CH2   . TRP A 1 721 ? -9.421  2.349   35.711  1.00 85.83  ? 824  TRP A CH2   1 
ATOM   5495 N  N     . GLN A 1 722 ? -2.915  2.892   40.724  1.00 92.58  ? 825  GLN A N     1 
ATOM   5496 C  CA    . GLN A 1 722 ? -2.432  2.766   42.094  1.00 93.84  ? 825  GLN A CA    1 
ATOM   5497 C  C     . GLN A 1 722 ? -1.104  3.490   42.281  1.00 94.07  ? 825  GLN A C     1 
ATOM   5498 O  O     . GLN A 1 722 ? -0.938  4.270   43.225  1.00 100.20 ? 825  GLN A O     1 
ATOM   5499 C  CB    . GLN A 1 722 ? -2.301  1.289   42.468  1.00 93.68  ? 825  GLN A CB    1 
ATOM   5500 C  CG    . GLN A 1 722 ? -2.616  0.987   43.925  1.00 99.47  ? 825  GLN A CG    1 
ATOM   5501 C  CD    . GLN A 1 722 ? -4.082  1.200   44.261  1.00 98.83  ? 825  GLN A CD    1 
ATOM   5502 O  OE1   . GLN A 1 722 ? -4.440  2.150   44.958  1.00 105.70 ? 825  GLN A OE1   1 
ATOM   5503 N  NE2   . GLN A 1 722 ? -4.937  0.312   43.768  1.00 93.69  ? 825  GLN A NE2   1 
ATOM   5504 N  N     . ASN A 1 723 ? -0.148  3.259   41.380  1.00 92.02  ? 826  ASN A N     1 
ATOM   5505 C  CA    . ASN A 1 723 ? 1.171   3.862   41.528  1.00 93.86  ? 826  ASN A CA    1 
ATOM   5506 C  C     . ASN A 1 723 ? 1.177   5.363   41.272  1.00 95.44  ? 826  ASN A C     1 
ATOM   5507 O  O     . ASN A 1 723 ? 2.182   6.017   41.570  1.00 97.05  ? 826  ASN A O     1 
ATOM   5508 C  CB    . ASN A 1 723 ? 2.167   3.165   40.602  1.00 86.54  ? 826  ASN A CB    1 
ATOM   5509 C  CG    . ASN A 1 723 ? 2.474   1.748   41.046  1.00 101.37 ? 826  ASN A CG    1 
ATOM   5510 O  OD1   . ASN A 1 723 ? 3.383   1.519   41.845  1.00 110.37 ? 826  ASN A OD1   1 
ATOM   5511 N  ND2   . ASN A 1 723 ? 1.708   0.790   40.538  1.00 97.67  ? 826  ASN A ND2   1 
ATOM   5512 N  N     . GLN A 1 724 ? 0.094   5.926   40.736  1.00 93.45  ? 827  GLN A N     1 
ATOM   5513 C  CA    . GLN A 1 724 ? -0.003  7.370   40.571  1.00 93.31  ? 827  GLN A CA    1 
ATOM   5514 C  C     . GLN A 1 724 ? -0.668  8.059   41.753  1.00 102.62 ? 827  GLN A C     1 
ATOM   5515 O  O     . GLN A 1 724 ? -0.525  9.278   41.902  1.00 102.43 ? 827  GLN A O     1 
ATOM   5516 C  CB    . GLN A 1 724 ? -0.777  7.713   39.295  1.00 101.33 ? 827  GLN A CB    1 
ATOM   5517 C  CG    . GLN A 1 724 ? -0.068  7.326   38.011  1.00 120.57 ? 827  GLN A CG    1 
ATOM   5518 C  CD    . GLN A 1 724 ? -0.753  7.891   36.785  1.00 108.98 ? 827  GLN A CD    1 
ATOM   5519 O  OE1   . GLN A 1 724 ? -1.653  8.724   36.892  1.00 115.99 ? 827  GLN A OE1   1 
ATOM   5520 N  NE2   . GLN A 1 724 ? -0.330  7.441   35.610  1.00 102.64 ? 827  GLN A NE2   1 
ATOM   5521 N  N     . GLY A 1 725 ? -1.384  7.314   42.591  1.00 100.37 ? 828  GLY A N     1 
ATOM   5522 C  CA    . GLY A 1 725 ? -2.112  7.882   43.704  1.00 100.71 ? 828  GLY A CA    1 
ATOM   5523 C  C     . GLY A 1 725 ? -3.620  7.816   43.593  1.00 104.24 ? 828  GLY A C     1 
ATOM   5524 O  O     . GLY A 1 725 ? -4.308  8.502   44.358  1.00 107.66 ? 828  GLY A O     1 
ATOM   5525 N  N     . LEU A 1 726 ? -4.155  7.022   42.668  1.00 105.79 ? 829  LEU A N     1 
ATOM   5526 C  CA    . LEU A 1 726 ? -5.597  6.874   42.484  1.00 101.28 ? 829  LEU A CA    1 
ATOM   5527 C  C     . LEU A 1 726 ? -6.007  5.527   43.070  1.00 107.12 ? 829  LEU A C     1 
ATOM   5528 O  O     . LEU A 1 726 ? -5.767  4.477   42.468  1.00 109.21 ? 829  LEU A O     1 
ATOM   5529 C  CB    . LEU A 1 726 ? -5.969  6.979   41.010  1.00 101.04 ? 829  LEU A CB    1 
ATOM   5530 C  CG    . LEU A 1 726 ? -5.514  8.246   40.285  1.00 111.54 ? 829  LEU A CG    1 
ATOM   5531 C  CD1   . LEU A 1 726 ? -5.941  8.212   38.825  1.00 98.78  ? 829  LEU A CD1   1 
ATOM   5532 C  CD2   . LEU A 1 726 ? -6.057  9.486   40.979  1.00 116.75 ? 829  LEU A CD2   1 
ATOM   5533 N  N     . ASP A 1 727 ? -6.626  5.559   44.250  1.00 110.10 ? 830  ASP A N     1 
ATOM   5534 C  CA    . ASP A 1 727 ? -7.059  4.339   44.928  1.00 107.29 ? 830  ASP A CA    1 
ATOM   5535 C  C     . ASP A 1 727 ? -8.415  3.928   44.360  1.00 107.45 ? 830  ASP A C     1 
ATOM   5536 O  O     . ASP A 1 727 ? -9.479  4.221   44.910  1.00 115.34 ? 830  ASP A O     1 
ATOM   5537 C  CB    . ASP A 1 727 ? -7.114  4.551   46.436  1.00 120.34 ? 830  ASP A CB    1 
ATOM   5538 C  CG    . ASP A 1 727 ? -7.140  3.245   47.212  1.00 122.75 ? 830  ASP A CG    1 
ATOM   5539 O  OD1   . ASP A 1 727 ? -7.651  2.236   46.682  1.00 118.79 ? 830  ASP A OD1   1 
ATOM   5540 O  OD2   . ASP A 1 727 ? -6.645  3.227   48.359  1.00 135.66 ? 830  ASP A OD2   1 
ATOM   5541 N  N     . LEU A 1 728 ? -8.367  3.238   43.223  1.00 100.98 ? 831  LEU A N     1 
ATOM   5542 C  CA    . LEU A 1 728 ? -9.548  2.655   42.594  1.00 96.42  ? 831  LEU A CA    1 
ATOM   5543 C  C     . LEU A 1 728 ? -9.379  1.143   42.629  1.00 93.92  ? 831  LEU A C     1 
ATOM   5544 O  O     . LEU A 1 728 ? -8.483  0.600   41.974  1.00 95.37  ? 831  LEU A O     1 
ATOM   5545 C  CB    . LEU A 1 728 ? -9.724  3.161   41.163  1.00 96.30  ? 831  LEU A CB    1 
ATOM   5546 C  CG    . LEU A 1 728 ? -9.783  4.677   40.967  1.00 95.99  ? 831  LEU A CG    1 
ATOM   5547 C  CD1   . LEU A 1 728 ? -10.048 5.016   39.509  1.00 93.29  ? 831  LEU A CD1   1 
ATOM   5548 C  CD2   . LEU A 1 728 ? -10.835 5.303   41.867  1.00 99.30  ? 831  LEU A CD2   1 
ATOM   5549 N  N     . ARG A 1 729 ? -10.232 0.465   43.391  1.00 89.35  ? 832  ARG A N     1 
ATOM   5550 C  CA    . ARG A 1 729 ? -10.067 -0.964  43.648  1.00 98.25  ? 832  ARG A CA    1 
ATOM   5551 C  C     . ARG A 1 729 ? -10.804 -1.753  42.573  1.00 91.91  ? 832  ARG A C     1 
ATOM   5552 O  O     . ARG A 1 729 ? -12.028 -1.900  42.616  1.00 93.94  ? 832  ARG A O     1 
ATOM   5553 C  CB    . ARG A 1 729 ? -10.563 -1.322  45.045  1.00 96.14  ? 832  ARG A CB    1 
ATOM   5554 C  CG    . ARG A 1 729 ? -9.965  -2.610  45.592  1.00 99.68  ? 832  ARG A CG    1 
ATOM   5555 C  CD    . ARG A 1 729 ? -10.289 -2.801  47.066  1.00 108.98 ? 832  ARG A CD    1 
ATOM   5556 N  NE    . ARG A 1 729 ? -10.033 -1.596  47.846  1.00 117.03 ? 832  ARG A NE    1 
ATOM   5557 C  CZ    . ARG A 1 729 ? -8.834  -1.201  48.253  1.00 119.20 ? 832  ARG A CZ    1 
ATOM   5558 N  NH1   . ARG A 1 729 ? -7.742  -1.886  47.956  1.00 116.94 ? 832  ARG A NH1   1 
ATOM   5559 N  NH2   . ARG A 1 729 ? -8.727  -0.087  48.972  1.00 115.27 ? 832  ARG A NH2   1 
ATOM   5560 N  N     . MET A 1 730 ? -10.054 -2.260  41.603  1.00 83.80  ? 833  MET A N     1 
ATOM   5561 C  CA    . MET A 1 730 ? -10.579 -3.194  40.623  1.00 84.03  ? 833  MET A CA    1 
ATOM   5562 C  C     . MET A 1 730 ? -10.455 -4.616  41.159  1.00 79.38  ? 833  MET A C     1 
ATOM   5563 O  O     . MET A 1 730 ? -9.677  -4.892  42.075  1.00 86.07  ? 833  MET A O     1 
ATOM   5564 C  CB    . MET A 1 730 ? -9.831  -3.062  39.295  1.00 88.91  ? 833  MET A CB    1 
ATOM   5565 C  CG    . MET A 1 730 ? -9.681  -1.629  38.809  1.00 86.78  ? 833  MET A CG    1 
ATOM   5566 S  SD    . MET A 1 730 ? -11.245 -0.899  38.294  1.00 97.12  ? 833  MET A SD    1 
ATOM   5567 C  CE    . MET A 1 730 ? -11.534 -1.769  36.755  1.00 88.31  ? 833  MET A CE    1 
ATOM   5568 N  N     . LEU A 1 731 ? -11.234 -5.524  40.577  1.00 76.79  ? 834  LEU A N     1 
ATOM   5569 C  CA    . LEU A 1 731 ? -11.240 -6.929  40.984  1.00 79.52  ? 834  LEU A CA    1 
ATOM   5570 C  C     . LEU A 1 731 ? -10.987 -7.801  39.762  1.00 74.39  ? 834  LEU A C     1 
ATOM   5571 O  O     . LEU A 1 731 ? -11.924 -8.360  39.175  1.00 73.81  ? 834  LEU A O     1 
ATOM   5572 C  CB    . LEU A 1 731 ? -12.553 -7.299  41.676  1.00 80.74  ? 834  LEU A CB    1 
ATOM   5573 C  CG    . LEU A 1 731 ? -12.591 -8.669  42.356  1.00 75.33  ? 834  LEU A CG    1 
ATOM   5574 C  CD1   . LEU A 1 731 ? -11.326 -8.896  43.162  1.00 88.63  ? 834  LEU A CD1   1 
ATOM   5575 C  CD2   . LEU A 1 731 ? -13.818 -8.785  43.246  1.00 76.95  ? 834  LEU A CD2   1 
ATOM   5576 N  N     . PRO A 1 732 ? -9.723  -7.941  39.348  1.00 66.06  ? 835  PRO A N     1 
ATOM   5577 C  CA    . PRO A 1 732 ? -9.380  -8.819  38.212  1.00 69.94  ? 835  PRO A CA    1 
ATOM   5578 C  C     . PRO A 1 732 ? -9.256  -10.280 38.636  1.00 67.55  ? 835  PRO A C     1 
ATOM   5579 O  O     . PRO A 1 732 ? -8.174  -10.818 38.870  1.00 70.76  ? 835  PRO A O     1 
ATOM   5580 C  CB    . PRO A 1 732 ? -8.045  -8.243  37.739  1.00 79.14  ? 835  PRO A CB    1 
ATOM   5581 C  CG    . PRO A 1 732 ? -7.417  -7.730  38.994  1.00 74.22  ? 835  PRO A CG    1 
ATOM   5582 C  CD    . PRO A 1 732 ? -8.544  -7.219  39.859  1.00 74.02  ? 835  PRO A CD    1 
ATOM   5583 N  N     . TYR A 1 733 ? -10.403 -10.947 38.734  1.00 72.91  ? 836  TYR A N     1 
ATOM   5584 C  CA    . TYR A 1 733 ? -10.431 -12.327 39.195  1.00 77.59  ? 836  TYR A CA    1 
ATOM   5585 C  C     . TYR A 1 733 ? -9.711  -13.244 38.209  1.00 77.27  ? 836  TYR A C     1 
ATOM   5586 O  O     . TYR A 1 733 ? -9.462  -12.894 37.052  1.00 75.30  ? 836  TYR A O     1 
ATOM   5587 C  CB    . TYR A 1 733 ? -11.873 -12.798 39.408  1.00 78.52  ? 836  TYR A CB    1 
ATOM   5588 C  CG    . TYR A 1 733 ? -12.761 -12.699 38.186  1.00 81.92  ? 836  TYR A CG    1 
ATOM   5589 C  CD1   . TYR A 1 733 ? -13.487 -11.543 37.921  1.00 81.49  ? 836  TYR A CD1   1 
ATOM   5590 C  CD2   . TYR A 1 733 ? -12.885 -13.767 37.306  1.00 81.22  ? 836  TYR A CD2   1 
ATOM   5591 C  CE1   . TYR A 1 733 ? -14.303 -11.451 36.807  1.00 85.16  ? 836  TYR A CE1   1 
ATOM   5592 C  CE2   . TYR A 1 733 ? -13.697 -13.684 36.194  1.00 83.82  ? 836  TYR A CE2   1 
ATOM   5593 C  CZ    . TYR A 1 733 ? -14.404 -12.525 35.948  1.00 85.82  ? 836  TYR A CZ    1 
ATOM   5594 O  OH    . TYR A 1 733 ? -15.211 -12.447 34.838  1.00 85.01  ? 836  TYR A OH    1 
ATOM   5595 N  N     . GLY A 1 734 ? -9.371  -14.436 38.690  1.00 81.59  ? 837  GLY A N     1 
ATOM   5596 C  CA    . GLY A 1 734 ? -8.607  -15.362 37.880  1.00 78.05  ? 837  GLY A CA    1 
ATOM   5597 C  C     . GLY A 1 734 ? -9.426  -15.950 36.747  1.00 79.25  ? 837  GLY A C     1 
ATOM   5598 O  O     . GLY A 1 734 ? -10.638 -16.142 36.849  1.00 88.55  ? 837  GLY A O     1 
ATOM   5599 N  N     . CYS A 1 735 ? -8.738  -16.238 35.646  1.00 80.08  ? 838  CYS A N     1 
ATOM   5600 C  CA    . CYS A 1 735 ? -9.358  -16.852 34.476  1.00 80.48  ? 838  CYS A CA    1 
ATOM   5601 C  C     . CYS A 1 735 ? -8.246  -17.430 33.620  1.00 73.53  ? 838  CYS A C     1 
ATOM   5602 O  O     . CYS A 1 735 ? -7.316  -16.707 33.249  1.00 75.05  ? 838  CYS A O     1 
ATOM   5603 C  CB    . CYS A 1 735 ? -10.181 -15.835 33.687  1.00 82.08  ? 838  CYS A CB    1 
ATOM   5604 S  SG    . CYS A 1 735 ? -10.971 -16.493 32.202  1.00 97.46  ? 838  CYS A SG    1 
ATOM   5605 N  N     . LEU A 1 736 ? -8.331  -18.722 33.313  1.00 66.00  ? 839  LEU A N     1 
ATOM   5606 C  CA    . LEU A 1 736 ? -7.265  -19.416 32.595  1.00 74.59  ? 839  LEU A CA    1 
ATOM   5607 C  C     . LEU A 1 736 ? -7.886  -20.342 31.560  1.00 83.47  ? 839  LEU A C     1 
ATOM   5608 O  O     . LEU A 1 736 ? -8.521  -21.338 31.919  1.00 83.75  ? 839  LEU A O     1 
ATOM   5609 C  CB    . LEU A 1 736 ? -6.374  -20.202 33.556  1.00 73.58  ? 839  LEU A CB    1 
ATOM   5610 C  CG    . LEU A 1 736 ? -5.244  -21.013 32.920  1.00 74.05  ? 839  LEU A CG    1 
ATOM   5611 C  CD1   . LEU A 1 736 ? -4.104  -20.103 32.481  1.00 74.50  ? 839  LEU A CD1   1 
ATOM   5612 C  CD2   . LEU A 1 736 ? -4.749  -22.088 33.874  1.00 74.59  ? 839  LEU A CD2   1 
ATOM   5613 N  N     . SER A 1 737 ? -7.702  -20.016 30.283  1.00 81.72  ? 840  SER A N     1 
ATOM   5614 C  CA    . SER A 1 737 ? -8.096  -20.926 29.216  1.00 75.82  ? 840  SER A CA    1 
ATOM   5615 C  C     . SER A 1 737 ? -7.160  -22.128 29.205  1.00 72.89  ? 840  SER A C     1 
ATOM   5616 O  O     . SER A 1 737 ? -5.936  -21.973 29.221  1.00 76.25  ? 840  SER A O     1 
ATOM   5617 C  CB    . SER A 1 737 ? -8.064  -20.208 27.867  1.00 83.13  ? 840  SER A CB    1 
ATOM   5618 O  OG    . SER A 1 737 ? -8.481  -21.066 26.817  1.00 84.41  ? 840  SER A OG    1 
ATOM   5619 N  N     . ILE A 1 738 ? -7.736  -23.331 29.187  1.00 71.28  ? 841  ILE A N     1 
ATOM   5620 C  CA    . ILE A 1 738 ? -6.966  -24.564 29.254  1.00 78.89  ? 841  ILE A CA    1 
ATOM   5621 C  C     . ILE A 1 738 ? -7.091  -25.390 27.980  1.00 80.95  ? 841  ILE A C     1 
ATOM   5622 O  O     . ILE A 1 738 ? -6.611  -26.523 27.932  1.00 75.06  ? 841  ILE A O     1 
ATOM   5623 C  CB    . ILE A 1 738 ? -7.360  -25.403 30.485  1.00 81.81  ? 841  ILE A CB    1 
ATOM   5624 C  CG1   . ILE A 1 738 ? -8.798  -25.906 30.349  1.00 82.12  ? 841  ILE A CG1   1 
ATOM   5625 C  CG2   . ILE A 1 738 ? -7.194  -24.588 31.759  1.00 79.90  ? 841  ILE A CG2   1 
ATOM   5626 C  CD1   . ILE A 1 738 ? -9.227  -26.833 31.465  1.00 84.46  ? 841  ILE A CD1   1 
ATOM   5627 N  N     . GLY A 1 739 ? -7.726  -24.848 26.946  1.00 89.58  ? 842  GLY A N     1 
ATOM   5628 C  CA    . GLY A 1 739 ? -7.863  -25.587 25.701  1.00 82.81  ? 842  GLY A CA    1 
ATOM   5629 C  C     . GLY A 1 739 ? -8.866  -24.936 24.776  1.00 83.97  ? 842  GLY A C     1 
ATOM   5630 O  O     . GLY A 1 739 ? -9.031  -23.711 24.775  1.00 88.48  ? 842  GLY A O     1 
ATOM   5631 N  N     . ASP A 1 740 ? -9.539  -25.775 23.992  1.00 88.33  ? 843  ASP A N     1 
ATOM   5632 C  CA    . ASP A 1 740 ? -10.482 -25.315 22.973  1.00 92.58  ? 843  ASP A CA    1 
ATOM   5633 C  C     . ASP A 1 740 ? -11.793 -24.941 23.653  1.00 89.73  ? 843  ASP A C     1 
ATOM   5634 O  O     . ASP A 1 740 ? -12.664 -25.783 23.882  1.00 92.21  ? 843  ASP A O     1 
ATOM   5635 C  CB    . ASP A 1 740 ? -10.686 -26.389 21.911  1.00 98.83  ? 843  ASP A CB    1 
ATOM   5636 C  CG    . ASP A 1 740 ? -11.420 -25.871 20.691  1.00 96.36  ? 843  ASP A CG    1 
ATOM   5637 O  OD1   . ASP A 1 740 ? -11.616 -24.642 20.587  1.00 102.32 ? 843  ASP A OD1   1 
ATOM   5638 O  OD2   . ASP A 1 740 ? -11.802 -26.697 19.835  1.00 101.02 ? 843  ASP A OD2   1 
ATOM   5639 N  N     . CYS A 1 741 ? -11.929 -23.653 23.977  1.00 91.29  ? 844  CYS A N     1 
ATOM   5640 C  CA    . CYS A 1 741 ? -13.139 -23.106 24.599  1.00 95.94  ? 844  CYS A CA    1 
ATOM   5641 C  C     . CYS A 1 741 ? -13.452 -23.790 25.929  1.00 91.16  ? 844  CYS A C     1 
ATOM   5642 O  O     . CYS A 1 741 ? -14.613 -24.022 26.273  1.00 89.85  ? 844  CYS A O     1 
ATOM   5643 C  CB    . CYS A 1 741 ? -14.336 -23.187 23.650  1.00 92.86  ? 844  CYS A CB    1 
ATOM   5644 S  SG    . CYS A 1 741 ? -14.218 -22.074 22.237  1.00 105.44 ? 844  CYS A SG    1 
ATOM   5645 N  N     . VAL A 1 742 ? -12.406 -24.116 26.684  1.00 84.06  ? 845  VAL A N     1 
ATOM   5646 C  CA    . VAL A 1 742 ? -12.536 -24.636 28.039  1.00 89.40  ? 845  VAL A CA    1 
ATOM   5647 C  C     . VAL A 1 742 ? -11.613 -23.833 28.943  1.00 86.70  ? 845  VAL A C     1 
ATOM   5648 O  O     . VAL A 1 742 ? -10.495 -23.484 28.548  1.00 90.37  ? 845  VAL A O     1 
ATOM   5649 C  CB    . VAL A 1 742 ? -12.207 -26.142 28.119  1.00 84.30  ? 845  VAL A CB    1 
ATOM   5650 C  CG1   . VAL A 1 742 ? -13.328 -26.962 27.510  1.00 84.48  ? 845  VAL A CG1   1 
ATOM   5651 C  CG2   . VAL A 1 742 ? -10.897 -26.437 27.415  1.00 84.96  ? 845  VAL A CG2   1 
ATOM   5652 N  N     . GLY A 1 743 ? -12.081 -23.531 30.148  1.00 82.36  ? 846  GLY A N     1 
ATOM   5653 C  CA    . GLY A 1 743 ? -11.274 -22.730 31.047  1.00 84.41  ? 846  GLY A CA    1 
ATOM   5654 C  C     . GLY A 1 743 ? -11.822 -22.753 32.456  1.00 79.49  ? 846  GLY A C     1 
ATOM   5655 O  O     . GLY A 1 743 ? -12.847 -23.377 32.744  1.00 77.42  ? 846  GLY A O     1 
ATOM   5656 N  N     . LEU A 1 744 ? -11.114 -22.050 33.335  1.00 76.89  ? 847  LEU A N     1 
ATOM   5657 C  CA    . LEU A 1 744 ? -11.444 -21.977 34.749  1.00 79.95  ? 847  LEU A CA    1 
ATOM   5658 C  C     . LEU A 1 744 ? -11.687 -20.528 35.141  1.00 78.99  ? 847  LEU A C     1 
ATOM   5659 O  O     . LEU A 1 744 ? -10.964 -19.627 34.704  1.00 79.83  ? 847  LEU A O     1 
ATOM   5660 C  CB    . LEU A 1 744 ? -10.322 -22.568 35.606  1.00 74.56  ? 847  LEU A CB    1 
ATOM   5661 C  CG    . LEU A 1 744 ? -9.775  -23.917 35.138  1.00 74.44  ? 847  LEU A CG    1 
ATOM   5662 C  CD1   . LEU A 1 744 ? -8.628  -24.365 36.021  1.00 73.02  ? 847  LEU A CD1   1 
ATOM   5663 C  CD2   . LEU A 1 744 ? -10.874 -24.966 35.114  1.00 73.74  ? 847  LEU A CD2   1 
ATOM   5664 N  N     . ILE A 1 745 ? -12.707 -20.308 35.965  1.00 79.11  ? 848  ILE A N     1 
ATOM   5665 C  CA    . ILE A 1 745 ? -13.050 -18.984 36.469  1.00 80.77  ? 848  ILE A CA    1 
ATOM   5666 C  C     . ILE A 1 745 ? -12.891 -18.997 37.982  1.00 79.12  ? 848  ILE A C     1 
ATOM   5667 O  O     . ILE A 1 745 ? -13.448 -19.867 38.660  1.00 77.96  ? 848  ILE A O     1 
ATOM   5668 C  CB    . ILE A 1 745 ? -14.483 -18.577 36.081  1.00 86.09  ? 848  ILE A CB    1 
ATOM   5669 C  CG1   . ILE A 1 745 ? -14.713 -18.758 34.579  1.00 78.85  ? 848  ILE A CG1   1 
ATOM   5670 C  CG2   . ILE A 1 745 ? -14.746 -17.140 36.496  1.00 86.53  ? 848  ILE A CG2   1 
ATOM   5671 C  CD1   . ILE A 1 745 ? -13.970 -17.763 33.721  1.00 85.57  ? 848  ILE A CD1   1 
ATOM   5672 N  N     . GLU A 1 746 ? -12.132 -18.038 38.506  1.00 81.94  ? 849  GLU A N     1 
ATOM   5673 C  CA    . GLU A 1 746 ? -11.986 -17.907 39.949  1.00 85.45  ? 849  GLU A CA    1 
ATOM   5674 C  C     . GLU A 1 746 ? -13.255 -17.323 40.555  1.00 79.90  ? 849  GLU A C     1 
ATOM   5675 O  O     . GLU A 1 746 ? -13.789 -16.325 40.062  1.00 80.97  ? 849  GLU A O     1 
ATOM   5676 C  CB    . GLU A 1 746 ? -10.788 -17.023 40.290  1.00 87.08  ? 849  GLU A CB    1 
ATOM   5677 C  CG    . GLU A 1 746 ? -10.758 -16.566 41.741  1.00 78.87  ? 849  GLU A CG    1 
ATOM   5678 C  CD    . GLU A 1 746 ? -9.666  -15.550 42.017  1.00 87.90  ? 849  GLU A CD    1 
ATOM   5679 O  OE1   . GLU A 1 746 ? -8.696  -15.484 41.232  1.00 91.79  ? 849  GLU A OE1   1 
ATOM   5680 O  OE2   . GLU A 1 746 ? -9.781  -14.813 43.019  1.00 87.56  ? 849  GLU A OE2   1 
ATOM   5681 N  N     . VAL A 1 747 ? -13.737 -17.946 41.624  1.00 81.83  ? 850  VAL A N     1 
ATOM   5682 C  CA    . VAL A 1 747 ? -14.907 -17.459 42.343  1.00 82.94  ? 850  VAL A CA    1 
ATOM   5683 C  C     . VAL A 1 747 ? -14.449 -16.505 43.435  1.00 79.11  ? 850  VAL A C     1 
ATOM   5684 O  O     . VAL A 1 747 ? -13.596 -16.853 44.260  1.00 82.18  ? 850  VAL A O     1 
ATOM   5685 C  CB    . VAL A 1 747 ? -15.712 -18.623 42.941  1.00 82.50  ? 850  VAL A CB    1 
ATOM   5686 C  CG1   . VAL A 1 747 ? -16.861 -18.089 43.773  1.00 83.49  ? 850  VAL A CG1   1 
ATOM   5687 C  CG2   . VAL A 1 747 ? -16.216 -19.542 41.843  1.00 82.14  ? 850  VAL A CG2   1 
ATOM   5688 N  N     . VAL A 1 748 ? -15.004 -15.303 43.437  1.00 72.41  ? 851  VAL A N     1 
ATOM   5689 C  CA    . VAL A 1 748 ? -14.787 -14.363 44.528  1.00 90.78  ? 851  VAL A CA    1 
ATOM   5690 C  C     . VAL A 1 748 ? -15.914 -14.539 45.535  1.00 93.92  ? 851  VAL A C     1 
ATOM   5691 O  O     . VAL A 1 748 ? -17.079 -14.732 45.164  1.00 91.44  ? 851  VAL A O     1 
ATOM   5692 C  CB    . VAL A 1 748 ? -14.698 -12.913 44.010  1.00 89.54  ? 851  VAL A CB    1 
ATOM   5693 C  CG1   . VAL A 1 748 ? -15.977 -12.507 43.319  1.00 93.64  ? 851  VAL A CG1   1 
ATOM   5694 C  CG2   . VAL A 1 748 ? -14.378 -11.955 45.148  1.00 89.80  ? 851  VAL A CG2   1 
ATOM   5695 N  N     . ARG A 1 749 ? -15.566 -14.500 46.815  1.00 94.56  ? 852  ARG A N     1 
ATOM   5696 C  CA    . ARG A 1 749 ? -16.509 -14.807 47.877  1.00 105.11 ? 852  ARG A CA    1 
ATOM   5697 C  C     . ARG A 1 749 ? -17.307 -13.572 48.283  1.00 106.31 ? 852  ARG A C     1 
ATOM   5698 O  O     . ARG A 1 749 ? -16.874 -12.431 48.103  1.00 105.66 ? 852  ARG A O     1 
ATOM   5699 C  CB    . ARG A 1 749 ? -15.775 -15.382 49.087  1.00 109.16 ? 852  ARG A CB    1 
ATOM   5700 C  CG    . ARG A 1 749 ? -15.205 -16.770 48.853  1.00 111.44 ? 852  ARG A CG    1 
ATOM   5701 C  CD    . ARG A 1 749 ? -14.060 -17.061 49.803  1.00 111.98 ? 852  ARG A CD    1 
ATOM   5702 N  NE    . ARG A 1 749 ? -13.864 -18.492 49.992  1.00 127.45 ? 852  ARG A NE    1 
ATOM   5703 C  CZ    . ARG A 1 749 ? -14.369 -19.186 51.003  1.00 137.00 ? 852  ARG A CZ    1 
ATOM   5704 N  NH1   . ARG A 1 749 ? -15.091 -18.605 51.947  1.00 143.75 ? 852  ARG A NH1   1 
ATOM   5705 N  NH2   . ARG A 1 749 ? -14.141 -20.494 51.070  1.00 122.18 ? 852  ARG A NH2   1 
ATOM   5706 N  N     . ASN A 1 750 ? -18.498 -13.825 48.832  1.00 101.97 ? 853  ASN A N     1 
ATOM   5707 C  CA    . ASN A 1 750 ? -19.378 -12.785 49.366  1.00 105.70 ? 853  ASN A CA    1 
ATOM   5708 C  C     . ASN A 1 750 ? -19.760 -11.754 48.308  1.00 103.16 ? 853  ASN A C     1 
ATOM   5709 O  O     . ASN A 1 750 ? -19.968 -10.580 48.618  1.00 103.59 ? 853  ASN A O     1 
ATOM   5710 C  CB    . ASN A 1 750 ? -18.747 -12.093 50.579  1.00 103.13 ? 853  ASN A CB    1 
ATOM   5711 C  CG    . ASN A 1 750 ? -18.454 -13.058 51.710  1.00 102.48 ? 853  ASN A CG    1 
ATOM   5712 O  OD1   . ASN A 1 750 ? -19.313 -13.325 52.551  1.00 112.99 ? 853  ASN A OD1   1 
ATOM   5713 N  ND2   . ASN A 1 750 ? -17.237 -13.586 51.737  1.00 97.75  ? 853  ASN A ND2   1 
ATOM   5714 N  N     . SER A 1 751 ? -19.865 -12.183 47.054  1.00 101.49 ? 854  SER A N     1 
ATOM   5715 C  CA    . SER A 1 751 ? -20.249 -11.312 45.953  1.00 99.26  ? 854  SER A CA    1 
ATOM   5716 C  C     . SER A 1 751 ? -21.607 -11.735 45.409  1.00 99.07  ? 854  SER A C     1 
ATOM   5717 O  O     . SER A 1 751 ? -21.921 -12.929 45.360  1.00 99.56  ? 854  SER A O     1 
ATOM   5718 C  CB    . SER A 1 751 ? -19.204 -11.345 44.836  1.00 98.70  ? 854  SER A CB    1 
ATOM   5719 O  OG    . SER A 1 751 ? -19.013 -12.666 44.361  1.00 98.36  ? 854  SER A OG    1 
ATOM   5720 N  N     . HIS A 1 752 ? -22.409 -10.752 45.007  1.00 98.61  ? 855  HIS A N     1 
ATOM   5721 C  CA    . HIS A 1 752 ? -23.748 -11.001 44.493  1.00 101.12 ? 855  HIS A CA    1 
ATOM   5722 C  C     . HIS A 1 752 ? -24.017 -10.074 43.319  1.00 102.43 ? 855  HIS A C     1 
ATOM   5723 O  O     . HIS A 1 752 ? -23.575 -8.922  43.314  1.00 100.91 ? 855  HIS A O     1 
ATOM   5724 C  CB    . HIS A 1 752 ? -24.814 -10.790 45.578  1.00 105.89 ? 855  HIS A CB    1 
ATOM   5725 C  CG    . HIS A 1 752 ? -24.485 -11.444 46.884  1.00 102.88 ? 855  HIS A CG    1 
ATOM   5726 N  ND1   . HIS A 1 752 ? -24.882 -12.726 47.196  1.00 102.55 ? 855  HIS A ND1   1 
ATOM   5727 C  CD2   . HIS A 1 752 ? -23.791 -10.993 47.955  1.00 104.29 ? 855  HIS A CD2   1 
ATOM   5728 C  CE1   . HIS A 1 752 ? -24.449 -13.036 48.405  1.00 111.92 ? 855  HIS A CE1   1 
ATOM   5729 N  NE2   . HIS A 1 752 ? -23.783 -12.002 48.887  1.00 109.36 ? 855  HIS A NE2   1 
ATOM   5730 N  N     . THR A 1 753 ? -24.745 -10.580 42.326  1.00 106.46 ? 856  THR A N     1 
ATOM   5731 C  CA    . THR A 1 753 ? -25.094 -9.766  41.174  1.00 108.36 ? 856  THR A CA    1 
ATOM   5732 C  C     . THR A 1 753 ? -26.199 -8.777  41.540  1.00 113.31 ? 856  THR A C     1 
ATOM   5733 O  O     . THR A 1 753 ? -26.863 -8.895  42.574  1.00 117.06 ? 856  THR A O     1 
ATOM   5734 C  CB    . THR A 1 753 ? -25.534 -10.642 40.001  1.00 108.49 ? 856  THR A CB    1 
ATOM   5735 O  OG1   . THR A 1 753 ? -26.849 -11.152 40.248  1.00 114.93 ? 856  THR A OG1   1 
ATOM   5736 C  CG2   . THR A 1 753 ? -24.574 -11.806 39.814  1.00 104.11 ? 856  THR A CG2   1 
ATOM   5737 N  N     . ILE A 1 754 ? -26.392 -7.785  40.669  1.00 116.73 ? 857  ILE A N     1 
ATOM   5738 C  CA    . ILE A 1 754 ? -27.420 -6.775  40.910  1.00 118.65 ? 857  ILE A CA    1 
ATOM   5739 C  C     . ILE A 1 754 ? -28.805 -7.407  40.882  1.00 123.73 ? 857  ILE A C     1 
ATOM   5740 O  O     . ILE A 1 754 ? -29.677 -7.065  41.691  1.00 129.36 ? 857  ILE A O     1 
ATOM   5741 C  CB    . ILE A 1 754 ? -27.295 -5.632  39.885  1.00 124.70 ? 857  ILE A CB    1 
ATOM   5742 C  CG1   . ILE A 1 754 ? -25.931 -4.953  40.012  1.00 122.58 ? 857  ILE A CG1   1 
ATOM   5743 C  CG2   . ILE A 1 754 ? -28.414 -4.619  40.070  1.00 129.45 ? 857  ILE A CG2   1 
ATOM   5744 C  CD1   . ILE A 1 754 ? -25.661 -4.387  41.389  1.00 112.22 ? 857  ILE A CD1   1 
ATOM   5745 N  N     . MET A 1 755 ? -29.028 -8.344  39.958  1.00 120.00 ? 858  MET A N     1 
ATOM   5746 C  CA    . MET A 1 755 ? -30.324 -9.009  39.876  1.00 120.59 ? 858  MET A CA    1 
ATOM   5747 C  C     . MET A 1 755 ? -30.594 -9.845  41.121  1.00 124.37 ? 858  MET A C     1 
ATOM   5748 O  O     . MET A 1 755 ? -31.738 -9.931  41.583  1.00 128.14 ? 858  MET A O     1 
ATOM   5749 C  CB    . MET A 1 755 ? -30.389 -9.874  38.619  1.00 117.40 ? 858  MET A CB    1 
ATOM   5750 C  CG    . MET A 1 755 ? -31.772 -10.413 38.304  1.00 118.72 ? 858  MET A CG    1 
ATOM   5751 S  SD    . MET A 1 755 ? -31.793 -11.377 36.782  1.00 129.18 ? 858  MET A SD    1 
ATOM   5752 C  CE    . MET A 1 755 ? -30.702 -12.727 37.223  1.00 124.63 ? 858  MET A CE    1 
ATOM   5753 N  N     . GLN A 1 756 ? -29.554 -10.468 41.680  1.00 119.17 ? 859  GLN A N     1 
ATOM   5754 C  CA    . GLN A 1 756 ? -29.722 -11.197 42.933  1.00 122.79 ? 859  GLN A CA    1 
ATOM   5755 C  C     . GLN A 1 756 ? -29.985 -10.242 44.090  1.00 126.08 ? 859  GLN A C     1 
ATOM   5756 O  O     . GLN A 1 756 ? -30.835 -10.515 44.945  1.00 134.91 ? 859  GLN A O     1 
ATOM   5757 C  CB    . GLN A 1 756 ? -28.487 -12.052 43.216  1.00 118.04 ? 859  GLN A CB    1 
ATOM   5758 C  CG    . GLN A 1 756 ? -28.260 -13.174 42.218  1.00 111.98 ? 859  GLN A CG    1 
ATOM   5759 C  CD    . GLN A 1 756 ? -26.955 -13.906 42.461  1.00 108.41 ? 859  GLN A CD    1 
ATOM   5760 O  OE1   . GLN A 1 756 ? -26.305 -13.713 43.488  1.00 111.42 ? 859  GLN A OE1   1 
ATOM   5761 N  NE2   . GLN A 1 756 ? -26.563 -14.747 41.512  1.00 112.71 ? 859  GLN A NE2   1 
ATOM   5762 N  N     . ILE A 1 757 ? -29.267 -9.118  44.131  1.00 124.77 ? 860  ILE A N     1 
ATOM   5763 C  CA    . ILE A 1 757 ? -29.472 -8.140  45.194  1.00 125.96 ? 860  ILE A CA    1 
ATOM   5764 C  C     . ILE A 1 757 ? -30.866 -7.531  45.100  1.00 131.37 ? 860  ILE A C     1 
ATOM   5765 O  O     . ILE A 1 757 ? -31.518 -7.279  46.121  1.00 133.46 ? 860  ILE A O     1 
ATOM   5766 C  CB    . ILE A 1 757 ? -28.371 -7.063  45.142  1.00 120.05 ? 860  ILE A CB    1 
ATOM   5767 C  CG1   . ILE A 1 757 ? -27.014 -7.668  45.509  1.00 114.91 ? 860  ILE A CG1   1 
ATOM   5768 C  CG2   . ILE A 1 757 ? -28.703 -5.902  46.064  1.00 117.82 ? 860  ILE A CG2   1 
ATOM   5769 N  N     . GLN A 1 758 ? -31.351 -7.298  43.878  1.00 125.92 ? 861  GLN A N     1 
ATOM   5770 C  CA    . GLN A 1 758 ? -32.680 -6.720  43.706  1.00 131.74 ? 861  GLN A CA    1 
ATOM   5771 C  C     . GLN A 1 758 ? -33.765 -7.664  44.211  1.00 137.55 ? 861  GLN A C     1 
ATOM   5772 O  O     . GLN A 1 758 ? -34.751 -7.220  44.812  1.00 140.54 ? 861  GLN A O     1 
ATOM   5773 C  CB    . GLN A 1 758 ? -32.908 -6.364  42.236  1.00 138.26 ? 861  GLN A CB    1 
ATOM   5774 C  CG    . GLN A 1 758 ? -34.248 -5.698  41.941  1.00 152.06 ? 861  GLN A CG    1 
ATOM   5775 C  CD    . GLN A 1 758 ? -35.345 -6.697  41.621  1.00 156.99 ? 861  GLN A CD    1 
ATOM   5776 O  OE1   . GLN A 1 758 ? -35.083 -7.884  41.421  1.00 156.98 ? 861  GLN A OE1   1 
ATOM   5777 N  NE2   . GLN A 1 758 ? -36.584 -6.220  41.572  1.00 154.68 ? 861  GLN A NE2   1 
ATOM   5778 N  N     . CYS A 1 759 ? -33.603 -8.968  43.979  1.00 136.63 ? 862  CYS A N     1 
ATOM   5779 C  CA    . CYS A 1 759 ? -34.586 -9.935  44.455  1.00 139.32 ? 862  CYS A CA    1 
ATOM   5780 C  C     . CYS A 1 759 ? -34.502 -10.153 45.960  1.00 141.01 ? 862  CYS A C     1 
ATOM   5781 O  O     . CYS A 1 759 ? -35.487 -10.591 46.565  1.00 144.84 ? 862  CYS A O     1 
ATOM   5782 C  CB    . CYS A 1 759 ? -34.411 -11.267 43.726  1.00 135.09 ? 862  CYS A CB    1 
ATOM   5783 S  SG    . CYS A 1 759 ? -34.747 -11.192 41.953  1.00 144.04 ? 862  CYS A SG    1 
ATOM   5784 N  N     . LYS A 1 760 ? -33.360 -9.859  46.573  1.00 139.15 ? 863  LYS A N     1 
ATOM   5785 C  CA    . LYS A 1 760 ? -33.180 -10.018 48.017  1.00 145.53 ? 863  LYS A CA    1 
ATOM   5786 C  C     . LYS A 1 760 ? -33.632 -8.774  48.778  1.00 146.92 ? 863  LYS A C     1 
ATOM   5787 O  O     . LYS A 1 760 ? -32.938 -8.271  49.660  1.00 140.43 ? 863  LYS A O     1 
ATOM   5788 C  CB    . LYS A 1 760 ? -31.724 -10.351 48.321  1.00 139.32 ? 863  LYS A CB    1 
ATOM   5789 C  CG    . LYS A 1 760 ? -31.292 -11.732 47.851  1.00 138.09 ? 863  LYS A CG    1 
ATOM   5790 C  CD    . LYS A 1 760 ? -29.780 -11.826 47.707  1.00 135.75 ? 863  LYS A CD    1 
ATOM   5791 C  CE    . LYS A 1 760 ? -29.070 -11.480 49.005  1.00 131.20 ? 863  LYS A CE    1 
ATOM   5792 N  NZ    . LYS A 1 760 ? -27.590 -11.518 48.848  1.00 114.73 ? 863  LYS A NZ    1 
ATOM   5793 N  N     . GLY A 1 761 ? -34.814 -8.271  48.434  1.00 149.52 ? 864  GLY A N     1 
ATOM   5794 C  CA    . GLY A 1 761 ? -35.357 -7.088  49.076  1.00 146.02 ? 864  GLY A CA    1 
ATOM   5795 C  C     . GLY A 1 761 ? -36.517 -6.473  48.317  1.00 141.75 ? 864  GLY A C     1 
ATOM   5796 O  O     . GLY A 1 761 ? -36.490 -5.292  47.971  1.00 132.37 ? 864  GLY A O     1 
ATOM   5797 N  N     . ASN A 1 770 ? -37.756 -0.231  44.853  1.00 141.24 ? 873  ASN A N     1 
ATOM   5798 C  CA    . ASN A 1 770 ? -37.132 -1.033  43.807  1.00 140.31 ? 873  ASN A CA    1 
ATOM   5799 C  C     . ASN A 1 770 ? -35.766 -0.458  43.439  1.00 145.38 ? 873  ASN A C     1 
ATOM   5800 O  O     . ASN A 1 770 ? -34.809 -1.200  43.221  1.00 147.97 ? 873  ASN A O     1 
ATOM   5801 C  CB    . ASN A 1 770 ? -38.036 -1.099  42.572  1.00 143.44 ? 873  ASN A CB    1 
ATOM   5802 C  CG    . ASN A 1 770 ? -37.734 -2.296  41.688  1.00 148.54 ? 873  ASN A CG    1 
ATOM   5803 O  OD1   . ASN A 1 770 ? -36.618 -2.815  41.680  1.00 150.65 ? 873  ASN A OD1   1 
ATOM   5804 N  ND2   . ASN A 1 770 ? -38.735 -2.740  40.936  1.00 139.27 ? 873  ASN A ND2   1 
ATOM   5805 N  N     . SER A 1 771 ? -35.683 0.873   43.380  1.00 140.33 ? 874  SER A N     1 
ATOM   5806 C  CA    . SER A 1 771 ? -34.434 1.526   43.000  1.00 134.82 ? 874  SER A CA    1 
ATOM   5807 C  C     . SER A 1 771 ? -33.487 1.672   44.185  1.00 129.88 ? 874  SER A C     1 
ATOM   5808 O  O     . SER A 1 771 ? -32.280 1.447   44.049  1.00 129.42 ? 874  SER A O     1 
ATOM   5809 C  CB    . SER A 1 771 ? -34.723 2.893   42.378  1.00 129.23 ? 874  SER A CB    1 
ATOM   5810 O  OG    . SER A 1 771 ? -35.488 2.761   41.194  1.00 130.31 ? 874  SER A OG    1 
ATOM   5811 N  N     . HIS A 1 772 ? -34.011 2.047   45.350  1.00 126.39 ? 875  HIS A N     1 
ATOM   5812 C  CA    . HIS A 1 772 ? -33.196 2.206   46.548  1.00 125.23 ? 875  HIS A CA    1 
ATOM   5813 C  C     . HIS A 1 772 ? -32.861 0.881   47.222  1.00 125.05 ? 875  HIS A C     1 
ATOM   5814 O  O     . HIS A 1 772 ? -32.308 0.890   48.327  1.00 121.84 ? 875  HIS A O     1 
ATOM   5815 C  CB    . HIS A 1 772 ? -33.901 3.128   47.548  1.00 119.18 ? 875  HIS A CB    1 
ATOM   5816 C  CG    . HIS A 1 772 ? -33.974 4.558   47.109  1.00 121.67 ? 875  HIS A CG    1 
ATOM   5817 N  ND1   . HIS A 1 772 ? -34.630 4.953   45.963  1.00 129.82 ? 875  HIS A ND1   1 
ATOM   5818 C  CD2   . HIS A 1 772 ? -33.473 5.687   47.663  1.00 118.15 ? 875  HIS A CD2   1 
ATOM   5819 C  CE1   . HIS A 1 772 ? -34.530 6.264   45.830  1.00 122.82 ? 875  HIS A CE1   1 
ATOM   5820 N  NE2   . HIS A 1 772 ? -33.833 6.733   46.849  1.00 116.55 ? 875  HIS A NE2   1 
ATOM   5821 N  N     . THR A 1 773 ? -33.180 -0.251  46.589  1.00 126.58 ? 876  THR A N     1 
ATOM   5822 C  CA    . THR A 1 773 ? -32.901 -1.546  47.202  1.00 123.86 ? 876  THR A CA    1 
ATOM   5823 C  C     . THR A 1 773 ? -31.402 -1.793  47.319  1.00 121.90 ? 876  THR A C     1 
ATOM   5824 O  O     . THR A 1 773 ? -30.936 -2.345  48.323  1.00 119.55 ? 876  THR A O     1 
ATOM   5825 C  CB    . THR A 1 773 ? -33.567 -2.664  46.401  1.00 128.77 ? 876  THR A CB    1 
ATOM   5826 O  OG1   . THR A 1 773 ? -33.214 -2.539  45.017  1.00 135.92 ? 876  THR A OG1   1 
ATOM   5827 C  CG2   . THR A 1 773 ? -35.081 -2.593  46.543  1.00 136.11 ? 876  THR A CG2   1 
ATOM   5828 N  N     . LEU A 1 774 ? -30.630 -1.391  46.305  1.00 121.61 ? 877  LEU A N     1 
ATOM   5829 C  CA    . LEU A 1 774 ? -29.183 -1.572  46.360  1.00 115.71 ? 877  LEU A CA    1 
ATOM   5830 C  C     . LEU A 1 774 ? -28.559 -0.718  47.456  1.00 117.49 ? 877  LEU A C     1 
ATOM   5831 O  O     . LEU A 1 774 ? -27.651 -1.171  48.163  1.00 115.72 ? 877  LEU A O     1 
ATOM   5832 C  CB    . LEU A 1 774 ? -28.560 -1.240  45.005  1.00 113.07 ? 877  LEU A CB    1 
ATOM   5833 C  CG    . LEU A 1 774 ? -27.031 -1.271  44.945  1.00 101.32 ? 877  LEU A CG    1 
ATOM   5834 C  CD1   . LEU A 1 774 ? -26.509 -2.680  45.173  1.00 92.00  ? 877  LEU A CD1   1 
ATOM   5835 C  CD2   . LEU A 1 774 ? -26.532 -0.715  43.620  1.00 107.04 ? 877  LEU A CD2   1 
ATOM   5836 N  N     . HIS A 1 775 ? -29.031 0.522   47.610  1.00 117.74 ? 878  HIS A N     1 
ATOM   5837 C  CA    . HIS A 1 775 ? -28.506 1.390   48.658  1.00 113.77 ? 878  HIS A CA    1 
ATOM   5838 C  C     . HIS A 1 775 ? -28.790 0.815   50.040  1.00 121.01 ? 878  HIS A C     1 
ATOM   5839 O  O     . HIS A 1 775 ? -27.915 0.816   50.915  1.00 121.95 ? 878  HIS A O     1 
ATOM   5840 C  CB    . HIS A 1 775 ? -29.103 2.791   48.520  1.00 112.62 ? 878  HIS A CB    1 
ATOM   5841 C  CG    . HIS A 1 775 ? -28.477 3.810   49.420  1.00 115.05 ? 878  HIS A CG    1 
ATOM   5842 N  ND1   . HIS A 1 775 ? -29.001 5.074   49.589  1.00 119.18 ? 878  HIS A ND1   1 
ATOM   5843 C  CD2   . HIS A 1 775 ? -27.369 3.756   50.196  1.00 113.81 ? 878  HIS A CD2   1 
ATOM   5844 C  CE1   . HIS A 1 775 ? -28.246 5.753   50.434  1.00 119.11 ? 878  HIS A CE1   1 
ATOM   5845 N  NE2   . HIS A 1 775 ? -27.248 4.976   50.817  1.00 117.13 ? 878  HIS A NE2   1 
ATOM   5846 N  N     . GLN A 1 776 ? -30.008 0.311   50.254  1.00 124.84 ? 879  GLN A N     1 
ATOM   5847 C  CA    . GLN A 1 776 ? -30.336 -0.309  51.533  1.00 123.30 ? 879  GLN A CA    1 
ATOM   5848 C  C     . GLN A 1 776 ? -29.585 -1.618  51.733  1.00 127.89 ? 879  GLN A C     1 
ATOM   5849 O  O     . GLN A 1 776 ? -29.321 -2.010  52.876  1.00 128.96 ? 879  GLN A O     1 
ATOM   5850 C  CB    . GLN A 1 776 ? -31.844 -0.546  51.633  1.00 124.13 ? 879  GLN A CB    1 
ATOM   5851 C  CG    . GLN A 1 776 ? -32.665 0.717   51.836  1.00 127.59 ? 879  GLN A CG    1 
ATOM   5852 C  CD    . GLN A 1 776 ? -32.540 1.277   53.241  1.00 141.21 ? 879  GLN A CD    1 
ATOM   5853 O  OE1   . GLN A 1 776 ? -31.990 0.631   54.134  1.00 132.97 ? 879  GLN A OE1   1 
ATOM   5854 N  NE2   . GLN A 1 776 ? -33.054 2.484   53.443  1.00 144.08 ? 879  GLN A NE2   1 
ATOM   5855 N  N     . TRP A 1 777 ? -29.231 -2.302  50.642  1.00 119.55 ? 880  TRP A N     1 
ATOM   5856 C  CA    . TRP A 1 777 ? -28.538 -3.580  50.759  1.00 117.04 ? 880  TRP A CA    1 
ATOM   5857 C  C     . TRP A 1 777 ? -27.151 -3.416  51.368  1.00 116.50 ? 880  TRP A C     1 
ATOM   5858 O  O     . TRP A 1 777 ? -26.659 -4.329  52.039  1.00 114.00 ? 880  TRP A O     1 
ATOM   5859 C  CB    . TRP A 1 777 ? -28.447 -4.249  49.388  1.00 116.29 ? 880  TRP A CB    1 
ATOM   5860 C  CG    . TRP A 1 777 ? -27.874 -5.633  49.418  1.00 115.81 ? 880  TRP A CG    1 
ATOM   5861 C  CD1   . TRP A 1 777 ? -28.551 -6.795  49.652  1.00 115.80 ? 880  TRP A CD1   1 
ATOM   5862 C  CD2   . TRP A 1 777 ? -26.508 -6.002  49.194  1.00 114.66 ? 880  TRP A CD2   1 
ATOM   5863 N  NE1   . TRP A 1 777 ? -27.690 -7.864  49.594  1.00 116.52 ? 880  TRP A NE1   1 
ATOM   5864 C  CE2   . TRP A 1 777 ? -26.430 -7.404  49.314  1.00 116.62 ? 880  TRP A CE2   1 
ATOM   5865 C  CE3   . TRP A 1 777 ? -25.344 -5.283  48.906  1.00 112.43 ? 880  TRP A CE3   1 
ATOM   5866 C  CZ2   . TRP A 1 777 ? -25.233 -8.101  49.156  1.00 120.23 ? 880  TRP A CZ2   1 
ATOM   5867 C  CZ3   . TRP A 1 777 ? -24.156 -5.977  48.750  1.00 114.09 ? 880  TRP A CZ3   1 
ATOM   5868 C  CH2   . TRP A 1 777 ? -24.110 -7.371  48.876  1.00 114.61 ? 880  TRP A CH2   1 
ATOM   5869 N  N     . LEU A 1 778 ? -26.510 -2.266  51.151  1.00 119.00 ? 881  LEU A N     1 
ATOM   5870 C  CA    . LEU A 1 778 ? -25.189 -2.033  51.725  1.00 118.55 ? 881  LEU A CA    1 
ATOM   5871 C  C     . LEU A 1 778 ? -25.279 -1.571  53.173  1.00 122.19 ? 881  LEU A C     1 
ATOM   5872 O  O     . LEU A 1 778 ? -24.456 -1.970  54.005  1.00 120.49 ? 881  LEU A O     1 
ATOM   5873 C  CB    . LEU A 1 778 ? -24.422 -1.009  50.888  1.00 117.40 ? 881  LEU A CB    1 
ATOM   5874 C  CG    . LEU A 1 778 ? -23.909 -1.478  49.526  1.00 106.82 ? 881  LEU A CG    1 
ATOM   5875 C  CD1   . LEU A 1 778 ? -23.201 -0.344  48.809  1.00 100.60 ? 881  LEU A CD1   1 
ATOM   5876 C  CD2   . LEU A 1 778 ? -22.981 -2.672  49.688  1.00 104.66 ? 881  LEU A CD2   1 
ATOM   5877 N  N     . LYS A 1 779 ? -26.268 -0.731  53.492  1.00 136.39 ? 882  LYS A N     1 
ATOM   5878 C  CA    . LYS A 1 779 ? -26.422 -0.258  54.864  1.00 129.81 ? 882  LYS A CA    1 
ATOM   5879 C  C     . LYS A 1 779 ? -26.756 -1.401  55.813  1.00 129.24 ? 882  LYS A C     1 
ATOM   5880 O  O     . LYS A 1 779 ? -26.400 -1.350  56.996  1.00 141.91 ? 882  LYS A O     1 
ATOM   5881 C  CB    . LYS A 1 779 ? -27.500 0.826   54.925  1.00 129.26 ? 882  LYS A CB    1 
ATOM   5882 C  CG    . LYS A 1 779 ? -27.651 1.488   56.287  1.00 146.17 ? 882  LYS A CG    1 
ATOM   5883 C  CD    . LYS A 1 779 ? -26.313 1.983   56.813  1.00 138.41 ? 882  LYS A CD    1 
ATOM   5884 C  CE    . LYS A 1 779 ? -26.480 2.797   58.085  1.00 147.53 ? 882  LYS A CE    1 
ATOM   5885 N  NZ    . LYS A 1 779 ? -27.259 4.043   57.844  1.00 152.08 ? 882  LYS A NZ    1 
ATOM   5886 N  N     . ASP A 1 780 ? -27.430 -2.440  55.318  1.00 123.58 ? 883  ASP A N     1 
ATOM   5887 C  CA    . ASP A 1 780 ? -27.706 -3.601  56.156  1.00 122.78 ? 883  ASP A CA    1 
ATOM   5888 C  C     . ASP A 1 780 ? -26.444 -4.410  56.427  1.00 125.98 ? 883  ASP A C     1 
ATOM   5889 O  O     . ASP A 1 780 ? -26.292 -4.970  57.519  1.00 118.52 ? 883  ASP A O     1 
ATOM   5890 C  CB    . ASP A 1 780 ? -28.768 -4.483  55.500  1.00 123.80 ? 883  ASP A CB    1 
ATOM   5891 C  CG    . ASP A 1 780 ? -30.093 -3.769  55.327  1.00 131.10 ? 883  ASP A CG    1 
ATOM   5892 O  OD1   . ASP A 1 780 ? -30.416 -2.902  56.166  1.00 134.39 ? 883  ASP A OD1   1 
ATOM   5893 O  OD2   . ASP A 1 780 ? -30.811 -4.075  54.351  1.00 129.90 ? 883  ASP A OD2   1 
ATOM   5894 N  N     . LYS A 1 781 ? -25.533 -4.479  55.458  1.00 122.09 ? 884  LYS A N     1 
ATOM   5895 C  CA    . LYS A 1 781 ? -24.311 -5.259  55.587  1.00 118.04 ? 884  LYS A CA    1 
ATOM   5896 C  C     . LYS A 1 781 ? -23.104 -4.405  55.955  1.00 117.41 ? 884  LYS A C     1 
ATOM   5897 O  O     . LYS A 1 781 ? -21.974 -4.904  55.938  1.00 114.41 ? 884  LYS A O     1 
ATOM   5898 C  CB    . LYS A 1 781 ? -24.043 -6.028  54.293  1.00 109.39 ? 884  LYS A CB    1 
ATOM   5899 C  CG    . LYS A 1 781 ? -25.281 -6.713  53.736  1.00 109.25 ? 884  LYS A CG    1 
ATOM   5900 C  CD    . LYS A 1 781 ? -24.930 -7.807  52.744  1.00 108.79 ? 884  LYS A CD    1 
ATOM   5901 C  CE    . LYS A 1 781 ? -24.260 -8.979  53.439  1.00 107.37 ? 884  LYS A CE    1 
ATOM   5902 N  NZ    . LYS A 1 781 ? -24.162 -10.169 52.550  1.00 112.43 ? 884  LYS A NZ    1 
ATOM   5903 N  N     . ASN A 1 782 ? -23.319 -3.132  56.285  1.00 121.00 ? 885  ASN A N     1 
ATOM   5904 C  CA    . ASN A 1 782 ? -22.256 -2.253  56.763  1.00 121.74 ? 885  ASN A CA    1 
ATOM   5905 C  C     . ASN A 1 782 ? -22.861 -1.310  57.790  1.00 127.16 ? 885  ASN A C     1 
ATOM   5906 O  O     . ASN A 1 782 ? -23.777 -0.549  57.462  1.00 128.92 ? 885  ASN A O     1 
ATOM   5907 C  CB    . ASN A 1 782 ? -21.619 -1.466  55.614  1.00 122.03 ? 885  ASN A CB    1 
ATOM   5908 C  CG    . ASN A 1 782 ? -20.987 -2.365  54.565  1.00 108.64 ? 885  ASN A CG    1 
ATOM   5909 O  OD1   . ASN A 1 782 ? -19.805 -2.701  54.648  1.00 96.94  ? 885  ASN A OD1   1 
ATOM   5910 N  ND2   . ASN A 1 782 ? -21.775 -2.756  53.569  1.00 108.42 ? 885  ASN A ND2   1 
ATOM   5911 N  N     . LYS A 1 783 ? -22.352 -1.357  59.023  1.00 139.37 ? 886  LYS A N     1 
ATOM   5912 C  CA    . LYS A 1 783 ? -22.902 -0.564  60.119  1.00 124.64 ? 886  LYS A CA    1 
ATOM   5913 C  C     . LYS A 1 783 ? -22.784 0.933   59.855  1.00 133.64 ? 886  LYS A C     1 
ATOM   5914 O  O     . LYS A 1 783 ? -22.195 1.352   58.853  1.00 145.15 ? 886  LYS A O     1 
ATOM   5915 C  CB    . LYS A 1 783 ? -22.205 -0.911  61.437  1.00 123.44 ? 886  LYS A CB    1 
ATOM   5916 C  CG    . LYS A 1 783 ? -22.465 -2.322  61.942  1.00 140.42 ? 886  LYS A CG    1 
ATOM   5917 C  CD    . LYS A 1 783 ? -21.362 -3.281  61.525  1.00 128.08 ? 886  LYS A CD    1 
ATOM   5918 C  CE    . LYS A 1 783 ? -21.568 -4.655  62.145  1.00 125.41 ? 886  LYS A CE    1 
ATOM   5919 N  NZ    . LYS A 1 783 ? -20.450 -5.586  61.832  1.00 118.81 ? 886  LYS A NZ    1 
ATOM   5920 N  N     . GLY A 1 784 ? -23.339 1.746   60.757  1.00 129.51 ? 887  GLY A N     1 
ATOM   5921 C  CA    . GLY A 1 784 ? -23.285 3.188   60.579  1.00 129.16 ? 887  GLY A CA    1 
ATOM   5922 C  C     . GLY A 1 784 ? -21.873 3.739   60.562  1.00 130.60 ? 887  GLY A C     1 
ATOM   5923 O  O     . GLY A 1 784 ? -21.624 4.799   59.982  1.00 131.24 ? 887  GLY A O     1 
ATOM   5924 N  N     . GLU A 1 785 ? -20.933 3.035   61.195  1.00 127.88 ? 888  GLU A N     1 
ATOM   5925 C  CA    . GLU A 1 785 ? -19.538 3.458   61.154  1.00 133.33 ? 888  GLU A CA    1 
ATOM   5926 C  C     . GLU A 1 785 ? -18.839 2.953   59.897  1.00 132.82 ? 888  GLU A C     1 
ATOM   5927 O  O     . GLU A 1 785 ? -18.037 3.678   59.296  1.00 131.05 ? 888  GLU A O     1 
ATOM   5928 C  CB    . GLU A 1 785 ? -18.810 2.979   62.410  1.00 127.60 ? 888  GLU A CB    1 
ATOM   5929 C  CG    . GLU A 1 785 ? -19.362 3.572   63.699  1.00 144.68 ? 888  GLU A CG    1 
ATOM   5930 C  CD    . GLU A 1 785 ? -18.658 3.050   64.938  1.00 144.00 ? 888  GLU A CD    1 
ATOM   5931 O  OE1   . GLU A 1 785 ? -17.825 2.128   64.809  1.00 137.87 ? 888  GLU A OE1   1 
ATOM   5932 O  OE2   . GLU A 1 785 ? -18.939 3.565   66.041  1.00 128.91 ? 888  GLU A OE2   1 
ATOM   5933 N  N     . ILE A 1 786 ? -19.134 1.717   59.480  1.00 127.69 ? 889  ILE A N     1 
ATOM   5934 C  CA    . ILE A 1 786 ? -18.567 1.176   58.245  1.00 121.81 ? 889  ILE A CA    1 
ATOM   5935 C  C     . ILE A 1 786 ? -19.298 1.669   57.007  1.00 122.40 ? 889  ILE A C     1 
ATOM   5936 O  O     . ILE A 1 786 ? -18.836 1.421   55.885  1.00 120.35 ? 889  ILE A O     1 
ATOM   5937 C  CB    . ILE A 1 786 ? -18.578 -0.365  58.279  1.00 118.82 ? 889  ILE A CB    1 
ATOM   5938 C  CG1   . ILE A 1 786 ? -18.264 -0.868  59.687  1.00 118.24 ? 889  ILE A CG1   1 
ATOM   5939 C  CG2   . ILE A 1 786 ? -17.555 -0.941  57.306  1.00 126.54 ? 889  ILE A CG2   1 
ATOM   5940 C  CD1   . ILE A 1 786 ? -18.143 -2.375  59.779  1.00 119.67 ? 889  ILE A CD1   1 
ATOM   5941 N  N     . TYR A 1 787 ? -20.421 2.371   57.178  1.00 122.99 ? 890  TYR A N     1 
ATOM   5942 C  CA    . TYR A 1 787 ? -21.183 2.860   56.033  1.00 117.13 ? 890  TYR A CA    1 
ATOM   5943 C  C     . TYR A 1 787 ? -20.328 3.749   55.138  1.00 113.32 ? 890  TYR A C     1 
ATOM   5944 O  O     . TYR A 1 787 ? -20.328 3.596   53.912  1.00 115.64 ? 890  TYR A O     1 
ATOM   5945 C  CB    . TYR A 1 787 ? -22.423 3.613   56.518  1.00 117.59 ? 890  TYR A CB    1 
ATOM   5946 C  CG    . TYR A 1 787 ? -23.215 4.295   55.423  1.00 108.59 ? 890  TYR A CG    1 
ATOM   5947 C  CD1   . TYR A 1 787 ? -24.109 3.581   54.638  1.00 107.25 ? 890  TYR A CD1   1 
ATOM   5948 C  CD2   . TYR A 1 787 ? -23.079 5.657   55.187  1.00 104.57 ? 890  TYR A CD2   1 
ATOM   5949 C  CE1   . TYR A 1 787 ? -24.840 4.202   53.643  1.00 105.48 ? 890  TYR A CE1   1 
ATOM   5950 C  CE2   . TYR A 1 787 ? -23.804 6.286   54.194  1.00 104.70 ? 890  TYR A CE2   1 
ATOM   5951 C  CZ    . TYR A 1 787 ? -24.684 5.554   53.425  1.00 104.93 ? 890  TYR A CZ    1 
ATOM   5952 O  OH    . TYR A 1 787 ? -25.408 6.177   52.435  1.00 112.80 ? 890  TYR A OH    1 
ATOM   5953 N  N     . ASP A 1 788 ? -19.582 4.681   55.737  1.00 110.35 ? 891  ASP A N     1 
ATOM   5954 C  CA    . ASP A 1 788 ? -18.754 5.585   54.945  1.00 110.72 ? 891  ASP A CA    1 
ATOM   5955 C  C     . ASP A 1 788 ? -17.625 4.849   54.235  1.00 114.76 ? 891  ASP A C     1 
ATOM   5956 O  O     . ASP A 1 788 ? -17.201 5.269   53.152  1.00 112.75 ? 891  ASP A O     1 
ATOM   5957 C  CB    . ASP A 1 788 ? -18.190 6.697   55.829  1.00 110.54 ? 891  ASP A CB    1 
ATOM   5958 C  CG    . ASP A 1 788 ? -19.124 7.886   55.931  1.00 113.91 ? 891  ASP A CG    1 
ATOM   5959 O  OD1   . ASP A 1 788 ? -20.187 7.864   55.275  1.00 113.39 ? 891  ASP A OD1   1 
ATOM   5960 O  OD2   . ASP A 1 788 ? -18.793 8.843   56.662  1.00 116.26 ? 891  ASP A OD2   1 
ATOM   5961 N  N     . ALA A 1 789 ? -17.125 3.759   54.819  1.00 119.49 ? 892  ALA A N     1 
ATOM   5962 C  CA    . ALA A 1 789 ? -16.099 2.972   54.147  1.00 109.83 ? 892  ALA A CA    1 
ATOM   5963 C  C     . ALA A 1 789 ? -16.678 2.128   53.020  1.00 114.09 ? 892  ALA A C     1 
ATOM   5964 O  O     . ALA A 1 789 ? -15.966 1.808   52.062  1.00 121.28 ? 892  ALA A O     1 
ATOM   5965 C  CB    . ALA A 1 789 ? -15.375 2.077   55.154  1.00 114.41 ? 892  ALA A CB    1 
ATOM   5966 N  N     . ALA A 1 790 ? -17.960 1.767   53.111  1.00 118.66 ? 893  ALA A N     1 
ATOM   5967 C  CA    . ALA A 1 790 ? -18.581 0.949   52.076  1.00 108.29 ? 893  ALA A CA    1 
ATOM   5968 C  C     . ALA A 1 790 ? -18.967 1.778   50.858  1.00 103.80 ? 893  ALA A C     1 
ATOM   5969 O  O     . ALA A 1 790 ? -18.760 1.342   49.720  1.00 106.65 ? 893  ALA A O     1 
ATOM   5970 C  CB    . ALA A 1 790 ? -19.806 0.229   52.638  1.00 112.84 ? 893  ALA A CB    1 
ATOM   5971 N  N     . ILE A 1 791 ? -19.536 2.967   51.071  1.00 106.96 ? 894  ILE A N     1 
ATOM   5972 C  CA    . ILE A 1 791 ? -19.890 3.817   49.939  1.00 104.79 ? 894  ILE A CA    1 
ATOM   5973 C  C     . ILE A 1 791 ? -18.638 4.358   49.264  1.00 105.45 ? 894  ILE A C     1 
ATOM   5974 O  O     . ILE A 1 791 ? -18.638 4.612   48.053  1.00 106.80 ? 894  ILE A O     1 
ATOM   5975 C  CB    . ILE A 1 791 ? -20.834 4.953   50.383  1.00 106.39 ? 894  ILE A CB    1 
ATOM   5976 C  CG1   . ILE A 1 791 ? -20.275 5.692   51.603  1.00 109.60 ? 894  ILE A CG1   1 
ATOM   5977 C  CG2   . ILE A 1 791 ? -22.225 4.406   50.674  1.00 100.51 ? 894  ILE A CG2   1 
ATOM   5978 C  CD1   . ILE A 1 791 ? -19.395 6.885   51.279  1.00 110.65 ? 894  ILE A CD1   1 
ATOM   5979 N  N     . ASP A 1 792 ? -17.556 4.544   50.023  1.00 106.93 ? 895  ASP A N     1 
ATOM   5980 C  CA    . ASP A 1 792 ? -16.305 4.995   49.426  1.00 104.41 ? 895  ASP A CA    1 
ATOM   5981 C  C     . ASP A 1 792 ? -15.731 3.924   48.507  1.00 101.96 ? 895  ASP A C     1 
ATOM   5982 O  O     . ASP A 1 792 ? -15.368 4.205   47.359  1.00 102.64 ? 895  ASP A O     1 
ATOM   5983 C  CB    . ASP A 1 792 ? -15.305 5.367   50.520  1.00 101.61 ? 895  ASP A CB    1 
ATOM   5984 C  CG    . ASP A 1 792 ? -14.079 6.069   49.976  1.00 97.25  ? 895  ASP A CG    1 
ATOM   5985 O  OD1   . ASP A 1 792 ? -14.206 7.230   49.532  1.00 95.64  ? 895  ASP A OD1   1 
ATOM   5986 O  OD2   . ASP A 1 792 ? -12.987 5.462   49.993  1.00 99.40  ? 895  ASP A OD2   1 
ATOM   5987 N  N     . LEU A 1 793 ? -15.655 2.683   48.994  1.00 100.75 ? 896  LEU A N     1 
ATOM   5988 C  CA    . LEU A 1 793 ? -15.205 1.578   48.154  1.00 98.70  ? 896  LEU A CA    1 
ATOM   5989 C  C     . LEU A 1 793 ? -16.123 1.378   46.955  1.00 99.21  ? 896  LEU A C     1 
ATOM   5990 O  O     . LEU A 1 793 ? -15.675 0.910   45.901  1.00 104.07 ? 896  LEU A O     1 
ATOM   5991 C  CB    . LEU A 1 793 ? -15.120 0.297   48.986  1.00 100.55 ? 896  LEU A CB    1 
ATOM   5992 C  CG    . LEU A 1 793 ? -14.696 -0.992  48.282  1.00 101.30 ? 896  LEU A CG    1 
ATOM   5993 C  CD1   . LEU A 1 793 ? -13.334 -0.825  47.633  1.00 100.67 ? 896  LEU A CD1   1 
ATOM   5994 C  CD2   . LEU A 1 793 ? -14.690 -2.158  49.260  1.00 97.26  ? 896  LEU A CD2   1 
ATOM   5995 N  N     . PHE A 1 794 ? -17.402 1.733   47.089  1.00 100.44 ? 897  PHE A N     1 
ATOM   5996 C  CA    . PHE A 1 794 ? -18.331 1.593   45.973  1.00 99.76  ? 897  PHE A CA    1 
ATOM   5997 C  C     . PHE A 1 794 ? -18.070 2.645   44.901  1.00 103.31 ? 897  PHE A C     1 
ATOM   5998 O  O     . PHE A 1 794 ? -18.067 2.332   43.705  1.00 102.19 ? 897  PHE A O     1 
ATOM   5999 C  CB    . PHE A 1 794 ? -19.770 1.682   46.479  1.00 98.81  ? 897  PHE A CB    1 
ATOM   6000 C  CG    . PHE A 1 794 ? -20.804 1.348   45.441  1.00 95.07  ? 897  PHE A CG    1 
ATOM   6001 C  CD1   . PHE A 1 794 ? -21.250 0.046   45.285  1.00 93.86  ? 897  PHE A CD1   1 
ATOM   6002 C  CD2   . PHE A 1 794 ? -21.336 2.335   44.628  1.00 102.22 ? 897  PHE A CD2   1 
ATOM   6003 C  CE1   . PHE A 1 794 ? -22.204 -0.267  44.336  1.00 97.05  ? 897  PHE A CE1   1 
ATOM   6004 C  CE2   . PHE A 1 794 ? -22.289 2.029   43.675  1.00 107.12 ? 897  PHE A CE2   1 
ATOM   6005 C  CZ    . PHE A 1 794 ? -22.724 0.726   43.529  1.00 103.98 ? 897  PHE A CZ    1 
ATOM   6006 N  N     . THR A 1 795 ? -17.852 3.897   45.310  1.00 113.32 ? 898  THR A N     1 
ATOM   6007 C  CA    . THR A 1 795 ? -17.616 4.960   44.338  1.00 115.06 ? 898  THR A CA    1 
ATOM   6008 C  C     . THR A 1 795 ? -16.282 4.777   43.626  1.00 114.72 ? 898  THR A C     1 
ATOM   6009 O  O     . THR A 1 795 ? -16.173 5.041   42.423  1.00 114.81 ? 898  THR A O     1 
ATOM   6010 C  CB    . THR A 1 795 ? -17.669 6.325   45.024  1.00 114.73 ? 898  THR A CB    1 
ATOM   6011 O  OG1   . THR A 1 795 ? -16.719 6.357   46.098  1.00 125.46 ? 898  THR A OG1   1 
ATOM   6012 C  CG2   . THR A 1 795 ? -19.059 6.593   45.576  1.00 122.26 ? 898  THR A CG2   1 
ATOM   6013 N  N     . ARG A 1 796 ? -15.256 4.324   44.350  1.00 103.55 ? 899  ARG A N     1 
ATOM   6014 C  CA    . ARG A 1 796 ? -13.941 4.163   43.739  1.00 100.52 ? 899  ARG A CA    1 
ATOM   6015 C  C     . ARG A 1 796 ? -13.903 2.973   42.789  1.00 97.43  ? 899  ARG A C     1 
ATOM   6016 O  O     . ARG A 1 796 ? -13.188 3.011   41.781  1.00 95.60  ? 899  ARG A O     1 
ATOM   6017 C  CB    . ARG A 1 796 ? -12.873 4.026   44.824  1.00 99.76  ? 899  ARG A CB    1 
ATOM   6018 C  CG    . ARG A 1 796 ? -12.865 5.180   45.815  1.00 105.97 ? 899  ARG A CG    1 
ATOM   6019 C  CD    . ARG A 1 796 ? -11.838 4.980   46.916  1.00 106.59 ? 899  ARG A CD    1 
ATOM   6020 N  NE    . ARG A 1 796 ? -10.563 5.601   46.584  1.00 114.55 ? 899  ARG A NE    1 
ATOM   6021 C  CZ    . ARG A 1 796 ? -10.269 6.873   46.820  1.00 114.53 ? 899  ARG A CZ    1 
ATOM   6022 N  NH1   . ARG A 1 796 ? -11.139 7.687   47.395  1.00 110.17 ? 899  ARG A NH1   1 
ATOM   6023 N  NH2   . ARG A 1 796 ? -9.075  7.339   46.468  1.00 120.91 ? 899  ARG A NH2   1 
ATOM   6024 N  N     . SER A 1 797 ? -14.663 1.914   43.082  1.00 98.84  ? 900  SER A N     1 
ATOM   6025 C  CA    . SER A 1 797 ? -14.725 0.778   42.169  1.00 94.47  ? 900  SER A CA    1 
ATOM   6026 C  C     . SER A 1 797 ? -15.565 1.084   40.936  1.00 95.16  ? 900  SER A C     1 
ATOM   6027 O  O     . SER A 1 797 ? -15.281 0.559   39.854  1.00 94.35  ? 900  SER A O     1 
ATOM   6028 C  CB    . SER A 1 797 ? -15.277 -0.454  42.889  1.00 92.24  ? 900  SER A CB    1 
ATOM   6029 O  OG    . SER A 1 797 ? -16.620 -0.257  43.293  1.00 93.53  ? 900  SER A OG    1 
ATOM   6030 N  N     . CYS A 1 798 ? -16.597 1.922   41.073  1.00 96.21  ? 901  CYS A N     1 
ATOM   6031 C  CA    . CYS A 1 798 ? -17.388 2.307   39.908  1.00 95.49  ? 901  CYS A CA    1 
ATOM   6032 C  C     . CYS A 1 798 ? -16.583 3.187   38.962  1.00 95.29  ? 901  CYS A C     1 
ATOM   6033 O  O     . CYS A 1 798 ? -16.645 3.009   37.741  1.00 97.89  ? 901  CYS A O     1 
ATOM   6034 C  CB    . CYS A 1 798 ? -18.666 3.024   40.344  1.00 95.26  ? 901  CYS A CB    1 
ATOM   6035 S  SG    . CYS A 1 798 ? -20.061 1.929   40.685  1.00 124.19 ? 901  CYS A SG    1 
ATOM   6036 N  N     . ALA A 1 799 ? -15.824 4.140   39.508  1.00 94.42  ? 902  ALA A N     1 
ATOM   6037 C  CA    . ALA A 1 799 ? -15.025 5.025   38.666  1.00 94.12  ? 902  ALA A CA    1 
ATOM   6038 C  C     . ALA A 1 799 ? -14.022 4.237   37.835  1.00 95.73  ? 902  ALA A C     1 
ATOM   6039 O  O     . ALA A 1 799 ? -13.731 4.600   36.688  1.00 90.98  ? 902  ALA A O     1 
ATOM   6040 C  CB    . ALA A 1 799 ? -14.308 6.064   39.528  1.00 94.20  ? 902  ALA A CB    1 
ATOM   6041 N  N     . GLY A 1 800 ? -13.487 3.151   38.393  1.00 91.53  ? 903  GLY A N     1 
ATOM   6042 C  CA    . GLY A 1 800 ? -12.543 2.341   37.642  1.00 90.90  ? 903  GLY A CA    1 
ATOM   6043 C  C     . GLY A 1 800 ? -13.201 1.595   36.497  1.00 91.88  ? 903  GLY A C     1 
ATOM   6044 O  O     . GLY A 1 800 ? -12.728 1.639   35.358  1.00 100.55 ? 903  GLY A O     1 
ATOM   6045 N  N     . TYR A 1 801 ? -14.308 0.903   36.780  1.00 90.91  ? 904  TYR A N     1 
ATOM   6046 C  CA    . TYR A 1 801 ? -14.980 0.137   35.737  1.00 91.21  ? 904  TYR A CA    1 
ATOM   6047 C  C     . TYR A 1 801 ? -15.738 1.038   34.769  1.00 100.00 ? 904  TYR A C     1 
ATOM   6048 O  O     . TYR A 1 801 ? -15.943 0.662   33.610  1.00 96.63  ? 904  TYR A O     1 
ATOM   6049 C  CB    . TYR A 1 801 ? -15.916 -0.897  36.362  1.00 85.12  ? 904  TYR A CB    1 
ATOM   6050 C  CG    . TYR A 1 801 ? -15.188 -2.117  36.880  1.00 89.13  ? 904  TYR A CG    1 
ATOM   6051 C  CD1   . TYR A 1 801 ? -14.917 -3.192  36.043  1.00 88.29  ? 904  TYR A CD1   1 
ATOM   6052 C  CD2   . TYR A 1 801 ? -14.762 -2.191  38.200  1.00 85.71  ? 904  TYR A CD2   1 
ATOM   6053 C  CE1   . TYR A 1 801 ? -14.247 -4.309  36.508  1.00 89.14  ? 904  TYR A CE1   1 
ATOM   6054 C  CE2   . TYR A 1 801 ? -14.089 -3.305  38.673  1.00 81.03  ? 904  TYR A CE2   1 
ATOM   6055 C  CZ    . TYR A 1 801 ? -13.836 -4.360  37.823  1.00 81.44  ? 904  TYR A CZ    1 
ATOM   6056 O  OH    . TYR A 1 801 ? -13.168 -5.471  38.285  1.00 77.25  ? 904  TYR A OH    1 
ATOM   6057 N  N     . CYS A 1 802 ? -16.156 2.225   35.216  1.00 95.00  ? 905  CYS A N     1 
ATOM   6058 C  CA    . CYS A 1 802 ? -16.765 3.175   34.291  1.00 95.95  ? 905  CYS A CA    1 
ATOM   6059 C  C     . CYS A 1 802 ? -15.757 3.636   33.246  1.00 94.11  ? 905  CYS A C     1 
ATOM   6060 O  O     . CYS A 1 802 ? -16.108 3.840   32.078  1.00 96.42  ? 905  CYS A O     1 
ATOM   6061 C  CB    . CYS A 1 802 ? -17.332 4.371   35.056  1.00 97.70  ? 905  CYS A CB    1 
ATOM   6062 S  SG    . CYS A 1 802 ? -18.183 5.588   34.028  1.00 124.13 ? 905  CYS A SG    1 
ATOM   6063 N  N     . VAL A 1 803 ? -14.496 3.795   33.648  1.00 92.34  ? 906  VAL A N     1 
ATOM   6064 C  CA    . VAL A 1 803 ? -13.458 4.216   32.714  1.00 90.08  ? 906  VAL A CA    1 
ATOM   6065 C  C     . VAL A 1 803 ? -12.906 3.022   31.943  1.00 91.72  ? 906  VAL A C     1 
ATOM   6066 O  O     . VAL A 1 803 ? -12.650 3.113   30.736  1.00 86.34  ? 906  VAL A O     1 
ATOM   6067 C  CB    . VAL A 1 803 ? -12.350 4.971   33.470  1.00 85.09  ? 906  VAL A CB    1 
ATOM   6068 C  CG1   . VAL A 1 803 ? -11.137 5.184   32.578  1.00 83.51  ? 906  VAL A CG1   1 
ATOM   6069 C  CG2   . VAL A 1 803 ? -12.878 6.303   33.982  1.00 87.53  ? 906  VAL A CG2   1 
ATOM   6070 N  N     . ALA A 1 804 ? -12.725 1.886   32.619  1.00 90.75  ? 907  ALA A N     1 
ATOM   6071 C  CA    . ALA A 1 804 ? -12.127 0.723   31.970  1.00 92.18  ? 907  ALA A CA    1 
ATOM   6072 C  C     . ALA A 1 804 ? -13.023 0.182   30.862  1.00 88.63  ? 907  ALA A C     1 
ATOM   6073 O  O     . ALA A 1 804 ? -12.551 -0.118  29.759  1.00 81.62  ? 907  ALA A O     1 
ATOM   6074 C  CB    . ALA A 1 804 ? -11.833 -0.363  33.005  1.00 84.45  ? 907  ALA A CB    1 
ATOM   6075 N  N     . THR A 1 805 ? -14.323 0.052   31.136  1.00 91.09  ? 908  THR A N     1 
ATOM   6076 C  CA    . THR A 1 805 ? -15.228 -0.508  30.138  1.00 91.30  ? 908  THR A CA    1 
ATOM   6077 C  C     . THR A 1 805 ? -15.431 0.438   28.962  1.00 88.47  ? 908  THR A C     1 
ATOM   6078 O  O     . THR A 1 805 ? -15.681 -0.018  27.841  1.00 90.15  ? 908  THR A O     1 
ATOM   6079 C  CB    . THR A 1 805 ? -16.573 -0.853  30.774  1.00 88.81  ? 908  THR A CB    1 
ATOM   6080 O  OG1   . THR A 1 805 ? -17.120 0.312   31.404  1.00 88.33  ? 908  THR A OG1   1 
ATOM   6081 C  CG2   . THR A 1 805 ? -16.407 -1.959  31.804  1.00 86.53  ? 908  THR A CG2   1 
ATOM   6082 N  N     . PHE A 1 806 ? -15.329 1.749   29.191  1.00 88.33  ? 909  PHE A N     1 
ATOM   6083 C  CA    . PHE A 1 806 ? -15.499 2.697   28.095  1.00 86.04  ? 909  PHE A CA    1 
ATOM   6084 C  C     . PHE A 1 806 ? -14.318 2.652   27.134  1.00 91.33  ? 909  PHE A C     1 
ATOM   6085 O  O     . PHE A 1 806 ? -14.504 2.645   25.912  1.00 97.41  ? 909  PHE A O     1 
ATOM   6086 C  CB    . PHE A 1 806 ? -15.690 4.111   28.642  1.00 88.11  ? 909  PHE A CB    1 
ATOM   6087 C  CG    . PHE A 1 806 ? -15.631 5.178   27.586  1.00 91.78  ? 909  PHE A CG    1 
ATOM   6088 C  CD1   . PHE A 1 806 ? -16.711 5.402   26.748  1.00 96.73  ? 909  PHE A CD1   1 
ATOM   6089 C  CD2   . PHE A 1 806 ? -14.495 5.956   27.430  1.00 87.95  ? 909  PHE A CD2   1 
ATOM   6090 C  CE1   . PHE A 1 806 ? -16.660 6.381   25.774  1.00 100.75 ? 909  PHE A CE1   1 
ATOM   6091 C  CE2   . PHE A 1 806 ? -14.438 6.936   26.459  1.00 93.22  ? 909  PHE A CE2   1 
ATOM   6092 C  CZ    . PHE A 1 806 ? -15.522 7.149   25.629  1.00 99.90  ? 909  PHE A CZ    1 
ATOM   6093 N  N     . ILE A 1 807 ? -13.095 2.625   27.669  1.00 87.85  ? 910  ILE A N     1 
ATOM   6094 C  CA    . ILE A 1 807 ? -11.910 2.621   26.817  1.00 83.06  ? 910  ILE A CA    1 
ATOM   6095 C  C     . ILE A 1 807 ? -11.837 1.334   26.005  1.00 84.69  ? 910  ILE A C     1 
ATOM   6096 O  O     . ILE A 1 807 ? -11.568 1.360   24.798  1.00 95.26  ? 910  ILE A O     1 
ATOM   6097 C  CB    . ILE A 1 807 ? -10.643 2.827   27.667  1.00 82.41  ? 910  ILE A CB    1 
ATOM   6098 C  CG1   . ILE A 1 807 ? -10.695 4.178   28.383  1.00 83.22  ? 910  ILE A CG1   1 
ATOM   6099 C  CG2   . ILE A 1 807 ? -9.395  2.725   26.803  1.00 82.65  ? 910  ILE A CG2   1 
ATOM   6100 C  CD1   . ILE A 1 807 ? -9.525  4.421   29.308  1.00 80.45  ? 910  ILE A CD1   1 
ATOM   6101 N  N     . LEU A 1 808 ? -12.082 0.192   26.646  1.00 80.33  ? 911  LEU A N     1 
ATOM   6102 C  CA    . LEU A 1 808 ? -11.983 -1.095  25.972  1.00 86.25  ? 911  LEU A CA    1 
ATOM   6103 C  C     . LEU A 1 808 ? -13.231 -1.455  25.178  1.00 91.56  ? 911  LEU A C     1 
ATOM   6104 O  O     . LEU A 1 808 ? -13.184 -2.407  24.392  1.00 97.87  ? 911  LEU A O     1 
ATOM   6105 C  CB    . LEU A 1 808 ? -11.692 -2.199  26.990  1.00 85.23  ? 911  LEU A CB    1 
ATOM   6106 C  CG    . LEU A 1 808 ? -10.389 -2.076  27.781  1.00 83.98  ? 911  LEU A CG    1 
ATOM   6107 C  CD1   . LEU A 1 808 ? -10.271 -3.213  28.783  1.00 92.27  ? 911  LEU A CD1   1 
ATOM   6108 C  CD2   . LEU A 1 808 ? -9.188  -2.055  26.849  1.00 72.13  ? 911  LEU A CD2   1 
ATOM   6109 N  N     . GLY A 1 809 ? -14.333 -0.729  25.358  1.00 90.23  ? 912  GLY A N     1 
ATOM   6110 C  CA    . GLY A 1 809 ? -15.567 -1.030  24.659  1.00 95.57  ? 912  GLY A CA    1 
ATOM   6111 C  C     . GLY A 1 809 ? -16.036 -2.457  24.856  1.00 100.31 ? 912  GLY A C     1 
ATOM   6112 O  O     . GLY A 1 809 ? -16.249 -3.186  23.883  1.00 106.55 ? 912  GLY A O     1 
ATOM   6113 N  N     . ILE A 1 810 ? -16.197 -2.870  26.111  1.00 102.89 ? 913  ILE A N     1 
ATOM   6114 C  CA    . ILE A 1 810 ? -16.592 -4.238  26.430  1.00 103.94 ? 913  ILE A CA    1 
ATOM   6115 C  C     . ILE A 1 810 ? -18.081 -4.403  26.150  1.00 103.81 ? 913  ILE A C     1 
ATOM   6116 O  O     . ILE A 1 810 ? -18.754 -3.453  25.736  1.00 106.61 ? 913  ILE A O     1 
ATOM   6117 C  CB    . ILE A 1 810 ? -16.256 -4.585  27.891  1.00 99.88  ? 913  ILE A CB    1 
ATOM   6118 C  CG1   . ILE A 1 810 ? -15.077 -3.742  28.376  1.00 92.39  ? 913  ILE A CG1   1 
ATOM   6119 C  CG2   . ILE A 1 810 ? -15.911 -6.060  28.027  1.00 106.92 ? 913  ILE A CG2   1 
ATOM   6120 N  N     . GLY A 1 811 ? -18.600 -5.611  26.365  1.00 104.83 ? 914  GLY A N     1 
ATOM   6121 C  CA    . GLY A 1 811 ? -20.018 -5.844  26.180  1.00 107.28 ? 914  GLY A CA    1 
ATOM   6122 C  C     . GLY A 1 811 ? -20.863 -4.999  27.113  1.00 107.03 ? 914  GLY A C     1 
ATOM   6123 O  O     . GLY A 1 811 ? -20.413 -4.526  28.157  1.00 107.81 ? 914  GLY A O     1 
ATOM   6124 N  N     . ASP A 1 812 ? -22.119 -4.809  26.718  1.00 108.07 ? 915  ASP A N     1 
ATOM   6125 C  CA    . ASP A 1 812 ? -23.016 -3.942  27.468  1.00 107.98 ? 915  ASP A CA    1 
ATOM   6126 C  C     . ASP A 1 812 ? -23.305 -4.522  28.847  1.00 107.81 ? 915  ASP A C     1 
ATOM   6127 O  O     . ASP A 1 812 ? -23.541 -5.723  29.000  1.00 115.18 ? 915  ASP A O     1 
ATOM   6128 C  CB    . ASP A 1 812 ? -24.319 -3.733  26.698  1.00 113.96 ? 915  ASP A CB    1 
ATOM   6129 C  CG    . ASP A 1 812 ? -24.100 -3.060  25.357  1.00 121.82 ? 915  ASP A CG    1 
ATOM   6130 O  OD1   . ASP A 1 812 ? -22.928 -2.827  24.991  1.00 120.25 ? 915  ASP A OD1   1 
ATOM   6131 O  OD2   . ASP A 1 812 ? -25.099 -2.762  24.668  1.00 131.79 ? 915  ASP A OD2   1 
ATOM   6132 N  N     . ARG A 1 813 ? -23.281 -3.654  29.855  1.00 106.85 ? 916  ARG A N     1 
ATOM   6133 C  CA    . ARG A 1 813 ? -23.503 -4.053  31.238  1.00 102.77 ? 916  ARG A CA    1 
ATOM   6134 C  C     . ARG A 1 813 ? -24.990 -4.039  31.566  1.00 101.20 ? 916  ARG A C     1 
ATOM   6135 O  O     . ARG A 1 813 ? -25.732 -3.164  31.112  1.00 103.91 ? 916  ARG A O     1 
ATOM   6136 C  CB    . ARG A 1 813 ? -22.752 -3.120  32.190  1.00 101.40 ? 916  ARG A CB    1 
ATOM   6137 C  CG    . ARG A 1 813 ? -21.424 -3.655  32.708  1.00 98.26  ? 916  ARG A CG    1 
ATOM   6138 C  CD    . ARG A 1 813 ? -20.493 -4.085  31.588  1.00 96.66  ? 916  ARG A CD    1 
ATOM   6139 N  NE    . ARG A 1 813 ? -20.542 -5.525  31.367  1.00 97.59  ? 916  ARG A NE    1 
ATOM   6140 C  CZ    . ARG A 1 813 ? -19.699 -6.192  30.592  1.00 101.42 ? 916  ARG A CZ    1 
ATOM   6141 N  NH1   . ARG A 1 813 ? -18.722 -5.579  29.945  1.00 109.51 ? 916  ARG A NH1   1 
ATOM   6142 N  NH2   . ARG A 1 813 ? -19.838 -7.508  30.465  1.00 102.84 ? 916  ARG A NH2   1 
ATOM   6143 N  N     . HIS A 1 814 ? -25.418 -5.014  32.363  1.00 101.81 ? 917  HIS A N     1 
ATOM   6144 C  CA    . HIS A 1 814 ? -26.801 -5.094  32.816  1.00 103.71 ? 917  HIS A CA    1 
ATOM   6145 C  C     . HIS A 1 814 ? -26.811 -5.654  34.235  1.00 105.19 ? 917  HIS A C     1 
ATOM   6146 O  O     . HIS A 1 814 ? -25.759 -5.841  34.855  1.00 104.06 ? 917  HIS A O     1 
ATOM   6147 C  CB    . HIS A 1 814 ? -27.643 -5.926  31.840  1.00 103.25 ? 917  HIS A CB    1 
ATOM   6148 C  CG    . HIS A 1 814 ? -27.059 -7.267  31.526  1.00 104.49 ? 917  HIS A CG    1 
ATOM   6149 N  ND1   . HIS A 1 814 ? -27.065 -8.312  32.425  1.00 104.80 ? 917  HIS A ND1   1 
ATOM   6150 C  CD2   . HIS A 1 814 ? -26.455 -7.737  30.408  1.00 104.78 ? 917  HIS A CD2   1 
ATOM   6151 C  CE1   . HIS A 1 814 ? -26.490 -9.366  31.875  1.00 105.70 ? 917  HIS A CE1   1 
ATOM   6152 N  NE2   . HIS A 1 814 ? -26.110 -9.044  30.652  1.00 105.67 ? 917  HIS A NE2   1 
ATOM   6153 N  N     . ASN A 1 815 ? -28.011 -5.927  34.754  1.00 103.18 ? 918  ASN A N     1 
ATOM   6154 C  CA    . ASN A 1 815 ? -28.164 -6.330  36.148  1.00 108.65 ? 918  ASN A CA    1 
ATOM   6155 C  C     . ASN A 1 815 ? -27.559 -7.696  36.450  1.00 108.96 ? 918  ASN A C     1 
ATOM   6156 O  O     . ASN A 1 815 ? -27.384 -8.025  37.628  1.00 110.51 ? 918  ASN A O     1 
ATOM   6157 C  CB    . ASN A 1 815 ? -29.644 -6.323  36.537  1.00 113.37 ? 918  ASN A CB    1 
ATOM   6158 C  CG    . ASN A 1 815 ? -30.472 -7.275  35.696  1.00 121.84 ? 918  ASN A CG    1 
ATOM   6159 O  OD1   . ASN A 1 815 ? -30.126 -7.574  34.553  1.00 121.32 ? 918  ASN A OD1   1 
ATOM   6160 N  ND2   . ASN A 1 815 ? -31.576 -7.754  36.259  1.00 113.79 ? 918  ASN A ND2   1 
ATOM   6161 N  N     . SER A 1 816 ? -27.243 -8.495  35.432  1.00 106.54 ? 919  SER A N     1 
ATOM   6162 C  CA    . SER A 1 816 ? -26.577 -9.774  35.638  1.00 106.39 ? 919  SER A CA    1 
ATOM   6163 C  C     . SER A 1 816 ? -25.096 -9.736  35.287  1.00 106.24 ? 919  SER A C     1 
ATOM   6164 O  O     . SER A 1 816 ? -24.386 -10.708 35.564  1.00 106.37 ? 919  SER A O     1 
ATOM   6165 C  CB    . SER A 1 816 ? -27.267 -10.874 34.820  1.00 108.22 ? 919  SER A CB    1 
ATOM   6166 O  OG    . SER A 1 816 ? -28.612 -11.047 35.230  1.00 114.05 ? 919  SER A OG    1 
ATOM   6167 N  N     . ASN A 1 817 ? -24.616 -8.647  34.689  1.00 108.55 ? 920  ASN A N     1 
ATOM   6168 C  CA    . ASN A 1 817 ? -23.201 -8.495  34.375  1.00 101.74 ? 920  ASN A CA    1 
ATOM   6169 C  C     . ASN A 1 817 ? -22.408 -7.839  35.495  1.00 103.21 ? 920  ASN A C     1 
ATOM   6170 O  O     . ASN A 1 817 ? -21.174 -7.898  35.475  1.00 108.38 ? 920  ASN A O     1 
ATOM   6171 C  CB    . ASN A 1 817 ? -23.026 -7.665  33.098  1.00 99.06  ? 920  ASN A CB    1 
ATOM   6172 C  CG    . ASN A 1 817 ? -23.182 -8.489  31.841  1.00 112.55 ? 920  ASN A CG    1 
ATOM   6173 O  OD1   . ASN A 1 817 ? -23.520 -9.671  31.896  1.00 131.58 ? 920  ASN A OD1   1 
ATOM   6174 N  ND2   . ASN A 1 817 ? -22.934 -7.868  30.694  1.00 116.19 ? 920  ASN A ND2   1 
ATOM   6175 N  N     . ILE A 1 818 ? -23.081 -7.220  36.461  1.00 100.93 ? 921  ILE A N     1 
ATOM   6176 C  CA    . ILE A 1 818 ? -22.437 -6.434  37.506  1.00 100.11 ? 921  ILE A CA    1 
ATOM   6177 C  C     . ILE A 1 818 ? -22.637 -7.140  38.839  1.00 101.36 ? 921  ILE A C     1 
ATOM   6178 O  O     . ILE A 1 818 ? -23.761 -7.530  39.180  1.00 102.57 ? 921  ILE A O     1 
ATOM   6179 C  CB    . ILE A 1 818 ? -22.998 -5.002  37.550  1.00 99.50  ? 921  ILE A CB    1 
ATOM   6180 C  CG1   . ILE A 1 818 ? -22.938 -4.369  36.158  1.00 96.40  ? 921  ILE A CG1   1 
ATOM   6181 C  CG2   . ILE A 1 818 ? -22.233 -4.161  38.555  1.00 97.93  ? 921  ILE A CG2   1 
ATOM   6182 C  CD1   . ILE A 1 818 ? -23.621 -3.024  36.066  1.00 94.56  ? 921  ILE A CD1   1 
ATOM   6183 N  N     . MET A 1 819 ? -21.551 -7.301  39.592  1.00 95.69  ? 922  MET A N     1 
ATOM   6184 C  CA    . MET A 1 819 ? -21.582 -7.957  40.890  1.00 96.50  ? 922  MET A CA    1 
ATOM   6185 C  C     . MET A 1 819 ? -21.018 -7.033  41.960  1.00 100.91 ? 922  MET A C     1 
ATOM   6186 O  O     . MET A 1 819 ? -20.133 -6.213  41.693  1.00 101.77 ? 922  MET A O     1 
ATOM   6187 C  CB    . MET A 1 819 ? -20.789 -9.267  40.873  1.00 93.41  ? 922  MET A CB    1 
ATOM   6188 C  CG    . MET A 1 819 ? -21.255 -10.268 39.834  1.00 98.47  ? 922  MET A CG    1 
ATOM   6189 S  SD    . MET A 1 819 ? -20.592 -11.912 40.155  1.00 102.98 ? 922  MET A SD    1 
ATOM   6190 C  CE    . MET A 1 819 ? -21.211 -12.196 41.811  1.00 98.61  ? 922  MET A CE    1 
ATOM   6191 N  N     . VAL A 1 820 ? -21.538 -7.175  43.178  1.00 100.79 ? 923  VAL A N     1 
ATOM   6192 C  CA    . VAL A 1 820 ? -21.137 -6.357  44.317  1.00 100.40 ? 923  VAL A CA    1 
ATOM   6193 C  C     . VAL A 1 820 ? -20.837 -7.272  45.498  1.00 100.62 ? 923  VAL A C     1 
ATOM   6194 O  O     . VAL A 1 820 ? -21.552 -8.253  45.732  1.00 99.80  ? 923  VAL A O     1 
ATOM   6195 C  CB    . VAL A 1 820 ? -22.226 -5.328  44.692  1.00 99.39  ? 923  VAL A CB    1 
ATOM   6196 C  CG1   . VAL A 1 820 ? -21.753 -4.436  45.830  1.00 99.75  ? 923  VAL A CG1   1 
ATOM   6197 C  CG2   . VAL A 1 820 ? -22.612 -4.490  43.481  1.00 99.33  ? 923  VAL A CG2   1 
ATOM   6198 N  N     . LYS A 1 821 ? -19.778 -6.952  46.239  1.00 101.73 ? 924  LYS A N     1 
ATOM   6199 C  CA    . LYS A 1 821 ? -19.418 -7.700  47.432  1.00 103.16 ? 924  LYS A CA    1 
ATOM   6200 C  C     . LYS A 1 821 ? -20.147 -7.137  48.652  1.00 107.97 ? 924  LYS A C     1 
ATOM   6201 O  O     . LYS A 1 821 ? -20.873 -6.142  48.574  1.00 107.54 ? 924  LYS A O     1 
ATOM   6202 C  CB    . LYS A 1 821 ? -17.907 -7.675  47.651  1.00 100.50 ? 924  LYS A CB    1 
ATOM   6203 C  CG    . LYS A 1 821 ? -17.095 -8.362  46.574  1.00 97.08  ? 924  LYS A CG    1 
ATOM   6204 C  CD    . LYS A 1 821 ? -15.615 -8.349  46.923  1.00 91.25  ? 924  LYS A CD    1 
ATOM   6205 C  CE    . LYS A 1 821 ? -15.347 -9.101  48.217  1.00 86.79  ? 924  LYS A CE    1 
ATOM   6206 N  N     . ASP A 1 822 ? -19.945 -7.785  49.802  1.00 109.25 ? 925  ASP A N     1 
ATOM   6207 C  CA    . ASP A 1 822 ? -20.564 -7.313  51.037  1.00 112.30 ? 925  ASP A CA    1 
ATOM   6208 C  C     . ASP A 1 822 ? -19.971 -5.981  51.479  1.00 115.52 ? 925  ASP A C     1 
ATOM   6209 O  O     . ASP A 1 822 ? -20.695 -5.103  51.963  1.00 105.93 ? 925  ASP A O     1 
ATOM   6210 C  CB    . ASP A 1 822 ? -20.405 -8.358  52.141  1.00 119.89 ? 925  ASP A CB    1 
ATOM   6211 C  CG    . ASP A 1 822 ? -21.200 -9.618  51.872  1.00 121.91 ? 925  ASP A CG    1 
ATOM   6212 O  OD1   . ASP A 1 822 ? -21.857 -9.694  50.812  1.00 121.21 ? 925  ASP A OD1   1 
ATOM   6213 O  OD2   . ASP A 1 822 ? -21.174 -10.531 52.725  1.00 110.63 ? 925  ASP A OD2   1 
ATOM   6214 N  N     . ASP A 1 823 ? -18.656 -5.813  51.323  1.00 102.22 ? 926  ASP A N     1 
ATOM   6215 C  CA    . ASP A 1 823 ? -17.996 -4.579  51.730  1.00 98.41  ? 926  ASP A CA    1 
ATOM   6216 C  C     . ASP A 1 823 ? -18.342 -3.398  50.835  1.00 99.64  ? 926  ASP A C     1 
ATOM   6217 O  O     . ASP A 1 823 ? -18.062 -2.255  51.213  1.00 98.42  ? 926  ASP A O     1 
ATOM   6218 C  CB    . ASP A 1 823 ? -16.478 -4.784  51.759  1.00 97.99  ? 926  ASP A CB    1 
ATOM   6219 C  CG    . ASP A 1 823 ? -15.934 -5.332  50.450  1.00 106.45 ? 926  ASP A CG    1 
ATOM   6220 O  OD1   . ASP A 1 823 ? -16.699 -5.416  49.467  1.00 109.12 ? 926  ASP A OD1   1 
ATOM   6221 O  OD2   . ASP A 1 823 ? -14.736 -5.686  50.403  1.00 98.52  ? 926  ASP A OD2   1 
ATOM   6222 N  N     . GLY A 1 824 ? -18.937 -3.640  49.671  1.00 104.97 ? 927  GLY A N     1 
ATOM   6223 C  CA    . GLY A 1 824 ? -19.275 -2.584  48.742  1.00 102.87 ? 927  GLY A CA    1 
ATOM   6224 C  C     . GLY A 1 824 ? -18.393 -2.489  47.516  1.00 101.06 ? 927  GLY A C     1 
ATOM   6225 O  O     . GLY A 1 824 ? -18.453 -1.474  46.813  1.00 99.40  ? 927  GLY A O     1 
ATOM   6226 N  N     . GLN A 1 825 ? -17.579 -3.504  47.237  1.00 108.89 ? 928  GLN A N     1 
ATOM   6227 C  CA    . GLN A 1 825 ? -16.715 -3.489  46.065  1.00 111.39 ? 928  GLN A CA    1 
ATOM   6228 C  C     . GLN A 1 825 ? -17.485 -3.976  44.845  1.00 97.79  ? 928  GLN A C     1 
ATOM   6229 O  O     . GLN A 1 825 ? -18.108 -5.043  44.878  1.00 98.01  ? 928  GLN A O     1 
ATOM   6230 C  CB    . GLN A 1 825 ? -15.483 -4.360  46.304  1.00 103.21 ? 928  GLN A CB    1 
ATOM   6231 C  CG    . GLN A 1 825 ? -14.489 -4.365  45.158  1.00 94.00  ? 928  GLN A CG    1 
ATOM   6232 C  CD    . GLN A 1 825 ? -13.256 -5.190  45.467  1.00 108.57 ? 928  GLN A CD    1 
ATOM   6233 O  OE1   . GLN A 1 825 ? -13.100 -5.701  46.577  1.00 106.82 ? 928  GLN A OE1   1 
ATOM   6234 N  NE2   . GLN A 1 825 ? -12.372 -5.327  44.484  1.00 96.38  ? 928  GLN A NE2   1 
ATOM   6235 N  N     . LEU A 1 826 ? -17.443 -3.194  43.770  1.00 100.00 ? 929  LEU A N     1 
ATOM   6236 C  CA    . LEU A 1 826 ? -18.174 -3.486  42.547  1.00 96.69  ? 929  LEU A CA    1 
ATOM   6237 C  C     . LEU A 1 826 ? -17.211 -3.937  41.455  1.00 87.92  ? 929  LEU A C     1 
ATOM   6238 O  O     . LEU A 1 826 ? -16.055 -3.509  41.409  1.00 84.00  ? 929  LEU A O     1 
ATOM   6239 C  CB    . LEU A 1 826 ? -18.966 -2.258  42.082  1.00 92.60  ? 929  LEU A CB    1 
ATOM   6240 C  CG    . LEU A 1 826 ? -19.959 -2.420  40.931  1.00 92.14  ? 929  LEU A CG    1 
ATOM   6241 C  CD1   . LEU A 1 826 ? -21.188 -1.567  41.181  1.00 98.54  ? 929  LEU A CD1   1 
ATOM   6242 C  CD2   . LEU A 1 826 ? -19.320 -2.048  39.599  1.00 92.80  ? 929  LEU A CD2   1 
ATOM   6243 N  N     . PHE A 1 827 ? -17.702 -4.809  40.575  1.00 87.87  ? 930  PHE A N     1 
ATOM   6244 C  CA    . PHE A 1 827 ? -16.899 -5.321  39.471  1.00 90.70  ? 930  PHE A CA    1 
ATOM   6245 C  C     . PHE A 1 827 ? -17.823 -5.942  38.432  1.00 89.32  ? 930  PHE A C     1 
ATOM   6246 O  O     . PHE A 1 827 ? -19.035 -6.056  38.634  1.00 91.25  ? 930  PHE A O     1 
ATOM   6247 C  CB    . PHE A 1 827 ? -15.854 -6.333  39.960  1.00 84.76  ? 930  PHE A CB    1 
ATOM   6248 C  CG    . PHE A 1 827 ? -16.441 -7.548  40.621  1.00 85.04  ? 930  PHE A CG    1 
ATOM   6249 C  CD1   . PHE A 1 827 ? -16.899 -7.492  41.929  1.00 91.72  ? 930  PHE A CD1   1 
ATOM   6250 C  CD2   . PHE A 1 827 ? -16.521 -8.751  39.940  1.00 77.30  ? 930  PHE A CD2   1 
ATOM   6251 C  CE1   . PHE A 1 827 ? -17.435 -8.609  42.539  1.00 90.18  ? 930  PHE A CE1   1 
ATOM   6252 C  CE2   . PHE A 1 827 ? -17.055 -9.872  40.546  1.00 84.99  ? 930  PHE A CE2   1 
ATOM   6253 C  CZ    . PHE A 1 827 ? -17.512 -9.800  41.846  1.00 88.96  ? 930  PHE A CZ    1 
ATOM   6254 N  N     . HIS A 1 828 ? -17.229 -6.336  37.306  1.00 88.69  ? 931  HIS A N     1 
ATOM   6255 C  CA    . HIS A 1 828 ? -17.936 -6.973  36.205  1.00 91.93  ? 931  HIS A CA    1 
ATOM   6256 C  C     . HIS A 1 828 ? -17.390 -8.380  35.996  1.00 91.49  ? 931  HIS A C     1 
ATOM   6257 O  O     . HIS A 1 828 ? -16.294 -8.716  36.455  1.00 89.12  ? 931  HIS A O     1 
ATOM   6258 C  CB    . HIS A 1 828 ? -17.803 -6.157  34.911  1.00 89.24  ? 931  HIS A CB    1 
ATOM   6259 C  CG    . HIS A 1 828 ? -18.284 -4.744  35.036  1.00 87.47  ? 931  HIS A CG    1 
ATOM   6260 N  ND1   . HIS A 1 828 ? -19.247 -4.362  35.945  1.00 96.66  ? 931  HIS A ND1   1 
ATOM   6261 C  CD2   . HIS A 1 828 ? -17.930 -3.620  34.370  1.00 86.78  ? 931  HIS A CD2   1 
ATOM   6262 C  CE1   . HIS A 1 828 ? -19.468 -3.065  35.831  1.00 94.71  ? 931  HIS A CE1   1 
ATOM   6263 N  NE2   . HIS A 1 828 ? -18.681 -2.590  34.882  1.00 90.21  ? 931  HIS A NE2   1 
ATOM   6264 N  N     . ILE A 1 829 ? -18.162 -9.209  35.291  1.00 97.31  ? 932  ILE A N     1 
ATOM   6265 C  CA    . ILE A 1 829 ? -17.802 -10.618 35.151  1.00 102.07 ? 932  ILE A CA    1 
ATOM   6266 C  C     . ILE A 1 829 ? -17.909 -11.103 33.710  1.00 99.79  ? 932  ILE A C     1 
ATOM   6267 O  O     . ILE A 1 829 ? -17.097 -11.924 33.267  1.00 108.77 ? 932  ILE A O     1 
ATOM   6268 C  CB    . ILE A 1 829 ? -18.662 -11.502 36.075  1.00 94.54  ? 932  ILE A CB    1 
ATOM   6269 C  CG1   . ILE A 1 829 ? -20.154 -11.264 35.829  1.00 104.82 ? 932  ILE A CG1   1 
ATOM   6270 C  CG2   . ILE A 1 829 ? -18.312 -11.253 37.528  1.00 97.62  ? 932  ILE A CG2   1 
ATOM   6271 C  CD1   . ILE A 1 829 ? -21.054 -12.214 36.588  1.00 100.15 ? 932  ILE A CD1   1 
ATOM   6272 N  N     . ASP A 1 830 ? -18.904 -10.613 32.970  1.00 101.80 ? 933  ASP A N     1 
ATOM   6273 C  CA    . ASP A 1 830 ? -19.228 -11.190 31.669  1.00 111.95 ? 933  ASP A CA    1 
ATOM   6274 C  C     . ASP A 1 830 ? -18.080 -11.050 30.676  1.00 105.69 ? 933  ASP A C     1 
ATOM   6275 O  O     . ASP A 1 830 ? -17.442 -12.048 30.325  1.00 122.92 ? 933  ASP A O     1 
ATOM   6276 C  CB    . ASP A 1 830 ? -20.497 -10.553 31.101  1.00 123.61 ? 933  ASP A CB    1 
ATOM   6277 C  CG    . ASP A 1 830 ? -20.977 -11.238 29.837  1.00 118.25 ? 933  ASP A CG    1 
ATOM   6278 O  OD1   . ASP A 1 830 ? -21.256 -12.455 29.891  1.00 114.16 ? 933  ASP A OD1   1 
ATOM   6279 O  OD2   . ASP A 1 830 ? -21.079 -10.560 28.793  1.00 133.87 ? 933  ASP A OD2   1 
ATOM   6280 N  N     . PHE A 1 831 ? -17.815 -9.825  30.218  1.00 107.96 ? 934  PHE A N     1 
ATOM   6281 C  CA    . PHE A 1 831 ? -16.737 -9.536  29.269  1.00 110.79 ? 934  PHE A CA    1 
ATOM   6282 C  C     . PHE A 1 831 ? -16.894 -10.374 27.995  1.00 117.35 ? 934  PHE A C     1 
ATOM   6283 O  O     . PHE A 1 831 ? -16.092 -11.256 27.683  1.00 114.48 ? 934  PHE A O     1 
ATOM   6284 C  CB    . PHE A 1 831 ? -15.361 -9.769  29.908  1.00 104.32 ? 934  PHE A CB    1 
ATOM   6285 C  CG    . PHE A 1 831 ? -15.104 -8.924  31.119  1.00 102.41 ? 934  PHE A CG    1 
ATOM   6286 C  CD1   . PHE A 1 831 ? -15.684 -7.673  31.245  1.00 101.72 ? 934  PHE A CD1   1 
ATOM   6287 C  CD2   . PHE A 1 831 ? -14.282 -9.383  32.135  1.00 96.76  ? 934  PHE A CD2   1 
ATOM   6288 C  CE1   . PHE A 1 831 ? -15.448 -6.896  32.361  1.00 95.26  ? 934  PHE A CE1   1 
ATOM   6289 C  CE2   . PHE A 1 831 ? -14.042 -8.610  33.252  1.00 88.42  ? 934  PHE A CE2   1 
ATOM   6290 C  CZ    . PHE A 1 831 ? -14.627 -7.365  33.366  1.00 87.08  ? 934  PHE A CZ    1 
ATOM   6291 N  N     . GLY A 1 832 ? -17.964 -10.068 27.267  1.00 117.78 ? 935  GLY A N     1 
ATOM   6292 C  CA    . GLY A 1 832 ? -18.254 -10.773 26.035  1.00 126.31 ? 935  GLY A CA    1 
ATOM   6293 C  C     . GLY A 1 832 ? -17.258 -10.471 24.936  1.00 127.40 ? 935  GLY A C     1 
ATOM   6294 O  O     . GLY A 1 832 ? -16.496 -11.348 24.517  1.00 124.71 ? 935  GLY A O     1 
ATOM   6295 N  N     . HIS A 1 833 ? -17.254 -9.227  24.464  1.00 130.92 ? 936  HIS A N     1 
ATOM   6296 C  CA    . HIS A 1 833 ? -16.356 -8.797  23.404  1.00 127.45 ? 936  HIS A CA    1 
ATOM   6297 C  C     . HIS A 1 833 ? -15.874 -7.385  23.696  1.00 126.87 ? 936  HIS A C     1 
ATOM   6298 O  O     . HIS A 1 833 ? -16.661 -6.520  24.088  1.00 138.32 ? 936  HIS A O     1 
ATOM   6299 C  CB    . HIS A 1 833 ? -17.042 -8.844  22.032  1.00 139.57 ? 936  HIS A CB    1 
ATOM   6300 C  CG    . HIS A 1 833 ? -17.313 -10.231 21.539  1.00 140.23 ? 936  HIS A CG    1 
ATOM   6301 N  ND1   . HIS A 1 833 ? -16.544 -11.315 21.906  1.00 139.59 ? 936  HIS A ND1   1 
ATOM   6302 C  CD2   . HIS A 1 833 ? -18.270 -10.713 20.711  1.00 135.92 ? 936  HIS A CD2   1 
ATOM   6303 C  CE1   . HIS A 1 833 ? -17.014 -12.403 21.323  1.00 136.82 ? 936  HIS A CE1   1 
ATOM   6304 N  NE2   . HIS A 1 833 ? -18.061 -12.065 20.593  1.00 135.27 ? 936  HIS A NE2   1 
ATOM   6305 N  N     . PHE A 1 834 ? -14.578 -7.163  23.505  1.00 118.33 ? 937  PHE A N     1 
ATOM   6306 C  CA    . PHE A 1 834 ? -13.963 -5.863  23.704  1.00 115.33 ? 937  PHE A CA    1 
ATOM   6307 C  C     . PHE A 1 834 ? -13.753 -5.179  22.354  1.00 116.10 ? 937  PHE A C     1 
ATOM   6308 O  O     . PHE A 1 834 ? -14.017 -5.750  21.292  1.00 118.54 ? 937  PHE A O     1 
ATOM   6309 C  CB    . PHE A 1 834 ? -12.648 -6.008  24.474  1.00 112.86 ? 937  PHE A CB    1 
ATOM   6310 C  CG    . PHE A 1 834 ? -11.741 -7.075  23.931  1.00 110.39 ? 937  PHE A CG    1 
ATOM   6311 C  CD1   . PHE A 1 834 ? -10.806 -6.775  22.955  1.00 110.98 ? 937  PHE A CD1   1 
ATOM   6312 C  CD2   . PHE A 1 834 ? -11.825 -8.377  24.395  1.00 106.14 ? 937  PHE A CD2   1 
ATOM   6313 C  CE1   . PHE A 1 834 ? -9.973  -7.753  22.452  1.00 109.37 ? 937  PHE A CE1   1 
ATOM   6314 C  CE2   . PHE A 1 834 ? -10.995 -9.360  23.896  1.00 106.57 ? 937  PHE A CE2   1 
ATOM   6315 C  CZ    . PHE A 1 834 ? -10.068 -9.046  22.922  1.00 109.91 ? 937  PHE A CZ    1 
ATOM   6316 N  N     . LEU A 1 835 ? -13.272 -3.941  22.405  1.00 115.29 ? 938  LEU A N     1 
ATOM   6317 C  CA    . LEU A 1 835 ? -13.076 -3.099  21.217  1.00 111.90 ? 938  LEU A CA    1 
ATOM   6318 C  C     . LEU A 1 835 ? -14.439 -2.912  20.542  1.00 120.05 ? 938  LEU A C     1 
ATOM   6319 O  O     . LEU A 1 835 ? -15.472 -2.829  21.219  1.00 125.95 ? 938  LEU A O     1 
ATOM   6320 C  CB    . LEU A 1 835 ? -11.996 -3.693  20.329  1.00 114.69 ? 938  LEU A CB    1 
ATOM   6321 C  CG    . LEU A 1 835 ? -10.617 -3.830  20.976  1.00 111.91 ? 938  LEU A CG    1 
ATOM   6322 C  CD1   . LEU A 1 835 ? -9.684  -4.653  20.104  1.00 111.53 ? 938  LEU A CD1   1 
ATOM   6323 C  CD2   . LEU A 1 835 ? -10.020 -2.461  21.253  1.00 111.88 ? 938  LEU A CD2   1 
ATOM   6324 N  N     . ASP A 1 836 ? -14.465 -2.840  19.215  1.00 122.19 ? 939  ASP A N     1 
ATOM   6325 C  CA    . ASP A 1 836 ? -15.728 -2.683  18.513  1.00 137.97 ? 939  ASP A CA    1 
ATOM   6326 C  C     . ASP A 1 836 ? -16.537 -3.977  18.581  1.00 146.52 ? 939  ASP A C     1 
ATOM   6327 O  O     . ASP A 1 836 ? -16.014 -5.056  18.875  1.00 140.41 ? 939  ASP A O     1 
ATOM   6328 C  CB    . ASP A 1 836 ? -15.485 -2.279  17.058  1.00 142.84 ? 939  ASP A CB    1 
ATOM   6329 C  CG    . ASP A 1 836 ? -16.742 -1.777  16.373  1.00 145.19 ? 939  ASP A CG    1 
ATOM   6330 O  OD1   . ASP A 1 836 ? -17.281 -0.737  16.807  1.00 145.49 ? 939  ASP A OD1   1 
ATOM   6331 O  OD2   . ASP A 1 836 ? -17.191 -2.421  15.402  1.00 149.82 ? 939  ASP A OD2   1 
ATOM   6332 N  N     . HIS A 1 837 ? -17.833 -3.853  18.315  1.00 149.49 ? 940  HIS A N     1 
ATOM   6333 C  CA    . HIS A 1 837 ? -18.733 -5.002  18.318  1.00 149.14 ? 940  HIS A CA    1 
ATOM   6334 C  C     . HIS A 1 837 ? -18.338 -6.016  17.248  1.00 151.66 ? 940  HIS A C     1 
ATOM   6335 O  O     . HIS A 1 837 ? -17.767 -5.656  16.218  1.00 150.53 ? 940  HIS A O     1 
ATOM   6336 C  CB    . HIS A 1 837 ? -20.179 -4.549  18.103  1.00 149.26 ? 940  HIS A CB    1 
ATOM   6337 C  CG    . HIS A 1 837 ? -20.390 -3.774  16.839  1.00 149.10 ? 940  HIS A CG    1 
ATOM   6338 N  ND1   . HIS A 1 837 ? -20.542 -2.404  16.823  1.00 149.61 ? 940  HIS A ND1   1 
ATOM   6339 C  CD2   . HIS A 1 837 ? -20.472 -4.176  15.549  1.00 144.82 ? 940  HIS A CD2   1 
ATOM   6340 C  CE1   . HIS A 1 837 ? -20.711 -1.996  15.578  1.00 145.16 ? 940  HIS A CE1   1 
ATOM   6341 N  NE2   . HIS A 1 837 ? -20.671 -3.052  14.785  1.00 144.27 ? 940  HIS A NE2   1 
ATOM   6342 N  N     . ARG A 1 846 ? -20.085 8.878   19.043  1.00 131.61 ? 949  ARG A N     1 
ATOM   6343 C  CA    . ARG A 1 846 ? -20.968 7.718   19.009  1.00 130.91 ? 949  ARG A CA    1 
ATOM   6344 C  C     . ARG A 1 846 ? -20.225 6.442   19.392  1.00 127.57 ? 949  ARG A C     1 
ATOM   6345 O  O     . ARG A 1 846 ? -20.459 5.382   18.810  1.00 126.36 ? 949  ARG A O     1 
ATOM   6346 C  CB    . ARG A 1 846 ? -21.600 7.555   17.623  1.00 140.05 ? 949  ARG A CB    1 
ATOM   6347 C  CG    . ARG A 1 846 ? -22.879 8.357   17.405  1.00 147.66 ? 949  ARG A CG    1 
ATOM   6348 C  CD    . ARG A 1 846 ? -22.603 9.846   17.289  1.00 153.40 ? 949  ARG A CD    1 
ATOM   6349 N  NE    . ARG A 1 846 ? -21.634 10.136  16.238  1.00 152.16 ? 949  ARG A NE    1 
ATOM   6350 C  CZ    . ARG A 1 846 ? -21.948 10.363  14.971  1.00 159.59 ? 949  ARG A CZ    1 
ATOM   6351 N  NH1   . ARG A 1 846 ? -23.205 10.347  14.556  1.00 160.89 ? 949  ARG A NH1   1 
ATOM   6352 N  NH2   . ARG A 1 846 ? -20.978 10.613  14.096  1.00 164.55 ? 949  ARG A NH2   1 
ATOM   6353 N  N     . GLU A 1 847 ? -19.325 6.550   20.364  1.00 122.07 ? 950  GLU A N     1 
ATOM   6354 C  CA    . GLU A 1 847 ? -18.661 5.374   20.904  1.00 120.65 ? 950  GLU A CA    1 
ATOM   6355 C  C     . GLU A 1 847 ? -19.534 4.717   21.965  1.00 119.79 ? 950  GLU A C     1 
ATOM   6356 O  O     . GLU A 1 847 ? -20.309 5.378   22.662  1.00 118.22 ? 950  GLU A O     1 
ATOM   6357 C  CB    . GLU A 1 847 ? -17.299 5.738   21.497  1.00 115.65 ? 950  GLU A CB    1 
ATOM   6358 C  CG    . GLU A 1 847 ? -16.160 5.770   20.486  1.00 111.81 ? 950  GLU A CG    1 
ATOM   6359 C  CD    . GLU A 1 847 ? -16.230 6.962   19.550  1.00 118.28 ? 950  GLU A CD    1 
ATOM   6360 O  OE1   . GLU A 1 847 ? -17.043 7.877   19.801  1.00 122.54 ? 950  GLU A OE1   1 
ATOM   6361 O  OE2   . GLU A 1 847 ? -15.466 6.985   18.562  1.00 111.83 ? 950  GLU A OE2   1 
ATOM   6362 N  N     . ARG A 1 848 ? -19.399 3.400   22.083  1.00 120.21 ? 951  ARG A N     1 
ATOM   6363 C  CA    . ARG A 1 848 ? -20.261 2.623   22.961  1.00 123.37 ? 951  ARG A CA    1 
ATOM   6364 C  C     . ARG A 1 848 ? -19.868 2.822   24.419  1.00 125.29 ? 951  ARG A C     1 
ATOM   6365 O  O     . ARG A 1 848 ? -18.691 2.715   24.776  1.00 124.22 ? 951  ARG A O     1 
ATOM   6366 C  CB    . ARG A 1 848 ? -20.192 1.143   22.591  1.00 135.70 ? 951  ARG A CB    1 
ATOM   6367 C  CG    . ARG A 1 848 ? -21.093 0.247   23.423  1.00 139.23 ? 951  ARG A CG    1 
ATOM   6368 C  CD    . ARG A 1 848 ? -21.158 -1.158  22.846  1.00 141.70 ? 951  ARG A CD    1 
ATOM   6369 N  NE    . ARG A 1 848 ? -21.778 -1.180  21.526  1.00 148.93 ? 951  ARG A NE    1 
ATOM   6370 C  CZ    . ARG A 1 848 ? -21.111 -1.233  20.381  1.00 163.22 ? 951  ARG A CZ    1 
ATOM   6371 N  NH1   . ARG A 1 848 ? -19.789 -1.288  20.352  1.00 150.95 ? 951  ARG A NH1   1 
ATOM   6372 N  NH2   . ARG A 1 848 ? -21.788 -1.231  19.236  1.00 161.59 ? 951  ARG A NH2   1 
ATOM   6373 N  N     . VAL A 1 849 ? -20.859 3.115   25.256  1.00 113.10 ? 952  VAL A N     1 
ATOM   6374 C  CA    . VAL A 1 849 ? -20.667 3.208   26.701  1.00 105.79 ? 952  VAL A CA    1 
ATOM   6375 C  C     . VAL A 1 849 ? -21.328 1.992   27.339  1.00 105.55 ? 952  VAL A C     1 
ATOM   6376 O  O     . VAL A 1 849 ? -22.542 2.008   27.594  1.00 105.69 ? 952  VAL A O     1 
ATOM   6377 C  CB    . VAL A 1 849 ? -21.237 4.519   27.264  1.00 103.31 ? 952  VAL A CB    1 
ATOM   6378 C  CG1   . VAL A 1 849 ? -21.050 4.575   28.773  1.00 108.57 ? 952  VAL A CG1   1 
ATOM   6379 C  CG2   . VAL A 1 849 ? -20.576 5.714   26.597  1.00 102.28 ? 952  VAL A CG2   1 
ATOM   6380 N  N     . PRO A 1 850 ? -20.581 0.916   27.601  1.00 104.72 ? 953  PRO A N     1 
ATOM   6381 C  CA    . PRO A 1 850 ? -21.226 -0.295  28.135  1.00 105.78 ? 953  PRO A CA    1 
ATOM   6382 C  C     . PRO A 1 850 ? -21.717 -0.139  29.563  1.00 105.92 ? 953  PRO A C     1 
ATOM   6383 O  O     . PRO A 1 850 ? -22.785 -0.663  29.903  1.00 103.88 ? 953  PRO A O     1 
ATOM   6384 C  CB    . PRO A 1 850 ? -20.123 -1.355  28.015  1.00 102.31 ? 953  PRO A CB    1 
ATOM   6385 C  CG    . PRO A 1 850 ? -18.852 -0.582  28.023  1.00 99.04  ? 953  PRO A CG    1 
ATOM   6386 C  CD    . PRO A 1 850 ? -19.144 0.721   27.345  1.00 100.43 ? 953  PRO A CD    1 
ATOM   6387 N  N     . PHE A 1 851 ? -20.970 0.561   30.414  1.00 114.76 ? 954  PHE A N     1 
ATOM   6388 C  CA    . PHE A 1 851 ? -21.384 0.806   31.792  1.00 106.42 ? 954  PHE A CA    1 
ATOM   6389 C  C     . PHE A 1 851 ? -22.135 2.132   31.835  1.00 115.34 ? 954  PHE A C     1 
ATOM   6390 O  O     . PHE A 1 851 ? -21.526 3.203   31.757  1.00 125.93 ? 954  PHE A O     1 
ATOM   6391 C  CB    . PHE A 1 851 ? -20.176 0.822   32.725  1.00 105.98 ? 954  PHE A CB    1 
ATOM   6392 C  CG    . PHE A 1 851 ? -20.527 0.673   34.181  1.00 117.75 ? 954  PHE A CG    1 
ATOM   6393 C  CD1   . PHE A 1 851 ? -21.837 0.449   34.578  1.00 117.84 ? 954  PHE A CD1   1 
ATOM   6394 C  CD2   . PHE A 1 851 ? -19.545 0.762   35.154  1.00 110.57 ? 954  PHE A CD2   1 
ATOM   6395 C  CE1   . PHE A 1 851 ? -22.159 0.314   35.914  1.00 113.14 ? 954  PHE A CE1   1 
ATOM   6396 C  CE2   . PHE A 1 851 ? -19.862 0.629   36.492  1.00 106.09 ? 954  PHE A CE2   1 
ATOM   6397 C  CZ    . PHE A 1 851 ? -21.170 0.404   36.873  1.00 116.22 ? 954  PHE A CZ    1 
ATOM   6398 N  N     . VAL A 1 852 ? -23.463 2.059   31.969  1.00 115.14 ? 955  VAL A N     1 
ATOM   6399 C  CA    . VAL A 1 852 ? -24.304 3.250   31.884  1.00 117.48 ? 955  VAL A CA    1 
ATOM   6400 C  C     . VAL A 1 852 ? -24.566 3.892   33.240  1.00 118.48 ? 955  VAL A C     1 
ATOM   6401 O  O     . VAL A 1 852 ? -25.051 5.034   33.287  1.00 121.00 ? 955  VAL A O     1 
ATOM   6402 C  CB    . VAL A 1 852 ? -25.640 2.907   31.193  1.00 113.63 ? 955  VAL A CB    1 
ATOM   6403 C  CG1   . VAL A 1 852 ? -26.593 2.229   32.167  1.00 120.30 ? 955  VAL A CG1   1 
ATOM   6404 C  CG2   . VAL A 1 852 ? -26.271 4.148   30.573  1.00 111.41 ? 955  VAL A CG2   1 
ATOM   6405 N  N     . LEU A 1 853 ? -24.252 3.207   34.341  1.00 117.36 ? 956  LEU A N     1 
ATOM   6406 C  CA    . LEU A 1 853 ? -24.485 3.725   35.688  1.00 124.53 ? 956  LEU A CA    1 
ATOM   6407 C  C     . LEU A 1 853 ? -25.943 4.126   35.879  1.00 122.57 ? 956  LEU A C     1 
ATOM   6408 O  O     . LEU A 1 853 ? -26.280 5.315   35.867  1.00 120.47 ? 956  LEU A O     1 
ATOM   6409 C  CB    . LEU A 1 853 ? -23.562 4.913   35.987  1.00 120.29 ? 956  LEU A CB    1 
ATOM   6410 C  CG    . LEU A 1 853 ? -22.181 4.635   36.590  1.00 117.56 ? 956  LEU A CG    1 
ATOM   6411 C  CD1   . LEU A 1 853 ? -22.305 3.877   37.902  1.00 114.86 ? 956  LEU A CD1   1 
ATOM   6412 C  CD2   . LEU A 1 853 ? -21.286 3.888   35.613  1.00 118.75 ? 956  LEU A CD2   1 
ATOM   6413 N  N     . THR A 1 854 ? -26.810 3.136   36.065  1.00 126.46 ? 957  THR A N     1 
ATOM   6414 C  CA    . THR A 1 854 ? -28.227 3.407   36.232  1.00 120.97 ? 957  THR A CA    1 
ATOM   6415 C  C     . THR A 1 854 ? -28.474 4.195   37.520  1.00 118.27 ? 957  THR A C     1 
ATOM   6416 O  O     . THR A 1 854 ? -27.577 4.409   38.340  1.00 116.24 ? 957  THR A O     1 
ATOM   6417 C  CB    . THR A 1 854 ? -29.027 2.105   36.248  1.00 123.97 ? 957  THR A CB    1 
ATOM   6418 O  OG1   . THR A 1 854 ? -28.631 1.304   37.370  1.00 117.87 ? 957  THR A OG1   1 
ATOM   6419 C  CG2   . THR A 1 854 ? -28.799 1.320   34.966  1.00 123.63 ? 957  THR A CG2   1 
ATOM   6420 N  N     . GLN A 1 855 ? -29.727 4.627   37.691  1.00 120.05 ? 958  GLN A N     1 
ATOM   6421 C  CA    . GLN A 1 855 ? -30.096 5.430   38.853  1.00 115.81 ? 958  GLN A CA    1 
ATOM   6422 C  C     . GLN A 1 855 ? -29.906 4.679   40.164  1.00 117.46 ? 958  GLN A C     1 
ATOM   6423 O  O     . GLN A 1 855 ? -29.769 5.316   41.214  1.00 119.59 ? 958  GLN A O     1 
ATOM   6424 C  CB    . GLN A 1 855 ? -31.547 5.903   38.731  1.00 114.51 ? 958  GLN A CB    1 
ATOM   6425 C  CG    . GLN A 1 855 ? -31.778 6.965   37.661  1.00 124.14 ? 958  GLN A CG    1 
ATOM   6426 C  CD    . GLN A 1 855 ? -31.759 6.409   36.245  1.00 116.17 ? 958  GLN A CD    1 
ATOM   6427 O  OE1   . GLN A 1 855 ? -31.534 5.217   36.030  1.00 113.44 ? 958  GLN A OE1   1 
ATOM   6428 N  NE2   . GLN A 1 855 ? -32.001 7.277   35.269  1.00 107.98 ? 958  GLN A NE2   1 
ATOM   6429 N  N     . ASP A 1 856 ? -29.897 3.345   40.130  1.00 117.71 ? 959  ASP A N     1 
ATOM   6430 C  CA    . ASP A 1 856 ? -29.634 2.582   41.344  1.00 118.21 ? 959  ASP A CA    1 
ATOM   6431 C  C     . ASP A 1 856 ? -28.215 2.820   41.844  1.00 117.85 ? 959  ASP A C     1 
ATOM   6432 O  O     . ASP A 1 856 ? -27.987 2.941   43.053  1.00 119.16 ? 959  ASP A O     1 
ATOM   6433 C  CB    . ASP A 1 856 ? -29.872 1.093   41.092  1.00 123.18 ? 959  ASP A CB    1 
ATOM   6434 C  CG    . ASP A 1 856 ? -31.333 0.768   40.847  1.00 143.03 ? 959  ASP A CG    1 
ATOM   6435 O  OD1   . ASP A 1 856 ? -31.904 1.291   39.866  1.00 141.62 ? 959  ASP A OD1   1 
ATOM   6436 O  OD2   . ASP A 1 856 ? -31.908 -0.015  41.632  1.00 142.33 ? 959  ASP A OD2   1 
ATOM   6437 N  N     . PHE A 1 857 ? -27.248 2.894   40.926  1.00 117.35 ? 960  PHE A N     1 
ATOM   6438 C  CA    . PHE A 1 857 ? -25.869 3.151   41.327  1.00 112.61 ? 960  PHE A CA    1 
ATOM   6439 C  C     . PHE A 1 857 ? -25.686 4.594   41.780  1.00 110.50 ? 960  PHE A C     1 
ATOM   6440 O  O     . PHE A 1 857 ? -24.907 4.867   42.700  1.00 114.96 ? 960  PHE A O     1 
ATOM   6441 C  CB    . PHE A 1 857 ? -24.914 2.833   40.177  1.00 114.69 ? 960  PHE A CB    1 
ATOM   6442 C  CG    . PHE A 1 857 ? -25.068 1.447   39.621  1.00 114.89 ? 960  PHE A CG    1 
ATOM   6443 C  CD1   . PHE A 1 857 ? -24.643 0.345   40.343  1.00 116.10 ? 960  PHE A CD1   1 
ATOM   6444 C  CD2   . PHE A 1 857 ? -25.623 1.249   38.369  1.00 116.76 ? 960  PHE A CD2   1 
ATOM   6445 C  CE1   . PHE A 1 857 ? -24.780 -0.931  39.829  1.00 120.36 ? 960  PHE A CE1   1 
ATOM   6446 C  CE2   . PHE A 1 857 ? -25.762 -0.024  37.849  1.00 116.58 ? 960  PHE A CE2   1 
ATOM   6447 C  CZ    . PHE A 1 857 ? -25.340 -1.116  38.581  1.00 116.89 ? 960  PHE A CZ    1 
ATOM   6448 N  N     . LEU A 1 858 ? -26.392 5.531   41.141  1.00 113.98 ? 961  LEU A N     1 
ATOM   6449 C  CA    . LEU A 1 858 ? -26.268 6.935   41.516  1.00 113.28 ? 961  LEU A CA    1 
ATOM   6450 C  C     . LEU A 1 858 ? -26.770 7.185   42.932  1.00 118.01 ? 961  LEU A C     1 
ATOM   6451 O  O     . LEU A 1 858 ? -26.242 8.057   43.632  1.00 117.35 ? 961  LEU A O     1 
ATOM   6452 C  CB    . LEU A 1 858 ? -27.028 7.813   40.521  1.00 112.60 ? 961  LEU A CB    1 
ATOM   6453 C  CG    . LEU A 1 858 ? -26.492 7.822   39.090  1.00 109.45 ? 961  LEU A CG    1 
ATOM   6454 C  CD1   . LEU A 1 858 ? -27.375 8.674   38.194  1.00 114.36 ? 961  LEU A CD1   1 
ATOM   6455 C  CD2   . LEU A 1 858 ? -25.059 8.322   39.068  1.00 105.56 ? 961  LEU A CD2   1 
ATOM   6456 N  N     . ILE A 1 859 ? -27.785 6.436   43.369  1.00 115.52 ? 962  ILE A N     1 
ATOM   6457 C  CA    . ILE A 1 859 ? -28.266 6.565   44.741  1.00 114.24 ? 962  ILE A CA    1 
ATOM   6458 C  C     . ILE A 1 859 ? -27.169 6.183   45.725  1.00 114.14 ? 962  ILE A C     1 
ATOM   6459 O  O     . ILE A 1 859 ? -26.967 6.851   46.746  1.00 118.44 ? 962  ILE A O     1 
ATOM   6460 C  CB    . ILE A 1 859 ? -29.534 5.715   44.946  1.00 118.93 ? 962  ILE A CB    1 
ATOM   6461 C  CG1   . ILE A 1 859 ? -30.688 6.254   44.098  1.00 119.63 ? 962  ILE A CG1   1 
ATOM   6462 C  CG2   . ILE A 1 859 ? -29.930 5.688   46.413  1.00 115.08 ? 962  ILE A CG2   1 
ATOM   6463 C  CD1   . ILE A 1 859 ? -31.205 7.599   44.553  1.00 121.56 ? 962  ILE A CD1   1 
ATOM   6464 N  N     . VAL A 1 860 ? -26.430 5.112   45.428  1.00 111.86 ? 963  VAL A N     1 
ATOM   6465 C  CA    . VAL A 1 860 ? -25.390 4.654   46.343  1.00 110.94 ? 963  VAL A CA    1 
ATOM   6466 C  C     . VAL A 1 860 ? -24.220 5.631   46.364  1.00 112.53 ? 963  VAL A C     1 
ATOM   6467 O  O     . VAL A 1 860 ? -23.625 5.883   47.419  1.00 112.15 ? 963  VAL A O     1 
ATOM   6468 C  CB    . VAL A 1 860 ? -24.935 3.234   45.961  1.00 105.96 ? 963  VAL A CB    1 
ATOM   6469 C  CG1   . VAL A 1 860 ? -23.945 2.704   46.984  1.00 102.53 ? 963  VAL A CG1   1 
ATOM   6470 C  CG2   . VAL A 1 860 ? -26.134 2.308   45.838  1.00 109.60 ? 963  VAL A CG2   1 
ATOM   6471 N  N     . ILE A 1 861 ? -23.874 6.196   45.206  1.00 113.96 ? 964  ILE A N     1 
ATOM   6472 C  CA    . ILE A 1 861 ? -22.728 7.097   45.127  1.00 112.14 ? 964  ILE A CA    1 
ATOM   6473 C  C     . ILE A 1 861 ? -22.990 8.375   45.913  1.00 112.95 ? 964  ILE A C     1 
ATOM   6474 O  O     . ILE A 1 861 ? -22.107 8.879   46.620  1.00 110.61 ? 964  ILE A O     1 
ATOM   6475 C  CB    . ILE A 1 861 ? -22.387 7.392   43.654  1.00 107.96 ? 964  ILE A CB    1 
ATOM   6476 C  CG1   . ILE A 1 861 ? -21.840 6.136   42.973  1.00 105.56 ? 964  ILE A CG1   1 
ATOM   6477 C  CG2   . ILE A 1 861 ? -21.395 8.543   43.543  1.00 99.98  ? 964  ILE A CG2   1 
ATOM   6478 C  CD1   . ILE A 1 861 ? -21.552 6.316   41.501  1.00 108.83 ? 964  ILE A CD1   1 
ATOM   6479 N  N     . SER A 1 862 ? -24.203 8.914   45.818  1.00 113.92 ? 965  SER A N     1 
ATOM   6480 C  CA    . SER A 1 862 ? -24.552 10.165  46.475  1.00 117.02 ? 965  SER A CA    1 
ATOM   6481 C  C     . SER A 1 862 ? -25.311 9.958   47.780  1.00 119.90 ? 965  SER A C     1 
ATOM   6482 O  O     . SER A 1 862 ? -25.867 10.921  48.316  1.00 122.79 ? 965  SER A O     1 
ATOM   6483 C  CB    . SER A 1 862 ? -25.369 11.044  45.527  1.00 125.21 ? 965  SER A CB    1 
ATOM   6484 O  OG    . SER A 1 862 ? -25.641 12.305  46.110  1.00 129.33 ? 965  SER A OG    1 
ATOM   6485 N  N     . LYS A 1 863 ? -25.342 8.733   48.296  1.00 119.62 ? 966  LYS A N     1 
ATOM   6486 C  CA    . LYS A 1 863 ? -26.001 8.393   49.573  1.00 121.52 ? 966  LYS A CA    1 
ATOM   6487 C  C     . LYS A 1 863 ? -27.469 8.821   49.463  1.00 126.20 ? 966  LYS A C     1 
ATOM   6488 O  O     . LYS A 1 863 ? -28.070 8.701   48.384  1.00 131.72 ? 966  LYS A O     1 
ATOM   6489 C  CB    . LYS A 1 863 ? -25.236 9.013   50.726  1.00 120.87 ? 966  LYS A CB    1 
ATOM   6490 C  CG    . LYS A 1 863 ? -23.727 8.849   50.636  1.00 113.51 ? 966  LYS A CG    1 
ATOM   6491 C  CD    . LYS A 1 863 ? -23.026 9.580   51.769  1.00 111.62 ? 966  LYS A CD    1 
ATOM   6492 C  CE    . LYS A 1 863 ? -21.534 9.694   51.510  1.00 111.04 ? 966  LYS A CE    1 
ATOM   6493 N  NZ    . LYS A 1 863 ? -20.800 10.280  52.666  1.00 114.49 ? 966  LYS A NZ    1 
ATOM   6494 N  N     . GLY A 1 864 ? -28.077 9.312   50.539  1.00 122.97 ? 967  GLY A N     1 
ATOM   6495 C  CA    . GLY A 1 864 ? -29.402 9.888   50.436  1.00 137.92 ? 967  GLY A CA    1 
ATOM   6496 C  C     . GLY A 1 864 ? -29.377 11.120  49.556  1.00 137.51 ? 967  GLY A C     1 
ATOM   6497 O  O     . GLY A 1 864 ? -28.823 12.153  49.944  1.00 142.62 ? 967  GLY A O     1 
ATOM   6498 N  N     . ALA A 1 865 ? -29.961 11.025  48.364  1.00 132.35 ? 968  ALA A N     1 
ATOM   6499 C  CA    . ALA A 1 865 ? -29.865 12.093  47.382  1.00 137.05 ? 968  ALA A CA    1 
ATOM   6500 C  C     . ALA A 1 865 ? -31.220 12.347  46.743  1.00 144.97 ? 968  ALA A C     1 
ATOM   6501 O  O     . ALA A 1 865 ? -31.931 11.406  46.377  1.00 143.36 ? 968  ALA A O     1 
ATOM   6502 C  CB    . ALA A 1 865 ? -28.838 11.756  46.297  1.00 141.38 ? 968  ALA A CB    1 
ATOM   6503 N  N     . GLN A 1 866 ? -31.565 13.628  46.607  1.00 148.48 ? 969  GLN A N     1 
ATOM   6504 C  CA    . GLN A 1 866 ? -32.802 13.994  45.927  1.00 161.21 ? 969  GLN A CA    1 
ATOM   6505 C  C     . GLN A 1 866 ? -32.692 13.755  44.427  1.00 172.30 ? 969  GLN A C     1 
ATOM   6506 O  O     . GLN A 1 866 ? -33.582 13.153  43.816  1.00 179.28 ? 969  GLN A O     1 
ATOM   6507 C  CB    . GLN A 1 866 ? -33.144 15.457  46.215  1.00 167.36 ? 969  GLN A CB    1 
ATOM   6508 C  CG    . GLN A 1 866 ? -34.369 15.965  45.471  1.00 172.41 ? 969  GLN A CG    1 
ATOM   6509 C  CD    . GLN A 1 866 ? -34.610 17.447  45.686  1.00 173.23 ? 969  GLN A CD    1 
ATOM   6510 O  OE1   . GLN A 1 866 ? -33.862 18.113  46.401  1.00 174.50 ? 969  GLN A OE1   1 
ATOM   6511 N  NE2   . GLN A 1 866 ? -35.659 17.972  45.063  1.00 170.73 ? 969  GLN A NE2   1 
ATOM   6512 N  N     . GLU A 1 867 ? -31.599 14.218  43.815  1.00 187.05 ? 970  GLU A N     1 
ATOM   6513 C  CA    . GLU A 1 867 ? -31.404 14.092  42.376  1.00 188.39 ? 970  GLU A CA    1 
ATOM   6514 C  C     . GLU A 1 867 ? -30.067 13.458  42.013  1.00 186.73 ? 970  GLU A C     1 
ATOM   6515 O  O     . GLU A 1 867 ? -29.678 13.504  40.839  1.00 194.57 ? 970  GLU A O     1 
ATOM   6516 C  CB    . GLU A 1 867 ? -31.524 15.462  41.696  1.00 194.85 ? 970  GLU A CB    1 
ATOM   6517 C  CG    . GLU A 1 867 ? -32.869 16.145  41.889  1.00 195.55 ? 970  GLU A CG    1 
ATOM   6518 C  CD    . GLU A 1 867 ? -33.983 15.487  41.098  1.00 199.41 ? 970  GLU A CD    1 
ATOM   6519 O  OE1   . GLU A 1 867 ? -33.680 14.711  40.167  1.00 209.76 ? 970  GLU A OE1   1 
ATOM   6520 O  OE2   . GLU A 1 867 ? -35.165 15.747  41.406  1.00 203.21 ? 970  GLU A OE2   1 
ATOM   6521 N  N     . CYS A 1 868 ? -29.348 12.890  42.985  1.00 159.88 ? 971  CYS A N     1 
ATOM   6522 C  CA    . CYS A 1 868 ? -28.074 12.209  42.763  1.00 152.75 ? 971  CYS A CA    1 
ATOM   6523 C  C     . CYS A 1 868 ? -26.990 13.154  42.250  1.00 149.67 ? 971  CYS A C     1 
ATOM   6524 O  O     . CYS A 1 868 ? -25.893 13.206  42.815  1.00 139.96 ? 971  CYS A O     1 
ATOM   6525 C  CB    . CYS A 1 868 ? -28.250 11.033  41.797  1.00 146.27 ? 971  CYS A CB    1 
ATOM   6526 S  SG    . CYS A 1 868 ? -29.454 9.799   42.340  1.00 138.04 ? 971  CYS A SG    1 
ATOM   6527 N  N     . THR A 1 869 ? -27.277 13.897  41.184  1.00 157.09 ? 972  THR A N     1 
ATOM   6528 C  CA    . THR A 1 869 ? -26.318 14.838  40.622  1.00 149.71 ? 972  THR A CA    1 
ATOM   6529 C  C     . THR A 1 869 ? -26.240 16.083  41.507  1.00 147.00 ? 972  THR A C     1 
ATOM   6530 O  O     . THR A 1 869 ? -26.819 16.136  42.596  1.00 150.19 ? 972  THR A O     1 
ATOM   6531 C  CB    . THR A 1 869 ? -26.692 15.184  39.182  1.00 151.08 ? 972  THR A CB    1 
ATOM   6532 O  OG1   . THR A 1 869 ? -27.997 15.775  39.152  1.00 162.12 ? 972  THR A OG1   1 
ATOM   6533 C  CG2   . THR A 1 869 ? -26.685 13.933  38.315  1.00 136.02 ? 972  THR A CG2   1 
ATOM   6534 N  N     . LYS A 1 870 ? -25.529 17.104  41.022  1.00 144.08 ? 973  LYS A N     1 
ATOM   6535 C  CA    . LYS A 1 870 ? -25.236 18.347  41.751  1.00 141.08 ? 973  LYS A CA    1 
ATOM   6536 C  C     . LYS A 1 870 ? -24.963 18.086  43.233  1.00 137.71 ? 973  LYS A C     1 
ATOM   6537 O  O     . LYS A 1 870 ? -25.486 18.758  44.126  1.00 141.29 ? 973  LYS A O     1 
ATOM   6538 C  CB    . LYS A 1 870 ? -26.347 19.387  41.556  1.00 146.82 ? 973  LYS A CB    1 
ATOM   6539 C  CG    . LYS A 1 870 ? -27.746 18.991  42.008  1.00 153.44 ? 973  LYS A CG    1 
ATOM   6540 C  CD    . LYS A 1 870 ? -28.714 20.156  41.875  1.00 162.05 ? 973  LYS A CD    1 
ATOM   6541 C  CE    . LYS A 1 870 ? -30.100 19.784  42.373  1.00 168.70 ? 973  LYS A CE    1 
ATOM   6542 N  NZ    . LYS A 1 870 ? -30.680 18.657  41.594  1.00 173.79 ? 973  LYS A NZ    1 
ATOM   6543 N  N     . THR A 1 871 ? -24.113 17.094  43.487  1.00 131.83 ? 974  THR A N     1 
ATOM   6544 C  CA    . THR A 1 871 ? -23.718 16.710  44.834  1.00 127.10 ? 974  THR A CA    1 
ATOM   6545 C  C     . THR A 1 871 ? -22.207 16.542  44.876  1.00 123.68 ? 974  THR A C     1 
ATOM   6546 O  O     . THR A 1 871 ? -21.603 16.062  43.912  1.00 123.56 ? 974  THR A O     1 
ATOM   6547 C  CB    . THR A 1 871 ? -24.407 15.406  45.268  1.00 127.50 ? 974  THR A CB    1 
ATOM   6548 O  OG1   . THR A 1 871 ? -25.826 15.545  45.128  1.00 135.80 ? 974  THR A OG1   1 
ATOM   6549 C  CG2   . THR A 1 871 ? -24.080 15.078  46.719  1.00 126.04 ? 974  THR A CG2   1 
ATOM   6550 N  N     . ARG A 1 872 ? -21.598 16.949  45.995  1.00 122.10 ? 975  ARG A N     1 
ATOM   6551 C  CA    . ARG A 1 872 ? -20.153 16.809  46.144  1.00 122.03 ? 975  ARG A CA    1 
ATOM   6552 C  C     . ARG A 1 872 ? -19.716 15.354  46.042  1.00 117.63 ? 975  ARG A C     1 
ATOM   6553 O  O     . ARG A 1 872 ? -18.613 15.073  45.559  1.00 118.88 ? 975  ARG A O     1 
ATOM   6554 C  CB    . ARG A 1 872 ? -19.699 17.408  47.475  1.00 129.41 ? 975  ARG A CB    1 
ATOM   6555 C  CG    . ARG A 1 872 ? -19.887 18.913  47.579  1.00 136.46 ? 975  ARG A CG    1 
ATOM   6556 C  CD    . ARG A 1 872 ? -19.387 19.433  48.917  1.00 148.86 ? 975  ARG A CD    1 
ATOM   6557 N  NE    . ARG A 1 872 ? -19.582 20.871  49.058  1.00 154.93 ? 975  ARG A NE    1 
ATOM   6558 C  CZ    . ARG A 1 872 ? -19.267 21.565  50.143  1.00 152.92 ? 975  ARG A CZ    1 
ATOM   6559 N  NH1   . ARG A 1 872 ? -18.736 20.984  51.206  1.00 151.53 ? 975  ARG A NH1   1 
ATOM   6560 N  NH2   . ARG A 1 872 ? -19.491 22.876  50.162  1.00 145.61 ? 975  ARG A NH2   1 
ATOM   6561 N  N     . GLU A 1 873 ? -20.558 14.419  46.490  1.00 116.25 ? 976  GLU A N     1 
ATOM   6562 C  CA    . GLU A 1 873 ? -20.247 13.003  46.315  1.00 117.18 ? 976  GLU A CA    1 
ATOM   6563 C  C     . GLU A 1 873 ? -20.156 12.642  44.838  1.00 114.50 ? 976  GLU A C     1 
ATOM   6564 O  O     . GLU A 1 873 ? -19.276 11.874  44.431  1.00 108.60 ? 976  GLU A O     1 
ATOM   6565 C  CB    . GLU A 1 873 ? -21.299 12.140  47.013  1.00 115.65 ? 976  GLU A CB    1 
ATOM   6566 C  CG    . GLU A 1 873 ? -20.987 11.823  48.467  1.00 120.09 ? 976  GLU A CG    1 
ATOM   6567 C  CD    . GLU A 1 873 ? -21.000 13.050  49.356  1.00 120.53 ? 976  GLU A CD    1 
ATOM   6568 O  OE1   . GLU A 1 873 ? -21.725 14.015  49.033  1.00 120.88 ? 976  GLU A OE1   1 
ATOM   6569 O  OE2   . GLU A 1 873 ? -20.282 13.048  50.379  1.00 115.94 ? 976  GLU A OE2   1 
ATOM   6570 N  N     . PHE A 1 874 ? -21.056 13.187  44.020  1.00 114.03 ? 977  PHE A N     1 
ATOM   6571 C  CA    . PHE A 1 874 ? -21.006 12.931  42.586  1.00 109.37 ? 977  PHE A CA    1 
ATOM   6572 C  C     . PHE A 1 874 ? -19.898 13.734  41.915  1.00 110.88 ? 977  PHE A C     1 
ATOM   6573 O  O     . PHE A 1 874 ? -19.274 13.255  40.961  1.00 107.73 ? 977  PHE A O     1 
ATOM   6574 C  CB    . PHE A 1 874 ? -22.360 13.248  41.951  1.00 114.17 ? 977  PHE A CB    1 
ATOM   6575 C  CG    . PHE A 1 874 ? -22.446 12.891  40.495  1.00 112.98 ? 977  PHE A CG    1 
ATOM   6576 C  CD1   . PHE A 1 874 ? -22.545 11.568  40.098  1.00 106.21 ? 977  PHE A CD1   1 
ATOM   6577 C  CD2   . PHE A 1 874 ? -22.436 13.879  39.524  1.00 113.43 ? 977  PHE A CD2   1 
ATOM   6578 C  CE1   . PHE A 1 874 ? -22.627 11.236  38.760  1.00 106.07 ? 977  PHE A CE1   1 
ATOM   6579 C  CE2   . PHE A 1 874 ? -22.518 13.553  38.184  1.00 115.55 ? 977  PHE A CE2   1 
ATOM   6580 C  CZ    . PHE A 1 874 ? -22.613 12.229  37.801  1.00 111.48 ? 977  PHE A CZ    1 
ATOM   6581 N  N     . GLU A 1 875 ? -19.639 14.952  42.399  1.00 111.97 ? 978  GLU A N     1 
ATOM   6582 C  CA    . GLU A 1 875 ? -18.549 15.749  41.845  1.00 110.54 ? 978  GLU A CA    1 
ATOM   6583 C  C     . GLU A 1 875 ? -17.200 15.096  42.113  1.00 109.34 ? 978  GLU A C     1 
ATOM   6584 O  O     . GLU A 1 875 ? -16.311 15.114  41.253  1.00 108.36 ? 978  GLU A O     1 
ATOM   6585 C  CB    . GLU A 1 875 ? -18.584 17.167  42.416  1.00 116.74 ? 978  GLU A CB    1 
ATOM   6586 C  CG    . GLU A 1 875 ? -19.805 17.978  42.007  1.00 119.82 ? 978  GLU A CG    1 
ATOM   6587 C  CD    . GLU A 1 875 ? -19.733 19.422  42.472  1.00 124.09 ? 978  GLU A CD    1 
ATOM   6588 O  OE1   . GLU A 1 875 ? -18.637 19.865  42.876  1.00 129.75 ? 978  GLU A OE1   1 
ATOM   6589 O  OE2   . GLU A 1 875 ? -20.772 20.114  42.434  1.00 119.18 ? 978  GLU A OE2   1 
ATOM   6590 N  N     . ARG A 1 876 ? -17.025 14.514  43.302  1.00 111.74 ? 979  ARG A N     1 
ATOM   6591 C  CA    . ARG A 1 876 ? -15.810 13.757  43.575  1.00 109.43 ? 979  ARG A CA    1 
ATOM   6592 C  C     . ARG A 1 876 ? -15.767 12.447  42.801  1.00 103.24 ? 979  ARG A C     1 
ATOM   6593 O  O     . ARG A 1 876 ? -14.679 11.904  42.588  1.00 104.20 ? 979  ARG A O     1 
ATOM   6594 C  CB    . ARG A 1 876 ? -15.675 13.481  45.074  1.00 113.96 ? 979  ARG A CB    1 
ATOM   6595 C  CG    . ARG A 1 876 ? -14.750 14.447  45.802  1.00 120.23 ? 979  ARG A CG    1 
ATOM   6596 C  CD    . ARG A 1 876 ? -15.388 15.814  45.993  1.00 129.54 ? 979  ARG A CD    1 
ATOM   6597 N  NE    . ARG A 1 876 ? -16.440 15.785  47.002  1.00 149.23 ? 979  ARG A NE    1 
ATOM   6598 C  CZ    . ARG A 1 876 ? -16.235 15.941  48.303  1.00 147.65 ? 979  ARG A CZ    1 
ATOM   6599 N  NH1   . ARG A 1 876 ? -15.023 16.152  48.791  1.00 146.92 ? 979  ARG A NH1   1 
ATOM   6600 N  NH2   . ARG A 1 876 ? -17.270 15.882  49.135  1.00 138.50 ? 979  ARG A NH2   1 
ATOM   6601 N  N     . PHE A 1 877 ? -16.920 11.923  42.382  1.00 102.53 ? 980  PHE A N     1 
ATOM   6602 C  CA    . PHE A 1 877 ? -16.919 10.749  41.517  1.00 99.98  ? 980  PHE A CA    1 
ATOM   6603 C  C     . PHE A 1 877 ? -16.522 11.119  40.095  1.00 103.57 ? 980  PHE A C     1 
ATOM   6604 O  O     . PHE A 1 877 ? -15.862 10.334  39.405  1.00 97.85  ? 980  PHE A O     1 
ATOM   6605 C  CB    . PHE A 1 877 ? -18.293 10.078  41.538  1.00 101.02 ? 980  PHE A CB    1 
ATOM   6606 C  CG    . PHE A 1 877 ? -18.431 8.946   40.561  1.00 98.30  ? 980  PHE A CG    1 
ATOM   6607 C  CD1   . PHE A 1 877 ? -17.935 7.689   40.862  1.00 99.06  ? 980  PHE A CD1   1 
ATOM   6608 C  CD2   . PHE A 1 877 ? -19.062 9.140   39.343  1.00 99.92  ? 980  PHE A CD2   1 
ATOM   6609 C  CE1   . PHE A 1 877 ? -18.062 6.644   39.964  1.00 101.44 ? 980  PHE A CE1   1 
ATOM   6610 C  CE2   . PHE A 1 877 ? -19.192 8.101   38.441  1.00 101.09 ? 980  PHE A CE2   1 
ATOM   6611 C  CZ    . PHE A 1 877 ? -18.692 6.851   38.752  1.00 103.08 ? 980  PHE A CZ    1 
ATOM   6612 N  N     . GLN A 1 878 ? -16.916 12.311  39.643  1.00 103.08 ? 981  GLN A N     1 
ATOM   6613 C  CA    . GLN A 1 878 ? -16.496 12.776  38.327  1.00 99.57  ? 981  GLN A CA    1 
ATOM   6614 C  C     . GLN A 1 878 ? -14.993 13.023  38.285  1.00 98.95  ? 981  GLN A C     1 
ATOM   6615 O  O     . GLN A 1 878 ? -14.343 12.758  37.267  1.00 104.52 ? 981  GLN A O     1 
ATOM   6616 C  CB    . GLN A 1 878 ? -17.265 14.042  37.952  1.00 101.39 ? 981  GLN A CB    1 
ATOM   6617 C  CG    . GLN A 1 878 ? -18.747 13.818  37.696  1.00 105.77 ? 981  GLN A CG    1 
ATOM   6618 C  CD    . GLN A 1 878 ? -19.473 15.098  37.328  1.00 112.46 ? 981  GLN A CD    1 
ATOM   6619 O  OE1   . GLN A 1 878 ? -19.260 16.144  37.942  1.00 112.12 ? 981  GLN A OE1   1 
ATOM   6620 N  NE2   . GLN A 1 878 ? -20.327 15.025  36.313  1.00 117.86 ? 981  GLN A NE2   1 
ATOM   6621 N  N     . GLU A 1 879 ? -14.421 13.524  39.384  1.00 98.33  ? 982  GLU A N     1 
ATOM   6622 C  CA    . GLU A 1 879 ? -12.979 13.745  39.429  1.00 100.36 ? 982  GLU A CA    1 
ATOM   6623 C  C     . GLU A 1 879 ? -12.214 12.429  39.377  1.00 97.75  ? 982  GLU A C     1 
ATOM   6624 O  O     . GLU A 1 879 ? -11.143 12.353  38.765  1.00 99.88  ? 982  GLU A O     1 
ATOM   6625 C  CB    . GLU A 1 879 ? -12.602 14.531  40.685  1.00 104.80 ? 982  GLU A CB    1 
ATOM   6626 C  CG    . GLU A 1 879 ? -12.931 16.013  40.624  1.00 109.74 ? 982  GLU A CG    1 
ATOM   6627 C  CD    . GLU A 1 879 ? -12.473 16.759  41.864  1.00 122.91 ? 982  GLU A CD    1 
ATOM   6628 O  OE1   . GLU A 1 879 ? -11.980 16.103  42.806  1.00 121.19 ? 982  GLU A OE1   1 
ATOM   6629 O  OE2   . GLU A 1 879 ? -12.602 18.001  41.896  1.00 130.15 ? 982  GLU A OE2   1 
ATOM   6630 N  N     . MET A 1 880 ? -12.745 11.382  40.014  1.00 94.34  ? 983  MET A N     1 
ATOM   6631 C  CA    . MET A 1 880 ? -12.075 10.087  39.978  1.00 97.21  ? 983  MET A CA    1 
ATOM   6632 C  C     . MET A 1 880 ? -12.039 9.513   38.569  1.00 98.09  ? 983  MET A C     1 
ATOM   6633 O  O     . MET A 1 880 ? -11.074 8.831   38.202  1.00 95.73  ? 983  MET A O     1 
ATOM   6634 C  CB    . MET A 1 880 ? -12.761 9.108   40.932  1.00 96.33  ? 983  MET A CB    1 
ATOM   6635 C  CG    . MET A 1 880 ? -12.564 9.430   42.402  1.00 88.53  ? 983  MET A CG    1 
ATOM   6636 S  SD    . MET A 1 880 ? -13.168 8.118   43.483  1.00 100.93 ? 983  MET A SD    1 
ATOM   6637 C  CE    . MET A 1 880 ? -14.920 8.146   43.120  1.00 101.28 ? 983  MET A CE    1 
ATOM   6638 N  N     . CYS A 1 881 ? -13.072 9.777   37.766  1.00 105.32 ? 984  CYS A N     1 
ATOM   6639 C  CA    . CYS A 1 881 ? -13.088 9.281   36.395  1.00 102.30 ? 984  CYS A CA    1 
ATOM   6640 C  C     . CYS A 1 881 ? -12.146 10.076  35.500  1.00 96.67  ? 984  CYS A C     1 
ATOM   6641 O  O     . CYS A 1 881 ? -11.427 9.494   34.680  1.00 93.24  ? 984  CYS A O     1 
ATOM   6642 C  CB    . CYS A 1 881 ? -14.512 9.320   35.839  1.00 97.16  ? 984  CYS A CB    1 
ATOM   6643 S  SG    . CYS A 1 881 ? -15.672 8.230   36.695  1.00 101.72 ? 984  CYS A SG    1 
ATOM   6644 N  N     . TYR A 1 882 ? -12.133 11.404  35.645  1.00 97.32  ? 985  TYR A N     1 
ATOM   6645 C  CA    . TYR A 1 882 ? -11.259 12.232  34.818  1.00 93.04  ? 985  TYR A CA    1 
ATOM   6646 C  C     . TYR A 1 882 ? -9.793  11.905  35.067  1.00 91.35  ? 985  TYR A C     1 
ATOM   6647 O  O     . TYR A 1 882 ? -9.007  11.781  34.121  1.00 91.98  ? 985  TYR A O     1 
ATOM   6648 C  CB    . TYR A 1 882 ? -11.521 13.715  35.087  1.00 102.17 ? 985  TYR A CB    1 
ATOM   6649 C  CG    . TYR A 1 882 ? -12.949 14.164  34.855  1.00 103.03 ? 985  TYR A CG    1 
ATOM   6650 C  CD1   . TYR A 1 882 ? -13.792 13.468  33.997  1.00 101.28 ? 985  TYR A CD1   1 
ATOM   6651 C  CD2   . TYR A 1 882 ? -13.452 15.289  35.495  1.00 106.30 ? 985  TYR A CD2   1 
ATOM   6652 C  CE1   . TYR A 1 882 ? -15.095 13.880  33.788  1.00 104.68 ? 985  TYR A CE1   1 
ATOM   6653 C  CE2   . TYR A 1 882 ? -14.752 15.708  35.292  1.00 106.64 ? 985  TYR A CE2   1 
ATOM   6654 C  CZ    . TYR A 1 882 ? -15.569 15.000  34.438  1.00 105.22 ? 985  TYR A CZ    1 
ATOM   6655 O  OH    . TYR A 1 882 ? -16.865 15.417  34.234  1.00 106.17 ? 985  TYR A OH    1 
ATOM   6656 N  N     . LYS A 1 883 ? -9.405  11.762  36.337  1.00 95.87  ? 986  LYS A N     1 
ATOM   6657 C  CA    . LYS A 1 883 ? -8.013  11.465  36.656  1.00 91.69  ? 986  LYS A CA    1 
ATOM   6658 C  C     . LYS A 1 883 ? -7.627  10.064  36.199  1.00 88.24  ? 986  LYS A C     1 
ATOM   6659 O  O     . LYS A 1 883 ? -6.491  9.838   35.766  1.00 86.50  ? 986  LYS A O     1 
ATOM   6660 C  CB    . LYS A 1 883 ? -7.775  11.628  38.157  1.00 93.76  ? 986  LYS A CB    1 
ATOM   6661 C  CG    . LYS A 1 883 ? -7.979  13.046  38.664  1.00 101.32 ? 986  LYS A CG    1 
ATOM   6662 C  CD    . LYS A 1 883 ? -7.869  13.114  40.178  1.00 103.33 ? 986  LYS A CD    1 
ATOM   6663 C  CE    . LYS A 1 883 ? -8.153  14.516  40.690  1.00 107.40 ? 986  LYS A CE    1 
ATOM   6664 N  NZ    . LYS A 1 883 ? -8.183  14.564  42.178  1.00 124.61 ? 986  LYS A NZ    1 
ATOM   6665 N  N     . ALA A 1 884 ? -8.556  9.110   36.289  1.00 86.40  ? 987  ALA A N     1 
ATOM   6666 C  CA    . ALA A 1 884 ? -8.266  7.755   35.830  1.00 85.10  ? 987  ALA A CA    1 
ATOM   6667 C  C     . ALA A 1 884 ? -8.209  7.689   34.311  1.00 87.19  ? 987  ALA A C     1 
ATOM   6668 O  O     . ALA A 1 884 ? -7.390  6.954   33.746  1.00 83.94  ? 987  ALA A O     1 
ATOM   6669 C  CB    . ALA A 1 884 ? -9.315  6.783   36.367  1.00 86.33  ? 987  ALA A CB    1 
ATOM   6670 N  N     . TYR A 1 885 ? -9.073  8.449   33.635  1.00 88.14  ? 988  TYR A N     1 
ATOM   6671 C  CA    . TYR A 1 885 ? -9.097  8.440   32.177  1.00 85.88  ? 988  TYR A CA    1 
ATOM   6672 C  C     . TYR A 1 885 ? -7.790  8.974   31.606  1.00 86.18  ? 988  TYR A C     1 
ATOM   6673 O  O     . TYR A 1 885 ? -7.163  8.334   30.754  1.00 86.02  ? 988  TYR A O     1 
ATOM   6674 C  CB    . TYR A 1 885 ? -10.288 9.257   31.674  1.00 87.27  ? 988  TYR A CB    1 
ATOM   6675 C  CG    . TYR A 1 885 ? -10.370 9.387   30.172  1.00 90.88  ? 988  TYR A CG    1 
ATOM   6676 C  CD1   . TYR A 1 885 ? -10.853 8.345   29.390  1.00 93.05  ? 988  TYR A CD1   1 
ATOM   6677 C  CD2   . TYR A 1 885 ? -9.976  10.557  29.534  1.00 97.57  ? 988  TYR A CD2   1 
ATOM   6678 C  CE1   . TYR A 1 885 ? -10.934 8.462   28.015  1.00 92.44  ? 988  TYR A CE1   1 
ATOM   6679 C  CE2   . TYR A 1 885 ? -10.054 10.684  28.160  1.00 91.25  ? 988  TYR A CE2   1 
ATOM   6680 C  CZ    . TYR A 1 885 ? -10.533 9.634   27.406  1.00 93.32  ? 988  TYR A CZ    1 
ATOM   6681 O  OH    . TYR A 1 885 ? -10.612 9.756   26.038  1.00 99.63  ? 988  TYR A OH    1 
ATOM   6682 N  N     . LEU A 1 886 ? -7.357  10.148  32.073  1.00 83.76  ? 989  LEU A N     1 
ATOM   6683 C  CA    . LEU A 1 886 ? -6.109  10.725  31.587  1.00 84.13  ? 989  LEU A CA    1 
ATOM   6684 C  C     . LEU A 1 886 ? -4.889  9.936   32.045  1.00 84.23  ? 989  LEU A C     1 
ATOM   6685 O  O     . LEU A 1 886 ? -3.822  10.065  31.436  1.00 85.24  ? 989  LEU A O     1 
ATOM   6686 C  CB    . LEU A 1 886 ? -5.994  12.182  32.036  1.00 91.06  ? 989  LEU A CB    1 
ATOM   6687 C  CG    . LEU A 1 886 ? -7.050  13.124  31.453  1.00 95.00  ? 989  LEU A CG    1 
ATOM   6688 C  CD1   . LEU A 1 886 ? -6.797  14.559  31.885  1.00 103.08 ? 989  LEU A CD1   1 
ATOM   6689 C  CD2   . LEU A 1 886 ? -7.087  13.016  29.935  1.00 94.66  ? 989  LEU A CD2   1 
ATOM   6690 N  N     . ALA A 1 887 ? -5.020  9.126   33.098  1.00 85.26  ? 990  ALA A N     1 
ATOM   6691 C  CA    . ALA A 1 887 ? -3.911  8.272   33.511  1.00 85.31  ? 990  ALA A CA    1 
ATOM   6692 C  C     . ALA A 1 887 ? -3.692  7.139   32.518  1.00 85.18  ? 990  ALA A C     1 
ATOM   6693 O  O     . ALA A 1 887 ? -2.549  6.832   32.159  1.00 85.98  ? 990  ALA A O     1 
ATOM   6694 C  CB    . ALA A 1 887 ? -4.167  7.717   34.912  1.00 88.73  ? 990  ALA A CB    1 
ATOM   6695 N  N     . ILE A 1 888 ? -4.776  6.507   32.062  1.00 86.01  ? 991  ILE A N     1 
ATOM   6696 C  CA    . ILE A 1 888 ? -4.662  5.450   31.063  1.00 84.20  ? 991  ILE A CA    1 
ATOM   6697 C  C     . ILE A 1 888 ? -4.280  6.031   29.708  1.00 82.94  ? 991  ILE A C     1 
ATOM   6698 O  O     . ILE A 1 888 ? -3.535  5.407   28.942  1.00 83.54  ? 991  ILE A O     1 
ATOM   6699 C  CB    . ILE A 1 888 ? -5.975  4.651   30.989  1.00 84.08  ? 991  ILE A CB    1 
ATOM   6700 C  CG1   . ILE A 1 888 ? -6.318  4.071   32.361  1.00 77.88  ? 991  ILE A CG1   1 
ATOM   6701 C  CG2   . ILE A 1 888 ? -5.876  3.544   29.951  1.00 84.01  ? 991  ILE A CG2   1 
ATOM   6702 C  CD1   . ILE A 1 888 ? -5.283  3.100   32.881  1.00 80.46  ? 991  ILE A CD1   1 
ATOM   6703 N  N     . ARG A 1 889 ? -4.774  7.230   29.391  1.00 84.04  ? 992  ARG A N     1 
ATOM   6704 C  CA    . ARG A 1 889 ? -4.411  7.876   28.134  1.00 81.26  ? 992  ARG A CA    1 
ATOM   6705 C  C     . ARG A 1 889 ? -2.913  8.150   28.058  1.00 85.50  ? 992  ARG A C     1 
ATOM   6706 O  O     . ARG A 1 889 ? -2.321  8.066   26.976  1.00 95.84  ? 992  ARG A O     1 
ATOM   6707 C  CB    . ARG A 1 889 ? -5.202  9.174   27.972  1.00 76.70  ? 992  ARG A CB    1 
ATOM   6708 C  CG    . ARG A 1 889 ? -4.890  9.948   26.706  1.00 89.43  ? 992  ARG A CG    1 
ATOM   6709 C  CD    . ARG A 1 889 ? -5.789  11.161  26.575  1.00 91.16  ? 992  ARG A CD    1 
ATOM   6710 N  NE    . ARG A 1 889 ? -5.511  11.912  25.358  1.00 92.34  ? 992  ARG A NE    1 
ATOM   6711 C  CZ    . ARG A 1 889 ? -4.701  12.960  25.295  1.00 100.81 ? 992  ARG A CZ    1 
ATOM   6712 N  NH1   . ARG A 1 889 ? -4.069  13.410  26.367  1.00 98.30  ? 992  ARG A NH1   1 
ATOM   6713 N  NH2   . ARG A 1 889 ? -4.522  13.573  24.129  1.00 101.71 ? 992  ARG A NH2   1 
ATOM   6714 N  N     . GLN A 1 890 ? -2.282  8.466   29.191  1.00 85.82  ? 993  GLN A N     1 
ATOM   6715 C  CA    . GLN A 1 890 ? -0.844  8.711   29.207  1.00 88.11  ? 993  GLN A CA    1 
ATOM   6716 C  C     . GLN A 1 890 ? -0.039  7.441   28.962  1.00 80.43  ? 993  GLN A C     1 
ATOM   6717 O  O     . GLN A 1 890 ? 1.153   7.526   28.651  1.00 82.92  ? 993  GLN A O     1 
ATOM   6718 C  CB    . GLN A 1 890 ? -0.439  9.345   30.540  1.00 95.56  ? 993  GLN A CB    1 
ATOM   6719 C  CG    . GLN A 1 890 ? 0.957   9.950   30.554  1.00 110.03 ? 993  GLN A CG    1 
ATOM   6720 C  CD    . GLN A 1 890 ? 1.478   10.177  31.959  1.00 120.68 ? 993  GLN A CD    1 
ATOM   6721 O  OE1   . GLN A 1 890 ? 0.736   10.057  32.935  1.00 126.31 ? 993  GLN A OE1   1 
ATOM   6722 N  NE2   . GLN A 1 890 ? 2.762   10.498  32.070  1.00 114.84 ? 993  GLN A NE2   1 
ATOM   6723 N  N     . HIS A 1 891 ? -0.659  6.269   29.096  1.00 79.69  ? 994  HIS A N     1 
ATOM   6724 C  CA    . HIS A 1 891 ? -0.007  4.993   28.833  1.00 82.62  ? 994  HIS A CA    1 
ATOM   6725 C  C     . HIS A 1 891 ? -0.625  4.284   27.632  1.00 83.60  ? 994  HIS A C     1 
ATOM   6726 O  O     . HIS A 1 891 ? -0.673  3.052   27.587  1.00 84.85  ? 994  HIS A O     1 
ATOM   6727 C  CB    . HIS A 1 891 ? -0.068  4.093   30.067  1.00 95.66  ? 994  HIS A CB    1 
ATOM   6728 C  CG    . HIS A 1 891 ? 0.623   4.662   31.266  1.00 92.23  ? 994  HIS A CG    1 
ATOM   6729 N  ND1   . HIS A 1 891 ? 0.082   5.677   32.026  1.00 94.18  ? 994  HIS A ND1   1 
ATOM   6730 C  CD2   . HIS A 1 891 ? 1.815   4.361   31.835  1.00 92.44  ? 994  HIS A CD2   1 
ATOM   6731 C  CE1   . HIS A 1 891 ? 0.910   5.975   33.011  1.00 92.49  ? 994  HIS A CE1   1 
ATOM   6732 N  NE2   . HIS A 1 891 ? 1.968   5.191   32.918  1.00 87.55  ? 994  HIS A NE2   1 
ATOM   6733 N  N     . ALA A 1 892 ? -1.102  5.055   26.652  1.00 85.53  ? 995  ALA A N     1 
ATOM   6734 C  CA    . ALA A 1 892 ? -1.805  4.467   25.516  1.00 79.72  ? 995  ALA A CA    1 
ATOM   6735 C  C     . ALA A 1 892 ? -0.903  3.530   24.723  1.00 79.07  ? 995  ALA A C     1 
ATOM   6736 O  O     . ALA A 1 892 ? -1.352  2.478   24.254  1.00 80.31  ? 995  ALA A O     1 
ATOM   6737 C  CB    . ALA A 1 892 ? -2.355  5.569   24.614  1.00 79.41  ? 995  ALA A CB    1 
ATOM   6738 N  N     . ASN A 1 893 ? 0.374   3.894   24.565  1.00 79.38  ? 996  ASN A N     1 
ATOM   6739 C  CA    . ASN A 1 893 ? 1.292   3.070   23.784  1.00 78.58  ? 996  ASN A CA    1 
ATOM   6740 C  C     . ASN A 1 893 ? 1.415   1.663   24.353  1.00 83.31  ? 996  ASN A C     1 
ATOM   6741 O  O     . ASN A 1 893 ? 1.582   0.701   23.593  1.00 81.08  ? 996  ASN A O     1 
ATOM   6742 C  CB    . ASN A 1 893 ? 2.668   3.734   23.719  1.00 76.27  ? 996  ASN A CB    1 
ATOM   6743 C  CG    . ASN A 1 893 ? 2.639   5.067   22.996  1.00 88.49  ? 996  ASN A CG    1 
ATOM   6744 O  OD1   . ASN A 1 893 ? 1.572   5.609   22.710  1.00 88.44  ? 996  ASN A OD1   1 
ATOM   6745 N  ND2   . ASN A 1 893 ? 3.817   5.604   22.702  1.00 93.19  ? 996  ASN A ND2   1 
ATOM   6746 N  N     . LEU A 1 894 ? 1.327   1.521   25.678  1.00 85.32  ? 997  LEU A N     1 
ATOM   6747 C  CA    . LEU A 1 894 ? 1.459   0.206   26.299  1.00 76.97  ? 997  LEU A CA    1 
ATOM   6748 C  C     . LEU A 1 894 ? 0.313   -0.714  25.896  1.00 83.16  ? 997  LEU A C     1 
ATOM   6749 O  O     . LEU A 1 894 ? 0.542   -1.835  25.425  1.00 76.84  ? 997  LEU A O     1 
ATOM   6750 C  CB    . LEU A 1 894 ? 1.524   0.351   27.820  1.00 84.62  ? 997  LEU A CB    1 
ATOM   6751 C  CG    . LEU A 1 894 ? 1.381   -0.929  28.649  1.00 78.91  ? 997  LEU A CG    1 
ATOM   6752 C  CD1   . LEU A 1 894 ? 2.479   -1.929  28.316  1.00 87.35  ? 997  LEU A CD1   1 
ATOM   6753 C  CD2   . LEU A 1 894 ? 1.384   -0.603  30.132  1.00 88.79  ? 997  LEU A CD2   1 
ATOM   6754 N  N     . PHE A 1 895 ? -0.930  -0.259  26.074  1.00 75.67  ? 998  PHE A N     1 
ATOM   6755 C  CA    . PHE A 1 895 ? -2.075  -1.105  25.753  1.00 78.95  ? 998  PHE A CA    1 
ATOM   6756 C  C     . PHE A 1 895 ? -2.156  -1.386  24.258  1.00 84.13  ? 998  PHE A C     1 
ATOM   6757 O  O     . PHE A 1 895 ? -2.514  -2.498  23.851  1.00 82.23  ? 998  PHE A O     1 
ATOM   6758 C  CB    . PHE A 1 895 ? -3.364  -0.457  26.254  1.00 76.51  ? 998  PHE A CB    1 
ATOM   6759 C  CG    . PHE A 1 895 ? -3.397  -0.255  27.740  1.00 82.81  ? 998  PHE A CG    1 
ATOM   6760 C  CD1   . PHE A 1 895 ? -3.684  -1.311  28.589  1.00 80.23  ? 998  PHE A CD1   1 
ATOM   6761 C  CD2   . PHE A 1 895 ? -3.136  0.990   28.288  1.00 82.06  ? 998  PHE A CD2   1 
ATOM   6762 C  CE1   . PHE A 1 895 ? -3.712  -1.129  29.957  1.00 80.87  ? 998  PHE A CE1   1 
ATOM   6763 C  CE2   . PHE A 1 895 ? -3.162  1.178   29.655  1.00 80.82  ? 998  PHE A CE2   1 
ATOM   6764 C  CZ    . PHE A 1 895 ? -3.450  0.117   30.491  1.00 89.57  ? 998  PHE A CZ    1 
ATOM   6765 N  N     . ILE A 1 896 ? -1.830  -0.393  23.427  1.00 80.76  ? 999  ILE A N     1 
ATOM   6766 C  CA    . ILE A 1 896 ? -1.780  -0.621  21.985  1.00 82.50  ? 999  ILE A CA    1 
ATOM   6767 C  C     . ILE A 1 896 ? -0.749  -1.693  21.656  1.00 87.30  ? 999  ILE A C     1 
ATOM   6768 O  O     . ILE A 1 896 ? -1.004  -2.597  20.850  1.00 83.51  ? 999  ILE A O     1 
ATOM   6769 C  CB    . ILE A 1 896 ? -1.488  0.696   21.242  1.00 85.77  ? 999  ILE A CB    1 
ATOM   6770 C  CG1   . ILE A 1 896 ? -2.629  1.694   21.447  1.00 77.93  ? 999  ILE A CG1   1 
ATOM   6771 C  CG2   . ILE A 1 896 ? -1.278  0.436   19.763  1.00 84.32  ? 999  ILE A CG2   1 
ATOM   6772 N  N     . ASN A 1 897 ? 0.429   -1.619  22.285  1.00 82.77  ? 1000 ASN A N     1 
ATOM   6773 C  CA    . ASN A 1 897 ? 1.438   -2.652  22.080  1.00 81.13  ? 1000 ASN A CA    1 
ATOM   6774 C  C     . ASN A 1 897 ? 0.993   -3.995  22.645  1.00 83.15  ? 1000 ASN A C     1 
ATOM   6775 O  O     . ASN A 1 897 ? 1.372   -5.044  22.113  1.00 84.82  ? 1000 ASN A O     1 
ATOM   6776 C  CB    . ASN A 1 897 ? 2.767   -2.230  22.707  1.00 81.64  ? 1000 ASN A CB    1 
ATOM   6777 C  CG    . ASN A 1 897 ? 3.493   -1.186  21.883  1.00 98.86  ? 1000 ASN A CG    1 
ATOM   6778 O  OD1   . ASN A 1 897 ? 3.273   -1.067  20.678  1.00 106.33 ? 1000 ASN A OD1   1 
ATOM   6779 N  ND2   . ASN A 1 897 ? 4.371   -0.427  22.529  1.00 102.34 ? 1000 ASN A ND2   1 
ATOM   6780 N  N     . LEU A 1 898 ? 0.197   -3.989  23.716  1.00 80.78  ? 1001 LEU A N     1 
ATOM   6781 C  CA    . LEU A 1 898 ? -0.315  -5.249  24.243  1.00 81.07  ? 1001 LEU A CA    1 
ATOM   6782 C  C     . LEU A 1 898 ? -1.372  -5.849  23.327  1.00 82.13  ? 1001 LEU A C     1 
ATOM   6783 O  O     . LEU A 1 898 ? -1.490  -7.076  23.242  1.00 85.94  ? 1001 LEU A O     1 
ATOM   6784 C  CB    . LEU A 1 898 ? -0.875  -5.045  25.649  1.00 86.84  ? 1001 LEU A CB    1 
ATOM   6785 C  CG    . LEU A 1 898 ? 0.168   -4.761  26.731  1.00 88.60  ? 1001 LEU A CG    1 
ATOM   6786 C  CD1   . LEU A 1 898 ? -0.496  -4.509  28.077  1.00 77.38  ? 1001 LEU A CD1   1 
ATOM   6787 C  CD2   . LEU A 1 898 ? 1.169   -5.904  26.823  1.00 80.47  ? 1001 LEU A CD2   1 
ATOM   6788 N  N     . PHE A 1 899 ? -2.145  -5.009  22.637  1.00 86.45  ? 1002 PHE A N     1 
ATOM   6789 C  CA    . PHE A 1 899 ? -3.104  -5.524  21.665  1.00 92.39  ? 1002 PHE A CA    1 
ATOM   6790 C  C     . PHE A 1 899 ? -2.405  -5.972  20.386  1.00 84.70  ? 1002 PHE A C     1 
ATOM   6791 O  O     . PHE A 1 899 ? -2.818  -6.957  19.761  1.00 82.58  ? 1002 PHE A O     1 
ATOM   6792 C  CB    . PHE A 1 899 ? -4.159  -4.465  21.348  1.00 87.56  ? 1002 PHE A CB    1 
ATOM   6793 C  CG    . PHE A 1 899 ? -5.261  -4.377  22.366  1.00 88.38  ? 1002 PHE A CG    1 
ATOM   6794 C  CD1   . PHE A 1 899 ? -6.127  -5.440  22.560  1.00 91.22  ? 1002 PHE A CD1   1 
ATOM   6795 C  CD2   . PHE A 1 899 ? -5.446  -3.223  23.109  1.00 91.87  ? 1002 PHE A CD2   1 
ATOM   6796 C  CE1   . PHE A 1 899 ? -7.149  -5.360  23.489  1.00 88.08  ? 1002 PHE A CE1   1 
ATOM   6797 C  CE2   . PHE A 1 899 ? -6.465  -3.136  24.038  1.00 84.22  ? 1002 PHE A CE2   1 
ATOM   6798 C  CZ    . PHE A 1 899 ? -7.319  -4.205  24.225  1.00 86.95  ? 1002 PHE A CZ    1 
ATOM   6799 N  N     . SER A 1 900 ? -1.347  -5.262  19.983  1.00 79.05  ? 1003 SER A N     1 
ATOM   6800 C  CA    . SER A 1 900 ? -0.647  -5.599  18.747  1.00 87.54  ? 1003 SER A CA    1 
ATOM   6801 C  C     . SER A 1 900 ? -0.063  -7.004  18.805  1.00 90.62  ? 1003 SER A C     1 
ATOM   6802 O  O     . SER A 1 900 ? -0.075  -7.732  17.806  1.00 99.95  ? 1003 SER A O     1 
ATOM   6803 C  CB    . SER A 1 900 ? 0.453   -4.574  18.471  1.00 83.93  ? 1003 SER A CB    1 
ATOM   6804 O  OG    . SER A 1 900 ? -0.094  -3.294  18.208  1.00 87.78  ? 1003 SER A OG    1 
ATOM   6805 N  N     . MET A 1 901 ? 0.444   -7.405  19.970  1.00 82.04  ? 1004 MET A N     1 
ATOM   6806 C  CA    . MET A 1 901 ? 1.042   -8.724  20.125  1.00 80.99  ? 1004 MET A CA    1 
ATOM   6807 C  C     . MET A 1 901 ? 0.008   -9.843  20.144  1.00 79.99  ? 1004 MET A C     1 
ATOM   6808 O  O     . MET A 1 901 ? 0.393   -11.016 20.134  1.00 79.89  ? 1004 MET A O     1 
ATOM   6809 C  CB    . MET A 1 901 ? 1.883   -8.754  21.403  1.00 85.81  ? 1004 MET A CB    1 
ATOM   6810 C  CG    . MET A 1 901 ? 2.995   -7.714  21.414  1.00 87.82  ? 1004 MET A CG    1 
ATOM   6811 S  SD    . MET A 1 901 ? 3.799   -7.494  23.014  1.00 99.72  ? 1004 MET A SD    1 
ATOM   6812 C  CE    . MET A 1 901 ? 4.705   -9.030  23.165  1.00 91.73  ? 1004 MET A CE    1 
ATOM   6813 N  N     . MET A 1 902 ? -1.283  -9.513  20.155  1.00 81.36  ? 1005 MET A N     1 
ATOM   6814 C  CA    . MET A 1 902 ? -2.350  -10.503 20.208  1.00 89.45  ? 1005 MET A CA    1 
ATOM   6815 C  C     . MET A 1 902 ? -3.007  -10.748 18.856  1.00 98.40  ? 1005 MET A C     1 
ATOM   6816 O  O     . MET A 1 902 ? -3.941  -11.551 18.775  1.00 98.82  ? 1005 MET A O     1 
ATOM   6817 C  CB    . MET A 1 902 ? -3.415  -10.072 21.222  1.00 89.82  ? 1005 MET A CB    1 
ATOM   6818 C  CG    . MET A 1 902 ? -2.900  -9.919  22.642  1.00 84.60  ? 1005 MET A CG    1 
ATOM   6819 S  SD    . MET A 1 902 ? -2.272  -11.466 23.320  1.00 90.07  ? 1005 MET A SD    1 
ATOM   6820 C  CE    . MET A 1 902 ? -3.749  -12.478 23.277  1.00 86.02  ? 1005 MET A CE    1 
ATOM   6821 N  N     . LEU A 1 903 ? -2.544  -10.080 17.797  1.00 103.15 ? 1006 LEU A N     1 
ATOM   6822 C  CA    . LEU A 1 903 ? -3.181  -10.229 16.492  1.00 107.76 ? 1006 LEU A CA    1 
ATOM   6823 C  C     . LEU A 1 903 ? -2.998  -11.631 15.928  1.00 117.81 ? 1006 LEU A C     1 
ATOM   6824 O  O     . LEU A 1 903 ? -3.889  -12.139 15.237  1.00 115.34 ? 1006 LEU A O     1 
ATOM   6825 C  CB    . LEU A 1 903 ? -2.631  -9.187  15.520  1.00 104.39 ? 1006 LEU A CB    1 
ATOM   6826 C  CG    . LEU A 1 903 ? -2.977  -7.741  15.870  1.00 101.11 ? 1006 LEU A CG    1 
ATOM   6827 C  CD1   . LEU A 1 903 ? -2.270  -6.779  14.938  1.00 111.71 ? 1006 LEU A CD1   1 
ATOM   6828 C  CD2   . LEU A 1 903 ? -4.481  -7.534  15.816  1.00 105.04 ? 1006 LEU A CD2   1 
ATOM   6829 N  N     . GLY A 1 904 ? -1.865  -12.272 16.210  1.00 148.41 ? 1007 GLY A N     1 
ATOM   6830 C  CA    . GLY A 1 904 ? -1.636  -13.628 15.744  1.00 149.64 ? 1007 GLY A CA    1 
ATOM   6831 C  C     . GLY A 1 904 ? -2.509  -14.677 16.401  1.00 146.68 ? 1007 GLY A C     1 
ATOM   6832 O  O     . GLY A 1 904 ? -2.476  -15.837 15.973  1.00 152.52 ? 1007 GLY A O     1 
ATOM   6833 N  N     . SER A 1 905 ? -3.280  -14.304 17.419  1.00 118.68 ? 1008 SER A N     1 
ATOM   6834 C  CA    . SER A 1 905 ? -4.165  -15.237 18.092  1.00 114.53 ? 1008 SER A CA    1 
ATOM   6835 C  C     . SER A 1 905 ? -5.474  -15.378 17.323  1.00 119.34 ? 1008 SER A C     1 
ATOM   6836 O  O     . SER A 1 905 ? -5.788  -14.596 16.422  1.00 123.28 ? 1008 SER A O     1 
ATOM   6837 C  CB    . SER A 1 905 ? -4.450  -14.775 19.520  1.00 110.87 ? 1008 SER A CB    1 
ATOM   6838 O  OG    . SER A 1 905 ? -3.261  -14.385 20.180  1.00 108.80 ? 1008 SER A OG    1 
ATOM   6839 N  N     . GLY A 1 906 ? -6.252  -16.386 17.703  1.00 113.18 ? 1009 GLY A N     1 
ATOM   6840 C  CA    . GLY A 1 906 ? -7.505  -16.660 17.028  1.00 112.60 ? 1009 GLY A CA    1 
ATOM   6841 C  C     . GLY A 1 906 ? -8.628  -15.754 17.482  1.00 116.06 ? 1009 GLY A C     1 
ATOM   6842 O  O     . GLY A 1 906 ? -9.801  -16.039 17.224  1.00 114.84 ? 1009 GLY A O     1 
ATOM   6843 N  N     . MET A 1 907 ? -8.281  -14.663 18.167  1.00 119.61 ? 1010 MET A N     1 
ATOM   6844 C  CA    . MET A 1 907 ? -9.255  -13.710 18.681  1.00 114.39 ? 1010 MET A CA    1 
ATOM   6845 C  C     . MET A 1 907 ? -10.072 -13.134 17.531  1.00 114.85 ? 1010 MET A C     1 
ATOM   6846 O  O     . MET A 1 907 ? -9.524  -12.421 16.681  1.00 119.05 ? 1010 MET A O     1 
ATOM   6847 C  CB    . MET A 1 907 ? -8.564  -12.577 19.443  1.00 122.05 ? 1010 MET A CB    1 
ATOM   6848 C  CG    . MET A 1 907 ? -7.462  -13.017 20.394  1.00 122.61 ? 1010 MET A CG    1 
ATOM   6849 S  SD    . MET A 1 907 ? -8.066  -13.726 21.937  1.00 112.11 ? 1010 MET A SD    1 
ATOM   6850 C  CE    . MET A 1 907 ? -8.897  -12.318 22.664  1.00 98.88  ? 1010 MET A CE    1 
ATOM   6851 N  N     . PRO A 1 908 ? -11.376 -13.414 17.467  1.00 118.94 ? 1011 PRO A N     1 
ATOM   6852 C  CA    . PRO A 1 908 ? -12.187 -12.872 16.364  1.00 115.23 ? 1011 PRO A CA    1 
ATOM   6853 C  C     . PRO A 1 908 ? -12.266 -11.357 16.359  1.00 115.98 ? 1011 PRO A C     1 
ATOM   6854 O  O     . PRO A 1 908 ? -12.542 -10.769 15.306  1.00 117.27 ? 1011 PRO A O     1 
ATOM   6855 C  CB    . PRO A 1 908 ? -13.568 -13.501 16.599  1.00 113.54 ? 1011 PRO A CB    1 
ATOM   6856 C  CG    . PRO A 1 908 ? -13.318 -14.675 17.496  1.00 115.52 ? 1011 PRO A CG    1 
ATOM   6857 C  CD    . PRO A 1 908 ? -12.168 -14.271 18.363  1.00 119.06 ? 1011 PRO A CD    1 
ATOM   6858 N  N     . GLU A 1 909 ? -12.042 -10.707 17.501  1.00 115.07 ? 1012 GLU A N     1 
ATOM   6859 C  CA    . GLU A 1 909 ? -12.065 -9.255  17.609  1.00 116.90 ? 1012 GLU A CA    1 
ATOM   6860 C  C     . GLU A 1 909 ? -10.664 -8.664  17.691  1.00 113.98 ? 1012 GLU A C     1 
ATOM   6861 O  O     . GLU A 1 909 ? -10.502 -7.516  18.117  1.00 112.66 ? 1012 GLU A O     1 
ATOM   6862 C  CB    . GLU A 1 909 ? -12.897 -8.823  18.819  1.00 115.06 ? 1012 GLU A CB    1 
ATOM   6863 C  CG    . GLU A 1 909 ? -12.404 -9.362  20.156  1.00 120.59 ? 1012 GLU A CG    1 
ATOM   6864 C  CD    . GLU A 1 909 ? -12.694 -10.841 20.341  1.00 123.01 ? 1012 GLU A CD    1 
ATOM   6865 O  OE1   . GLU A 1 909 ? -13.875 -11.237 20.252  1.00 118.73 ? 1012 GLU A OE1   1 
ATOM   6866 O  OE2   . GLU A 1 909 ? -11.733 -11.610 20.554  1.00 130.25 ? 1012 GLU A OE2   1 
ATOM   6867 N  N     . LEU A 1 910 ? -9.650  -9.427  17.299  1.00 114.88 ? 1013 LEU A N     1 
ATOM   6868 C  CA    . LEU A 1 910 ? -8.281  -8.930  17.255  1.00 110.97 ? 1013 LEU A CA    1 
ATOM   6869 C  C     . LEU A 1 910 ? -7.555  -9.554  16.066  1.00 113.13 ? 1013 LEU A C     1 
ATOM   6870 O  O     . LEU A 1 910 ? -6.493  -10.165 16.202  1.00 109.31 ? 1013 LEU A O     1 
ATOM   6871 C  CB    . LEU A 1 910 ? -7.552  -9.216  18.567  1.00 108.24 ? 1013 LEU A CB    1 
ATOM   6872 C  CG    . LEU A 1 910 ? -7.512  -8.079  19.590  1.00 102.99 ? 1013 LEU A CG    1 
ATOM   6873 C  CD1   . LEU A 1 910 ? -6.688  -8.492  20.795  1.00 102.03 ? 1013 LEU A CD1   1 
ATOM   6874 C  CD2   . LEU A 1 910 ? -6.944  -6.823  18.957  1.00 99.96  ? 1013 LEU A CD2   1 
ATOM   6875 N  N     . GLN A 1 911 ? -8.132  -9.406  14.875  1.00 117.91 ? 1014 GLN A N     1 
ATOM   6876 C  CA    . GLN A 1 911 ? -7.526  -9.914  13.651  1.00 117.04 ? 1014 GLN A CA    1 
ATOM   6877 C  C     . GLN A 1 911 ? -6.791  -8.839  12.865  1.00 111.29 ? 1014 GLN A C     1 
ATOM   6878 O  O     . GLN A 1 911 ? -5.675  -9.077  12.395  1.00 105.76 ? 1014 GLN A O     1 
ATOM   6879 C  CB    . GLN A 1 911 ? -8.590  -10.559 12.758  1.00 116.71 ? 1014 GLN A CB    1 
ATOM   6880 C  CG    . GLN A 1 911 ? -9.246  -11.794 13.361  1.00 121.92 ? 1014 GLN A CG    1 
ATOM   6881 C  CD    . GLN A 1 911 ? -8.265  -12.934 13.575  1.00 133.18 ? 1014 GLN A CD    1 
ATOM   6882 O  OE1   . GLN A 1 911 ? -7.620  -13.029 14.622  1.00 122.10 ? 1014 GLN A OE1   1 
ATOM   6883 N  NE2   . GLN A 1 911 ? -8.149  -13.808 12.582  1.00 132.90 ? 1014 GLN A NE2   1 
ATOM   6884 N  N     . SER A 1 912 ? -7.386  -7.660  12.722  1.00 117.14 ? 1015 SER A N     1 
ATOM   6885 C  CA    . SER A 1 912 ? -6.808  -6.568  11.954  1.00 126.73 ? 1015 SER A CA    1 
ATOM   6886 C  C     . SER A 1 912 ? -6.375  -5.440  12.880  1.00 131.66 ? 1015 SER A C     1 
ATOM   6887 O  O     . SER A 1 912 ? -6.761  -5.378  14.051  1.00 126.46 ? 1015 SER A O     1 
ATOM   6888 C  CB    . SER A 1 912 ? -7.810  -6.044  10.918  1.00 132.71 ? 1015 SER A CB    1 
ATOM   6889 O  OG    . SER A 1 912 ? -8.949  -5.487  11.552  1.00 129.91 ? 1015 SER A OG    1 
ATOM   6890 N  N     . PHE A 1 913 ? -5.562  -4.535  12.332  1.00 145.30 ? 1016 PHE A N     1 
ATOM   6891 C  CA    . PHE A 1 913 ? -5.171  -3.334  13.060  1.00 136.80 ? 1016 PHE A CA    1 
ATOM   6892 C  C     . PHE A 1 913 ? -6.309  -2.332  13.189  1.00 133.16 ? 1016 PHE A C     1 
ATOM   6893 O  O     . PHE A 1 913 ? -6.138  -1.312  13.865  1.00 137.68 ? 1016 PHE A O     1 
ATOM   6894 C  CB    . PHE A 1 913 ? -3.974  -2.667  12.378  1.00 139.12 ? 1016 PHE A CB    1 
ATOM   6895 C  CG    . PHE A 1 913 ? -2.664  -3.359  12.632  1.00 149.07 ? 1016 PHE A CG    1 
ATOM   6896 C  CD1   . PHE A 1 913 ? -2.218  -4.364  11.790  1.00 153.75 ? 1016 PHE A CD1   1 
ATOM   6897 C  CD2   . PHE A 1 913 ? -1.875  -2.997  13.712  1.00 146.31 ? 1016 PHE A CD2   1 
ATOM   6898 C  CE1   . PHE A 1 913 ? -1.010  -4.998  12.023  1.00 151.91 ? 1016 PHE A CE1   1 
ATOM   6899 C  CE2   . PHE A 1 913 ? -0.667  -3.627  13.951  1.00 136.00 ? 1016 PHE A CE2   1 
ATOM   6900 C  CZ    . PHE A 1 913 ? -0.233  -4.627  13.105  1.00 142.28 ? 1016 PHE A CZ    1 
ATOM   6901 N  N     . ASP A 1 914 ? -7.456  -2.590  12.558  1.00 127.69 ? 1017 ASP A N     1 
ATOM   6902 C  CA    . ASP A 1 914 ? -8.602  -1.700  12.692  1.00 126.69 ? 1017 ASP A CA    1 
ATOM   6903 C  C     . ASP A 1 914 ? -9.309  -1.883  14.028  1.00 126.67 ? 1017 ASP A C     1 
ATOM   6904 O  O     . ASP A 1 914 ? -9.869  -0.921  14.564  1.00 124.06 ? 1017 ASP A O     1 
ATOM   6905 C  CB    . ASP A 1 914 ? -9.585  -1.931  11.544  1.00 132.68 ? 1017 ASP A CB    1 
ATOM   6906 C  CG    . ASP A 1 914 ? -8.915  -1.882  10.184  1.00 128.52 ? 1017 ASP A CG    1 
ATOM   6907 O  OD1   . ASP A 1 914 ? -7.927  -1.132  10.030  1.00 126.93 ? 1017 ASP A OD1   1 
ATOM   6908 O  OD2   . ASP A 1 914 ? -9.377  -2.598  9.270   1.00 119.10 ? 1017 ASP A OD2   1 
ATOM   6909 N  N     . ASP A 1 915 ? -9.298  -3.103  14.574  1.00 138.46 ? 1018 ASP A N     1 
ATOM   6910 C  CA    . ASP A 1 915 ? -9.895  -3.332  15.886  1.00 126.90 ? 1018 ASP A CA    1 
ATOM   6911 C  C     . ASP A 1 915 ? -9.100  -2.630  16.979  1.00 120.45 ? 1018 ASP A C     1 
ATOM   6912 O  O     . ASP A 1 915 ? -9.682  -2.066  17.913  1.00 128.09 ? 1018 ASP A O     1 
ATOM   6913 C  CB    . ASP A 1 915 ? -9.983  -4.831  16.170  1.00 125.61 ? 1018 ASP A CB    1 
ATOM   6914 C  CG    . ASP A 1 915 ? -10.760 -5.581  15.107  1.00 139.35 ? 1018 ASP A CG    1 
ATOM   6915 O  OD1   . ASP A 1 915 ? -11.748 -5.023  14.585  1.00 153.02 ? 1018 ASP A OD1   1 
ATOM   6916 O  OD2   . ASP A 1 915 ? -10.382 -6.729  14.792  1.00 137.86 ? 1018 ASP A OD2   1 
ATOM   6917 N  N     . ILE A 1 916 ? -7.769  -2.654  16.877  1.00 112.83 ? 1019 ILE A N     1 
ATOM   6918 C  CA    . ILE A 1 916 ? -6.932  -1.971  17.858  1.00 108.98 ? 1019 ILE A CA    1 
ATOM   6919 C  C     . ILE A 1 916 ? -7.143  -0.465  17.791  1.00 107.92 ? 1019 ILE A C     1 
ATOM   6920 O  O     . ILE A 1 916 ? -6.938  0.243   18.785  1.00 103.76 ? 1019 ILE A O     1 
ATOM   6921 C  CB    . ILE A 1 916 ? -5.454  -2.349  17.645  1.00 107.36 ? 1019 ILE A CB    1 
ATOM   6922 C  CG1   . ILE A 1 916 ? -5.298  -3.870  17.608  1.00 104.71 ? 1019 ILE A CG1   1 
ATOM   6923 C  CG2   . ILE A 1 916 ? -4.579  -1.766  18.746  1.00 99.28  ? 1019 ILE A CG2   1 
ATOM   6924 C  CD1   . ILE A 1 916 ? -3.862  -4.328  17.497  1.00 100.26 ? 1019 ILE A CD1   1 
ATOM   6925 N  N     . ALA A 1 917 ? -7.570  0.051   16.638  1.00 109.10 ? 1020 ALA A N     1 
ATOM   6926 C  CA    . ALA A 1 917 ? -7.824  1.480   16.501  1.00 104.66 ? 1020 ALA A CA    1 
ATOM   6927 C  C     . ALA A 1 917 ? -8.997  1.959   17.346  1.00 99.51  ? 1020 ALA A C     1 
ATOM   6928 O  O     . ALA A 1 917 ? -9.208  3.173   17.444  1.00 99.15  ? 1020 ALA A O     1 
ATOM   6929 C  CB    . ALA A 1 917 ? -8.071  1.831   15.032  1.00 105.82 ? 1020 ALA A CB    1 
ATOM   6930 N  N     . TYR A 1 918 ? -9.760  1.048   17.954  1.00 100.96 ? 1021 TYR A N     1 
ATOM   6931 C  CA    . TYR A 1 918 ? -10.895 1.464   18.772  1.00 99.98  ? 1021 TYR A CA    1 
ATOM   6932 C  C     . TYR A 1 918 ? -10.431 2.230   20.005  1.00 99.26  ? 1021 TYR A C     1 
ATOM   6933 O  O     . TYR A 1 918 ? -10.982 3.288   20.332  1.00 99.55  ? 1021 TYR A O     1 
ATOM   6934 C  CB    . TYR A 1 918 ? -11.733 0.249   19.172  1.00 103.86 ? 1021 TYR A CB    1 
ATOM   6935 C  CG    . TYR A 1 918 ? -13.043 0.609   19.839  1.00 106.78 ? 1021 TYR A CG    1 
ATOM   6936 C  CD1   . TYR A 1 918 ? -14.140 1.005   19.085  1.00 103.57 ? 1021 TYR A CD1   1 
ATOM   6937 C  CD2   . TYR A 1 918 ? -13.184 0.553   21.221  1.00 107.05 ? 1021 TYR A CD2   1 
ATOM   6938 C  CE1   . TYR A 1 918 ? -15.341 1.336   19.686  1.00 107.53 ? 1021 TYR A CE1   1 
ATOM   6939 C  CE2   . TYR A 1 918 ? -14.383 0.882   21.832  1.00 103.04 ? 1021 TYR A CE2   1 
ATOM   6940 C  CZ    . TYR A 1 918 ? -15.457 1.272   21.059  1.00 107.38 ? 1021 TYR A CZ    1 
ATOM   6941 O  OH    . TYR A 1 918 ? -16.652 1.601   21.660  1.00 105.33 ? 1021 TYR A OH    1 
ATOM   6942 N  N     . ILE A 1 919 ? -9.414  1.713   20.703  1.00 95.73  ? 1022 ILE A N     1 
ATOM   6943 C  CA    . ILE A 1 919 ? -8.894  2.413   21.873  1.00 91.79  ? 1022 ILE A CA    1 
ATOM   6944 C  C     . ILE A 1 919 ? -8.275  3.746   21.486  1.00 89.61  ? 1022 ILE A C     1 
ATOM   6945 O  O     . ILE A 1 919 ? -8.199  4.655   22.317  1.00 86.39  ? 1022 ILE A O     1 
ATOM   6946 C  CB    . ILE A 1 919 ? -7.874  1.543   22.642  1.00 92.29  ? 1022 ILE A CB    1 
ATOM   6947 C  CG1   . ILE A 1 919 ? -6.653  1.237   21.775  1.00 89.33  ? 1022 ILE A CG1   1 
ATOM   6948 C  CG2   . ILE A 1 919 ? -8.526  0.262   23.141  1.00 90.10  ? 1022 ILE A CG2   1 
ATOM   6949 N  N     . ARG A 1 920 ? -7.833  3.892   20.234  1.00 94.13  ? 1023 ARG A N     1 
ATOM   6950 C  CA    . ARG A 1 920 ? -7.346  5.189   19.780  1.00 89.95  ? 1023 ARG A CA    1 
ATOM   6951 C  C     . ARG A 1 920 ? -8.471  6.215   19.730  1.00 86.30  ? 1023 ARG A C     1 
ATOM   6952 O  O     . ARG A 1 920 ? -8.225  7.413   19.909  1.00 84.35  ? 1023 ARG A O     1 
ATOM   6953 C  CB    . ARG A 1 920 ? -6.677  5.049   18.411  1.00 90.24  ? 1023 ARG A CB    1 
ATOM   6954 C  CG    . ARG A 1 920 ? -5.865  6.263   17.982  1.00 103.03 ? 1023 ARG A CG    1 
ATOM   6955 C  CD    . ARG A 1 920 ? -5.169  6.025   16.648  1.00 99.24  ? 1023 ARG A CD    1 
ATOM   6956 N  NE    . ARG A 1 920 ? -4.370  7.173   16.232  1.00 91.28  ? 1023 ARG A NE    1 
ATOM   6957 N  N     . LYS A 1 921 ? -9.707  5.764   19.502  1.00 82.43  ? 1024 LYS A N     1 
ATOM   6958 C  CA    . LYS A 1 921 ? -10.855 6.665   19.528  1.00 89.04  ? 1024 LYS A CA    1 
ATOM   6959 C  C     . LYS A 1 921 ? -11.271 6.990   20.958  1.00 94.81  ? 1024 LYS A C     1 
ATOM   6960 O  O     . LYS A 1 921 ? -11.441 8.161   21.313  1.00 93.74  ? 1024 LYS A O     1 
ATOM   6961 C  CB    . LYS A 1 921 ? -12.031 6.048   18.767  1.00 94.63  ? 1024 LYS A CB    1 
ATOM   6962 C  CG    . LYS A 1 921 ? -11.696 5.534   17.377  1.00 113.47 ? 1024 LYS A CG    1 
ATOM   6963 C  CD    . LYS A 1 921 ? -12.925 4.921   16.718  1.00 117.67 ? 1024 LYS A CD    1 
ATOM   6964 C  CE    . LYS A 1 921 ? -12.604 4.359   15.342  1.00 112.14 ? 1024 LYS A CE    1 
ATOM   6965 N  NZ    . LYS A 1 921 ? -11.629 3.235   15.408  1.00 107.07 ? 1024 LYS A NZ    1 
ATOM   6966 N  N     . THR A 1 922 ? -11.444 5.958   21.790  1.00 92.28  ? 1025 THR A N     1 
ATOM   6967 C  CA    . THR A 1 922 ? -11.915 6.172   23.155  1.00 91.02  ? 1025 THR A CA    1 
ATOM   6968 C  C     . THR A 1 922 ? -10.910 6.961   23.983  1.00 90.07  ? 1025 THR A C     1 
ATOM   6969 O  O     . THR A 1 922 ? -11.294 7.639   24.943  1.00 92.96  ? 1025 THR A O     1 
ATOM   6970 C  CB    . THR A 1 922 ? -12.215 4.830   23.824  1.00 90.24  ? 1025 THR A CB    1 
ATOM   6971 O  OG1   . THR A 1 922 ? -11.043 4.006   23.796  1.00 89.67  ? 1025 THR A OG1   1 
ATOM   6972 C  CG2   . THR A 1 922 ? -13.346 4.116   23.101  1.00 93.37  ? 1025 THR A CG2   1 
ATOM   6973 N  N     . LEU A 1 923 ? -9.627  6.888   23.636  1.00 86.00  ? 1026 LEU A N     1 
ATOM   6974 C  CA    . LEU A 1 923 ? -8.605  7.669   24.320  1.00 86.20  ? 1026 LEU A CA    1 
ATOM   6975 C  C     . LEU A 1 923 ? -8.368  9.030   23.680  1.00 91.52  ? 1026 LEU A C     1 
ATOM   6976 O  O     . LEU A 1 923 ? -7.682  9.864   24.283  1.00 88.71  ? 1026 LEU A O     1 
ATOM   6977 C  CB    . LEU A 1 923 ? -7.287  6.889   24.370  1.00 86.35  ? 1026 LEU A CB    1 
ATOM   6978 C  CG    . LEU A 1 923 ? -7.265  5.648   25.264  1.00 84.78  ? 1026 LEU A CG    1 
ATOM   6979 C  CD1   . LEU A 1 923 ? -5.980  4.859   25.060  1.00 78.10  ? 1026 LEU A CD1   1 
ATOM   6980 C  CD2   . LEU A 1 923 ? -7.427  6.043   26.721  1.00 73.02  ? 1026 LEU A CD2   1 
ATOM   6981 N  N     . ALA A 1 924 ? -8.916  9.271   22.487  1.00 90.11  ? 1027 ALA A N     1 
ATOM   6982 C  CA    . ALA A 1 924 ? -8.791  10.551  21.788  1.00 86.02  ? 1027 ALA A CA    1 
ATOM   6983 C  C     . ALA A 1 924 ? -7.326  10.957  21.639  1.00 89.13  ? 1027 ALA A C     1 
ATOM   6984 O  O     . ALA A 1 924 ? -6.923  12.073  21.976  1.00 93.47  ? 1027 ALA A O     1 
ATOM   6985 C  CB    . ALA A 1 924 ? -9.594  11.642  22.497  1.00 89.68  ? 1027 ALA A CB    1 
ATOM   6986 N  N     . LEU A 1 925 ? -6.523  10.029  21.113  1.00 80.92  ? 1028 LEU A N     1 
ATOM   6987 C  CA    . LEU A 1 925 ? -5.081  10.235  21.041  1.00 90.24  ? 1028 LEU A CA    1 
ATOM   6988 C  C     . LEU A 1 925 ? -4.691  11.372  20.107  1.00 98.16  ? 1028 LEU A C     1 
ATOM   6989 O  O     . LEU A 1 925 ? -3.611  11.948  20.275  1.00 96.06  ? 1028 LEU A O     1 
ATOM   6990 C  CB    . LEU A 1 925 ? -4.391  8.942   20.605  1.00 90.60  ? 1028 LEU A CB    1 
ATOM   6991 C  CG    . LEU A 1 925 ? -4.585  7.763   21.557  1.00 89.75  ? 1028 LEU A CG    1 
ATOM   6992 C  CD1   . LEU A 1 925 ? -3.754  6.567   21.124  1.00 87.81  ? 1028 LEU A CD1   1 
ATOM   6993 C  CD2   . LEU A 1 925 ? -4.240  8.180   22.977  1.00 91.50  ? 1028 LEU A CD2   1 
ATOM   6994 N  N     . ASP A 1 926 ? -5.536  11.712  19.135  1.00 105.71 ? 1029 ASP A N     1 
ATOM   6995 C  CA    . ASP A 1 926 ? -5.214  12.778  18.196  1.00 105.17 ? 1029 ASP A CA    1 
ATOM   6996 C  C     . ASP A 1 926 ? -5.502  14.167  18.749  1.00 108.98 ? 1029 ASP A C     1 
ATOM   6997 O  O     . ASP A 1 926 ? -5.142  15.158  18.103  1.00 112.08 ? 1029 ASP A O     1 
ATOM   6998 C  CB    . ASP A 1 926 ? -5.983  12.578  16.889  1.00 108.82 ? 1029 ASP A CB    1 
ATOM   6999 C  CG    . ASP A 1 926 ? -5.679  11.246  16.232  1.00 121.96 ? 1029 ASP A CG    1 
ATOM   7000 O  OD1   . ASP A 1 926 ? -4.904  10.457  16.813  1.00 115.72 ? 1029 ASP A OD1   1 
ATOM   7001 O  OD2   . ASP A 1 926 ? -6.214  10.987  15.133  1.00 134.63 ? 1029 ASP A OD2   1 
ATOM   7002 N  N     . LYS A 1 927 ? -6.131  14.268  19.916  1.00 110.16 ? 1030 LYS A N     1 
ATOM   7003 C  CA    . LYS A 1 927 ? -6.476  15.547  20.513  1.00 106.45 ? 1030 LYS A CA    1 
ATOM   7004 C  C     . LYS A 1 927 ? -5.590  15.827  21.720  1.00 103.97 ? 1030 LYS A C     1 
ATOM   7005 O  O     . LYS A 1 927 ? -4.928  14.935  22.256  1.00 103.58 ? 1030 LYS A O     1 
ATOM   7006 C  CB    . LYS A 1 927 ? -7.951  15.579  20.930  1.00 102.64 ? 1030 LYS A CB    1 
ATOM   7007 C  CG    . LYS A 1 927 ? -8.913  15.152  19.834  1.00 118.88 ? 1030 LYS A CG    1 
ATOM   7008 C  CD    . LYS A 1 927 ? -10.317 15.668  20.098  1.00 118.61 ? 1030 LYS A CD    1 
ATOM   7009 C  CE    . LYS A 1 927 ? -10.815 15.250  21.470  1.00 124.52 ? 1030 LYS A CE    1 
ATOM   7010 N  NZ    . LYS A 1 927 ? -12.140 15.856  21.780  1.00 132.48 ? 1030 LYS A NZ    1 
ATOM   7011 N  N     . THR A 1 928 ? -5.585  17.089  22.141  1.00 105.01 ? 1031 THR A N     1 
ATOM   7012 C  CA    . THR A 1 928 ? -4.829  17.480  23.319  1.00 105.02 ? 1031 THR A CA    1 
ATOM   7013 C  C     . THR A 1 928 ? -5.485  16.917  24.579  1.00 103.36 ? 1031 THR A C     1 
ATOM   7014 O  O     . THR A 1 928 ? -6.602  16.394  24.556  1.00 101.01 ? 1031 THR A O     1 
ATOM   7015 C  CB    . THR A 1 928 ? -4.722  19.003  23.410  1.00 105.35 ? 1031 THR A CB    1 
ATOM   7016 O  OG1   . THR A 1 928 ? -6.030  19.569  23.556  1.00 106.37 ? 1031 THR A OG1   1 
ATOM   7017 C  CG2   . THR A 1 928 ? -4.072  19.566  22.157  1.00 108.66 ? 1031 THR A CG2   1 
ATOM   7018 N  N     . GLU A 1 929 ? -4.766  17.032  25.699  1.00 107.74 ? 1032 GLU A N     1 
ATOM   7019 C  CA    . GLU A 1 929 ? -5.274  16.496  26.958  1.00 101.89 ? 1032 GLU A CA    1 
ATOM   7020 C  C     . GLU A 1 929 ? -6.531  17.233  27.405  1.00 98.72  ? 1032 GLU A C     1 
ATOM   7021 O  O     . GLU A 1 929 ? -7.463  16.621  27.939  1.00 95.23  ? 1032 GLU A O     1 
ATOM   7022 C  CB    . GLU A 1 929 ? -4.188  16.571  28.031  1.00 102.73 ? 1032 GLU A CB    1 
ATOM   7023 C  CG    . GLU A 1 929 ? -4.431  15.675  29.233  1.00 108.41 ? 1032 GLU A CG    1 
ATOM   7024 C  CD    . GLU A 1 929 ? -3.254  15.654  30.188  1.00 107.66 ? 1032 GLU A CD    1 
ATOM   7025 O  OE1   . GLU A 1 929 ? -2.468  16.625  30.187  1.00 105.39 ? 1032 GLU A OE1   1 
ATOM   7026 O  OE2   . GLU A 1 929 ? -3.110  14.664  30.934  1.00 112.04 ? 1032 GLU A OE2   1 
ATOM   7027 N  N     . GLN A 1 930 ? -6.574  18.551  27.192  1.00 104.36 ? 1033 GLN A N     1 
ATOM   7028 C  CA    . GLN A 1 930 ? -7.780  19.318  27.491  1.00 101.71 ? 1033 GLN A CA    1 
ATOM   7029 C  C     . GLN A 1 930 ? -8.953  18.856  26.636  1.00 103.11 ? 1033 GLN A C     1 
ATOM   7030 O  O     . GLN A 1 930 ? -10.072 18.695  27.136  1.00 101.60 ? 1033 GLN A O     1 
ATOM   7031 C  CB    . GLN A 1 930 ? -7.515  20.808  27.275  1.00 105.91 ? 1033 GLN A CB    1 
ATOM   7032 C  CG    . GLN A 1 930 ? -8.761  21.677  27.208  1.00 109.55 ? 1033 GLN A CG    1 
ATOM   7033 C  CD    . GLN A 1 930 ? -9.258  22.102  28.575  1.00 101.85 ? 1033 GLN A CD    1 
ATOM   7034 O  OE1   . GLN A 1 930 ? -10.046 21.400  29.208  1.00 106.37 ? 1033 GLN A OE1   1 
ATOM   7035 N  NE2   . GLN A 1 930 ? -8.801  23.262  29.034  1.00 91.05  ? 1033 GLN A NE2   1 
ATOM   7036 N  N     . GLU A 1 931 ? -8.715  18.635  25.341  1.00 101.62 ? 1034 GLU A N     1 
ATOM   7037 C  CA    . GLU A 1 931 ? -9.793  18.221  24.451  1.00 102.60 ? 1034 GLU A CA    1 
ATOM   7038 C  C     . GLU A 1 931 ? -10.191 16.772  24.699  1.00 99.62  ? 1034 GLU A C     1 
ATOM   7039 O  O     . GLU A 1 931 ? -11.372 16.422  24.599  1.00 100.30 ? 1034 GLU A O     1 
ATOM   7040 C  CB    . GLU A 1 931 ? -9.375  18.422  22.996  1.00 109.13 ? 1034 GLU A CB    1 
ATOM   7041 C  CG    . GLU A 1 931 ? -9.123  19.873  22.624  1.00 108.73 ? 1034 GLU A CG    1 
ATOM   7042 C  CD    . GLU A 1 931 ? -8.378  20.018  21.313  1.00 112.50 ? 1034 GLU A CD    1 
ATOM   7043 O  OE1   . GLU A 1 931 ? -7.808  19.012  20.839  1.00 112.12 ? 1034 GLU A OE1   1 
ATOM   7044 O  OE2   . GLU A 1 931 ? -8.361  21.137  20.757  1.00 119.24 ? 1034 GLU A OE2   1 
ATOM   7045 N  N     . ALA A 1 932 ? -9.222  15.913  25.023  1.00 98.21  ? 1035 ALA A N     1 
ATOM   7046 C  CA    . ALA A 1 932 ? -9.538  14.513  25.280  1.00 96.75  ? 1035 ALA A CA    1 
ATOM   7047 C  C     . ALA A 1 932 ? -10.397 14.355  26.526  1.00 99.71  ? 1035 ALA A C     1 
ATOM   7048 O  O     . ALA A 1 932 ? -11.127 13.365  26.654  1.00 100.71 ? 1035 ALA A O     1 
ATOM   7049 C  CB    . ALA A 1 932 ? -8.255  13.695  25.409  1.00 95.76  ? 1035 ALA A CB    1 
ATOM   7050 N  N     . LEU A 1 933 ? -10.323 15.311  27.451  1.00 100.35 ? 1036 LEU A N     1 
ATOM   7051 C  CA    . LEU A 1 933 ? -11.182 15.269  28.626  1.00 95.43  ? 1036 LEU A CA    1 
ATOM   7052 C  C     . LEU A 1 933 ? -12.606 15.684  28.277  1.00 97.19  ? 1036 LEU A C     1 
ATOM   7053 O  O     . LEU A 1 933 ? -13.570 15.028  28.687  1.00 97.23  ? 1036 LEU A O     1 
ATOM   7054 C  CB    . LEU A 1 933 ? -10.609 16.163  29.725  1.00 96.47  ? 1036 LEU A CB    1 
ATOM   7055 C  CG    . LEU A 1 933 ? -11.250 15.980  31.099  1.00 94.25  ? 1036 LEU A CG    1 
ATOM   7056 C  CD1   . LEU A 1 933 ? -11.090 14.541  31.561  1.00 91.98  ? 1036 LEU A CD1   1 
ATOM   7057 C  CD2   . LEU A 1 933 ? -10.649 16.945  32.105  1.00 110.03 ? 1036 LEU A CD2   1 
ATOM   7058 N  N     . GLU A 1 934 ? -12.754 16.769  27.510  1.00 98.42  ? 1037 GLU A N     1 
ATOM   7059 C  CA    . GLU A 1 934 ? -14.078 17.189  27.060  1.00 100.26 ? 1037 GLU A CA    1 
ATOM   7060 C  C     . GLU A 1 934 ? -14.747 16.115  26.213  1.00 101.66 ? 1037 GLU A C     1 
ATOM   7061 O  O     . GLU A 1 934 ? -15.978 15.998  26.217  1.00 102.52 ? 1037 GLU A O     1 
ATOM   7062 C  CB    . GLU A 1 934 ? -13.973 18.495  26.273  1.00 99.30  ? 1037 GLU A CB    1 
ATOM   7063 C  CG    . GLU A 1 934 ? -13.358 19.645  27.051  1.00 101.21 ? 1037 GLU A CG    1 
ATOM   7064 C  CD    . GLU A 1 934 ? -13.125 20.871  26.188  1.00 115.09 ? 1037 GLU A CD    1 
ATOM   7065 O  OE1   . GLU A 1 934 ? -13.140 20.738  24.945  1.00 123.86 ? 1037 GLU A OE1   1 
ATOM   7066 O  OE2   . GLU A 1 934 ? -12.928 21.968  26.751  1.00 115.64 ? 1037 GLU A OE2   1 
ATOM   7067 N  N     . TYR A 1 935 ? -13.956 15.328  25.479  1.00 97.74  ? 1038 TYR A N     1 
ATOM   7068 C  CA    . TYR A 1 935 ? -14.506 14.211  24.718  1.00 99.35  ? 1038 TYR A CA    1 
ATOM   7069 C  C     . TYR A 1 935 ? -15.139 13.182  25.647  1.00 99.90  ? 1038 TYR A C     1 
ATOM   7070 O  O     . TYR A 1 935 ? -16.317 12.839  25.504  1.00 102.97 ? 1038 TYR A O     1 
ATOM   7071 C  CB    . TYR A 1 935 ? -13.407 13.576  23.863  1.00 99.47  ? 1038 TYR A CB    1 
ATOM   7072 C  CG    . TYR A 1 935 ? -13.736 12.193  23.344  1.00 99.83  ? 1038 TYR A CG    1 
ATOM   7073 C  CD1   . TYR A 1 935 ? -14.621 12.016  22.287  1.00 98.50  ? 1038 TYR A CD1   1 
ATOM   7074 C  CD2   . TYR A 1 935 ? -13.151 11.064  23.903  1.00 102.10 ? 1038 TYR A CD2   1 
ATOM   7075 C  CE1   . TYR A 1 935 ? -14.918 10.752  21.808  1.00 100.51 ? 1038 TYR A CE1   1 
ATOM   7076 C  CE2   . TYR A 1 935 ? -13.443 9.798   23.432  1.00 101.15 ? 1038 TYR A CE2   1 
ATOM   7077 C  CZ    . TYR A 1 935 ? -14.327 9.647   22.385  1.00 101.61 ? 1038 TYR A CZ    1 
ATOM   7078 O  OH    . TYR A 1 935 ? -14.619 8.388   21.915  1.00 104.01 ? 1038 TYR A OH    1 
ATOM   7079 N  N     . PHE A 1 936 ? -14.367 12.689  26.619  1.00 100.45 ? 1039 PHE A N     1 
ATOM   7080 C  CA    . PHE A 1 936 ? -14.894 11.703  27.559  1.00 100.38 ? 1039 PHE A CA    1 
ATOM   7081 C  C     . PHE A 1 936 ? -16.101 12.245  28.314  1.00 98.56  ? 1039 PHE A C     1 
ATOM   7082 O  O     . PHE A 1 936 ? -17.037 11.498  28.620  1.00 96.37  ? 1039 PHE A O     1 
ATOM   7083 C  CB    . PHE A 1 936 ? -13.800 11.272  28.538  1.00 96.26  ? 1039 PHE A CB    1 
ATOM   7084 C  CG    . PHE A 1 936 ? -14.287 10.355  29.625  1.00 93.84  ? 1039 PHE A CG    1 
ATOM   7085 C  CD1   . PHE A 1 936 ? -14.460 9.003   29.383  1.00 94.08  ? 1039 PHE A CD1   1 
ATOM   7086 C  CD2   . PHE A 1 936 ? -14.571 10.847  30.889  1.00 91.75  ? 1039 PHE A CD2   1 
ATOM   7087 C  CE1   . PHE A 1 936 ? -14.908 8.158   30.380  1.00 90.99  ? 1039 PHE A CE1   1 
ATOM   7088 C  CE2   . PHE A 1 936 ? -15.021 10.007  31.890  1.00 88.31  ? 1039 PHE A CE2   1 
ATOM   7089 C  CZ    . PHE A 1 936 ? -15.189 8.661   31.635  1.00 90.22  ? 1039 PHE A CZ    1 
ATOM   7090 N  N     . MET A 1 937 ? -16.101 13.545  28.618  1.00 97.56  ? 1040 MET A N     1 
ATOM   7091 C  CA    . MET A 1 937 ? -17.239 14.144  29.302  1.00 104.25 ? 1040 MET A CA    1 
ATOM   7092 C  C     . MET A 1 937 ? -18.499 14.142  28.448  1.00 112.13 ? 1040 MET A C     1 
ATOM   7093 O  O     . MET A 1 937 ? -19.602 14.234  28.997  1.00 115.37 ? 1040 MET A O     1 
ATOM   7094 C  CB    . MET A 1 937 ? -16.906 15.576  29.729  1.00 107.71 ? 1040 MET A CB    1 
ATOM   7095 C  CG    . MET A 1 937 ? -15.852 15.672  30.820  1.00 107.97 ? 1040 MET A CG    1 
ATOM   7096 S  SD    . MET A 1 937 ? -15.575 17.363  31.378  1.00 112.26 ? 1040 MET A SD    1 
ATOM   7097 C  CE    . MET A 1 937 ? -17.206 17.782  31.986  1.00 128.14 ? 1040 MET A CE    1 
ATOM   7098 N  N     . LYS A 1 938 ? -18.365 14.034  27.125  1.00 126.07 ? 1041 LYS A N     1 
ATOM   7099 C  CA    . LYS A 1 938 ? -19.539 14.090  26.261  1.00 122.75 ? 1041 LYS A CA    1 
ATOM   7100 C  C     . LYS A 1 938 ? -20.238 12.738  26.173  1.00 122.74 ? 1041 LYS A C     1 
ATOM   7101 O  O     . LYS A 1 938 ? -21.466 12.661  26.289  1.00 127.45 ? 1041 LYS A O     1 
ATOM   7102 C  CB    . LYS A 1 938 ? -19.151 14.584  24.866  1.00 125.69 ? 1041 LYS A CB    1 
ATOM   7103 C  CG    . LYS A 1 938 ? -20.346 14.798  23.951  1.00 130.55 ? 1041 LYS A CG    1 
ATOM   7104 C  CD    . LYS A 1 938 ? -19.948 15.438  22.636  1.00 126.83 ? 1041 LYS A CD    1 
ATOM   7105 C  CE    . LYS A 1 938 ? -21.171 15.701  21.773  1.00 138.40 ? 1041 LYS A CE    1 
ATOM   7106 N  NZ    . LYS A 1 938 ? -20.814 16.335  20.474  1.00 170.20 ? 1041 LYS A NZ    1 
ATOM   7107 N  N     . GLN A 1 939 ? -19.478 11.658  25.964  1.00 114.43 ? 1042 GLN A N     1 
ATOM   7108 C  CA    . GLN A 1 939 ? -20.100 10.340  25.875  1.00 116.00 ? 1042 GLN A CA    1 
ATOM   7109 C  C     . GLN A 1 939 ? -20.739 9.929   27.193  1.00 111.90 ? 1042 GLN A C     1 
ATOM   7110 O  O     . GLN A 1 939 ? -21.746 9.211   27.192  1.00 111.35 ? 1042 GLN A O     1 
ATOM   7111 C  CB    . GLN A 1 939 ? -19.082 9.289   25.433  1.00 113.64 ? 1042 GLN A CB    1 
ATOM   7112 C  CG    . GLN A 1 939 ? -18.847 9.255   23.934  1.00 112.99 ? 1042 GLN A CG    1 
ATOM   7113 C  CD    . GLN A 1 939 ? -17.954 10.380  23.472  1.00 117.69 ? 1042 GLN A CD    1 
ATOM   7114 O  OE1   . GLN A 1 939 ? -16.922 10.649  24.081  1.00 124.97 ? 1042 GLN A OE1   1 
ATOM   7115 N  NE2   . GLN A 1 939 ? -18.348 11.050  22.395  1.00 114.78 ? 1042 GLN A NE2   1 
ATOM   7116 N  N     . MET A 1 940 ? -20.175 10.365  28.322  1.00 115.16 ? 1043 MET A N     1 
ATOM   7117 C  CA    . MET A 1 940 ? -20.826 10.118  29.604  1.00 114.28 ? 1043 MET A CA    1 
ATOM   7118 C  C     . MET A 1 940 ? -22.132 10.893  29.709  1.00 113.67 ? 1043 MET A C     1 
ATOM   7119 O  O     . MET A 1 940 ? -23.138 10.364  30.196  1.00 115.07 ? 1043 MET A O     1 
ATOM   7120 C  CB    . MET A 1 940 ? -19.888 10.485  30.754  1.00 109.97 ? 1043 MET A CB    1 
ATOM   7121 C  CG    . MET A 1 940 ? -18.640 9.619   30.854  1.00 101.98 ? 1043 MET A CG    1 
ATOM   7122 S  SD    . MET A 1 940 ? -18.999 7.869   31.101  1.00 101.57 ? 1043 MET A SD    1 
ATOM   7123 C  CE    . MET A 1 940 ? -18.627 7.211   29.477  1.00 110.58 ? 1043 MET A CE    1 
ATOM   7124 N  N     . ASN A 1 941 ? -22.138 12.146  29.250  1.00 117.19 ? 1044 ASN A N     1 
ATOM   7125 C  CA    . ASN A 1 941 ? -23.366 12.932  29.258  1.00 121.31 ? 1044 ASN A CA    1 
ATOM   7126 C  C     . ASN A 1 941 ? -24.393 12.361  28.287  1.00 124.08 ? 1044 ASN A C     1 
ATOM   7127 O  O     . ASN A 1 941 ? -25.593 12.342  28.585  1.00 127.67 ? 1044 ASN A O     1 
ATOM   7128 C  CB    . ASN A 1 941 ? -23.053 14.390  28.918  1.00 124.01 ? 1044 ASN A CB    1 
ATOM   7129 C  CG    . ASN A 1 941 ? -24.248 15.302  29.099  1.00 130.67 ? 1044 ASN A CG    1 
ATOM   7130 O  OD1   . ASN A 1 941 ? -24.495 15.811  30.192  1.00 133.09 ? 1044 ASN A OD1   1 
ATOM   7131 N  ND2   . ASN A 1 941 ? -24.996 15.520  28.022  1.00 131.19 ? 1044 ASN A ND2   1 
ATOM   7132 N  N     . ASP A 1 942 ? -23.940 11.883  27.124  1.00 124.62 ? 1045 ASP A N     1 
ATOM   7133 C  CA    . ASP A 1 942 ? -24.865 11.323  26.143  1.00 119.68 ? 1045 ASP A CA    1 
ATOM   7134 C  C     . ASP A 1 942 ? -25.446 9.997   26.618  1.00 118.29 ? 1045 ASP A C     1 
ATOM   7135 O  O     . ASP A 1 942 ? -26.635 9.725   26.410  1.00 120.93 ? 1045 ASP A O     1 
ATOM   7136 C  CB    . ASP A 1 942 ? -24.162 11.147  24.797  1.00 121.98 ? 1045 ASP A CB    1 
ATOM   7137 C  CG    . ASP A 1 942 ? -23.744 12.467  24.181  1.00 129.85 ? 1045 ASP A CG    1 
ATOM   7138 O  OD1   . ASP A 1 942 ? -24.346 13.504  24.533  1.00 132.10 ? 1045 ASP A OD1   1 
ATOM   7139 O  OD2   . ASP A 1 942 ? -22.818 12.467  23.343  1.00 129.90 ? 1045 ASP A OD2   1 
ATOM   7140 N  N     . ALA A 1 943 ? -24.626 9.158   27.255  1.00 120.42 ? 1046 ALA A N     1 
ATOM   7141 C  CA    . ALA A 1 943 ? -25.106 7.879   27.762  1.00 118.35 ? 1046 ALA A CA    1 
ATOM   7142 C  C     . ALA A 1 943 ? -25.971 8.024   29.005  1.00 118.48 ? 1046 ALA A C     1 
ATOM   7143 O  O     . ALA A 1 943 ? -26.795 7.144   29.275  1.00 116.79 ? 1046 ALA A O     1 
ATOM   7144 C  CB    . ALA A 1 943 ? -23.925 6.955   28.068  1.00 112.82 ? 1046 ALA A CB    1 
ATOM   7145 N  N     . HIS A 1 944 ? -25.808 9.108   29.764  1.00 118.08 ? 1047 HIS A N     1 
ATOM   7146 C  CA    . HIS A 1 944 ? -26.560 9.319   30.993  1.00 120.10 ? 1047 HIS A CA    1 
ATOM   7147 C  C     . HIS A 1 944 ? -27.641 10.381  30.850  1.00 124.51 ? 1047 HIS A C     1 
ATOM   7148 O  O     . HIS A 1 944 ? -28.369 10.635  31.816  1.00 130.24 ? 1047 HIS A O     1 
ATOM   7149 C  CB    . HIS A 1 944 ? -25.615 9.699   32.141  1.00 120.93 ? 1047 HIS A CB    1 
ATOM   7150 C  CG    . HIS A 1 944 ? -24.554 8.678   32.419  1.00 117.58 ? 1047 HIS A CG    1 
ATOM   7151 N  ND1   . HIS A 1 944 ? -23.649 8.809   33.450  1.00 119.91 ? 1047 HIS A ND1   1 
ATOM   7152 C  CD2   . HIS A 1 944 ? -24.250 7.512   31.800  1.00 116.79 ? 1047 HIS A CD2   1 
ATOM   7153 C  CE1   . HIS A 1 944 ? -22.835 7.768   33.455  1.00 121.53 ? 1047 HIS A CE1   1 
ATOM   7154 N  NE2   . HIS A 1 944 ? -23.178 6.966   32.463  1.00 118.57 ? 1047 HIS A NE2   1 
ATOM   7155 N  N     . HIS A 1 945 ? -27.760 11.006  29.677  1.00 125.57 ? 1048 HIS A N     1 
ATOM   7156 C  CA    . HIS A 1 945 ? -28.799 12.003  29.404  1.00 128.24 ? 1048 HIS A CA    1 
ATOM   7157 C  C     . HIS A 1 945 ? -28.686 13.199  30.347  1.00 125.60 ? 1048 HIS A C     1 
ATOM   7158 O  O     . HIS A 1 945 ? -29.689 13.794  30.747  1.00 127.28 ? 1048 HIS A O     1 
ATOM   7159 C  CB    . HIS A 1 945 ? -30.199 11.384  29.475  1.00 131.10 ? 1048 HIS A CB    1 
ATOM   7160 C  CG    . HIS A 1 945 ? -30.370 10.170  28.615  1.00 138.39 ? 1048 HIS A CG    1 
ATOM   7161 N  ND1   . HIS A 1 945 ? -31.401 9.272   28.795  1.00 144.54 ? 1048 HIS A ND1   1 
ATOM   7162 C  CD2   . HIS A 1 945 ? -29.647 9.706   27.568  1.00 132.33 ? 1048 HIS A CD2   1 
ATOM   7163 C  CE1   . HIS A 1 945 ? -31.303 8.306   27.899  1.00 144.30 ? 1048 HIS A CE1   1 
ATOM   7164 N  NE2   . HIS A 1 945 ? -30.248 8.546   27.142  1.00 138.57 ? 1048 HIS A NE2   1 
ATOM   7165 N  N     . GLY A 1 946 ? -27.458 13.554  30.705  1.00 124.58 ? 1049 GLY A N     1 
ATOM   7166 C  CA    . GLY A 1 946 ? -27.186 14.682  31.569  1.00 128.63 ? 1049 GLY A CA    1 
ATOM   7167 C  C     . GLY A 1 946 ? -26.221 14.319  32.675  1.00 135.61 ? 1049 GLY A C     1 
ATOM   7168 O  O     . GLY A 1 946 ? -25.731 13.195  32.774  1.00 133.91 ? 1049 GLY A O     1 
ATOM   7169 N  N     . GLY A 1 947 ? -25.949 15.309  33.524  1.00 132.89 ? 1050 GLY A N     1 
ATOM   7170 C  CA    . GLY A 1 947 ? -25.061 15.137  34.650  1.00 129.46 ? 1050 GLY A CA    1 
ATOM   7171 C  C     . GLY A 1 947 ? -23.599 15.406  34.366  1.00 129.42 ? 1050 GLY A C     1 
ATOM   7172 O  O     . GLY A 1 947 ? -22.810 15.502  35.315  1.00 127.42 ? 1050 GLY A O     1 
ATOM   7173 N  N     . TRP A 1 948 ? -23.210 15.527  33.100  1.00 133.65 ? 1051 TRP A N     1 
ATOM   7174 C  CA    . TRP A 1 948 ? -21.827 15.783  32.706  1.00 132.78 ? 1051 TRP A CA    1 
ATOM   7175 C  C     . TRP A 1 948 ? -21.761 16.989  31.777  1.00 142.29 ? 1051 TRP A C     1 
ATOM   7176 O  O     . TRP A 1 948 ? -21.203 16.936  30.679  1.00 142.13 ? 1051 TRP A O     1 
ATOM   7177 C  CB    . TRP A 1 948 ? -21.208 14.556  32.039  1.00 125.06 ? 1051 TRP A CB    1 
ATOM   7178 C  CG    . TRP A 1 948 ? -21.262 13.305  32.869  1.00 119.81 ? 1051 TRP A CG    1 
ATOM   7179 C  CD1   . TRP A 1 948 ? -22.368 12.554  33.149  1.00 118.89 ? 1051 TRP A CD1   1 
ATOM   7180 C  CD2   . TRP A 1 948 ? -20.160 12.646  33.507  1.00 115.89 ? 1051 TRP A CD2   1 
ATOM   7181 N  NE1   . TRP A 1 948 ? -22.024 11.478  33.930  1.00 116.90 ? 1051 TRP A NE1   1 
ATOM   7182 C  CE2   . TRP A 1 948 ? -20.675 11.510  34.163  1.00 114.66 ? 1051 TRP A CE2   1 
ATOM   7183 C  CE3   . TRP A 1 948 ? -18.789 12.910  33.590  1.00 112.58 ? 1051 TRP A CE3   1 
ATOM   7184 C  CZ2   . TRP A 1 948 ? -19.867 10.639  34.893  1.00 108.59 ? 1051 TRP A CZ2   1 
ATOM   7185 C  CZ3   . TRP A 1 948 ? -17.989 12.043  34.316  1.00 108.57 ? 1051 TRP A CZ3   1 
ATOM   7186 C  CH2   . TRP A 1 948 ? -18.531 10.922  34.958  1.00 105.10 ? 1051 TRP A CH2   1 
ATOM   7187 N  N     . THR A 1 949 ? -22.343 18.105  32.215  1.00 153.00 ? 1052 THR A N     1 
ATOM   7188 C  CA    . THR A 1 949 ? -22.356 19.323  31.413  1.00 165.19 ? 1052 THR A CA    1 
ATOM   7189 C  C     . THR A 1 949 ? -21.229 20.258  31.834  1.00 177.70 ? 1052 THR A C     1 
ATOM   7190 O  O     . THR A 1 949 ? -20.191 20.328  31.166  1.00 178.87 ? 1052 THR A O     1 
ATOM   7191 C  CB    . THR A 1 949 ? -23.707 20.032  31.534  1.00 163.60 ? 1052 THR A CB    1 
ATOM   7192 O  OG1   . THR A 1 949 ? -23.973 20.329  32.910  1.00 167.22 ? 1052 THR A OG1   1 
ATOM   7193 C  CG2   . THR A 1 949 ? -24.821 19.153  30.985  1.00 154.61 ? 1052 THR A CG2   1 
ATOM   7194 N  N     . THR A 1 950 ? -21.433 20.982  32.938  1.00 202.74 ? 1053 THR A N     1 
ATOM   7195 C  CA    . THR A 1 950 ? -20.434 21.891  33.507  1.00 204.09 ? 1053 THR A CA    1 
ATOM   7196 C  C     . THR A 1 950 ? -19.981 22.950  32.504  1.00 200.92 ? 1053 THR A C     1 
ATOM   7197 O  O     . THR A 1 950 ? -18.840 23.418  32.553  1.00 200.54 ? 1053 THR A O     1 
ATOM   7198 C  CB    . THR A 1 950 ? -19.222 21.125  34.050  1.00 200.93 ? 1053 THR A CB    1 
ATOM   7199 O  OG1   . THR A 1 950 ? -18.468 20.580  32.961  1.00 195.36 ? 1053 THR A OG1   1 
ATOM   7200 C  CG2   . THR A 1 950 ? -19.670 19.995  34.966  1.00 194.75 ? 1053 THR A CG2   1 
ATOM   7201 N  N     . LYS A 1 951 ? -20.865 23.341  31.592  1.00 184.51 ? 1054 LYS A N     1 
ATOM   7202 C  CA    . LYS A 1 951 ? -20.546 24.375  30.613  1.00 175.77 ? 1054 LYS A CA    1 
ATOM   7203 C  C     . LYS A 1 951 ? -21.494 25.562  30.745  1.00 167.79 ? 1054 LYS A C     1 
ATOM   7204 O  O     . LYS A 1 951 ? -21.654 26.123  31.829  1.00 165.51 ? 1054 LYS A O     1 
ATOM   7205 C  CB    . LYS A 1 951 ? -20.604 23.812  29.191  1.00 171.15 ? 1054 LYS A CB    1 
ATOM   7206 C  CG    . LYS A 1 951 ? -19.537 22.772  28.887  1.00 167.84 ? 1054 LYS A CG    1 
ATOM   7207 C  CD    . LYS A 1 951 ? -19.579 22.355  27.426  1.00 158.82 ? 1054 LYS A CD    1 
ATOM   7208 C  CE    . LYS A 1 951 ? -18.482 21.352  27.106  1.00 159.37 ? 1054 LYS A CE    1 
ATOM   7209 N  NZ    . LYS A 1 951 ? -18.491 20.957  25.670  1.00 157.03 ? 1054 LYS A NZ    1 
ATOM   7210 N  N     . THR B 2 4   ? 1.646   -31.995 77.210  1.00 148.91 ? 3    THR B N     1 
ATOM   7211 C  CA    . THR B 2 4   ? 0.310   -31.459 77.442  1.00 144.42 ? 3    THR B CA    1 
ATOM   7212 C  C     . THR B 2 4   ? -0.532  -32.428 78.266  1.00 144.33 ? 3    THR B C     1 
ATOM   7213 O  O     . THR B 2 4   ? 0.002   -33.287 78.969  1.00 142.48 ? 3    THR B O     1 
ATOM   7214 C  CB    . THR B 2 4   ? -0.414  -31.156 76.118  1.00 138.46 ? 3    THR B CB    1 
ATOM   7215 O  OG1   . THR B 2 4   ? -0.511  -32.355 75.339  1.00 141.33 ? 3    THR B OG1   1 
ATOM   7216 C  CG2   . THR B 2 4   ? 0.344   -30.102 75.325  1.00 132.92 ? 3    THR B CG2   1 
ATOM   7217 N  N     . SER B 2 5   ? -1.853  -32.283 78.178  1.00 141.87 ? 4    SER B N     1 
ATOM   7218 C  CA    . SER B 2 5   ? -2.797  -33.150 78.884  1.00 142.33 ? 4    SER B CA    1 
ATOM   7219 C  C     . SER B 2 5   ? -3.874  -33.582 77.893  1.00 149.49 ? 4    SER B C     1 
ATOM   7220 O  O     . SER B 2 5   ? -4.775  -32.803 77.567  1.00 141.35 ? 4    SER B O     1 
ATOM   7221 C  CB    . SER B 2 5   ? -3.403  -32.441 80.092  1.00 135.74 ? 4    SER B CB    1 
ATOM   7222 O  OG    . SER B 2 5   ? -2.435  -32.239 81.107  1.00 127.03 ? 4    SER B OG    1 
ATOM   7223 N  N     . ALA B 2 6   ? -3.777  -34.823 77.417  1.00 164.64 ? 5    ALA B N     1 
ATOM   7224 C  CA    . ALA B 2 6   ? -4.749  -35.350 76.467  1.00 149.73 ? 5    ALA B CA    1 
ATOM   7225 C  C     . ALA B 2 6   ? -6.100  -35.522 77.150  1.00 147.87 ? 5    ALA B C     1 
ATOM   7226 O  O     . ALA B 2 6   ? -6.219  -36.254 78.138  1.00 136.62 ? 5    ALA B O     1 
ATOM   7227 C  CB    . ALA B 2 6   ? -4.263  -36.677 75.891  1.00 139.06 ? 5    ALA B CB    1 
ATOM   7228 N  N     . VAL B 2 7   ? -7.116  -34.852 76.619  1.00 142.81 ? 6    VAL B N     1 
ATOM   7229 C  CA    . VAL B 2 7   ? -8.446  -34.835 77.219  1.00 142.73 ? 6    VAL B CA    1 
ATOM   7230 C  C     . VAL B 2 7   ? -9.257  -36.013 76.692  1.00 148.69 ? 6    VAL B C     1 
ATOM   7231 O  O     . VAL B 2 7   ? -9.166  -36.342 75.501  1.00 152.95 ? 6    VAL B O     1 
ATOM   7232 C  CB    . VAL B 2 7   ? -9.155  -33.503 76.932  1.00 134.92 ? 6    VAL B CB    1 
ATOM   7233 C  CG1   . VAL B 2 7   ? -10.465 -33.418 77.688  1.00 130.87 ? 6    VAL B CG1   1 
ATOM   7234 C  CG2   . VAL B 2 7   ? -8.250  -32.338 77.287  1.00 126.92 ? 6    VAL B CG2   1 
ATOM   7235 N  N     . PRO B 2 8   ? -10.053 -36.682 77.533  1.00 147.47 ? 7    PRO B N     1 
ATOM   7236 C  CA    . PRO B 2 8   ? -10.969 -37.708 77.017  1.00 161.81 ? 7    PRO B CA    1 
ATOM   7237 C  C     . PRO B 2 8   ? -12.157 -37.099 76.288  1.00 176.99 ? 7    PRO B C     1 
ATOM   7238 O  O     . PRO B 2 8   ? -12.195 -35.885 76.058  1.00 181.91 ? 7    PRO B O     1 
ATOM   7239 C  CB    . PRO B 2 8   ? -11.407 -38.454 78.283  1.00 157.35 ? 7    PRO B CB    1 
ATOM   7240 C  CG    . PRO B 2 8   ? -11.273 -37.442 79.368  1.00 150.33 ? 7    PRO B CG    1 
ATOM   7241 C  CD    . PRO B 2 8   ? -10.063 -36.626 79.005  1.00 144.69 ? 7    PRO B CD    1 
ATOM   7242 N  N     . SER B 2 9   ? -13.129 -37.933 75.932  1.00 179.24 ? 8    SER B N     1 
ATOM   7243 C  CA    . SER B 2 9   ? -14.331 -37.521 75.192  1.00 182.24 ? 8    SER B CA    1 
ATOM   7244 C  C     . SER B 2 9   ? -13.886 -36.865 73.880  1.00 186.26 ? 8    SER B C     1 
ATOM   7245 O  O     . SER B 2 9   ? -12.856 -37.241 73.305  1.00 181.92 ? 8    SER B O     1 
ATOM   7246 C  CB    . SER B 2 9   ? -15.218 -36.650 76.071  1.00 174.52 ? 8    SER B CB    1 
ATOM   7247 O  OG    . SER B 2 9   ? -14.602 -35.407 76.364  1.00 172.74 ? 8    SER B OG    1 
ATOM   7248 N  N     . ASP B 2 10  ? -14.652 -35.890 73.399  1.00 197.67 ? 9    ASP B N     1 
ATOM   7249 C  CA    . ASP B 2 10  ? -14.336 -35.183 72.165  1.00 195.02 ? 9    ASP B CA    1 
ATOM   7250 C  C     . ASP B 2 10  ? -15.220 -33.950 72.074  1.00 188.93 ? 9    ASP B C     1 
ATOM   7251 O  O     . ASP B 2 10  ? -16.225 -33.833 72.783  1.00 189.23 ? 9    ASP B O     1 
ATOM   7252 C  CB    . ASP B 2 10  ? -14.529 -36.075 70.933  1.00 199.36 ? 9    ASP B CB    1 
ATOM   7253 C  CG    . ASP B 2 10  ? -15.894 -36.735 70.899  1.00 202.39 ? 9    ASP B CG    1 
ATOM   7254 O  OD1   . ASP B 2 10  ? -16.647 -36.609 71.887  1.00 201.89 ? 9    ASP B OD1   1 
ATOM   7255 O  OD2   . ASP B 2 10  ? -16.214 -37.382 69.880  1.00 205.81 ? 9    ASP B OD2   1 
ATOM   7256 N  N     . ASN B 2 11  ? -14.831 -33.035 71.187  1.00 176.17 ? 10   ASN B N     1 
ATOM   7257 C  CA    . ASN B 2 11  ? -15.555 -31.788 70.949  1.00 168.01 ? 10   ASN B CA    1 
ATOM   7258 C  C     . ASN B 2 11  ? -15.750 -31.018 72.257  1.00 164.70 ? 10   ASN B C     1 
ATOM   7259 O  O     . ASN B 2 11  ? -16.868 -30.759 72.706  1.00 156.00 ? 10   ASN B O     1 
ATOM   7260 C  CB    . ASN B 2 11  ? -16.893 -32.058 70.256  1.00 173.87 ? 10   ASN B CB    1 
ATOM   7261 C  CG    . ASN B 2 11  ? -17.455 -30.828 69.569  1.00 173.17 ? 10   ASN B CG    1 
ATOM   7262 O  OD1   . ASN B 2 11  ? -17.108 -29.697 69.910  1.00 165.89 ? 10   ASN B OD1   1 
ATOM   7263 N  ND2   . ASN B 2 11  ? -18.329 -31.044 68.594  1.00 175.27 ? 10   ASN B ND2   1 
ATOM   7264 N  N     . LEU B 2 12  ? -14.624 -30.659 72.866  1.00 154.65 ? 11   LEU B N     1 
ATOM   7265 C  CA    . LEU B 2 12  ? -14.651 -29.967 74.141  1.00 131.93 ? 11   LEU B CA    1 
ATOM   7266 C  C     . LEU B 2 12  ? -15.166 -28.539 73.965  1.00 119.46 ? 11   LEU B C     1 
ATOM   7267 O  O     . LEU B 2 12  ? -14.919 -27.903 72.937  1.00 121.87 ? 11   LEU B O     1 
ATOM   7268 C  CB    . LEU B 2 12  ? -13.257 -29.933 74.755  1.00 125.11 ? 11   LEU B CB    1 
ATOM   7269 C  CG    . LEU B 2 12  ? -12.466 -31.234 74.649  1.00 138.05 ? 11   LEU B CG    1 
ATOM   7270 C  CD1   . LEU B 2 12  ? -11.022 -31.003 75.054  1.00 134.97 ? 11   LEU B CD1   1 
ATOM   7271 C  CD2   . LEU B 2 12  ? -13.111 -32.313 75.501  1.00 147.49 ? 11   LEU B CD2   1 
ATOM   7272 N  N     . PRO B 2 13  ? -15.886 -28.014 74.954  1.00 111.40 ? 12   PRO B N     1 
ATOM   7273 C  CA    . PRO B 2 13  ? -16.283 -26.603 74.895  1.00 106.33 ? 12   PRO B CA    1 
ATOM   7274 C  C     . PRO B 2 13  ? -15.062 -25.697 74.933  1.00 102.40 ? 12   PRO B C     1 
ATOM   7275 O  O     . PRO B 2 13  ? -14.093 -25.957 75.649  1.00 105.63 ? 12   PRO B O     1 
ATOM   7276 C  CB    . PRO B 2 13  ? -17.162 -26.428 76.140  1.00 97.22  ? 12   PRO B CB    1 
ATOM   7277 C  CG    . PRO B 2 13  ? -16.754 -27.535 77.055  1.00 99.26  ? 12   PRO B CG    1 
ATOM   7278 C  CD    . PRO B 2 13  ? -16.394 -28.684 76.163  1.00 104.60 ? 12   PRO B CD    1 
ATOM   7279 N  N     . THR B 2 14  ? -15.110 -24.632 74.138  1.00 97.70  ? 13   THR B N     1 
ATOM   7280 C  CA    . THR B 2 14  ? -14.019 -23.672 74.040  1.00 93.48  ? 13   THR B CA    1 
ATOM   7281 C  C     . THR B 2 14  ? -14.519 -22.312 74.504  1.00 93.52  ? 13   THR B C     1 
ATOM   7282 O  O     . THR B 2 14  ? -15.516 -21.802 73.982  1.00 92.26  ? 13   THR B O     1 
ATOM   7283 C  CB    . THR B 2 14  ? -13.480 -23.590 72.611  1.00 94.35  ? 13   THR B CB    1 
ATOM   7284 O  OG1   . THR B 2 14  ? -12.975 -24.872 72.219  1.00 96.53  ? 13   THR B OG1   1 
ATOM   7285 C  CG2   . THR B 2 14  ? -12.361 -22.560 72.522  1.00 93.45  ? 13   THR B CG2   1 
ATOM   7286 N  N     . TYR B 2 15  ? -13.828 -21.732 75.479  1.00 90.23  ? 14   TYR B N     1 
ATOM   7287 C  CA    . TYR B 2 15  ? -14.194 -20.447 76.058  1.00 95.93  ? 14   TYR B CA    1 
ATOM   7288 C  C     . TYR B 2 15  ? -13.180 -19.402 75.614  1.00 94.69  ? 14   TYR B C     1 
ATOM   7289 O  O     . TYR B 2 15  ? -11.994 -19.503 75.945  1.00 102.17 ? 14   TYR B O     1 
ATOM   7290 C  CB    . TYR B 2 15  ? -14.249 -20.530 77.584  1.00 97.21  ? 14   TYR B CB    1 
ATOM   7291 C  CG    . TYR B 2 15  ? -15.248 -21.533 78.117  1.00 94.05  ? 14   TYR B CG    1 
ATOM   7292 C  CD1   . TYR B 2 15  ? -14.949 -22.889 78.155  1.00 96.43  ? 14   TYR B CD1   1 
ATOM   7293 C  CD2   . TYR B 2 15  ? -16.487 -21.124 78.593  1.00 92.74  ? 14   TYR B CD2   1 
ATOM   7294 C  CE1   . TYR B 2 15  ? -15.856 -23.807 78.643  1.00 97.06  ? 14   TYR B CE1   1 
ATOM   7295 C  CE2   . TYR B 2 15  ? -17.400 -22.039 79.085  1.00 93.53  ? 14   TYR B CE2   1 
ATOM   7296 C  CZ    . TYR B 2 15  ? -17.078 -23.379 79.108  1.00 92.75  ? 14   TYR B CZ    1 
ATOM   7297 O  OH    . TYR B 2 15  ? -17.979 -24.298 79.595  1.00 89.67  ? 14   TYR B OH    1 
ATOM   7298 N  N     . LYS B 2 16  ? -13.647 -18.405 74.862  1.00 97.47  ? 15   LYS B N     1 
ATOM   7299 C  CA    . LYS B 2 16  ? -12.784 -17.322 74.394  1.00 102.32 ? 15   LYS B CA    1 
ATOM   7300 C  C     . LYS B 2 16  ? -12.774 -16.227 75.456  1.00 92.37  ? 15   LYS B C     1 
ATOM   7301 O  O     . LYS B 2 16  ? -13.523 -15.249 75.402  1.00 94.80  ? 15   LYS B O     1 
ATOM   7302 C  CB    . LYS B 2 16  ? -13.253 -16.804 73.041  1.00 104.63 ? 15   LYS B CB    1 
ATOM   7303 C  CG    . LYS B 2 16  ? -13.152 -17.827 71.923  1.00 106.42 ? 15   LYS B CG    1 
ATOM   7304 C  CD    . LYS B 2 16  ? -13.582 -17.240 70.591  1.00 116.35 ? 15   LYS B CD    1 
ATOM   7305 C  CE    . LYS B 2 16  ? -13.476 -18.268 69.476  1.00 126.24 ? 15   LYS B CE    1 
ATOM   7306 N  NZ    . LYS B 2 16  ? -13.873 -17.697 68.159  1.00 128.07 ? 15   LYS B NZ    1 
ATOM   7307 N  N     . LEU B 2 17  ? -11.905 -16.408 76.447  1.00 86.43  ? 16   LEU B N     1 
ATOM   7308 C  CA    . LEU B 2 17  ? -11.768 -15.438 77.525  1.00 95.22  ? 16   LEU B CA    1 
ATOM   7309 C  C     . LEU B 2 17  ? -10.870 -14.294 77.073  1.00 86.04  ? 16   LEU B C     1 
ATOM   7310 O  O     . LEU B 2 17  ? -9.740  -14.518 76.629  1.00 84.05  ? 16   LEU B O     1 
ATOM   7311 C  CB    . LEU B 2 17  ? -11.194 -16.105 78.774  1.00 92.26  ? 16   LEU B CB    1 
ATOM   7312 C  CG    . LEU B 2 17  ? -11.892 -17.393 79.215  1.00 85.07  ? 16   LEU B CG    1 
ATOM   7313 C  CD1   . LEU B 2 17  ? -11.211 -17.980 80.440  1.00 88.50  ? 16   LEU B CD1   1 
ATOM   7314 C  CD2   . LEU B 2 17  ? -13.365 -17.137 79.483  1.00 86.32  ? 16   LEU B CD2   1 
ATOM   7315 N  N     . VAL B 2 18  ? -11.372 -13.068 77.184  1.00 85.20  ? 17   VAL B N     1 
ATOM   7316 C  CA    . VAL B 2 18  ? -10.667 -11.880 76.718  1.00 87.84  ? 17   VAL B CA    1 
ATOM   7317 C  C     . VAL B 2 18  ? -10.293 -11.032 77.926  1.00 89.35  ? 17   VAL B C     1 
ATOM   7318 O  O     . VAL B 2 18  ? -11.155 -10.686 78.744  1.00 89.39  ? 17   VAL B O     1 
ATOM   7319 C  CB    . VAL B 2 18  ? -11.519 -11.081 75.717  1.00 94.45  ? 17   VAL B CB    1 
ATOM   7320 C  CG1   . VAL B 2 18  ? -10.719 -9.933  75.143  1.00 91.93  ? 17   VAL B CG1   1 
ATOM   7321 C  CG2   . VAL B 2 18  ? -12.021 -11.992 74.605  1.00 87.09  ? 17   VAL B CG2   1 
ATOM   7322 N  N     . VAL B 2 19  ? -9.011  -10.699 78.036  1.00 88.79  ? 18   VAL B N     1 
ATOM   7323 C  CA    . VAL B 2 19  ? -8.479  -9.927  79.153  1.00 87.73  ? 18   VAL B CA    1 
ATOM   7324 C  C     . VAL B 2 19  ? -8.236  -8.506  78.660  1.00 92.61  ? 18   VAL B C     1 
ATOM   7325 O  O     . VAL B 2 19  ? -7.357  -8.271  77.824  1.00 101.54 ? 18   VAL B O     1 
ATOM   7326 C  CB    . VAL B 2 19  ? -7.193  -10.554 79.705  1.00 85.91  ? 18   VAL B CB    1 
ATOM   7327 C  CG1   . VAL B 2 19  ? -6.619  -9.694  80.811  1.00 87.06  ? 18   VAL B CG1   1 
ATOM   7328 C  CG2   . VAL B 2 19  ? -7.462  -11.964 80.207  1.00 83.82  ? 18   VAL B CG2   1 
ATOM   7329 N  N     . VAL B 2 20  ? -9.008  -7.553  79.179  1.00 95.60  ? 19   VAL B N     1 
ATOM   7330 C  CA    . VAL B 2 20  ? -8.926  -6.164  78.748  1.00 98.53  ? 19   VAL B CA    1 
ATOM   7331 C  C     . VAL B 2 20  ? -8.581  -5.287  79.944  1.00 96.27  ? 19   VAL B C     1 
ATOM   7332 O  O     . VAL B 2 20  ? -8.867  -5.627  81.096  1.00 91.91  ? 19   VAL B O     1 
ATOM   7333 C  CB    . VAL B 2 20  ? -10.237 -5.693  78.082  1.00 96.15  ? 19   VAL B CB    1 
ATOM   7334 C  CG1   . VAL B 2 20  ? -10.552 -6.555  76.872  1.00 97.50  ? 19   VAL B CG1   1 
ATOM   7335 C  CG2   . VAL B 2 20  ? -11.382 -5.735  79.075  1.00 105.43 ? 19   VAL B CG2   1 
ATOM   7336 N  N     . GLY B 2 21  ? -7.960  -4.152  79.658  1.00 101.51 ? 20   GLY B N     1 
ATOM   7337 C  CA    . GLY B 2 21  ? -7.523  -3.239  80.695  1.00 93.56  ? 20   GLY B CA    1 
ATOM   7338 C  C     . GLY B 2 21  ? -6.454  -2.306  80.177  1.00 101.29 ? 20   GLY B C     1 
ATOM   7339 O  O     . GLY B 2 21  ? -5.877  -2.508  79.109  1.00 115.29 ? 20   GLY B O     1 
ATOM   7340 N  N     . ASP B 2 22  ? -6.190  -1.269  80.968  1.00 104.57 ? 21   ASP B N     1 
ATOM   7341 C  CA    . ASP B 2 22  ? -5.242  -0.236  80.577  1.00 107.48 ? 21   ASP B CA    1 
ATOM   7342 C  C     . ASP B 2 22  ? -3.815  -0.782  80.561  1.00 108.87 ? 21   ASP B C     1 
ATOM   7343 O  O     . ASP B 2 22  ? -3.539  -1.911  80.974  1.00 104.31 ? 21   ASP B O     1 
ATOM   7344 C  CB    . ASP B 2 22  ? -5.333  0.961   81.523  1.00 118.62 ? 21   ASP B CB    1 
ATOM   7345 C  CG    . ASP B 2 22  ? -6.680  1.651   81.462  1.00 127.41 ? 21   ASP B CG    1 
ATOM   7346 O  OD1   . ASP B 2 22  ? -7.547  1.200   80.684  1.00 125.58 ? 21   ASP B OD1   1 
ATOM   7347 O  OD2   . ASP B 2 22  ? -6.868  2.646   82.192  1.00 128.87 ? 21   ASP B OD2   1 
ATOM   7348 N  N     . GLY B 2 23  ? -2.897  0.051   80.076  1.00 121.22 ? 22   GLY B N     1 
ATOM   7349 C  CA    . GLY B 2 23  ? -1.507  -0.351  80.003  1.00 118.77 ? 22   GLY B CA    1 
ATOM   7350 C  C     . GLY B 2 23  ? -0.851  -0.384  81.370  1.00 123.65 ? 22   GLY B C     1 
ATOM   7351 O  O     . GLY B 2 23  ? -1.211  0.360   82.282  1.00 141.65 ? 22   GLY B O     1 
ATOM   7352 N  N     . GLY B 2 24  ? 0.132   -1.272  81.509  1.00 117.66 ? 23   GLY B N     1 
ATOM   7353 C  CA    . GLY B 2 24  ? 0.817   -1.457  82.770  1.00 122.66 ? 23   GLY B CA    1 
ATOM   7354 C  C     . GLY B 2 24  ? -0.012  -2.082  83.868  1.00 109.93 ? 23   GLY B C     1 
ATOM   7355 O  O     . GLY B 2 24  ? 0.478   -2.200  84.997  1.00 109.87 ? 23   GLY B O     1 
ATOM   7356 N  N     . VAL B 2 25  ? -1.247  -2.493  83.575  1.00 110.22 ? 24   VAL B N     1 
ATOM   7357 C  CA    . VAL B 2 25  ? -2.118  -3.048  84.605  1.00 111.13 ? 24   VAL B CA    1 
ATOM   7358 C  C     . VAL B 2 25  ? -1.639  -4.432  85.028  1.00 106.52 ? 24   VAL B C     1 
ATOM   7359 O  O     . VAL B 2 25  ? -1.588  -4.747  86.223  1.00 110.73 ? 24   VAL B O     1 
ATOM   7360 C  CB    . VAL B 2 25  ? -3.573  -3.071  84.105  1.00 104.60 ? 24   VAL B CB    1 
ATOM   7361 C  CG1   . VAL B 2 25  ? -4.396  -4.040  84.918  1.00 107.79 ? 24   VAL B CG1   1 
ATOM   7362 C  CG2   . VAL B 2 25  ? -4.175  -1.676  84.178  1.00 104.81 ? 24   VAL B CG2   1 
ATOM   7363 N  N     . GLY B 2 26  ? -1.280  -5.275  84.065  1.00 98.64  ? 25   GLY B N     1 
ATOM   7364 C  CA    . GLY B 2 26  ? -0.776  -6.598  84.378  1.00 99.51  ? 25   GLY B CA    1 
ATOM   7365 C  C     . GLY B 2 26  ? -1.498  -7.709  83.644  1.00 94.42  ? 25   GLY B C     1 
ATOM   7366 O  O     . GLY B 2 26  ? -1.427  -8.873  84.046  1.00 100.96 ? 25   GLY B O     1 
ATOM   7367 N  N     . LYS B 2 27  ? -2.194  -7.355  82.560  1.00 98.63  ? 26   LYS B N     1 
ATOM   7368 C  CA    . LYS B 2 27  ? -2.934  -8.351  81.791  1.00 92.39  ? 26   LYS B CA    1 
ATOM   7369 C  C     . LYS B 2 27  ? -2.015  -9.450  81.273  1.00 90.37  ? 26   LYS B C     1 
ATOM   7370 O  O     . LYS B 2 27  ? -2.382  -10.631 81.275  1.00 88.24  ? 26   LYS B O     1 
ATOM   7371 C  CB    . LYS B 2 27  ? -3.657  -7.679  80.626  1.00 88.71  ? 26   LYS B CB    1 
ATOM   7372 C  CG    . LYS B 2 27  ? -4.596  -6.564  81.031  1.00 93.28  ? 26   LYS B CG    1 
ATOM   7373 C  CD    . LYS B 2 27  ? -5.254  -5.951  79.810  1.00 98.33  ? 26   LYS B CD    1 
ATOM   7374 C  CE    . LYS B 2 27  ? -4.226  -5.335  78.878  1.00 107.56 ? 26   LYS B CE    1 
ATOM   7375 N  NZ    . LYS B 2 27  ? -3.490  -4.221  79.536  1.00 107.84 ? 26   LYS B NZ    1 
ATOM   7376 N  N     . SER B 2 28  ? -0.816  -9.081  80.823  1.00 94.84  ? 27   SER B N     1 
ATOM   7377 C  CA    . SER B 2 28  ? 0.106   -10.072 80.282  1.00 93.39  ? 27   SER B CA    1 
ATOM   7378 C  C     . SER B 2 28  ? 0.675   -10.955 81.387  1.00 87.65  ? 27   SER B C     1 
ATOM   7379 O  O     . SER B 2 28  ? 0.660   -12.187 81.277  1.00 83.89  ? 27   SER B O     1 
ATOM   7380 C  CB    . SER B 2 28  ? 1.226   -9.376  79.507  1.00 97.68  ? 27   SER B CB    1 
ATOM   7381 O  OG    . SER B 2 28  ? 0.719   -8.681  78.377  1.00 83.94  ? 27   SER B OG    1 
ATOM   7382 N  N     . ALA B 2 29  ? 1.166   -10.342 82.468  1.00 94.34  ? 28   ALA B N     1 
ATOM   7383 C  CA    . ALA B 2 29  ? 1.792   -11.111 83.542  1.00 94.66  ? 28   ALA B CA    1 
ATOM   7384 C  C     . ALA B 2 29  ? 0.805   -12.078 84.185  1.00 87.96  ? 28   ALA B C     1 
ATOM   7385 O  O     . ALA B 2 29  ? 1.177   -13.197 84.560  1.00 88.30  ? 28   ALA B O     1 
ATOM   7386 C  CB    . ALA B 2 29  ? 2.379   -10.165 84.589  1.00 102.83 ? 28   ALA B CB    1 
ATOM   7387 N  N     . LEU B 2 30  ? -0.457  -11.666 84.324  1.00 87.83  ? 29   LEU B N     1 
ATOM   7388 C  CA    . LEU B 2 30  ? -1.477  -12.574 84.837  1.00 87.94  ? 29   LEU B CA    1 
ATOM   7389 C  C     . LEU B 2 30  ? -1.666  -13.770 83.914  1.00 86.26  ? 29   LEU B C     1 
ATOM   7390 O  O     . LEU B 2 30  ? -1.812  -14.907 84.378  1.00 86.61  ? 29   LEU B O     1 
ATOM   7391 C  CB    . LEU B 2 30  ? -2.798  -11.828 85.021  1.00 91.41  ? 29   LEU B CB    1 
ATOM   7392 C  CG    . LEU B 2 30  ? -2.870  -10.837 86.184  1.00 90.94  ? 29   LEU B CG    1 
ATOM   7393 C  CD1   . LEU B 2 30  ? -4.163  -10.040 86.129  1.00 90.07  ? 29   LEU B CD1   1 
ATOM   7394 C  CD2   . LEU B 2 30  ? -2.743  -11.565 87.512  1.00 96.61  ? 29   LEU B CD2   1 
ATOM   7395 N  N     . THR B 2 31  ? -1.655  -13.531 82.599  1.00 96.90  ? 30   THR B N     1 
ATOM   7396 C  CA    . THR B 2 31  ? -1.869  -14.609 81.639  1.00 82.94  ? 30   THR B CA    1 
ATOM   7397 C  C     . THR B 2 31  ? -0.662  -15.537 81.566  1.00 83.01  ? 30   THR B C     1 
ATOM   7398 O  O     . THR B 2 31  ? -0.818  -16.761 81.483  1.00 82.68  ? 30   THR B O     1 
ATOM   7399 C  CB    . THR B 2 31  ? -2.184  -14.023 80.263  1.00 83.22  ? 30   THR B CB    1 
ATOM   7400 O  OG1   . THR B 2 31  ? -3.240  -13.061 80.384  1.00 83.35  ? 30   THR B OG1   1 
ATOM   7401 C  CG2   . THR B 2 31  ? -2.618  -15.117 79.298  1.00 85.60  ? 30   THR B CG2   1 
ATOM   7402 N  N     . ILE B 2 32  ? 0.551   -14.975 81.595  1.00 83.55  ? 31   ILE B N     1 
ATOM   7403 C  CA    . ILE B 2 32  ? 1.752   -15.806 81.591  1.00 83.86  ? 31   ILE B CA    1 
ATOM   7404 C  C     . ILE B 2 32  ? 1.827   -16.639 82.863  1.00 92.83  ? 31   ILE B C     1 
ATOM   7405 O  O     . ILE B 2 32  ? 2.296   -17.784 82.842  1.00 97.18  ? 31   ILE B O     1 
ATOM   7406 C  CB    . ILE B 2 32  ? 3.012   -14.935 81.409  1.00 89.98  ? 31   ILE B CB    1 
ATOM   7407 C  CG1   . ILE B 2 32  ? 2.905   -14.089 80.139  1.00 84.08  ? 31   ILE B CG1   1 
ATOM   7408 C  CG2   . ILE B 2 32  ? 4.262   -15.800 81.348  1.00 84.72  ? 31   ILE B CG2   1 
ATOM   7409 C  CD1   . ILE B 2 32  ? 2.774   -14.901 78.877  1.00 80.98  ? 31   ILE B CD1   1 
ATOM   7410 N  N     . GLN B 2 33  ? 1.361   -16.088 83.986  1.00 89.97  ? 32   GLN B N     1 
ATOM   7411 C  CA    . GLN B 2 33  ? 1.331   -16.856 85.225  1.00 88.54  ? 32   GLN B CA    1 
ATOM   7412 C  C     . GLN B 2 33  ? 0.330   -18.002 85.138  1.00 88.33  ? 32   GLN B C     1 
ATOM   7413 O  O     . GLN B 2 33  ? 0.607   -19.112 85.605  1.00 95.44  ? 32   GLN B O     1 
ATOM   7414 C  CB    . GLN B 2 33  ? 0.996   -15.938 86.401  1.00 99.31  ? 32   GLN B CB    1 
ATOM   7415 C  CG    . GLN B 2 33  ? 1.112   -16.605 87.762  1.00 92.22  ? 32   GLN B CG    1 
ATOM   7416 C  CD    . GLN B 2 33  ? 2.549   -16.898 88.141  1.00 93.39  ? 32   GLN B CD    1 
ATOM   7417 O  OE1   . GLN B 2 33  ? 3.392   -16.001 88.163  1.00 93.99  ? 32   GLN B OE1   1 
ATOM   7418 N  NE2   . GLN B 2 33  ? 2.838   -18.159 88.437  1.00 93.83  ? 32   GLN B NE2   1 
ATOM   7419 N  N     . PHE B 2 34  ? -0.835  -17.756 84.536  1.00 86.70  ? 33   PHE B N     1 
ATOM   7420 C  CA    . PHE B 2 34  ? -1.859  -18.793 84.466  1.00 90.76  ? 33   PHE B CA    1 
ATOM   7421 C  C     . PHE B 2 34  ? -1.476  -19.914 83.505  1.00 96.52  ? 33   PHE B C     1 
ATOM   7422 O  O     . PHE B 2 34  ? -1.835  -21.074 83.738  1.00 100.16 ? 33   PHE B O     1 
ATOM   7423 C  CB    . PHE B 2 34  ? -3.198  -18.175 84.064  1.00 86.76  ? 33   PHE B CB    1 
ATOM   7424 C  CG    . PHE B 2 34  ? -4.299  -19.179 83.877  1.00 95.24  ? 33   PHE B CG    1 
ATOM   7425 C  CD1   . PHE B 2 34  ? -4.734  -19.958 84.938  1.00 97.22  ? 33   PHE B CD1   1 
ATOM   7426 C  CD2   . PHE B 2 34  ? -4.907  -19.337 82.643  1.00 88.57  ? 33   PHE B CD2   1 
ATOM   7427 C  CE1   . PHE B 2 34  ? -5.749  -20.881 84.769  1.00 97.02  ? 33   PHE B CE1   1 
ATOM   7428 C  CE2   . PHE B 2 34  ? -5.924  -20.256 82.468  1.00 86.73  ? 33   PHE B CE2   1 
ATOM   7429 C  CZ    . PHE B 2 34  ? -6.345  -21.030 83.533  1.00 96.75  ? 33   PHE B CZ    1 
ATOM   7430 N  N     . PHE B 2 35  ? -0.749  -19.598 82.432  1.00 88.45  ? 34   PHE B N     1 
ATOM   7431 C  CA    . PHE B 2 35  ? -0.396  -20.584 81.415  1.00 89.66  ? 34   PHE B CA    1 
ATOM   7432 C  C     . PHE B 2 35  ? 0.982   -21.200 81.615  1.00 88.69  ? 34   PHE B C     1 
ATOM   7433 O  O     . PHE B 2 35  ? 1.163   -22.391 81.345  1.00 89.10  ? 34   PHE B O     1 
ATOM   7434 C  CB    . PHE B 2 35  ? -0.465  -19.956 80.019  1.00 86.11  ? 34   PHE B CB    1 
ATOM   7435 C  CG    . PHE B 2 35  ? -1.860  -19.821 79.486  1.00 80.60  ? 34   PHE B CG    1 
ATOM   7436 C  CD1   . PHE B 2 35  ? -2.464  -20.873 78.819  1.00 80.42  ? 34   PHE B CD1   1 
ATOM   7437 C  CD2   . PHE B 2 35  ? -2.569  -18.646 79.653  1.00 83.91  ? 34   PHE B CD2   1 
ATOM   7438 C  CE1   . PHE B 2 35  ? -3.748  -20.751 78.329  1.00 81.03  ? 34   PHE B CE1   1 
ATOM   7439 C  CE2   . PHE B 2 35  ? -3.854  -18.521 79.165  1.00 81.59  ? 34   PHE B CE2   1 
ATOM   7440 C  CZ    . PHE B 2 35  ? -4.443  -19.578 78.503  1.00 78.12  ? 34   PHE B CZ    1 
ATOM   7441 N  N     . ALA B 2 36  ? 1.962   -20.423 82.076  1.00 90.53  ? 35   ALA B N     1 
ATOM   7442 C  CA    . ALA B 2 36  ? 3.329   -20.907 82.202  1.00 95.43  ? 35   ALA B CA    1 
ATOM   7443 C  C     . ALA B 2 36  ? 3.838   -20.935 83.635  1.00 104.87 ? 35   ALA B C     1 
ATOM   7444 O  O     . ALA B 2 36  ? 4.962   -21.399 83.863  1.00 107.02 ? 35   ALA B O     1 
ATOM   7445 C  CB    . ALA B 2 36  ? 4.274   -20.057 81.342  1.00 89.44  ? 35   ALA B CB    1 
ATOM   7446 N  N     . LYS B 2 37  ? 3.051   -20.457 84.602  1.00 109.44 ? 36   LYS B N     1 
ATOM   7447 C  CA    . LYS B 2 37  ? 3.432   -20.456 86.015  1.00 112.99 ? 36   LYS B CA    1 
ATOM   7448 C  C     . LYS B 2 37  ? 4.744   -19.703 86.234  1.00 116.83 ? 36   LYS B C     1 
ATOM   7449 O  O     . LYS B 2 37  ? 5.649   -20.168 86.929  1.00 115.59 ? 36   LYS B O     1 
ATOM   7450 C  CB    . LYS B 2 37  ? 3.519   -21.883 86.565  1.00 128.89 ? 36   LYS B CB    1 
ATOM   7451 C  CG    . LYS B 2 37  ? 2.255   -22.700 86.358  1.00 137.03 ? 36   LYS B CG    1 
ATOM   7452 C  CD    . LYS B 2 37  ? 1.047   -22.000 86.954  1.00 138.41 ? 36   LYS B CD    1 
ATOM   7453 C  CE    . LYS B 2 37  ? -0.245  -22.672 86.524  1.00 139.97 ? 36   LYS B CE    1 
ATOM   7454 N  NZ    . LYS B 2 37  ? -1.436  -21.884 86.938  1.00 129.71 ? 36   LYS B NZ    1 
ATOM   7455 N  N     . ILE B 2 38  ? 4.840   -18.521 85.630  1.00 101.28 ? 37   ILE B N     1 
ATOM   7456 C  CA    . ILE B 2 38  ? 6.036   -17.695 85.744  1.00 101.85 ? 37   ILE B CA    1 
ATOM   7457 C  C     . ILE B 2 38  ? 5.624   -16.231 85.673  1.00 97.19  ? 37   ILE B C     1 
ATOM   7458 O  O     . ILE B 2 38  ? 4.768   -15.849 84.870  1.00 96.78  ? 37   ILE B O     1 
ATOM   7459 C  CB    . ILE B 2 38  ? 7.073   -18.054 84.656  1.00 96.17  ? 37   ILE B CB    1 
ATOM   7460 C  CG1   . ILE B 2 38  ? 8.303   -17.150 84.759  1.00 107.97 ? 37   ILE B CG1   1 
ATOM   7461 C  CG2   . ILE B 2 38  ? 6.460   -17.964 83.273  1.00 105.30 ? 37   ILE B CG2   1 
ATOM   7462 C  CD1   . ILE B 2 38  ? 9.368   -17.463 83.736  1.00 115.20 ? 37   ILE B CD1   1 
ATOM   7463 N  N     . PHE B 2 39  ? 6.230   -15.415 86.533  1.00 99.76  ? 38   PHE B N     1 
ATOM   7464 C  CA    . PHE B 2 39  ? 5.978   -13.981 86.558  1.00 103.44 ? 38   PHE B CA    1 
ATOM   7465 C  C     . PHE B 2 39  ? 6.975   -13.268 85.654  1.00 98.94  ? 38   PHE B C     1 
ATOM   7466 O  O     . PHE B 2 39  ? 8.177   -13.550 85.699  1.00 100.00 ? 38   PHE B O     1 
ATOM   7467 C  CB    . PHE B 2 39  ? 6.073   -13.441 87.986  1.00 95.91  ? 38   PHE B CB    1 
ATOM   7468 C  CG    . PHE B 2 39  ? 6.160   -11.942 88.066  1.00 96.59  ? 38   PHE B CG    1 
ATOM   7469 C  CD1   . PHE B 2 39  ? 5.059   -11.152 87.780  1.00 95.75  ? 38   PHE B CD1   1 
ATOM   7470 C  CD2   . PHE B 2 39  ? 7.343   -11.324 88.435  1.00 100.57 ? 38   PHE B CD2   1 
ATOM   7471 C  CE1   . PHE B 2 39  ? 5.135   -9.775  87.857  1.00 96.51  ? 38   PHE B CE1   1 
ATOM   7472 C  CE2   . PHE B 2 39  ? 7.427   -9.946  88.513  1.00 107.21 ? 38   PHE B CE2   1 
ATOM   7473 C  CZ    . PHE B 2 39  ? 6.320   -9.171  88.224  1.00 103.46 ? 38   PHE B CZ    1 
ATOM   7474 N  N     . VAL B 2 40  ? 6.475   -12.348 84.840  1.00 91.79  ? 39   VAL B N     1 
ATOM   7475 C  CA    . VAL B 2 40  ? 7.294   -11.578 83.910  1.00 101.81 ? 39   VAL B CA    1 
ATOM   7476 C  C     . VAL B 2 40  ? 7.426   -10.160 84.456  1.00 97.76  ? 39   VAL B C     1 
ATOM   7477 O  O     . VAL B 2 40  ? 6.411   -9.471  84.623  1.00 97.64  ? 39   VAL B O     1 
ATOM   7478 C  CB    . VAL B 2 40  ? 6.696   -11.570 82.496  1.00 102.56 ? 39   VAL B CB    1 
ATOM   7479 C  CG1   . VAL B 2 40  ? 7.438   -10.579 81.641  1.00 103.78 ? 39   VAL B CG1   1 
ATOM   7480 C  CG2   . VAL B 2 40  ? 6.764   -12.961 81.883  1.00 87.60  ? 39   VAL B CG2   1 
ATOM   7481 N  N     . PRO B 2 41  ? 8.639   -9.683  84.743  1.00 98.95  ? 40   PRO B N     1 
ATOM   7482 C  CA    . PRO B 2 41  ? 8.790   -8.341  85.318  1.00 103.22 ? 40   PRO B CA    1 
ATOM   7483 C  C     . PRO B 2 41  ? 9.112   -7.265  84.291  1.00 109.30 ? 40   PRO B C     1 
ATOM   7484 O  O     . PRO B 2 41  ? 9.069   -6.072  84.611  1.00 108.10 ? 40   PRO B O     1 
ATOM   7485 C  CB    . PRO B 2 41  ? 9.949   -8.529  86.300  1.00 103.23 ? 40   PRO B CB    1 
ATOM   7486 C  CG    . PRO B 2 41  ? 10.818  -9.549  85.615  1.00 113.08 ? 40   PRO B CG    1 
ATOM   7487 C  CD    . PRO B 2 41  ? 9.895   -10.452 84.811  1.00 100.49 ? 40   PRO B CD    1 
ATOM   7488 N  N     . ASP B 2 42  ? 9.436   -7.663  83.063  1.00 109.99 ? 41   ASP B N     1 
ATOM   7489 C  CA    . ASP B 2 42  ? 9.890   -6.709  82.063  1.00 109.32 ? 41   ASP B CA    1 
ATOM   7490 C  C     . ASP B 2 42  ? 8.712   -5.952  81.450  1.00 111.46 ? 41   ASP B C     1 
ATOM   7491 O  O     . ASP B 2 42  ? 7.541   -6.243  81.709  1.00 110.35 ? 41   ASP B O     1 
ATOM   7492 C  CB    . ASP B 2 42  ? 10.700  -7.413  80.974  1.00 107.17 ? 41   ASP B CB    1 
ATOM   7493 C  CG    . ASP B 2 42  ? 9.963   -8.588  80.361  1.00 114.23 ? 41   ASP B CG    1 
ATOM   7494 O  OD1   . ASP B 2 42  ? 8.940   -8.366  79.679  1.00 115.75 ? 41   ASP B OD1   1 
ATOM   7495 O  OD2   . ASP B 2 42  ? 10.414  -9.737  80.554  1.00 114.11 ? 41   ASP B OD2   1 
ATOM   7496 N  N     . TYR B 2 43  ? 9.043   -4.968  80.619  1.00 114.66 ? 42   TYR B N     1 
ATOM   7497 C  CA    . TYR B 2 43  ? 8.073   -4.080  79.982  1.00 114.18 ? 42   TYR B CA    1 
ATOM   7498 C  C     . TYR B 2 43  ? 8.011   -4.426  78.496  1.00 118.50 ? 42   TYR B C     1 
ATOM   7499 O  O     . TYR B 2 43  ? 8.802   -3.929  77.693  1.00 122.90 ? 42   TYR B O     1 
ATOM   7500 C  CB    . TYR B 2 43  ? 8.456   -2.614  80.209  1.00 116.26 ? 42   TYR B CB    1 
ATOM   7501 C  CG    . TYR B 2 43  ? 7.642   -1.608  79.420  1.00 115.62 ? 42   TYR B CG    1 
ATOM   7502 C  CD1   . TYR B 2 43  ? 6.358   -1.257  79.817  1.00 115.78 ? 42   TYR B CD1   1 
ATOM   7503 C  CD2   . TYR B 2 43  ? 8.168   -0.993  78.291  1.00 126.41 ? 42   TYR B CD2   1 
ATOM   7504 C  CE1   . TYR B 2 43  ? 5.616   -0.332  79.103  1.00 122.36 ? 42   TYR B CE1   1 
ATOM   7505 C  CE2   . TYR B 2 43  ? 7.434   -0.069  77.570  1.00 130.07 ? 42   TYR B CE2   1 
ATOM   7506 C  CZ    . TYR B 2 43  ? 6.160   0.260   77.981  1.00 135.18 ? 42   TYR B CZ    1 
ATOM   7507 O  OH    . TYR B 2 43  ? 5.428   1.179   77.263  1.00 132.83 ? 42   TYR B OH    1 
ATOM   7508 N  N     . ASP B 2 44  ? 7.064   -5.295  78.135  1.00 124.42 ? 43   ASP B N     1 
ATOM   7509 C  CA    . ASP B 2 44  ? 6.780   -5.648  76.744  1.00 112.17 ? 43   ASP B CA    1 
ATOM   7510 C  C     . ASP B 2 44  ? 5.314   -5.341  76.469  1.00 107.07 ? 43   ASP B C     1 
ATOM   7511 O  O     . ASP B 2 44  ? 4.437   -6.181  76.728  1.00 101.62 ? 43   ASP B O     1 
ATOM   7512 C  CB    . ASP B 2 44  ? 7.089   -7.117  76.458  1.00 110.83 ? 43   ASP B CB    1 
ATOM   7513 C  CG    . ASP B 2 44  ? 8.575   -7.396  76.347  1.00 130.19 ? 43   ASP B CG    1 
ATOM   7514 O  OD1   . ASP B 2 44  ? 9.380   -6.576  76.836  1.00 147.44 ? 43   ASP B OD1   1 
ATOM   7515 O  OD2   . ASP B 2 44  ? 8.939   -8.437  75.759  1.00 129.09 ? 43   ASP B OD2   1 
ATOM   7516 N  N     . PRO B 2 45  ? 5.000   -4.151  75.959  1.00 110.80 ? 44   PRO B N     1 
ATOM   7517 C  CA    . PRO B 2 45  ? 3.604   -3.836  75.625  1.00 108.60 ? 44   PRO B CA    1 
ATOM   7518 C  C     . PRO B 2 45  ? 3.054   -4.805  74.588  1.00 103.57 ? 44   PRO B C     1 
ATOM   7519 O  O     . PRO B 2 45  ? 3.688   -5.081  73.567  1.00 96.86  ? 44   PRO B O     1 
ATOM   7520 C  CB    . PRO B 2 45  ? 3.684   -2.406  75.081  1.00 114.52 ? 44   PRO B CB    1 
ATOM   7521 C  CG    . PRO B 2 45  ? 4.920   -1.844  75.685  1.00 116.41 ? 44   PRO B CG    1 
ATOM   7522 C  CD    . PRO B 2 45  ? 5.886   -2.989  75.782  1.00 113.74 ? 44   PRO B CD    1 
ATOM   7523 N  N     . THR B 2 46  ? 1.861   -5.321  74.862  1.00 98.33  ? 45   THR B N     1 
ATOM   7524 C  CA    . THR B 2 46  ? 1.245   -6.344  74.031  1.00 91.25  ? 45   THR B CA    1 
ATOM   7525 C  C     . THR B 2 46  ? 0.309   -5.709  73.012  1.00 98.83  ? 45   THR B C     1 
ATOM   7526 O  O     . THR B 2 46  ? -0.446  -4.786  73.332  1.00 101.38 ? 45   THR B O     1 
ATOM   7527 C  CB    . THR B 2 46  ? 0.475   -7.341  74.901  1.00 91.77  ? 45   THR B CB    1 
ATOM   7528 O  OG1   . THR B 2 46  ? 1.346   -7.858  75.916  1.00 109.14 ? 45   THR B OG1   1 
ATOM   7529 C  CG2   . THR B 2 46  ? -0.055  -8.493  74.063  1.00 83.03  ? 45   THR B CG2   1 
ATOM   7530 N  N     . ILE B 2 47  ? 0.368   -6.206  71.776  1.00 89.79  ? 46   ILE B N     1 
ATOM   7531 C  CA    . ILE B 2 47  ? -0.531  -5.754  70.721  1.00 91.08  ? 46   ILE B CA    1 
ATOM   7532 C  C     . ILE B 2 47  ? -1.779  -6.627  70.737  1.00 86.03  ? 46   ILE B C     1 
ATOM   7533 O  O     . ILE B 2 47  ? -2.886  -6.136  70.986  1.00 92.56  ? 46   ILE B O     1 
ATOM   7534 C  CB    . ILE B 2 47  ? 0.163   -5.780  69.347  1.00 107.44 ? 46   ILE B CB    1 
ATOM   7535 C  CG1   . ILE B 2 47  ? 1.452   -4.955  69.399  1.00 96.48  ? 46   ILE B CG1   1 
ATOM   7536 C  CG2   . ILE B 2 47  ? -0.769  -5.245  68.271  1.00 94.96  ? 46   ILE B CG2   1 
ATOM   7537 C  CD1   . ILE B 2 47  ? 2.374   -5.180  68.229  1.00 88.79  ? 46   ILE B CD1   1 
ATOM   7538 N  N     . GLU B 2 48  ? -1.609  -7.926  70.473  1.00 83.21  ? 47   GLU B N     1 
ATOM   7539 C  CA    . GLU B 2 48  ? -2.675  -8.907  70.657  1.00 86.62  ? 47   GLU B CA    1 
ATOM   7540 C  C     . GLU B 2 48  ? -2.130  -10.328 70.569  1.00 89.31  ? 47   GLU B C     1 
ATOM   7541 O  O     . GLU B 2 48  ? -1.839  -10.822 69.475  1.00 86.58  ? 47   GLU B O     1 
ATOM   7542 C  CB    . GLU B 2 48  ? -3.796  -8.717  69.632  1.00 87.38  ? 47   GLU B CB    1 
ATOM   7543 C  CG    . GLU B 2 48  ? -4.866  -9.799  69.706  1.00 90.22  ? 47   GLU B CG    1 
ATOM   7544 C  CD    . GLU B 2 48  ? -6.226  -9.323  69.234  1.00 97.04  ? 47   GLU B CD    1 
ATOM   7545 O  OE1   . GLU B 2 48  ? -6.541  -8.129  69.428  1.00 97.53  ? 47   GLU B OE1   1 
ATOM   7546 O  OE2   . GLU B 2 48  ? -6.980  -10.145 68.671  1.00 89.66  ? 47   GLU B OE2   1 
ATOM   7547 N  N     . ASP B 2 49  ? -1.988  -10.989 71.716  1.00 96.03  ? 48   ASP B N     1 
ATOM   7548 C  CA    . ASP B 2 49  ? -1.474  -12.348 71.792  1.00 93.44  ? 48   ASP B CA    1 
ATOM   7549 C  C     . ASP B 2 49  ? -2.559  -13.293 72.295  1.00 90.73  ? 48   ASP B C     1 
ATOM   7550 O  O     . ASP B 2 49  ? -3.455  -12.893 73.044  1.00 96.64  ? 48   ASP B O     1 
ATOM   7551 C  CB    . ASP B 2 49  ? -0.249  -12.419 72.711  1.00 90.71  ? 48   ASP B CB    1 
ATOM   7552 C  CG    . ASP B 2 49  ? 0.858   -11.462 72.292  1.00 100.41 ? 48   ASP B CG    1 
ATOM   7553 O  OD1   . ASP B 2 49  ? 0.689   -10.746 71.282  1.00 93.46  ? 48   ASP B OD1   1 
ATOM   7554 O  OD2   . ASP B 2 49  ? 1.902   -11.424 72.977  1.00 103.25 ? 48   ASP B OD2   1 
ATOM   7555 N  N     . SER B 2 50  ? -2.473  -14.555 71.876  1.00 81.95  ? 49   SER B N     1 
ATOM   7556 C  CA    . SER B 2 50  ? -3.439  -15.576 72.255  1.00 84.83  ? 49   SER B CA    1 
ATOM   7557 C  C     . SER B 2 50  ? -2.732  -16.748 72.922  1.00 85.20  ? 49   SER B C     1 
ATOM   7558 O  O     . SER B 2 50  ? -1.559  -17.024 72.653  1.00 79.25  ? 49   SER B O     1 
ATOM   7559 C  CB    . SER B 2 50  ? -4.235  -16.075 71.041  1.00 87.93  ? 49   SER B CB    1 
ATOM   7560 O  OG    . SER B 2 50  ? -3.419  -16.836 70.166  1.00 85.47  ? 49   SER B OG    1 
ATOM   7561 N  N     . TYR B 2 51  ? -3.461  -17.439 73.797  1.00 86.04  ? 50   TYR B N     1 
ATOM   7562 C  CA    . TYR B 2 51  ? -2.928  -18.562 74.555  1.00 89.94  ? 50   TYR B CA    1 
ATOM   7563 C  C     . TYR B 2 51  ? -3.992  -19.644 74.658  1.00 85.94  ? 50   TYR B C     1 
ATOM   7564 O  O     . TYR B 2 51  ? -5.173  -19.346 74.855  1.00 83.63  ? 50   TYR B O     1 
ATOM   7565 C  CB    . TYR B 2 51  ? -2.477  -18.132 75.959  1.00 81.49  ? 50   TYR B CB    1 
ATOM   7566 C  CG    . TYR B 2 51  ? -1.427  -17.041 75.972  1.00 79.22  ? 50   TYR B CG    1 
ATOM   7567 C  CD1   . TYR B 2 51  ? -1.788  -15.701 75.898  1.00 80.08  ? 50   TYR B CD1   1 
ATOM   7568 C  CD2   . TYR B 2 51  ? -0.077  -17.351 76.065  1.00 77.71  ? 50   TYR B CD2   1 
ATOM   7569 C  CE1   . TYR B 2 51  ? -0.834  -14.701 75.910  1.00 80.19  ? 50   TYR B CE1   1 
ATOM   7570 C  CE2   . TYR B 2 51  ? 0.885   -16.357 76.081  1.00 76.64  ? 50   TYR B CE2   1 
ATOM   7571 C  CZ    . TYR B 2 51  ? 0.501   -15.034 76.003  1.00 82.93  ? 50   TYR B CZ    1 
ATOM   7572 O  OH    . TYR B 2 51  ? 1.453   -14.041 76.015  1.00 85.26  ? 50   TYR B OH    1 
ATOM   7573 N  N     . LEU B 2 52  ? -3.569  -20.900 74.531  1.00 86.56  ? 51   LEU B N     1 
ATOM   7574 C  CA    . LEU B 2 52  ? -4.484  -22.032 74.518  1.00 91.71  ? 51   LEU B CA    1 
ATOM   7575 C  C     . LEU B 2 52  ? -4.014  -23.083 75.513  1.00 101.35 ? 51   LEU B C     1 
ATOM   7576 O  O     . LEU B 2 52  ? -2.810  -23.309 75.668  1.00 114.35 ? 51   LEU B O     1 
ATOM   7577 C  CB    . LEU B 2 52  ? -4.590  -22.635 73.111  1.00 95.32  ? 51   LEU B CB    1 
ATOM   7578 C  CG    . LEU B 2 52  ? -5.882  -23.366 72.738  1.00 98.21  ? 51   LEU B CG    1 
ATOM   7579 C  CD1   . LEU B 2 52  ? -6.111  -23.292 71.236  1.00 99.52  ? 51   LEU B CD1   1 
ATOM   7580 C  CD2   . LEU B 2 52  ? -5.852  -24.815 73.198  1.00 103.12 ? 51   LEU B CD2   1 
ATOM   7581 N  N     . LYS B 2 53  ? -4.972  -23.724 76.181  1.00 97.93  ? 52   LYS B N     1 
ATOM   7582 C  CA    . LYS B 2 53  ? -4.668  -24.738 77.180  1.00 99.74  ? 52   LYS B CA    1 
ATOM   7583 C  C     . LYS B 2 53  ? -5.917  -25.571 77.435  1.00 101.78 ? 52   LYS B C     1 
ATOM   7584 O  O     . LYS B 2 53  ? -7.042  -25.091 77.269  1.00 97.86  ? 52   LYS B O     1 
ATOM   7585 C  CB    . LYS B 2 53  ? -4.166  -24.099 78.482  1.00 96.32  ? 52   LYS B CB    1 
ATOM   7586 C  CG    . LYS B 2 53  ? -3.819  -25.073 79.596  1.00 102.53 ? 52   LYS B CG    1 
ATOM   7587 C  CD    . LYS B 2 53  ? -3.369  -24.339 80.852  1.00 115.65 ? 52   LYS B CD    1 
ATOM   7588 C  CE    . LYS B 2 53  ? -4.358  -23.250 81.242  1.00 92.67  ? 52   LYS B CE    1 
ATOM   7589 N  NZ    . LYS B 2 53  ? -5.750  -23.768 81.328  1.00 98.88  ? 52   LYS B NZ    1 
ATOM   7590 N  N     . HIS B 2 54  ? -5.703  -26.826 77.823  1.00 107.57 ? 53   HIS B N     1 
ATOM   7591 C  CA    . HIS B 2 54  ? -6.770  -27.734 78.226  1.00 107.78 ? 53   HIS B CA    1 
ATOM   7592 C  C     . HIS B 2 54  ? -6.672  -27.961 79.729  1.00 101.12 ? 53   HIS B C     1 
ATOM   7593 O  O     . HIS B 2 54  ? -5.642  -28.433 80.222  1.00 100.74 ? 53   HIS B O     1 
ATOM   7594 C  CB    . HIS B 2 54  ? -6.675  -29.065 77.479  1.00 108.09 ? 53   HIS B CB    1 
ATOM   7595 C  CG    . HIS B 2 54  ? -6.960  -28.963 76.013  1.00 111.43 ? 53   HIS B CG    1 
ATOM   7596 N  ND1   . HIS B 2 54  ? -7.074  -30.070 75.200  1.00 113.10 ? 53   HIS B ND1   1 
ATOM   7597 C  CD2   . HIS B 2 54  ? -7.154  -27.888 75.213  1.00 120.41 ? 53   HIS B CD2   1 
ATOM   7598 C  CE1   . HIS B 2 54  ? -7.328  -29.682 73.963  1.00 115.20 ? 53   HIS B CE1   1 
ATOM   7599 N  NE2   . HIS B 2 54  ? -7.380  -28.362 73.943  1.00 115.00 ? 53   HIS B NE2   1 
ATOM   7600 N  N     . THR B 2 55  ? -7.738  -27.626 80.454  1.00 99.22  ? 54   THR B N     1 
ATOM   7601 C  CA    . THR B 2 55  ? -7.778  -27.822 81.895  1.00 96.27  ? 54   THR B CA    1 
ATOM   7602 C  C     . THR B 2 55  ? -9.172  -28.267 82.310  1.00 93.02  ? 54   THR B C     1 
ATOM   7603 O  O     . THR B 2 55  ? -10.161 -27.988 81.628  1.00 92.68  ? 54   THR B O     1 
ATOM   7604 C  CB    . THR B 2 55  ? -7.387  -26.546 82.660  1.00 94.78  ? 54   THR B CB    1 
ATOM   7605 O  OG1   . THR B 2 55  ? -7.189  -26.859 84.044  1.00 106.42 ? 54   THR B OG1   1 
ATOM   7606 C  CG2   . THR B 2 55  ? -8.476  -25.490 82.542  1.00 89.68  ? 54   THR B CG2   1 
ATOM   7607 N  N     . GLU B 2 56  ? -9.239  -28.972 83.434  1.00 99.54  ? 55   GLU B N     1 
ATOM   7608 C  CA    . GLU B 2 56  ? -10.502 -29.435 83.992  1.00 95.37  ? 55   GLU B CA    1 
ATOM   7609 C  C     . GLU B 2 56  ? -10.930 -28.475 85.095  1.00 90.92  ? 55   GLU B C     1 
ATOM   7610 O  O     . GLU B 2 56  ? -10.166 -28.219 86.031  1.00 95.62  ? 55   GLU B O     1 
ATOM   7611 C  CB    . GLU B 2 56  ? -10.377 -30.858 84.534  1.00 88.94  ? 55   GLU B CB    1 
ATOM   7612 C  CG    . GLU B 2 56  ? -11.709 -31.494 84.897  1.00 99.32  ? 55   GLU B CG    1 
ATOM   7613 C  CD    . GLU B 2 56  ? -11.554 -32.838 85.586  1.00 109.54 ? 55   GLU B CD    1 
ATOM   7614 O  OE1   . GLU B 2 56  ? -10.487 -33.085 86.186  1.00 108.16 ? 55   GLU B OE1   1 
ATOM   7615 O  OE2   . GLU B 2 56  ? -12.501 -33.650 85.526  1.00 116.67 ? 55   GLU B OE2   1 
ATOM   7616 N  N     . ILE B 2 57  ? -12.141 -27.940 84.974  1.00 93.77  ? 56   ILE B N     1 
ATOM   7617 C  CA    . ILE B 2 57  ? -12.706 -27.015 85.949  1.00 98.09  ? 56   ILE B CA    1 
ATOM   7618 C  C     . ILE B 2 57  ? -14.003 -27.614 86.472  1.00 101.98 ? 56   ILE B C     1 
ATOM   7619 O  O     . ILE B 2 57  ? -14.894 -27.955 85.686  1.00 101.67 ? 56   ILE B O     1 
ATOM   7620 C  CB    . ILE B 2 57  ? -12.954 -25.623 85.341  1.00 92.74  ? 56   ILE B CB    1 
ATOM   7621 C  CG1   . ILE B 2 57  ? -11.661 -25.060 84.750  1.00 90.77  ? 56   ILE B CG1   1 
ATOM   7622 C  CG2   . ILE B 2 57  ? -13.520 -24.677 86.393  1.00 99.14  ? 56   ILE B CG2   1 
ATOM   7623 C  CD1   . ILE B 2 57  ? -11.808 -23.670 84.175  1.00 92.35  ? 56   ILE B CD1   1 
ATOM   7624 N  N     . ASP B 2 58  ? -14.103 -27.739 87.796  1.00 99.32  ? 57   ASP B N     1 
ATOM   7625 C  CA    . ASP B 2 58  ? -15.273 -28.331 88.446  1.00 102.47 ? 57   ASP B CA    1 
ATOM   7626 C  C     . ASP B 2 58  ? -15.594 -29.702 87.854  1.00 107.37 ? 57   ASP B C     1 
ATOM   7627 O  O     . ASP B 2 58  ? -16.753 -30.036 87.594  1.00 103.84 ? 57   ASP B O     1 
ATOM   7628 C  CB    . ASP B 2 58  ? -16.482 -27.397 88.359  1.00 100.83 ? 57   ASP B CB    1 
ATOM   7629 C  CG    . ASP B 2 58  ? -16.251 -26.076 89.072  1.00 104.53 ? 57   ASP B CG    1 
ATOM   7630 O  OD1   . ASP B 2 58  ? -15.479 -26.052 90.054  1.00 99.63  ? 57   ASP B OD1   1 
ATOM   7631 O  OD2   . ASP B 2 58  ? -16.842 -25.060 88.649  1.00 110.06 ? 57   ASP B OD2   1 
ATOM   7632 N  N     . ASN B 2 59  ? -14.545 -30.496 87.630  1.00 119.66 ? 58   ASN B N     1 
ATOM   7633 C  CA    . ASN B 2 59  ? -14.656 -31.847 87.076  1.00 127.13 ? 58   ASN B CA    1 
ATOM   7634 C  C     . ASN B 2 59  ? -15.264 -31.846 85.675  1.00 118.62 ? 58   ASN B C     1 
ATOM   7635 O  O     . ASN B 2 59  ? -15.931 -32.804 85.276  1.00 120.26 ? 58   ASN B O     1 
ATOM   7636 C  CB    . ASN B 2 59  ? -15.455 -32.767 88.005  1.00 113.93 ? 58   ASN B CB    1 
ATOM   7637 C  CG    . ASN B 2 59  ? -14.796 -32.940 89.358  1.00 127.95 ? 58   ASN B CG    1 
ATOM   7638 O  OD1   . ASN B 2 59  ? -15.372 -32.601 90.391  1.00 137.30 ? 58   ASN B OD1   1 
ATOM   7639 N  ND2   . ASN B 2 59  ? -13.578 -33.470 89.357  1.00 131.26 ? 58   ASN B ND2   1 
ATOM   7640 N  N     . GLN B 2 60  ? -15.029 -30.781 84.910  1.00 104.74 ? 59   GLN B N     1 
ATOM   7641 C  CA    . GLN B 2 60  ? -15.563 -30.663 83.555  1.00 106.70 ? 59   GLN B CA    1 
ATOM   7642 C  C     . GLN B 2 60  ? -14.489 -30.052 82.664  1.00 98.39  ? 59   GLN B C     1 
ATOM   7643 O  O     . GLN B 2 60  ? -14.176 -28.864 82.791  1.00 93.95  ? 59   GLN B O     1 
ATOM   7644 C  CB    . GLN B 2 60  ? -16.835 -29.817 83.532  1.00 110.16 ? 59   GLN B CB    1 
ATOM   7645 C  CG    . GLN B 2 60  ? -17.382 -29.566 82.138  1.00 117.32 ? 59   GLN B CG    1 
ATOM   7646 C  CD    . GLN B 2 60  ? -18.610 -28.679 82.147  1.00 131.46 ? 59   GLN B CD    1 
ATOM   7647 O  OE1   . GLN B 2 60  ? -19.148 -28.353 83.206  1.00 112.15 ? 59   GLN B OE1   1 
ATOM   7648 N  NE2   . GLN B 2 60  ? -19.061 -28.280 80.961  1.00 139.28 ? 59   GLN B NE2   1 
ATOM   7649 N  N     . TRP B 2 61  ? -13.938 -30.860 81.762  1.00 99.93  ? 60   TRP B N     1 
ATOM   7650 C  CA    . TRP B 2 61  ? -12.874 -30.392 80.885  1.00 96.29  ? 60   TRP B CA    1 
ATOM   7651 C  C     . TRP B 2 61  ? -13.380 -29.308 79.939  1.00 94.09  ? 60   TRP B C     1 
ATOM   7652 O  O     . TRP B 2 61  ? -14.564 -29.250 79.595  1.00 94.53  ? 60   TRP B O     1 
ATOM   7653 C  CB    . TRP B 2 61  ? -12.298 -31.556 80.082  1.00 87.42  ? 60   TRP B CB    1 
ATOM   7654 C  CG    . TRP B 2 61  ? -11.442 -32.479 80.888  1.00 97.51  ? 60   TRP B CG    1 
ATOM   7655 C  CD1   . TRP B 2 61  ? -11.847 -33.586 81.573  1.00 104.28 ? 60   TRP B CD1   1 
ATOM   7656 C  CD2   . TRP B 2 61  ? -10.027 -32.377 81.089  1.00 97.95  ? 60   TRP B CD2   1 
ATOM   7657 N  NE1   . TRP B 2 61  ? -10.773 -34.180 82.191  1.00 103.69 ? 60   TRP B NE1   1 
ATOM   7658 C  CE2   . TRP B 2 61  ? -9.644  -33.457 81.909  1.00 103.33 ? 60   TRP B CE2   1 
ATOM   7659 C  CE3   . TRP B 2 61  ? -9.048  -31.477 80.657  1.00 96.69  ? 60   TRP B CE3   1 
ATOM   7660 C  CZ2   . TRP B 2 61  ? -8.323  -33.661 82.305  1.00 102.91 ? 60   TRP B CZ2   1 
ATOM   7661 C  CZ3   . TRP B 2 61  ? -7.738  -31.682 81.050  1.00 98.08  ? 60   TRP B CZ3   1 
ATOM   7662 C  CH2   . TRP B 2 61  ? -7.388  -32.765 81.866  1.00 102.94 ? 60   TRP B CH2   1 
ATOM   7663 N  N     . ALA B 2 62  ? -12.460 -28.446 79.513  1.00 86.39  ? 61   ALA B N     1 
ATOM   7664 C  CA    . ALA B 2 62  ? -12.794 -27.342 78.627  1.00 91.83  ? 61   ALA B CA    1 
ATOM   7665 C  C     . ALA B 2 62  ? -11.518 -26.801 78.000  1.00 97.18  ? 61   ALA B C     1 
ATOM   7666 O  O     . ALA B 2 62  ? -10.430 -26.920 78.570  1.00 95.55  ? 61   ALA B O     1 
ATOM   7667 C  CB    . ALA B 2 62  ? -13.532 -26.227 79.374  1.00 92.94  ? 61   ALA B CB    1 
ATOM   7668 N  N     . ILE B 2 63  ? -11.667 -26.205 76.820  1.00 93.23  ? 62   ILE B N     1 
ATOM   7669 C  CA    . ILE B 2 63  ? -10.569 -25.565 76.108  1.00 91.84  ? 62   ILE B CA    1 
ATOM   7670 C  C     . ILE B 2 63  ? -10.615 -24.073 76.403  1.00 88.44  ? 62   ILE B C     1 
ATOM   7671 O  O     . ILE B 2 63  ? -11.675 -23.443 76.295  1.00 93.51  ? 62   ILE B O     1 
ATOM   7672 C  CB    . ILE B 2 63  ? -10.653 -25.834 74.595  1.00 100.96 ? 62   ILE B CB    1 
ATOM   7673 C  CG1   . ILE B 2 63  ? -10.552 -27.335 74.316  1.00 105.83 ? 62   ILE B CG1   1 
ATOM   7674 C  CG2   . ILE B 2 63  ? -9.566  -25.068 73.847  1.00 89.62  ? 62   ILE B CG2   1 
ATOM   7675 C  CD1   . ILE B 2 63  ? -10.586 -27.688 72.848  1.00 105.32 ? 62   ILE B CD1   1 
ATOM   7676 N  N     . LEU B 2 64  ? -9.473  -23.506 76.779  1.00 84.96  ? 63   LEU B N     1 
ATOM   7677 C  CA    . LEU B 2 64  ? -9.374  -22.098 77.141  1.00 90.20  ? 63   LEU B CA    1 
ATOM   7678 C  C     . LEU B 2 64  ? -8.544  -21.370 76.095  1.00 90.52  ? 63   LEU B C     1 
ATOM   7679 O  O     . LEU B 2 64  ? -7.352  -21.653 75.936  1.00 89.79  ? 63   LEU B O     1 
ATOM   7680 C  CB    . LEU B 2 64  ? -8.756  -21.925 78.529  1.00 96.28  ? 63   LEU B CB    1 
ATOM   7681 C  CG    . LEU B 2 64  ? -9.670  -22.060 79.752  1.00 87.74  ? 63   LEU B CG    1 
ATOM   7682 C  CD1   . LEU B 2 64  ? -10.206 -23.477 79.913  1.00 86.62  ? 63   LEU B CD1   1 
ATOM   7683 C  CD2   . LEU B 2 64  ? -8.935  -21.620 81.008  1.00 99.26  ? 63   LEU B CD2   1 
ATOM   7684 N  N     . ASP B 2 65  ? -9.175  -20.440 75.386  1.00 90.17  ? 64   ASP B N     1 
ATOM   7685 C  CA    . ASP B 2 65  ? -8.499  -19.573 74.424  1.00 90.85  ? 64   ASP B CA    1 
ATOM   7686 C  C     . ASP B 2 65  ? -8.511  -18.168 75.016  1.00 86.05  ? 64   ASP B C     1 
ATOM   7687 O  O     . ASP B 2 65  ? -9.525  -17.467 74.953  1.00 96.11  ? 64   ASP B O     1 
ATOM   7688 C  CB    . ASP B 2 65  ? -9.183  -19.624 73.060  1.00 99.49  ? 64   ASP B CB    1 
ATOM   7689 C  CG    . ASP B 2 65  ? -8.380  -18.922 71.977  1.00 110.54 ? 64   ASP B CG    1 
ATOM   7690 O  OD1   . ASP B 2 65  ? -7.312  -19.445 71.592  1.00 104.78 ? 64   ASP B OD1   1 
ATOM   7691 O  OD2   . ASP B 2 65  ? -8.819  -17.850 71.508  1.00 110.33 ? 64   ASP B OD2   1 
ATOM   7692 N  N     . VAL B 2 66  ? -7.388  -17.765 75.602  1.00 85.54  ? 65   VAL B N     1 
ATOM   7693 C  CA    . VAL B 2 66  ? -7.277  -16.494 76.307  1.00 87.81  ? 65   VAL B CA    1 
ATOM   7694 C  C     . VAL B 2 66  ? -6.561  -15.495 75.411  1.00 84.27  ? 65   VAL B C     1 
ATOM   7695 O  O     . VAL B 2 66  ? -5.486  -15.786 74.873  1.00 92.44  ? 65   VAL B O     1 
ATOM   7696 C  CB    . VAL B 2 66  ? -6.546  -16.664 77.649  1.00 84.30  ? 65   VAL B CB    1 
ATOM   7697 C  CG1   . VAL B 2 66  ? -6.402  -15.323 78.349  1.00 85.11  ? 65   VAL B CG1   1 
ATOM   7698 C  CG2   . VAL B 2 66  ? -7.299  -17.648 78.530  1.00 81.89  ? 65   VAL B CG2   1 
ATOM   7699 N  N     . LEU B 2 67  ? -7.155  -14.315 75.254  1.00 83.01  ? 66   LEU B N     1 
ATOM   7700 C  CA    . LEU B 2 67  ? -6.667  -13.288 74.344  1.00 85.24  ? 66   LEU B CA    1 
ATOM   7701 C  C     . LEU B 2 67  ? -6.136  -12.117 75.163  1.00 82.32  ? 66   LEU B C     1 
ATOM   7702 O  O     . LEU B 2 67  ? -6.896  -11.471 75.894  1.00 84.83  ? 66   LEU B O     1 
ATOM   7703 C  CB    . LEU B 2 67  ? -7.782  -12.842 73.396  1.00 82.79  ? 66   LEU B CB    1 
ATOM   7704 C  CG    . LEU B 2 67  ? -7.407  -12.130 72.095  1.00 91.36  ? 66   LEU B CG    1 
ATOM   7705 C  CD1   . LEU B 2 67  ? -8.467  -12.387 71.037  1.00 110.24 ? 66   LEU B CD1   1 
ATOM   7706 C  CD2   . LEU B 2 67  ? -7.244  -10.639 72.322  1.00 90.78  ? 66   LEU B CD2   1 
ATOM   7707 N  N     . ASP B 2 68  ? -4.838  -11.848 75.039  1.00 78.32  ? 67   ASP B N     1 
ATOM   7708 C  CA    . ASP B 2 68  ? -4.176  -10.776 75.782  1.00 83.38  ? 67   ASP B CA    1 
ATOM   7709 C  C     . ASP B 2 68  ? -4.227  -9.509  74.937  1.00 86.18  ? 67   ASP B C     1 
ATOM   7710 O  O     . ASP B 2 68  ? -3.406  -9.314  74.036  1.00 89.00  ? 67   ASP B O     1 
ATOM   7711 C  CB    . ASP B 2 68  ? -2.742  -11.170 76.124  1.00 86.19  ? 67   ASP B CB    1 
ATOM   7712 C  CG    . ASP B 2 68  ? -2.047  -10.152 77.013  1.00 90.67  ? 67   ASP B CG    1 
ATOM   7713 O  OD1   . ASP B 2 68  ? -2.724  -9.240  77.536  1.00 86.06  ? 67   ASP B OD1   1 
ATOM   7714 O  OD2   . ASP B 2 68  ? -0.814  -10.267 77.185  1.00 88.06  ? 67   ASP B OD2   1 
ATOM   7715 N  N     . THR B 2 69  ? -5.185  -8.636  75.238  1.00 83.41  ? 68   THR B N     1 
ATOM   7716 C  CA    . THR B 2 69  ? -5.409  -7.440  74.438  1.00 87.67  ? 68   THR B CA    1 
ATOM   7717 C  C     . THR B 2 69  ? -4.309  -6.408  74.685  1.00 91.83  ? 68   THR B C     1 
ATOM   7718 O  O     . THR B 2 69  ? -3.349  -6.636  75.429  1.00 108.96 ? 68   THR B O     1 
ATOM   7719 C  CB    . THR B 2 69  ? -6.779  -6.844  74.750  1.00 91.63  ? 68   THR B CB    1 
ATOM   7720 O  OG1   . THR B 2 69  ? -6.803  -6.383  76.106  1.00 104.80 ? 68   THR B OG1   1 
ATOM   7721 C  CG2   . THR B 2 69  ? -7.860  -7.887  74.563  1.00 91.62  ? 68   THR B CG2   1 
ATOM   7722 N  N     . ALA B 2 70  ? -4.461  -5.251  74.047  1.00 90.12  ? 69   ALA B N     1 
ATOM   7723 C  CA    . ALA B 2 70  ? -3.529  -4.141  74.177  1.00 96.07  ? 69   ALA B CA    1 
ATOM   7724 C  C     . ALA B 2 70  ? -4.002  -3.166  75.252  1.00 113.49 ? 69   ALA B C     1 
ATOM   7725 O  O     . ALA B 2 70  ? -5.127  -3.241  75.752  1.00 112.65 ? 69   ALA B O     1 
ATOM   7726 C  CB    . ALA B 2 70  ? -3.365  -3.419  72.838  1.00 101.05 ? 69   ALA B CB    1 
ATOM   7727 N  N     . GLY B 2 71  ? -3.120  -2.233  75.599  1.00 115.96 ? 70   GLY B N     1 
ATOM   7728 C  CA    . GLY B 2 71  ? -3.427  -1.254  76.623  1.00 117.95 ? 70   GLY B CA    1 
ATOM   7729 C  C     . GLY B 2 71  ? -2.909  0.135   76.312  1.00 136.70 ? 70   GLY B C     1 
ATOM   7730 O  O     . GLY B 2 71  ? -3.350  1.116   76.918  1.00 153.39 ? 70   GLY B O     1 
ATOM   7731 N  N     . GLN B 2 72  ? -1.978  0.235   75.362  1.00 142.05 ? 71   GLN B N     1 
ATOM   7732 C  CA    . GLN B 2 72  ? -1.391  1.522   75.004  1.00 158.24 ? 71   GLN B CA    1 
ATOM   7733 C  C     . GLN B 2 72  ? -2.366  2.452   74.291  1.00 166.38 ? 71   GLN B C     1 
ATOM   7734 O  O     . GLN B 2 72  ? -1.988  3.593   73.998  1.00 170.15 ? 71   GLN B O     1 
ATOM   7735 C  CB    . GLN B 2 72  ? -0.158  1.310   74.125  1.00 159.50 ? 71   GLN B CB    1 
ATOM   7736 C  CG    . GLN B 2 72  ? 1.028   0.698   74.847  1.00 155.33 ? 71   GLN B CG    1 
ATOM   7737 C  CD    . GLN B 2 72  ? 2.257   0.611   73.965  1.00 157.55 ? 71   GLN B CD    1 
ATOM   7738 O  OE1   . GLN B 2 72  ? 2.161   0.310   72.774  1.00 162.32 ? 71   GLN B OE1   1 
ATOM   7739 N  NE2   . GLN B 2 72  ? 3.420   0.884   74.543  1.00 154.60 ? 71   GLN B NE2   1 
ATOM   7740 N  N     . GLU B 2 73  ? -3.582  1.988   73.983  1.00 170.84 ? 72   GLU B N     1 
ATOM   7741 C  CA    . GLU B 2 73  ? -4.621  2.772   73.318  1.00 173.76 ? 72   GLU B CA    1 
ATOM   7742 C  C     . GLU B 2 73  ? -4.237  3.115   71.880  1.00 172.74 ? 72   GLU B C     1 
ATOM   7743 O  O     . GLU B 2 73  ? -5.088  3.550   71.096  1.00 166.82 ? 72   GLU B O     1 
ATOM   7744 C  CB    . GLU B 2 73  ? -4.936  4.047   74.112  1.00 178.92 ? 72   GLU B CB    1 
ATOM   7745 C  CG    . GLU B 2 73  ? -6.252  4.723   73.736  1.00 179.84 ? 72   GLU B CG    1 
ATOM   7746 C  CD    . GLU B 2 73  ? -7.467  3.891   74.102  1.00 179.66 ? 72   GLU B CD    1 
ATOM   7747 O  OE1   . GLU B 2 73  ? -7.383  3.102   75.067  1.00 185.53 ? 72   GLU B OE1   1 
ATOM   7748 O  OE2   . GLU B 2 73  ? -8.506  4.027   73.422  1.00 169.91 ? 72   GLU B OE2   1 
ATOM   7749 N  N     . GLU B 2 74  ? -2.965  2.917   71.519  1.00 183.70 ? 73   GLU B N     1 
ATOM   7750 C  CA    . GLU B 2 74  ? -2.552  3.087   70.130  1.00 180.75 ? 73   GLU B CA    1 
ATOM   7751 C  C     . GLU B 2 74  ? -3.318  2.147   69.213  1.00 180.37 ? 73   GLU B C     1 
ATOM   7752 O  O     . GLU B 2 74  ? -3.579  2.482   68.052  1.00 179.12 ? 73   GLU B O     1 
ATOM   7753 C  CB    . GLU B 2 74  ? -1.049  2.844   69.991  1.00 180.28 ? 73   GLU B CB    1 
ATOM   7754 C  CG    . GLU B 2 74  ? -0.210  3.454   71.099  1.00 189.20 ? 73   GLU B CG    1 
ATOM   7755 C  CD    . GLU B 2 74  ? 1.272   3.201   70.912  1.00 195.81 ? 73   GLU B CD    1 
ATOM   7756 O  OE1   . GLU B 2 74  ? 1.664   2.732   69.822  1.00 188.28 ? 73   GLU B OE1   1 
ATOM   7757 O  OE2   . GLU B 2 74  ? 2.045   3.468   71.856  1.00 193.87 ? 73   GLU B OE2   1 
ATOM   7758 N  N     . PHE B 2 75  ? -3.681  0.973   69.714  1.00 157.74 ? 74   PHE B N     1 
ATOM   7759 C  CA    . PHE B 2 75  ? -4.490  0.003   68.979  1.00 148.46 ? 74   PHE B CA    1 
ATOM   7760 C  C     . PHE B 2 75  ? -5.937  0.042   69.449  1.00 148.34 ? 74   PHE B C     1 
ATOM   7761 O  O     . PHE B 2 75  ? -6.521  -0.976  69.820  1.00 146.89 ? 74   PHE B O     1 
ATOM   7762 C  CB    . PHE B 2 75  ? -3.896  -1.392  69.130  1.00 136.98 ? 74   PHE B CB    1 
ATOM   7763 C  CG    . PHE B 2 75  ? -2.432  -1.462  68.801  1.00 139.50 ? 74   PHE B CG    1 
ATOM   7764 C  CD1   . PHE B 2 75  ? -2.012  -1.669  67.497  1.00 139.36 ? 74   PHE B CD1   1 
ATOM   7765 C  CD2   . PHE B 2 75  ? -1.476  -1.310  69.793  1.00 134.01 ? 74   PHE B CD2   1 
ATOM   7766 C  CE1   . PHE B 2 75  ? -0.665  -1.729  67.189  1.00 130.29 ? 74   PHE B CE1   1 
ATOM   7767 C  CE2   . PHE B 2 75  ? -0.128  -1.368  69.491  1.00 133.54 ? 74   PHE B CE2   1 
ATOM   7768 C  CZ    . PHE B 2 75  ? 0.278   -1.578  68.187  1.00 125.88 ? 74   PHE B CZ    1 
ATOM   7769 N  N     . SER B 2 76  ? -6.528  1.240   69.443  1.00 150.85 ? 75   SER B N     1 
ATOM   7770 C  CA    . SER B 2 76  ? -7.920  1.411   69.845  1.00 150.95 ? 75   SER B CA    1 
ATOM   7771 C  C     . SER B 2 76  ? -8.889  0.652   68.947  1.00 149.24 ? 75   SER B C     1 
ATOM   7772 O  O     . SER B 2 76  ? -10.061 0.508   69.313  1.00 147.12 ? 75   SER B O     1 
ATOM   7773 C  CB    . SER B 2 76  ? -8.282  2.898   69.862  1.00 151.62 ? 75   SER B CB    1 
ATOM   7774 O  OG    . SER B 2 76  ? -9.626  3.093   70.264  1.00 150.33 ? 75   SER B OG    1 
ATOM   7775 N  N     . ALA B 2 77  ? -8.437  0.176   67.787  1.00 147.24 ? 76   ALA B N     1 
ATOM   7776 C  CA    . ALA B 2 77  ? -9.230  -0.731  66.969  1.00 140.64 ? 76   ALA B CA    1 
ATOM   7777 C  C     . ALA B 2 77  ? -9.108  -2.146  67.521  1.00 141.35 ? 76   ALA B C     1 
ATOM   7778 O  O     . ALA B 2 77  ? -8.703  -2.331  68.674  1.00 144.30 ? 76   ALA B O     1 
ATOM   7779 C  CB    . ALA B 2 77  ? -8.783  -0.676  65.507  1.00 136.98 ? 76   ALA B CB    1 
ATOM   7780 N  N     . MET B 2 78  ? -9.481  -3.145  66.717  1.00 139.50 ? 77   MET B N     1 
ATOM   7781 C  CA    . MET B 2 78  ? -9.424  -4.555  67.099  1.00 136.15 ? 77   MET B CA    1 
ATOM   7782 C  C     . MET B 2 78  ? -10.342 -4.879  68.274  1.00 135.58 ? 77   MET B C     1 
ATOM   7783 O  O     . MET B 2 78  ? -10.578 -6.055  68.567  1.00 132.66 ? 77   MET B O     1 
ATOM   7784 C  CB    . MET B 2 78  ? -7.989  -4.977  67.436  1.00 130.36 ? 77   MET B CB    1 
ATOM   7785 C  CG    . MET B 2 78  ? -6.975  -4.706  66.338  1.00 136.57 ? 77   MET B CG    1 
ATOM   7786 S  SD    . MET B 2 78  ? -5.325  -5.324  66.735  1.00 123.77 ? 77   MET B SD    1 
ATOM   7787 C  CE    . MET B 2 78  ? -5.557  -7.090  66.536  1.00 90.50  ? 77   MET B CE    1 
ATOM   7788 N  N     . ARG B 2 79  ? -10.860 -3.853  68.958  1.00 141.62 ? 78   ARG B N     1 
ATOM   7789 C  CA    . ARG B 2 79  ? -11.751 -4.088  70.089  1.00 135.17 ? 78   ARG B CA    1 
ATOM   7790 C  C     . ARG B 2 79  ? -13.043 -4.751  69.638  1.00 139.06 ? 78   ARG B C     1 
ATOM   7791 O  O     . ARG B 2 79  ? -13.520 -5.697  70.273  1.00 139.07 ? 78   ARG B O     1 
ATOM   7792 C  CB    . ARG B 2 79  ? -12.059 -2.773  70.806  1.00 145.24 ? 78   ARG B CB    1 
ATOM   7793 C  CG    . ARG B 2 79  ? -10.844 -2.009  71.303  1.00 151.13 ? 78   ARG B CG    1 
ATOM   7794 C  CD    . ARG B 2 79  ? -11.275 -0.815  72.143  1.00 154.43 ? 78   ARG B CD    1 
ATOM   7795 N  NE    . ARG B 2 79  ? -10.161 0.064   72.479  1.00 162.28 ? 78   ARG B NE    1 
ATOM   7796 C  CZ    . ARG B 2 79  ? -9.373  -0.094  73.533  1.00 155.35 ? 78   ARG B CZ    1 
ATOM   7797 N  NH1   . ARG B 2 79  ? -9.539  -1.101  74.375  1.00 153.33 ? 78   ARG B NH1   1 
ATOM   7798 N  NH2   . ARG B 2 79  ? -8.393  0.779   73.747  1.00 162.40 ? 78   ARG B NH2   1 
ATOM   7799 N  N     . GLU B 2 80  ? -13.618 -4.268  68.535  1.00 137.75 ? 79   GLU B N     1 
ATOM   7800 C  CA    . GLU B 2 80  ? -14.874 -4.817  68.038  1.00 137.63 ? 79   GLU B CA    1 
ATOM   7801 C  C     . GLU B 2 80  ? -14.758 -6.301  67.720  1.00 133.22 ? 79   GLU B C     1 
ATOM   7802 O  O     . GLU B 2 80  ? -15.763 -7.019  67.742  1.00 130.20 ? 79   GLU B O     1 
ATOM   7803 C  CB    . GLU B 2 80  ? -15.324 -4.045  66.795  1.00 155.42 ? 79   GLU B CB    1 
ATOM   7804 C  CG    . GLU B 2 80  ? -14.489 -4.305  65.537  1.00 154.81 ? 79   GLU B CG    1 
ATOM   7805 C  CD    . GLU B 2 80  ? -13.053 -3.813  65.649  1.00 152.06 ? 79   GLU B CD    1 
ATOM   7806 O  OE1   . GLU B 2 80  ? -12.774 -2.960  66.520  1.00 152.94 ? 79   GLU B OE1   1 
ATOM   7807 O  OE2   . GLU B 2 80  ? -12.200 -4.284  64.868  1.00 145.48 ? 79   GLU B OE2   1 
ATOM   7808 N  N     . GLN B 2 81  ? -13.548 -6.783  67.433  1.00 135.27 ? 80   GLN B N     1 
ATOM   7809 C  CA    . GLN B 2 81  ? -13.389 -8.171  67.017  1.00 134.01 ? 80   GLN B CA    1 
ATOM   7810 C  C     . GLN B 2 81  ? -13.521 -9.123  68.201  1.00 129.14 ? 80   GLN B C     1 
ATOM   7811 O  O     . GLN B 2 81  ? -14.374 -10.019 68.199  1.00 127.20 ? 80   GLN B O     1 
ATOM   7812 C  CB    . GLN B 2 81  ? -12.044 -8.358  66.314  1.00 136.20 ? 80   GLN B CB    1 
ATOM   7813 C  CG    . GLN B 2 81  ? -11.858 -9.747  65.730  1.00 137.03 ? 80   GLN B CG    1 
ATOM   7814 C  CD    . GLN B 2 81  ? -12.985 -10.141 64.793  1.00 138.55 ? 80   GLN B CD    1 
ATOM   7815 O  OE1   . GLN B 2 81  ? -13.506 -9.315  64.042  1.00 137.99 ? 80   GLN B OE1   1 
ATOM   7816 N  NE2   . GLN B 2 81  ? -13.370 -11.411 64.835  1.00 137.25 ? 80   GLN B NE2   1 
ATOM   7817 N  N     . TYR B 2 82  ? -12.687 -8.946  69.227  1.00 126.20 ? 81   TYR B N     1 
ATOM   7818 C  CA    . TYR B 2 82  ? -12.740 -9.856  70.364  1.00 117.41 ? 81   TYR B CA    1 
ATOM   7819 C  C     . TYR B 2 82  ? -13.925 -9.587  71.281  1.00 117.41 ? 81   TYR B C     1 
ATOM   7820 O  O     . TYR B 2 82  ? -14.308 -10.476 72.049  1.00 114.16 ? 81   TYR B O     1 
ATOM   7821 C  CB    . TYR B 2 82  ? -11.431 -9.808  71.164  1.00 108.74 ? 81   TYR B CB    1 
ATOM   7822 C  CG    . TYR B 2 82  ? -10.972 -8.441  71.636  1.00 108.90 ? 81   TYR B CG    1 
ATOM   7823 C  CD1   . TYR B 2 82  ? -11.676 -7.739  72.608  1.00 113.24 ? 81   TYR B CD1   1 
ATOM   7824 C  CD2   . TYR B 2 82  ? -9.801  -7.877  71.145  1.00 106.73 ? 81   TYR B CD2   1 
ATOM   7825 C  CE1   . TYR B 2 82  ? -11.246 -6.503  73.051  1.00 114.48 ? 81   TYR B CE1   1 
ATOM   7826 C  CE2   . TYR B 2 82  ? -9.363  -6.641  71.584  1.00 109.53 ? 81   TYR B CE2   1 
ATOM   7827 C  CZ    . TYR B 2 82  ? -10.089 -5.960  72.537  1.00 115.50 ? 81   TYR B CZ    1 
ATOM   7828 O  OH    . TYR B 2 82  ? -9.656  -4.730  72.976  1.00 125.50 ? 81   TYR B OH    1 
ATOM   7829 N  N     . MET B 2 83  ? -14.516 -8.394  71.219  1.00 119.76 ? 82   MET B N     1 
ATOM   7830 C  CA    . MET B 2 83  ? -15.710 -8.103  72.002  1.00 116.66 ? 82   MET B CA    1 
ATOM   7831 C  C     . MET B 2 83  ? -16.981 -8.654  71.369  1.00 117.63 ? 82   MET B C     1 
ATOM   7832 O  O     . MET B 2 83  ? -18.064 -8.468  71.932  1.00 120.68 ? 82   MET B O     1 
ATOM   7833 C  CB    . MET B 2 83  ? -15.851 -6.593  72.220  1.00 114.64 ? 82   MET B CB    1 
ATOM   7834 C  CG    . MET B 2 83  ? -14.813 -6.002  73.162  1.00 113.87 ? 82   MET B CG    1 
ATOM   7835 S  SD    . MET B 2 83  ? -15.056 -4.239  73.457  1.00 130.11 ? 82   MET B SD    1 
ATOM   7836 C  CE    . MET B 2 83  ? -13.683 -3.881  74.549  1.00 128.81 ? 82   MET B CE    1 
ATOM   7837 N  N     . ARG B 2 84  ? -16.878 -9.320  70.221  1.00 118.23 ? 83   ARG B N     1 
ATOM   7838 C  CA    . ARG B 2 84  ? -18.007 -9.987  69.584  1.00 122.98 ? 83   ARG B CA    1 
ATOM   7839 C  C     . ARG B 2 84  ? -17.925 -11.502 69.657  1.00 121.13 ? 83   ARG B C     1 
ATOM   7840 O  O     . ARG B 2 84  ? -18.949 -12.161 69.851  1.00 127.63 ? 83   ARG B O     1 
ATOM   7841 C  CB    . ARG B 2 84  ? -18.118 -9.564  68.114  1.00 129.06 ? 83   ARG B CB    1 
ATOM   7842 C  CG    . ARG B 2 84  ? -18.738 -8.193  67.901  1.00 133.94 ? 83   ARG B CG    1 
ATOM   7843 C  CD    . ARG B 2 84  ? -18.747 -7.815  66.429  1.00 137.71 ? 83   ARG B CD    1 
ATOM   7844 N  NE    . ARG B 2 84  ? -17.405 -7.817  65.861  1.00 147.61 ? 83   ARG B NE    1 
ATOM   7845 C  CZ    . ARG B 2 84  ? -17.114 -7.453  64.620  1.00 143.96 ? 83   ARG B CZ    1 
ATOM   7846 N  NH1   . ARG B 2 84  ? -18.053 -7.044  63.782  1.00 145.48 ? 83   ARG B NH1   1 
ATOM   7847 N  NH2   . ARG B 2 84  ? -15.850 -7.499  64.209  1.00 142.13 ? 83   ARG B NH2   1 
ATOM   7848 N  N     . THR B 2 85  ? -16.730 -12.070 69.505  1.00 118.94 ? 84   THR B N     1 
ATOM   7849 C  CA    . THR B 2 85  ? -16.542 -13.513 69.571  1.00 119.08 ? 84   THR B CA    1 
ATOM   7850 C  C     . THR B 2 85  ? -16.186 -14.006 70.967  1.00 109.95 ? 84   THR B C     1 
ATOM   7851 O  O     . THR B 2 85  ? -16.140 -15.222 71.184  1.00 106.91 ? 84   THR B O     1 
ATOM   7852 C  CB    . THR B 2 85  ? -15.449 -13.949 68.586  1.00 115.50 ? 84   THR B CB    1 
ATOM   7853 O  OG1   . THR B 2 85  ? -14.238 -13.236 68.863  1.00 116.92 ? 84   THR B OG1   1 
ATOM   7854 C  CG2   . THR B 2 85  ? -15.878 -13.667 67.156  1.00 113.11 ? 84   THR B CG2   1 
ATOM   7855 N  N     . GLY B 2 86  ? -15.942 -13.102 71.915  1.00 112.14 ? 85   GLY B N     1 
ATOM   7856 C  CA    . GLY B 2 86  ? -15.542 -13.510 73.252  1.00 111.04 ? 85   GLY B CA    1 
ATOM   7857 C  C     . GLY B 2 86  ? -16.721 -14.026 74.055  1.00 106.29 ? 85   GLY B C     1 
ATOM   7858 O  O     . GLY B 2 86  ? -17.794 -13.414 74.072  1.00 107.03 ? 85   GLY B O     1 
ATOM   7859 N  N     . ASP B 2 87  ? -16.521 -15.161 74.725  1.00 103.02 ? 86   ASP B N     1 
ATOM   7860 C  CA    . ASP B 2 87  ? -17.547 -15.729 75.589  1.00 111.65 ? 86   ASP B CA    1 
ATOM   7861 C  C     . ASP B 2 87  ? -17.520 -15.151 76.996  1.00 100.89 ? 86   ASP B C     1 
ATOM   7862 O  O     . ASP B 2 87  ? -18.521 -15.256 77.714  1.00 102.81 ? 86   ASP B O     1 
ATOM   7863 C  CB    . ASP B 2 87  ? -17.390 -17.250 75.667  1.00 107.29 ? 86   ASP B CB    1 
ATOM   7864 C  CG    . ASP B 2 87  ? -17.293 -17.893 74.301  1.00 106.55 ? 86   ASP B CG    1 
ATOM   7865 O  OD1   . ASP B 2 87  ? -17.385 -17.162 73.293  1.00 116.08 ? 86   ASP B OD1   1 
ATOM   7866 O  OD2   . ASP B 2 87  ? -17.122 -19.129 74.235  1.00 111.21 ? 86   ASP B OD2   1 
ATOM   7867 N  N     . GLY B 2 88  ? -16.406 -14.551 77.401  1.00 98.89  ? 87   GLY B N     1 
ATOM   7868 C  CA    . GLY B 2 88  ? -16.293 -13.956 78.718  1.00 100.38 ? 87   GLY B CA    1 
ATOM   7869 C  C     . GLY B 2 88  ? -15.177 -12.939 78.730  1.00 98.71  ? 87   GLY B C     1 
ATOM   7870 O  O     . GLY B 2 88  ? -14.248 -12.996 77.918  1.00 97.55  ? 87   GLY B O     1 
ATOM   7871 N  N     . PHE B 2 89  ? -15.277 -12.000 79.667  1.00 92.20  ? 88   PHE B N     1 
ATOM   7872 C  CA    . PHE B 2 89  ? -14.339 -10.892 79.746  1.00 94.25  ? 88   PHE B CA    1 
ATOM   7873 C  C     . PHE B 2 89  ? -13.798 -10.755 81.160  1.00 100.21 ? 88   PHE B C     1 
ATOM   7874 O  O     . PHE B 2 89  ? -14.484 -11.050 82.142  1.00 97.90  ? 88   PHE B O     1 
ATOM   7875 C  CB    . PHE B 2 89  ? -14.991 -9.578  79.305  1.00 97.26  ? 88   PHE B CB    1 
ATOM   7876 C  CG    . PHE B 2 89  ? -15.405 -9.568  77.866  1.00 107.39 ? 88   PHE B CG    1 
ATOM   7877 C  CD1   . PHE B 2 89  ? -16.661 -10.010 77.490  1.00 109.23 ? 88   PHE B CD1   1 
ATOM   7878 C  CD2   . PHE B 2 89  ? -14.532 -9.127  76.886  1.00 101.96 ? 88   PHE B CD2   1 
ATOM   7879 C  CE1   . PHE B 2 89  ? -17.041 -10.007 76.164  1.00 107.59 ? 88   PHE B CE1   1 
ATOM   7880 C  CE2   . PHE B 2 89  ? -14.908 -9.121  75.560  1.00 103.02 ? 88   PHE B CE2   1 
ATOM   7881 C  CZ    . PHE B 2 89  ? -16.165 -9.562  75.199  1.00 108.92 ? 88   PHE B CZ    1 
ATOM   7882 N  N     . LEU B 2 90  ? -12.554 -10.295 81.246  1.00 99.67  ? 89   LEU B N     1 
ATOM   7883 C  CA    . LEU B 2 90  ? -11.855 -10.095 82.511  1.00 88.64  ? 89   LEU B CA    1 
ATOM   7884 C  C     . LEU B 2 90  ? -11.406 -8.638  82.555  1.00 95.94  ? 89   LEU B C     1 
ATOM   7885 O  O     . LEU B 2 90  ? -10.382 -8.280  81.966  1.00 95.26  ? 89   LEU B O     1 
ATOM   7886 C  CB    . LEU B 2 90  ? -10.675 -11.055 82.636  1.00 84.68  ? 89   LEU B CB    1 
ATOM   7887 C  CG    . LEU B 2 90  ? -10.415 -11.694 84.000  1.00 93.66  ? 89   LEU B CG    1 
ATOM   7888 C  CD1   . LEU B 2 90  ? -11.636 -12.466 84.470  1.00 97.54  ? 89   LEU B CD1   1 
ATOM   7889 C  CD2   . LEU B 2 90  ? -9.199  -12.604 83.941  1.00 85.82  ? 89   LEU B CD2   1 
ATOM   7890 N  N     . ILE B 2 91  ? -12.182 -7.796  83.231  1.00 115.22 ? 90   ILE B N     1 
ATOM   7891 C  CA    . ILE B 2 91  ? -11.819 -6.394  83.408  1.00 108.99 ? 90   ILE B CA    1 
ATOM   7892 C  C     . ILE B 2 91  ? -10.729 -6.317  84.469  1.00 100.70 ? 90   ILE B C     1 
ATOM   7893 O  O     . ILE B 2 91  ? -10.952 -6.682  85.627  1.00 101.57 ? 90   ILE B O     1 
ATOM   7894 C  CB    . ILE B 2 91  ? -13.037 -5.548  83.806  1.00 104.18 ? 90   ILE B CB    1 
ATOM   7895 C  CG1   . ILE B 2 91  ? -14.223 -5.840  82.884  1.00 102.68 ? 90   ILE B CG1   1 
ATOM   7896 C  CG2   . ILE B 2 91  ? -12.688 -4.068  83.770  1.00 107.74 ? 90   ILE B CG2   1 
ATOM   7897 C  CD1   . ILE B 2 91  ? -14.035 -5.349  81.470  1.00 120.82 ? 90   ILE B CD1   1 
ATOM   7898 N  N     . VAL B 2 92  ? -9.547  -5.845  84.077  1.00 90.76  ? 91   VAL B N     1 
ATOM   7899 C  CA    . VAL B 2 92  ? -8.377  -5.837  84.945  1.00 99.31  ? 91   VAL B CA    1 
ATOM   7900 C  C     . VAL B 2 92  ? -7.918  -4.398  85.138  1.00 103.44 ? 91   VAL B C     1 
ATOM   7901 O  O     . VAL B 2 92  ? -7.712  -3.670  84.160  1.00 99.21  ? 91   VAL B O     1 
ATOM   7902 C  CB    . VAL B 2 92  ? -7.238  -6.699  84.370  1.00 95.84  ? 91   VAL B CB    1 
ATOM   7903 C  CG1   . VAL B 2 92  ? -6.213  -7.008  85.447  1.00 99.30  ? 91   VAL B CG1   1 
ATOM   7904 C  CG2   . VAL B 2 92  ? -7.791  -7.981  83.779  1.00 87.28  ? 91   VAL B CG2   1 
ATOM   7905 N  N     . TYR B 2 93  ? -7.758  -3.994  86.397  1.00 104.75 ? 92   TYR B N     1 
ATOM   7906 C  CA    . TYR B 2 93  ? -7.215  -2.688  86.741  1.00 111.57 ? 92   TYR B CA    1 
ATOM   7907 C  C     . TYR B 2 93  ? -6.123  -2.865  87.788  1.00 115.03 ? 92   TYR B C     1 
ATOM   7908 O  O     . TYR B 2 93  ? -5.990  -3.922  88.410  1.00 116.62 ? 92   TYR B O     1 
ATOM   7909 C  CB    . TYR B 2 93  ? -8.307  -1.729  87.242  1.00 118.16 ? 92   TYR B CB    1 
ATOM   7910 C  CG    . TYR B 2 93  ? -8.703  -1.904  88.693  1.00 121.57 ? 92   TYR B CG    1 
ATOM   7911 C  CD1   . TYR B 2 93  ? -9.673  -2.827  89.064  1.00 117.72 ? 92   TYR B CD1   1 
ATOM   7912 C  CD2   . TYR B 2 93  ? -8.123  -1.128  89.691  1.00 122.74 ? 92   TYR B CD2   1 
ATOM   7913 C  CE1   . TYR B 2 93  ? -10.043 -2.982  90.389  1.00 113.67 ? 92   TYR B CE1   1 
ATOM   7914 C  CE2   . TYR B 2 93  ? -8.485  -1.278  91.015  1.00 125.51 ? 92   TYR B CE2   1 
ATOM   7915 C  CZ    . TYR B 2 93  ? -9.445  -2.206  91.359  1.00 120.87 ? 92   TYR B CZ    1 
ATOM   7916 O  OH    . TYR B 2 93  ? -9.809  -2.356  92.678  1.00 124.77 ? 92   TYR B OH    1 
ATOM   7917 N  N     . SER B 2 94  ? -5.334  -1.811  87.976  1.00 114.88 ? 93   SER B N     1 
ATOM   7918 C  CA    . SER B 2 94  ? -4.200  -1.824  88.889  1.00 123.97 ? 93   SER B CA    1 
ATOM   7919 C  C     . SER B 2 94  ? -4.530  -0.996  90.123  1.00 136.64 ? 93   SER B C     1 
ATOM   7920 O  O     . SER B 2 94  ? -4.993  0.144   90.006  1.00 148.60 ? 93   SER B O     1 
ATOM   7921 C  CB    . SER B 2 94  ? -2.945  -1.282  88.201  1.00 120.25 ? 93   SER B CB    1 
ATOM   7922 O  OG    . SER B 2 94  ? -1.810  -1.401  89.038  1.00 127.60 ? 93   SER B OG    1 
ATOM   7923 N  N     . VAL B 2 95  ? -4.292  -1.571  91.307  1.00 127.98 ? 94   VAL B N     1 
ATOM   7924 C  CA    . VAL B 2 95  ? -4.560  -0.858  92.555  1.00 136.14 ? 94   VAL B CA    1 
ATOM   7925 C  C     . VAL B 2 95  ? -3.519  0.205   92.860  1.00 144.86 ? 94   VAL B C     1 
ATOM   7926 O  O     . VAL B 2 95  ? -3.719  1.005   93.783  1.00 140.86 ? 94   VAL B O     1 
ATOM   7927 C  CB    . VAL B 2 95  ? -4.643  -1.825  93.750  1.00 128.86 ? 94   VAL B CB    1 
ATOM   7928 C  CG1   . VAL B 2 95  ? -5.671  -2.914  93.485  1.00 121.80 ? 94   VAL B CG1   1 
ATOM   7929 C  CG2   . VAL B 2 95  ? -3.279  -2.425  94.045  1.00 125.56 ? 94   VAL B CG2   1 
ATOM   7930 N  N     . THR B 2 96  ? -2.411  0.233   92.122  1.00 144.74 ? 95   THR B N     1 
ATOM   7931 C  CA    . THR B 2 96  ? -1.396  1.265   92.274  1.00 151.29 ? 95   THR B CA    1 
ATOM   7932 C  C     . THR B 2 96  ? -1.475  2.322   91.182  1.00 152.95 ? 95   THR B C     1 
ATOM   7933 O  O     . THR B 2 96  ? -0.633  3.225   91.147  1.00 158.96 ? 95   THR B O     1 
ATOM   7934 C  CB    . THR B 2 96  ? 0.003   0.641   92.289  1.00 152.92 ? 95   THR B CB    1 
ATOM   7935 O  OG1   . THR B 2 96  ? 0.974   1.645   92.610  1.00 162.78 ? 95   THR B OG1   1 
ATOM   7936 C  CG2   . THR B 2 96  ? 0.336   0.042   90.931  1.00 133.51 ? 95   THR B CG2   1 
ATOM   7937 N  N     . ASP B 2 97  ? -2.463  2.232   90.296  1.00 160.38 ? 96   ASP B N     1 
ATOM   7938 C  CA    . ASP B 2 97  ? -2.662  3.196   89.215  1.00 167.02 ? 96   ASP B CA    1 
ATOM   7939 C  C     . ASP B 2 97  ? -4.124  3.630   89.251  1.00 166.45 ? 96   ASP B C     1 
ATOM   7940 O  O     . ASP B 2 97  ? -5.011  2.873   88.846  1.00 167.47 ? 96   ASP B O     1 
ATOM   7941 C  CB    . ASP B 2 97  ? -2.288  2.593   87.863  1.00 158.63 ? 96   ASP B CB    1 
ATOM   7942 C  CG    . ASP B 2 97  ? -2.502  3.557   86.711  1.00 164.69 ? 96   ASP B CG    1 
ATOM   7943 O  OD1   . ASP B 2 97  ? -1.775  4.570   86.636  1.00 172.12 ? 96   ASP B OD1   1 
ATOM   7944 O  OD2   . ASP B 2 97  ? -3.394  3.299   85.876  1.00 157.73 ? 96   ASP B OD2   1 
ATOM   7945 N  N     . LYS B 2 98  ? -4.370  4.847   89.746  1.00 152.03 ? 97   LYS B N     1 
ATOM   7946 C  CA    . LYS B 2 98  ? -5.738  5.352   89.818  1.00 149.98 ? 97   LYS B CA    1 
ATOM   7947 C  C     . LYS B 2 98  ? -6.367  5.473   88.436  1.00 145.29 ? 97   LYS B C     1 
ATOM   7948 O  O     . LYS B 2 98  ? -7.570  5.233   88.280  1.00 142.77 ? 97   LYS B O     1 
ATOM   7949 C  CB    . LYS B 2 98  ? -5.760  6.705   90.530  1.00 151.38 ? 97   LYS B CB    1 
ATOM   7950 C  CG    . LYS B 2 98  ? -7.139  7.341   90.611  1.00 145.44 ? 97   LYS B CG    1 
ATOM   7951 C  CD    . LYS B 2 98  ? -7.073  8.752   91.165  1.00 144.08 ? 97   LYS B CD    1 
ATOM   7952 C  CE    . LYS B 2 98  ? -8.431  9.432   91.099  1.00 148.72 ? 97   LYS B CE    1 
ATOM   7953 N  NZ    . LYS B 2 98  ? -9.467  8.683   91.863  1.00 156.94 ? 97   LYS B NZ    1 
ATOM   7954 N  N     . ALA B 2 99  ? -5.571  5.827   87.422  1.00 147.59 ? 98   ALA B N     1 
ATOM   7955 C  CA    . ALA B 2 99  ? -6.109  6.009   86.077  1.00 145.11 ? 98   ALA B CA    1 
ATOM   7956 C  C     . ALA B 2 99  ? -6.731  4.730   85.534  1.00 144.31 ? 98   ALA B C     1 
ATOM   7957 O  O     . ALA B 2 99  ? -7.676  4.789   84.740  1.00 140.74 ? 98   ALA B O     1 
ATOM   7958 C  CB    . ALA B 2 99  ? -5.011  6.503   85.135  1.00 139.82 ? 98   ALA B CB    1 
ATOM   7959 N  N     . SER B 2 100 ? -6.218  3.568   85.946  1.00 140.78 ? 99   SER B N     1 
ATOM   7960 C  CA    . SER B 2 100 ? -6.792  2.303   85.506  1.00 137.20 ? 99   SER B CA    1 
ATOM   7961 C  C     . SER B 2 100 ? -8.178  2.062   86.090  1.00 136.22 ? 99   SER B C     1 
ATOM   7962 O  O     . SER B 2 100 ? -8.962  1.310   85.501  1.00 136.08 ? 99   SER B O     1 
ATOM   7963 C  CB    . SER B 2 100 ? -5.865  1.147   85.882  1.00 137.51 ? 99   SER B CB    1 
ATOM   7964 O  OG    . SER B 2 100 ? -5.653  1.101   87.283  1.00 135.97 ? 99   SER B OG    1 
ATOM   7965 N  N     . PHE B 2 101 ? -8.499  2.684   87.226  1.00 138.82 ? 100  PHE B N     1 
ATOM   7966 C  CA    . PHE B 2 101 ? -9.790  2.451   87.860  1.00 138.60 ? 100  PHE B CA    1 
ATOM   7967 C  C     . PHE B 2 101 ? -10.909 3.244   87.195  1.00 139.91 ? 100  PHE B C     1 
ATOM   7968 O  O     . PHE B 2 101 ? -12.049 2.768   87.140  1.00 137.02 ? 100  PHE B O     1 
ATOM   7969 C  CB    . PHE B 2 101 ? -9.716  2.797   89.349  1.00 135.19 ? 100  PHE B CB    1 
ATOM   7970 C  CG    . PHE B 2 101 ? -10.777 2.133   90.178  1.00 125.69 ? 100  PHE B CG    1 
ATOM   7971 C  CD1   . PHE B 2 101 ? -11.489 1.052   89.683  1.00 127.10 ? 100  PHE B CD1   1 
ATOM   7972 C  CD2   . PHE B 2 101 ? -11.070 2.593   91.450  1.00 132.63 ? 100  PHE B CD2   1 
ATOM   7973 C  CE1   . PHE B 2 101 ? -12.466 0.441   90.441  1.00 124.68 ? 100  PHE B CE1   1 
ATOM   7974 C  CE2   . PHE B 2 101 ? -12.047 1.986   92.214  1.00 135.95 ? 100  PHE B CE2   1 
ATOM   7975 C  CZ    . PHE B 2 101 ? -12.746 0.909   91.708  1.00 132.37 ? 100  PHE B CZ    1 
ATOM   7976 N  N     . GLU B 2 102 ? -10.614 4.446   86.692  1.00 146.19 ? 101  GLU B N     1 
ATOM   7977 C  CA    . GLU B 2 102 ? -11.645 5.221   86.010  1.00 143.75 ? 101  GLU B CA    1 
ATOM   7978 C  C     . GLU B 2 102 ? -12.031 4.594   84.678  1.00 153.22 ? 101  GLU B C     1 
ATOM   7979 O  O     . GLU B 2 102 ? -13.176 4.740   84.238  1.00 167.53 ? 101  GLU B O     1 
ATOM   7980 C  CB    . GLU B 2 102 ? -11.182 6.662   85.794  1.00 146.83 ? 101  GLU B CB    1 
ATOM   7981 C  CG    . GLU B 2 102 ? -11.185 7.515   87.051  1.00 165.29 ? 101  GLU B CG    1 
ATOM   7982 C  CD    . GLU B 2 102 ? -9.918  7.360   87.865  1.00 160.64 ? 101  GLU B CD    1 
ATOM   7983 O  OE1   . GLU B 2 102 ? -8.821  7.505   87.287  1.00 167.22 ? 101  GLU B OE1   1 
ATOM   7984 O  OE2   . GLU B 2 102 ? -10.019 7.091   89.081  1.00 160.73 ? 101  GLU B OE2   1 
ATOM   7985 N  N     . HIS B 2 103 ? -11.103 3.897   84.026  1.00 143.43 ? 102  HIS B N     1 
ATOM   7986 C  CA    . HIS B 2 103 ? -11.384 3.276   82.739  1.00 142.22 ? 102  HIS B CA    1 
ATOM   7987 C  C     . HIS B 2 103 ? -12.120 1.948   82.863  1.00 139.68 ? 102  HIS B C     1 
ATOM   7988 O  O     . HIS B 2 103 ? -12.347 1.292   81.841  1.00 140.67 ? 102  HIS B O     1 
ATOM   7989 C  CB    . HIS B 2 103 ? -10.084 3.067   81.957  1.00 140.43 ? 102  HIS B CB    1 
ATOM   7990 C  CG    . HIS B 2 103 ? -9.392  4.340   81.579  1.00 141.53 ? 102  HIS B CG    1 
ATOM   7991 N  ND1   . HIS B 2 103 ? -8.471  4.958   82.397  1.00 144.72 ? 102  HIS B ND1   1 
ATOM   7992 C  CD2   . HIS B 2 103 ? -9.488  5.113   80.471  1.00 138.69 ? 102  HIS B CD2   1 
ATOM   7993 C  CE1   . HIS B 2 103 ? -8.028  6.055   81.809  1.00 139.78 ? 102  HIS B CE1   1 
ATOM   7994 N  NE2   . HIS B 2 103 ? -8.630  6.172   80.639  1.00 136.77 ? 102  HIS B NE2   1 
ATOM   7995 N  N     . VAL B 2 104 ? -12.496 1.536   84.075  1.00 141.31 ? 103  VAL B N     1 
ATOM   7996 C  CA    . VAL B 2 104 ? -13.198 0.267   84.240  1.00 139.31 ? 103  VAL B CA    1 
ATOM   7997 C  C     . VAL B 2 104 ? -14.570 0.326   83.578  1.00 145.12 ? 103  VAL B C     1 
ATOM   7998 O  O     . VAL B 2 104 ? -14.921 -0.535  82.763  1.00 140.06 ? 103  VAL B O     1 
ATOM   7999 C  CB    . VAL B 2 104 ? -13.303 -0.102  85.730  1.00 139.04 ? 103  VAL B CB    1 
ATOM   8000 C  CG1   . VAL B 2 104 ? -14.200 -1.315  85.910  1.00 129.73 ? 103  VAL B CG1   1 
ATOM   8001 C  CG2   . VAL B 2 104 ? -11.921 -0.371  86.304  1.00 134.04 ? 103  VAL B CG2   1 
ATOM   8002 N  N     . ASP B 2 105 ? -15.367 1.343   83.915  1.00 167.90 ? 104  ASP B N     1 
ATOM   8003 C  CA    . ASP B 2 105 ? -16.653 1.513   83.250  1.00 169.48 ? 104  ASP B CA    1 
ATOM   8004 C  C     . ASP B 2 105 ? -16.503 1.959   81.801  1.00 171.30 ? 104  ASP B C     1 
ATOM   8005 O  O     . ASP B 2 105 ? -17.476 1.883   81.043  1.00 176.16 ? 104  ASP B O     1 
ATOM   8006 C  CB    . ASP B 2 105 ? -17.527 2.505   84.025  1.00 176.79 ? 104  ASP B CB    1 
ATOM   8007 C  CG    . ASP B 2 105 ? -16.862 3.856   84.214  1.00 179.67 ? 104  ASP B CG    1 
ATOM   8008 O  OD1   . ASP B 2 105 ? -15.740 4.051   83.707  1.00 177.42 ? 104  ASP B OD1   1 
ATOM   8009 O  OD2   . ASP B 2 105 ? -17.467 4.727   84.874  1.00 186.06 ? 104  ASP B OD2   1 
ATOM   8010 N  N     . ARG B 2 106 ? -15.315 2.422   81.405  1.00 153.59 ? 105  ARG B N     1 
ATOM   8011 C  CA    . ARG B 2 106 ? -15.063 2.716   79.999  1.00 148.19 ? 105  ARG B CA    1 
ATOM   8012 C  C     . ARG B 2 106 ? -15.081 1.440   79.165  1.00 141.89 ? 105  ARG B C     1 
ATOM   8013 O  O     . ARG B 2 106 ? -15.630 1.424   78.057  1.00 149.03 ? 105  ARG B O     1 
ATOM   8014 C  CB    . ARG B 2 106 ? -13.728 3.450   79.855  1.00 147.74 ? 105  ARG B CB    1 
ATOM   8015 C  CG    . ARG B 2 106 ? -13.345 3.845   78.435  1.00 146.92 ? 105  ARG B CG    1 
ATOM   8016 C  CD    . ARG B 2 106 ? -12.358 2.857   77.827  1.00 142.72 ? 105  ARG B CD    1 
ATOM   8017 N  NE    . ARG B 2 106 ? -11.632 3.428   76.699  1.00 157.53 ? 105  ARG B NE    1 
ATOM   8018 C  CZ    . ARG B 2 106 ? -12.110 3.516   75.466  1.00 157.65 ? 105  ARG B CZ    1 
ATOM   8019 N  NH1   . ARG B 2 106 ? -13.329 3.101   75.167  1.00 152.73 ? 105  ARG B NH1   1 
ATOM   8020 N  NH2   . ARG B 2 106 ? -11.347 4.037   74.510  1.00 158.28 ? 105  ARG B NH2   1 
ATOM   8021 N  N     . PHE B 2 107 ? -14.483 0.363   79.679  1.00 138.61 ? 106  PHE B N     1 
ATOM   8022 C  CA    . PHE B 2 107 ? -14.574 -0.938  79.028  1.00 131.34 ? 106  PHE B CA    1 
ATOM   8023 C  C     . PHE B 2 107 ? -15.931 -1.596  79.227  1.00 132.38 ? 106  PHE B C     1 
ATOM   8024 O  O     . PHE B 2 107 ? -16.318 -2.444  78.416  1.00 126.51 ? 106  PHE B O     1 
ATOM   8025 C  CB    . PHE B 2 107 ? -13.488 -1.882  79.551  1.00 121.72 ? 106  PHE B CB    1 
ATOM   8026 C  CG    . PHE B 2 107 ? -12.099 -1.515  79.119  1.00 117.36 ? 106  PHE B CG    1 
ATOM   8027 C  CD1   . PHE B 2 107 ? -11.666 -1.788  77.833  1.00 119.45 ? 106  PHE B CD1   1 
ATOM   8028 C  CD2   . PHE B 2 107 ? -11.219 -0.917  80.004  1.00 116.77 ? 106  PHE B CD2   1 
ATOM   8029 C  CE1   . PHE B 2 107 ? -10.385 -1.458  77.434  1.00 118.61 ? 106  PHE B CE1   1 
ATOM   8030 C  CE2   . PHE B 2 107 ? -9.938  -0.584  79.612  1.00 113.78 ? 106  PHE B CE2   1 
ATOM   8031 C  CZ    . PHE B 2 107 ? -9.520  -0.855  78.325  1.00 117.94 ? 106  PHE B CZ    1 
ATOM   8032 N  N     . HIS B 2 108 ? -16.657 -1.231  80.286  1.00 136.52 ? 107  HIS B N     1 
ATOM   8033 C  CA    . HIS B 2 108 ? -17.931 -1.883  80.565  1.00 137.34 ? 107  HIS B CA    1 
ATOM   8034 C  C     . HIS B 2 108 ? -18.994 -1.483  79.551  1.00 137.44 ? 107  HIS B C     1 
ATOM   8035 O  O     . HIS B 2 108 ? -19.743 -2.335  79.060  1.00 134.07 ? 107  HIS B O     1 
ATOM   8036 C  CB    . HIS B 2 108 ? -18.391 -1.553  81.985  1.00 141.40 ? 107  HIS B CB    1 
ATOM   8037 C  CG    . HIS B 2 108 ? -19.656 -2.247  82.384  1.00 138.20 ? 107  HIS B CG    1 
ATOM   8038 N  ND1   . HIS B 2 108 ? -20.886 -1.627  82.358  1.00 139.21 ? 107  HIS B ND1   1 
ATOM   8039 C  CD2   . HIS B 2 108 ? -19.880 -3.511  82.815  1.00 134.48 ? 107  HIS B CD2   1 
ATOM   8040 C  CE1   . HIS B 2 108 ? -21.814 -2.478  82.758  1.00 143.72 ? 107  HIS B CE1   1 
ATOM   8041 N  NE2   . HIS B 2 108 ? -21.230 -3.628  83.041  1.00 140.62 ? 107  HIS B NE2   1 
ATOM   8042 N  N     . GLN B 2 109 ? -19.077 -0.191  79.223  1.00 144.06 ? 108  GLN B N     1 
ATOM   8043 C  CA    . GLN B 2 109 ? -20.062 0.247   78.240  1.00 145.47 ? 108  GLN B CA    1 
ATOM   8044 C  C     . GLN B 2 109 ? -19.678 -0.188  76.833  1.00 145.13 ? 108  GLN B C     1 
ATOM   8045 O  O     . GLN B 2 109 ? -20.553 -0.341  75.974  1.00 153.51 ? 108  GLN B O     1 
ATOM   8046 C  CB    . GLN B 2 109 ? -20.238 1.765   78.303  1.00 158.05 ? 108  GLN B CB    1 
ATOM   8047 C  CG    . GLN B 2 109 ? -19.025 2.562   77.860  1.00 163.74 ? 108  GLN B CG    1 
ATOM   8048 C  CD    . GLN B 2 109 ? -19.278 4.057   77.878  1.00 176.35 ? 108  GLN B CD    1 
ATOM   8049 O  OE1   . GLN B 2 109 ? -20.206 4.533   78.532  1.00 176.01 ? 108  GLN B OE1   1 
ATOM   8050 N  NE2   . GLN B 2 109 ? -18.455 4.806   77.153  1.00 173.81 ? 108  GLN B NE2   1 
ATOM   8051 N  N     . LEU B 2 110 ? -18.384 -0.392  76.576  1.00 139.85 ? 109  LEU B N     1 
ATOM   8052 C  CA    . LEU B 2 110 ? -17.964 -0.921  75.283  1.00 135.56 ? 109  LEU B CA    1 
ATOM   8053 C  C     . LEU B 2 110 ? -18.419 -2.364  75.112  1.00 132.89 ? 109  LEU B C     1 
ATOM   8054 O  O     . LEU B 2 110 ? -19.032 -2.716  74.099  1.00 135.41 ? 109  LEU B O     1 
ATOM   8055 C  CB    . LEU B 2 110 ? -16.446 -0.816  75.135  1.00 132.21 ? 109  LEU B CB    1 
ATOM   8056 C  CG    . LEU B 2 110 ? -15.920 0.318   74.255  1.00 133.44 ? 109  LEU B CG    1 
ATOM   8057 C  CD1   . LEU B 2 110 ? -16.295 1.671   74.840  1.00 147.03 ? 109  LEU B CD1   1 
ATOM   8058 C  CD2   . LEU B 2 110 ? -14.414 0.196   74.077  1.00 129.68 ? 109  LEU B CD2   1 
ATOM   8059 N  N     . ILE B 2 111 ? -18.130 -3.212  76.100  1.00 131.89 ? 110  ILE B N     1 
ATOM   8060 C  CA    . ILE B 2 111 ? -18.507 -4.620  76.008  1.00 129.02 ? 110  ILE B CA    1 
ATOM   8061 C  C     . ILE B 2 111 ? -20.022 -4.767  75.962  1.00 132.84 ? 110  ILE B C     1 
ATOM   8062 O  O     . ILE B 2 111 ? -20.559 -5.561  75.181  1.00 131.20 ? 110  ILE B O     1 
ATOM   8063 C  CB    . ILE B 2 111 ? -17.894 -5.411  77.179  1.00 122.33 ? 110  ILE B CB    1 
ATOM   8064 C  CG1   . ILE B 2 111 ? -16.367 -5.378  77.101  1.00 120.21 ? 110  ILE B CG1   1 
ATOM   8065 C  CG2   . ILE B 2 111 ? -18.401 -6.846  77.182  1.00 113.11 ? 110  ILE B CG2   1 
ATOM   8066 C  CD1   . ILE B 2 111 ? -15.685 -6.037  78.276  1.00 118.30 ? 110  ILE B CD1   1 
ATOM   8067 N  N     . LEU B 2 112 ? -20.736 -3.998  76.788  1.00 145.56 ? 111  LEU B N     1 
ATOM   8068 C  CA    . LEU B 2 112 ? -22.189 -4.118  76.832  1.00 144.03 ? 111  LEU B CA    1 
ATOM   8069 C  C     . LEU B 2 112 ? -22.837 -3.625  75.544  1.00 148.42 ? 111  LEU B C     1 
ATOM   8070 O  O     . LEU B 2 112 ? -23.858 -4.177  75.117  1.00 155.60 ? 111  LEU B O     1 
ATOM   8071 C  CB    . LEU B 2 112 ? -22.741 -3.358  78.040  1.00 145.59 ? 111  LEU B CB    1 
ATOM   8072 C  CG    . LEU B 2 112 ? -24.203 -3.600  78.426  1.00 155.76 ? 111  LEU B CG    1 
ATOM   8073 C  CD1   . LEU B 2 112 ? -24.357 -3.586  79.938  1.00 143.79 ? 111  LEU B CD1   1 
ATOM   8074 C  CD2   . LEU B 2 112 ? -25.123 -2.565  77.791  1.00 152.86 ? 111  LEU B CD2   1 
ATOM   8075 N  N     . ARG B 2 113 ? -22.266 -2.597  74.912  1.00 140.69 ? 112  ARG B N     1 
ATOM   8076 C  CA    . ARG B 2 113 ? -22.832 -2.089  73.666  1.00 140.41 ? 112  ARG B CA    1 
ATOM   8077 C  C     . ARG B 2 113 ? -22.461 -2.969  72.479  1.00 134.19 ? 112  ARG B C     1 
ATOM   8078 O  O     . ARG B 2 113 ? -23.318 -3.279  71.644  1.00 137.13 ? 112  ARG B O     1 
ATOM   8079 C  CB    . ARG B 2 113 ? -22.375 -0.648  73.429  1.00 145.81 ? 112  ARG B CB    1 
ATOM   8080 C  CG    . ARG B 2 113 ? -22.622 -0.136  72.019  1.00 148.07 ? 112  ARG B CG    1 
ATOM   8081 C  CD    . ARG B 2 113 ? -22.486 1.377   71.947  1.00 154.41 ? 112  ARG B CD    1 
ATOM   8082 N  NE    . ARG B 2 113 ? -21.273 1.857   72.599  1.00 158.83 ? 112  ARG B NE    1 
ATOM   8083 C  CZ    . ARG B 2 113 ? -20.099 1.985   71.998  1.00 151.63 ? 112  ARG B CZ    1 
ATOM   8084 N  NH1   . ARG B 2 113 ? -19.934 1.662   70.725  1.00 151.16 ? 112  ARG B NH1   1 
ATOM   8085 N  NH2   . ARG B 2 113 ? -19.062 2.448   72.691  1.00 149.06 ? 112  ARG B NH2   1 
ATOM   8086 N  N     . VAL B 2 114 ? -21.194 -3.381  72.387  1.00 136.09 ? 113  VAL B N     1 
ATOM   8087 C  CA    . VAL B 2 114 ? -20.769 -4.239  71.283  1.00 129.10 ? 113  VAL B CA    1 
ATOM   8088 C  C     . VAL B 2 114 ? -21.497 -5.577  71.336  1.00 133.41 ? 113  VAL B C     1 
ATOM   8089 O  O     . VAL B 2 114 ? -21.929 -6.107  70.304  1.00 133.20 ? 113  VAL B O     1 
ATOM   8090 C  CB    . VAL B 2 114 ? -19.239 -4.418  71.303  1.00 120.89 ? 113  VAL B CB    1 
ATOM   8091 C  CG1   . VAL B 2 114 ? -18.808 -5.455  70.280  1.00 120.83 ? 113  VAL B CG1   1 
ATOM   8092 C  CG2   . VAL B 2 114 ? -18.551 -3.089  71.028  1.00 115.16 ? 113  VAL B CG2   1 
ATOM   8093 N  N     . LYS B 2 115 ? -21.651 -6.143  72.535  1.00 134.23 ? 114  LYS B N     1 
ATOM   8094 C  CA    . LYS B 2 115 ? -22.458 -7.349  72.685  1.00 139.62 ? 114  LYS B CA    1 
ATOM   8095 C  C     . LYS B 2 115 ? -23.941 -7.073  72.484  1.00 143.44 ? 114  LYS B C     1 
ATOM   8096 O  O     . LYS B 2 115 ? -24.685 -7.989  72.116  1.00 144.26 ? 114  LYS B O     1 
ATOM   8097 C  CB    . LYS B 2 115 ? -22.232 -7.973  74.063  1.00 136.24 ? 114  LYS B CB    1 
ATOM   8098 C  CG    . LYS B 2 115 ? -20.926 -8.738  74.200  1.00 122.92 ? 114  LYS B CG    1 
ATOM   8099 C  CD    . LYS B 2 115 ? -20.968 -10.033 73.407  1.00 121.57 ? 114  LYS B CD    1 
ATOM   8100 C  CE    . LYS B 2 115 ? -19.652 -10.784 73.501  1.00 116.51 ? 114  LYS B CE    1 
ATOM   8101 N  NZ    . LYS B 2 115 ? -19.702 -12.079 72.768  1.00 114.68 ? 114  LYS B NZ    1 
ATOM   8102 N  N     . ASP B 2 116 ? -24.378 -5.834  72.713  1.00 144.25 ? 115  ASP B N     1 
ATOM   8103 C  CA    . ASP B 2 116 ? -25.780 -5.439  72.588  1.00 148.26 ? 115  ASP B CA    1 
ATOM   8104 C  C     . ASP B 2 116 ? -26.679 -6.347  73.424  1.00 144.65 ? 115  ASP B C     1 
ATOM   8105 O  O     . ASP B 2 116 ? -27.683 -6.885  72.952  1.00 142.64 ? 115  ASP B O     1 
ATOM   8106 C  CB    . ASP B 2 116 ? -26.218 -5.421  71.122  1.00 160.75 ? 115  ASP B CB    1 
ATOM   8107 C  CG    . ASP B 2 116 ? -27.478 -4.604  70.900  1.00 161.69 ? 115  ASP B CG    1 
ATOM   8108 O  OD1   . ASP B 2 116 ? -27.399 -3.358  70.961  1.00 158.83 ? 115  ASP B OD1   1 
ATOM   8109 O  OD2   . ASP B 2 116 ? -28.547 -5.206  70.666  1.00 162.79 ? 115  ASP B OD2   1 
ATOM   8110 N  N     . ARG B 2 117 ? -26.299 -6.520  74.686  1.00 147.31 ? 116  ARG B N     1 
ATOM   8111 C  CA    . ARG B 2 117 ? -27.048 -7.327  75.635  1.00 146.73 ? 116  ARG B CA    1 
ATOM   8112 C  C     . ARG B 2 117 ? -27.234 -6.539  76.923  1.00 148.99 ? 116  ARG B C     1 
ATOM   8113 O  O     . ARG B 2 117 ? -26.586 -5.514  77.153  1.00 147.02 ? 116  ARG B O     1 
ATOM   8114 C  CB    . ARG B 2 117 ? -26.342 -8.659  75.922  1.00 146.01 ? 116  ARG B CB    1 
ATOM   8115 C  CG    . ARG B 2 117 ? -26.234 -9.580  74.720  1.00 146.72 ? 116  ARG B CG    1 
ATOM   8116 C  CD    . ARG B 2 117 ? -27.607 -9.984  74.212  1.00 147.54 ? 116  ARG B CD    1 
ATOM   8117 N  NE    . ARG B 2 117 ? -27.522 -10.929 73.105  1.00 154.36 ? 116  ARG B NE    1 
ATOM   8118 C  CZ    . ARG B 2 117 ? -28.571 -11.482 72.512  1.00 153.71 ? 116  ARG B CZ    1 
ATOM   8119 N  NH1   . ARG B 2 117 ? -29.807 -11.205 72.895  1.00 153.15 ? 116  ARG B NH1   1 
ATOM   8120 N  NH2   . ARG B 2 117 ? -28.375 -12.337 71.512  1.00 144.43 ? 116  ARG B NH2   1 
ATOM   8121 N  N     . GLU B 2 118 ? -28.140 -7.033  77.770  1.00 154.51 ? 117  GLU B N     1 
ATOM   8122 C  CA    . GLU B 2 118 ? -28.354 -6.405  79.069  1.00 154.57 ? 117  GLU B CA    1 
ATOM   8123 C  C     . GLU B 2 118 ? -27.143 -6.574  79.976  1.00 155.12 ? 117  GLU B C     1 
ATOM   8124 O  O     . GLU B 2 118 ? -26.885 -5.718  80.830  1.00 153.33 ? 117  GLU B O     1 
ATOM   8125 C  CB    . GLU B 2 118 ? -29.609 -6.980  79.733  1.00 158.17 ? 117  GLU B CB    1 
ATOM   8126 C  CG    . GLU B 2 118 ? -29.442 -8.375  80.334  1.00 165.22 ? 117  GLU B CG    1 
ATOM   8127 C  CD    . GLU B 2 118 ? -29.101 -9.435  79.300  1.00 166.88 ? 117  GLU B CD    1 
ATOM   8128 O  OE1   . GLU B 2 118 ? -29.552 -9.307  78.142  1.00 161.57 ? 117  GLU B OE1   1 
ATOM   8129 O  OE2   . GLU B 2 118 ? -28.375 -10.392 79.644  1.00 161.05 ? 117  GLU B OE2   1 
ATOM   8130 N  N     . SER B 2 119 ? -26.389 -7.657  79.798  1.00 154.17 ? 118  SER B N     1 
ATOM   8131 C  CA    . SER B 2 119 ? -25.201 -7.950  80.589  1.00 147.01 ? 118  SER B CA    1 
ATOM   8132 C  C     . SER B 2 119 ? -24.482 -9.121  79.939  1.00 138.06 ? 118  SER B C     1 
ATOM   8133 O  O     . SER B 2 119 ? -25.051 -9.838  79.111  1.00 137.61 ? 118  SER B O     1 
ATOM   8134 C  CB    . SER B 2 119 ? -25.550 -8.271  82.046  1.00 144.42 ? 118  SER B CB    1 
ATOM   8135 O  OG    . SER B 2 119 ? -26.415 -9.390  82.127  1.00 148.26 ? 118  SER B OG    1 
ATOM   8136 N  N     . PHE B 2 120 ? -23.224 -9.309  80.329  1.00 129.65 ? 119  PHE B N     1 
ATOM   8137 C  CA    . PHE B 2 120 ? -22.398 -10.372 79.776  1.00 121.95 ? 119  PHE B CA    1 
ATOM   8138 C  C     . PHE B 2 120 ? -21.419 -10.827 80.846  1.00 118.79 ? 119  PHE B C     1 
ATOM   8139 O  O     . PHE B 2 120 ? -21.046 -10.031 81.717  1.00 112.54 ? 119  PHE B O     1 
ATOM   8140 C  CB    . PHE B 2 120 ? -21.645 -9.899  78.522  1.00 120.55 ? 119  PHE B CB    1 
ATOM   8141 C  CG    . PHE B 2 120 ? -21.186 -11.019 77.634  1.00 116.51 ? 119  PHE B CG    1 
ATOM   8142 C  CD1   . PHE B 2 120 ? -22.092 -11.709 76.846  1.00 115.34 ? 119  PHE B CD1   1 
ATOM   8143 C  CD2   . PHE B 2 120 ? -19.852 -11.386 77.592  1.00 114.40 ? 119  PHE B CD2   1 
ATOM   8144 C  CE1   . PHE B 2 120 ? -21.676 -12.745 76.033  1.00 114.94 ? 119  PHE B CE1   1 
ATOM   8145 C  CE2   . PHE B 2 120 ? -19.430 -12.419 76.779  1.00 114.51 ? 119  PHE B CE2   1 
ATOM   8146 C  CZ    . PHE B 2 120 ? -20.343 -13.101 76.000  1.00 116.82 ? 119  PHE B CZ    1 
ATOM   8147 N  N     . PRO B 2 121 ? -21.008 -12.107 80.830  1.00 115.93 ? 120  PRO B N     1 
ATOM   8148 C  CA    . PRO B 2 121 ? -20.016 -12.584 81.805  1.00 111.26 ? 120  PRO B CA    1 
ATOM   8149 C  C     . PRO B 2 121 ? -18.767 -11.719 81.894  1.00 107.56 ? 120  PRO B C     1 
ATOM   8150 O  O     . PRO B 2 121 ? -17.952 -11.677 80.968  1.00 110.61 ? 120  PRO B O     1 
ATOM   8151 C  CB    . PRO B 2 121 ? -19.682 -13.988 81.289  1.00 113.47 ? 120  PRO B CB    1 
ATOM   8152 C  CG    . PRO B 2 121 ? -20.950 -14.444 80.656  1.00 115.96 ? 120  PRO B CG    1 
ATOM   8153 C  CD    . PRO B 2 121 ? -21.595 -13.217 80.058  1.00 116.73 ? 120  PRO B CD    1 
ATOM   8154 N  N     . MET B 2 122 ? -18.619 -11.022 83.019  1.00 107.21 ? 121  MET B N     1 
ATOM   8155 C  CA    . MET B 2 122 ? -17.459 -10.186 83.290  1.00 107.54 ? 121  MET B CA    1 
ATOM   8156 C  C     . MET B 2 122 ? -17.020 -10.404 84.730  1.00 106.87 ? 121  MET B C     1 
ATOM   8157 O  O     . MET B 2 122 ? -17.828 -10.754 85.593  1.00 107.06 ? 121  MET B O     1 
ATOM   8158 C  CB    . MET B 2 122 ? -17.762 -8.699  83.063  1.00 110.32 ? 121  MET B CB    1 
ATOM   8159 C  CG    . MET B 2 122 ? -18.177 -8.344  81.649  1.00 107.54 ? 121  MET B CG    1 
ATOM   8160 S  SD    . MET B 2 122 ? -18.882 -6.688  81.553  1.00 124.64 ? 121  MET B SD    1 
ATOM   8161 C  CE    . MET B 2 122 ? -20.404 -6.918  82.471  1.00 110.68 ? 121  MET B CE    1 
ATOM   8162 N  N     . ILE B 2 123 ? -15.728 -10.197 84.981  1.00 104.87 ? 122  ILE B N     1 
ATOM   8163 C  CA    . ILE B 2 123 ? -15.165 -10.267 86.326  1.00 106.24 ? 122  ILE B CA    1 
ATOM   8164 C  C     . ILE B 2 123 ? -14.158 -9.138  86.484  1.00 107.07 ? 122  ILE B C     1 
ATOM   8165 O  O     . ILE B 2 123 ? -13.257 -8.981  85.653  1.00 98.25  ? 122  ILE B O     1 
ATOM   8166 C  CB    . ILE B 2 123 ? -14.496 -11.626 86.615  1.00 103.80 ? 122  ILE B CB    1 
ATOM   8167 C  CG1   . ILE B 2 123 ? -15.550 -12.725 86.759  1.00 101.02 ? 122  ILE B CG1   1 
ATOM   8168 C  CG2   . ILE B 2 123 ? -13.638 -11.544 87.871  1.00 92.76  ? 122  ILE B CG2   1 
ATOM   8169 C  CD1   . ILE B 2 123 ? -14.997 -14.036 87.264  1.00 98.68  ? 122  ILE B CD1   1 
ATOM   8170 N  N     . LEU B 2 124 ? -14.313 -8.349  87.545  1.00 103.50 ? 123  LEU B N     1 
ATOM   8171 C  CA    . LEU B 2 124 ? -13.387 -7.261  87.824  1.00 102.44 ? 123  LEU B CA    1 
ATOM   8172 C  C     . LEU B 2 124 ? -12.179 -7.798  88.581  1.00 98.58  ? 123  LEU B C     1 
ATOM   8173 O  O     . LEU B 2 124 ? -12.326 -8.569  89.534  1.00 108.79 ? 123  LEU B O     1 
ATOM   8174 C  CB    . LEU B 2 124 ? -14.080 -6.161  88.628  1.00 101.49 ? 123  LEU B CB    1 
ATOM   8175 C  CG    . LEU B 2 124 ? -13.277 -4.878  88.846  1.00 102.53 ? 123  LEU B CG    1 
ATOM   8176 C  CD1   . LEU B 2 124 ? -12.754 -4.346  87.522  1.00 105.67 ? 123  LEU B CD1   1 
ATOM   8177 C  CD2   . LEU B 2 124 ? -14.125 -3.829  89.542  1.00 109.20 ? 123  LEU B CD2   1 
ATOM   8178 N  N     . VAL B 2 125 ? -10.987 -7.394  88.154  1.00 98.73  ? 124  VAL B N     1 
ATOM   8179 C  CA    . VAL B 2 125 ? -9.734  -7.906  88.698  1.00 100.71 ? 124  VAL B CA    1 
ATOM   8180 C  C     . VAL B 2 125 ? -8.920  -6.734  89.226  1.00 106.41 ? 124  VAL B C     1 
ATOM   8181 O  O     . VAL B 2 125 ? -8.498  -5.865  88.452  1.00 104.35 ? 124  VAL B O     1 
ATOM   8182 C  CB    . VAL B 2 125 ? -8.935  -8.693  87.648  1.00 100.46 ? 124  VAL B CB    1 
ATOM   8183 C  CG1   . VAL B 2 125 ? -7.584  -9.101  88.212  1.00 97.84  ? 124  VAL B CG1   1 
ATOM   8184 C  CG2   . VAL B 2 125 ? -9.721  -9.912  87.191  1.00 99.21  ? 124  VAL B CG2   1 
ATOM   8185 N  N     . ALA B 2 126 ? -8.698  -6.714  90.538  1.00 111.50 ? 125  ALA B N     1 
ATOM   8186 C  CA    . ALA B 2 126 ? -7.821  -5.732  91.173  1.00 118.07 ? 125  ALA B CA    1 
ATOM   8187 C  C     . ALA B 2 126 ? -6.434  -6.353  91.280  1.00 123.55 ? 125  ALA B C     1 
ATOM   8188 O  O     . ALA B 2 126 ? -6.189  -7.212  92.131  1.00 114.98 ? 125  ALA B O     1 
ATOM   8189 C  CB    . ALA B 2 126 ? -8.362  -5.324  92.538  1.00 110.89 ? 125  ALA B CB    1 
ATOM   8190 N  N     . ASN B 2 127 ? -5.524  -5.922  90.414  1.00 105.83 ? 126  ASN B N     1 
ATOM   8191 C  CA    . ASN B 2 127 ? -4.196  -6.510  90.326  1.00 105.28 ? 126  ASN B CA    1 
ATOM   8192 C  C     . ASN B 2 127 ? -3.185  -5.691  91.124  1.00 108.01 ? 126  ASN B C     1 
ATOM   8193 O  O     . ASN B 2 127 ? -3.452  -4.565  91.551  1.00 112.75 ? 126  ASN B O     1 
ATOM   8194 C  CB    . ASN B 2 127 ? -3.762  -6.622  88.861  1.00 109.79 ? 126  ASN B CB    1 
ATOM   8195 C  CG    . ASN B 2 127 ? -2.692  -7.674  88.651  1.00 106.32 ? 126  ASN B CG    1 
ATOM   8196 O  OD1   . ASN B 2 127 ? -2.584  -8.628  89.421  1.00 100.33 ? 126  ASN B OD1   1 
ATOM   8197 N  ND2   . ASN B 2 127 ? -1.893  -7.505  87.603  1.00 104.07 ? 126  ASN B ND2   1 
ATOM   8198 N  N     . LYS B 2 128 ? -2.010  -6.293  91.332  1.00 109.46 ? 127  LYS B N     1 
ATOM   8199 C  CA    . LYS B 2 128 ? -0.868  -5.647  91.987  1.00 112.80 ? 127  LYS B CA    1 
ATOM   8200 C  C     . LYS B 2 128 ? -1.142  -5.346  93.460  1.00 116.43 ? 127  LYS B C     1 
ATOM   8201 O  O     . LYS B 2 128 ? -0.686  -4.332  93.990  1.00 119.19 ? 127  LYS B O     1 
ATOM   8202 C  CB    . LYS B 2 128 ? -0.446  -4.368  91.259  1.00 115.71 ? 127  LYS B CB    1 
ATOM   8203 C  CG    . LYS B 2 128 ? 0.096   -4.571  89.859  1.00 115.02 ? 127  LYS B CG    1 
ATOM   8204 C  CD    . LYS B 2 128 ? 0.745   -3.290  89.367  1.00 116.22 ? 127  LYS B CD    1 
ATOM   8205 C  CE    . LYS B 2 128 ? 1.318   -3.442  87.974  1.00 98.33  ? 127  LYS B CE    1 
ATOM   8206 N  NZ    . LYS B 2 128 ? 2.005   -2.196  87.543  1.00 98.91  ? 127  LYS B NZ    1 
ATOM   8207 N  N     . VAL B 2 129 ? -1.875  -6.233  94.140  1.00 112.84 ? 128  VAL B N     1 
ATOM   8208 C  CA    . VAL B 2 129 ? -2.115  -6.027  95.567  1.00 113.73 ? 128  VAL B CA    1 
ATOM   8209 C  C     . VAL B 2 129 ? -0.912  -6.411  96.413  1.00 119.67 ? 128  VAL B C     1 
ATOM   8210 O  O     . VAL B 2 129 ? -0.915  -6.167  97.627  1.00 139.06 ? 128  VAL B O     1 
ATOM   8211 C  CB    . VAL B 2 129 ? -3.368  -6.791  96.040  1.00 112.04 ? 128  VAL B CB    1 
ATOM   8212 C  CG1   . VAL B 2 129 ? -4.406  -6.859  94.928  1.00 108.94 ? 128  VAL B CG1   1 
ATOM   8213 C  CG2   . VAL B 2 129 ? -3.007  -8.171  96.535  1.00 111.56 ? 128  VAL B CG2   1 
ATOM   8214 N  N     . ASP B 2 130 ? 0.127   -6.992  95.806  1.00 115.63 ? 129  ASP B N     1 
ATOM   8215 C  CA    . ASP B 2 130 ? 1.380   -7.237  96.508  1.00 113.16 ? 129  ASP B CA    1 
ATOM   8216 C  C     . ASP B 2 130 ? 2.143   -5.954  96.806  1.00 123.52 ? 129  ASP B C     1 
ATOM   8217 O  O     . ASP B 2 130 ? 3.142   -6.002  97.532  1.00 133.68 ? 129  ASP B O     1 
ATOM   8218 C  CB    . ASP B 2 130 ? 2.266   -8.178  95.690  1.00 117.90 ? 129  ASP B CB    1 
ATOM   8219 C  CG    . ASP B 2 130 ? 2.571   -7.634  94.306  1.00 120.54 ? 129  ASP B CG    1 
ATOM   8220 O  OD1   . ASP B 2 130 ? 1.723   -6.901  93.754  1.00 114.35 ? 129  ASP B OD1   1 
ATOM   8221 O  OD2   . ASP B 2 130 ? 3.656   -7.937  93.768  1.00 120.83 ? 129  ASP B OD2   1 
ATOM   8222 N  N     . LEU B 2 131 ? 1.703   -4.819  96.265  1.00 125.77 ? 130  LEU B N     1 
ATOM   8223 C  CA    . LEU B 2 131 ? 2.364   -3.541  96.491  1.00 133.70 ? 130  LEU B CA    1 
ATOM   8224 C  C     . LEU B 2 131 ? 1.464   -2.607  97.291  1.00 141.80 ? 130  LEU B C     1 
ATOM   8225 O  O     . LEU B 2 131 ? 1.084   -1.537  96.806  1.00 145.99 ? 130  LEU B O     1 
ATOM   8226 C  CB    . LEU B 2 131 ? 2.745   -2.896  95.157  1.00 131.98 ? 130  LEU B CB    1 
ATOM   8227 C  CG    . LEU B 2 131 ? 3.576   -3.753  94.201  1.00 127.06 ? 130  LEU B CG    1 
ATOM   8228 C  CD1   . LEU B 2 131 ? 3.664   -3.094  92.834  1.00 119.72 ? 130  LEU B CD1   1 
ATOM   8229 C  CD2   . LEU B 2 131 ? 4.965   -4.001  94.773  1.00 122.61 ? 130  LEU B CD2   1 
ATOM   8230 N  N     . MET B 2 132 ? 1.116   -3.004  98.518  1.00 139.60 ? 131  MET B N     1 
ATOM   8231 C  CA    . MET B 2 132 ? 0.227   -2.187  99.336  1.00 145.42 ? 131  MET B CA    1 
ATOM   8232 C  C     . MET B 2 132 ? 0.891   -0.905  99.817  1.00 147.43 ? 131  MET B C     1 
ATOM   8233 O  O     . MET B 2 132 ? 0.185   0.042   100.181 1.00 152.04 ? 131  MET B O     1 
ATOM   8234 C  CB    . MET B 2 132 ? -0.278  -2.992  100.534 1.00 160.25 ? 131  MET B CB    1 
ATOM   8235 C  CG    . MET B 2 132 ? -1.096  -4.214  100.157 1.00 158.12 ? 131  MET B CG    1 
ATOM   8236 S  SD    . MET B 2 132 ? -1.808  -5.036  101.594 1.00 161.80 ? 131  MET B SD    1 
ATOM   8237 C  CE    . MET B 2 132 ? -0.347  -5.268  102.601 1.00 129.04 ? 131  MET B CE    1 
ATOM   8238 N  N     . HIS B 2 133 ? 2.224   -0.850  99.831  1.00 148.66 ? 132  HIS B N     1 
ATOM   8239 C  CA    . HIS B 2 133 ? 2.919   0.377   100.201 1.00 149.79 ? 132  HIS B CA    1 
ATOM   8240 C  C     . HIS B 2 133 ? 2.718   1.493   99.185  1.00 150.28 ? 132  HIS B C     1 
ATOM   8241 O  O     . HIS B 2 133 ? 3.020   2.650   99.493  1.00 147.18 ? 132  HIS B O     1 
ATOM   8242 C  CB    . HIS B 2 133 ? 4.413   0.100   100.384 1.00 147.12 ? 132  HIS B CB    1 
ATOM   8243 C  CG    . HIS B 2 133 ? 5.084   -0.434  99.158  1.00 155.52 ? 132  HIS B CG    1 
ATOM   8244 N  ND1   . HIS B 2 133 ? 5.072   -1.771  98.824  1.00 152.43 ? 132  HIS B ND1   1 
ATOM   8245 C  CD2   . HIS B 2 133 ? 5.788   0.190   98.184  1.00 158.41 ? 132  HIS B CD2   1 
ATOM   8246 C  CE1   . HIS B 2 133 ? 5.739   -1.948  97.698  1.00 151.37 ? 132  HIS B CE1   1 
ATOM   8247 N  NE2   . HIS B 2 133 ? 6.183   -0.773  97.288  1.00 154.06 ? 132  HIS B NE2   1 
ATOM   8248 N  N     . LEU B 2 134 ? 2.220   1.174   97.986  1.00 153.04 ? 133  LEU B N     1 
ATOM   8249 C  CA    . LEU B 2 134 ? 1.880   2.176   96.982  1.00 159.05 ? 133  LEU B CA    1 
ATOM   8250 C  C     . LEU B 2 134 ? 0.476   1.960   96.427  1.00 155.79 ? 133  LEU B C     1 
ATOM   8251 O  O     . LEU B 2 134 ? 0.181   2.402   95.312  1.00 154.15 ? 133  LEU B O     1 
ATOM   8252 C  CB    . LEU B 2 134 ? 2.903   2.177   95.843  1.00 158.96 ? 133  LEU B CB    1 
ATOM   8253 C  CG    . LEU B 2 134 ? 4.317   2.645   96.188  1.00 163.91 ? 133  LEU B CG    1 
ATOM   8254 C  CD1   . LEU B 2 134 ? 5.220   2.572   94.966  1.00 151.25 ? 133  LEU B CD1   1 
ATOM   8255 C  CD2   . LEU B 2 134 ? 4.292   4.055   96.758  1.00 168.30 ? 133  LEU B CD2   1 
ATOM   8256 N  N     . ARG B 2 135 ? -0.391  1.287   97.180  1.00 143.05 ? 134  ARG B N     1 
ATOM   8257 C  CA    . ARG B 2 135 ? -1.745  1.019   96.713  1.00 140.46 ? 134  ARG B CA    1 
ATOM   8258 C  C     . ARG B 2 135 ? -2.584  2.290   96.772  1.00 140.56 ? 134  ARG B C     1 
ATOM   8259 O  O     . ARG B 2 135 ? -2.574  3.008   97.777  1.00 145.29 ? 134  ARG B O     1 
ATOM   8260 C  CB    . ARG B 2 135 ? -2.382  -0.087  97.553  1.00 129.18 ? 134  ARG B CB    1 
ATOM   8261 C  CG    . ARG B 2 135 ? -3.818  -0.411  97.179  1.00 123.04 ? 134  ARG B CG    1 
ATOM   8262 C  CD    . ARG B 2 135 ? -4.231  -1.774  97.712  1.00 114.16 ? 134  ARG B CD    1 
ATOM   8263 N  NE    . ARG B 2 135 ? -5.617  -2.092  97.391  1.00 113.01 ? 134  ARG B NE    1 
ATOM   8264 C  CZ    . ARG B 2 135 ? -6.149  -3.303  97.485  1.00 112.17 ? 134  ARG B CZ    1 
ATOM   8265 N  NH1   . ARG B 2 135 ? -5.431  -4.345  97.872  1.00 112.28 ? 134  ARG B NH1   1 
ATOM   8266 N  NH2   . ARG B 2 135 ? -7.431  -3.474  97.177  1.00 111.32 ? 134  ARG B NH2   1 
ATOM   8267 N  N     . LYS B 2 136 ? -3.312  2.567   95.691  1.00 142.66 ? 135  LYS B N     1 
ATOM   8268 C  CA    . LYS B 2 136 ? -4.106  3.781   95.581  1.00 142.64 ? 135  LYS B CA    1 
ATOM   8269 C  C     . LYS B 2 136 ? -5.601  3.524   95.464  1.00 140.82 ? 135  LYS B C     1 
ATOM   8270 O  O     . LYS B 2 136 ? -6.370  4.486   95.356  1.00 141.73 ? 135  LYS B O     1 
ATOM   8271 C  CB    . LYS B 2 136 ? -3.637  4.614   94.379  1.00 152.73 ? 135  LYS B CB    1 
ATOM   8272 C  CG    . LYS B 2 136 ? -2.196  5.088   94.475  1.00 158.44 ? 135  LYS B CG    1 
ATOM   8273 C  CD    . LYS B 2 136 ? -1.795  5.876   93.239  1.00 165.53 ? 135  LYS B CD    1 
ATOM   8274 C  CE    . LYS B 2 136 ? -0.361  6.369   93.336  1.00 170.72 ? 135  LYS B CE    1 
ATOM   8275 N  NZ    . LYS B 2 136 ? 0.051   7.104   92.107  1.00 150.79 ? 135  LYS B NZ    1 
ATOM   8276 N  N     . ILE B 2 137 ? -6.037  2.267   95.470  1.00 135.43 ? 136  ILE B N     1 
ATOM   8277 C  CA    . ILE B 2 137 ? -7.454  1.924   95.434  1.00 134.43 ? 136  ILE B CA    1 
ATOM   8278 C  C     . ILE B 2 137 ? -7.717  0.892   96.520  1.00 136.80 ? 136  ILE B C     1 
ATOM   8279 O  O     . ILE B 2 137 ? -7.154  -0.209  96.485  1.00 129.81 ? 136  ILE B O     1 
ATOM   8280 C  CB    . ILE B 2 137 ? -7.895  1.387   94.062  1.00 131.47 ? 136  ILE B CB    1 
ATOM   8281 C  CG1   . ILE B 2 137 ? -7.864  2.499   93.009  1.00 141.82 ? 136  ILE B CG1   1 
ATOM   8282 C  CG2   . ILE B 2 137 ? -9.287  0.782   94.153  1.00 127.70 ? 136  ILE B CG2   1 
ATOM   8283 C  CD1   . ILE B 2 137 ? -6.553  2.605   92.256  1.00 147.50 ? 136  ILE B CD1   1 
ATOM   8284 N  N     . THR B 2 138 ? -8.570  1.245   97.479  1.00 137.03 ? 137  THR B N     1 
ATOM   8285 C  CA    . THR B 2 138 ? -8.890  0.353   98.580  1.00 137.12 ? 137  THR B CA    1 
ATOM   8286 C  C     . THR B 2 138 ? -9.726  -0.828  98.089  1.00 137.44 ? 137  THR B C     1 
ATOM   8287 O  O     . THR B 2 138 ? -10.232 -0.848  96.963  1.00 140.94 ? 137  THR B O     1 
ATOM   8288 C  CB    . THR B 2 138 ? -9.641  1.106   99.676  1.00 153.43 ? 137  THR B CB    1 
ATOM   8289 O  OG1   . THR B 2 138 ? -10.892 1.575   99.158  1.00 148.76 ? 137  THR B OG1   1 
ATOM   8290 C  CG2   . THR B 2 138 ? -8.824  2.296   100.156 1.00 158.81 ? 137  THR B CG2   1 
ATOM   8291 N  N     . ARG B 2 139 ? -9.867  -1.830  98.961  1.00 140.61 ? 138  ARG B N     1 
ATOM   8292 C  CA    . ARG B 2 139 ? -10.701 -2.982  98.630  1.00 136.54 ? 138  ARG B CA    1 
ATOM   8293 C  C     . ARG B 2 139 ? -12.168 -2.585  98.522  1.00 147.06 ? 138  ARG B C     1 
ATOM   8294 O  O     . ARG B 2 139 ? -12.901 -3.115  97.678  1.00 140.22 ? 138  ARG B O     1 
ATOM   8295 C  CB    . ARG B 2 139 ? -10.512 -4.084  99.674  1.00 120.64 ? 138  ARG B CB    1 
ATOM   8296 C  CG    . ARG B 2 139 ? -11.508 -5.229  99.563  1.00 114.46 ? 138  ARG B CG    1 
ATOM   8297 C  CD    . ARG B 2 139 ? -11.202 -6.335  100.560 1.00 122.25 ? 138  ARG B CD    1 
ATOM   8298 N  NE    . ARG B 2 139 ? -10.095 -7.177  100.123 1.00 118.71 ? 138  ARG B NE    1 
ATOM   8299 C  CZ    . ARG B 2 139 ? -10.241 -8.320  99.467  1.00 124.90 ? 138  ARG B CZ    1 
ATOM   8300 N  NH1   . ARG B 2 139 ? -11.437 -8.799  99.169  1.00 124.01 ? 138  ARG B NH1   1 
ATOM   8301 N  NH2   . ARG B 2 139 ? -9.158  -9.001  99.101  1.00 123.79 ? 138  ARG B NH2   1 
ATOM   8302 N  N     . GLU B 2 140 ? -12.611 -1.644  99.360  1.00 176.23 ? 139  GLU B N     1 
ATOM   8303 C  CA    . GLU B 2 140 ? -14.002 -1.208  99.316  1.00 170.14 ? 139  GLU B CA    1 
ATOM   8304 C  C     . GLU B 2 140 ? -14.314 -0.444  98.035  1.00 173.61 ? 139  GLU B C     1 
ATOM   8305 O  O     . GLU B 2 140 ? -15.438 -0.524  97.528  1.00 180.69 ? 139  GLU B O     1 
ATOM   8306 C  CB    . GLU B 2 140 ? -14.323 -0.349  100.540 1.00 170.18 ? 139  GLU B CB    1 
ATOM   8307 C  CG    . GLU B 2 140 ? -14.365 -1.114  101.861 1.00 202.63 ? 139  GLU B CG    1 
ATOM   8308 C  CD    . GLU B 2 140 ? -12.988 -1.497  102.378 1.00 195.77 ? 139  GLU B CD    1 
ATOM   8309 O  OE1   . GLU B 2 140 ? -11.979 -1.111  101.748 1.00 174.62 ? 139  GLU B OE1   1 
ATOM   8310 O  OE2   . GLU B 2 140 ? -12.914 -2.184  103.419 1.00 193.11 ? 139  GLU B OE2   1 
ATOM   8311 N  N     . GLN B 2 141 ? -13.341 0.299   97.501  1.00 147.79 ? 140  GLN B N     1 
ATOM   8312 C  CA    . GLN B 2 141 ? -13.555 0.986   96.232  1.00 144.16 ? 140  GLN B CA    1 
ATOM   8313 C  C     . GLN B 2 141 ? -13.754 -0.009  95.095  1.00 142.49 ? 140  GLN B C     1 
ATOM   8314 O  O     . GLN B 2 141 ? -14.574 0.221   94.198  1.00 137.45 ? 140  GLN B O     1 
ATOM   8315 C  CB    . GLN B 2 141 ? -12.383 1.919   95.932  1.00 141.62 ? 140  GLN B CB    1 
ATOM   8316 C  CG    . GLN B 2 141 ? -12.389 3.205   96.741  1.00 136.74 ? 140  GLN B CG    1 
ATOM   8317 C  CD    . GLN B 2 141 ? -11.242 4.126   96.376  1.00 131.71 ? 140  GLN B CD    1 
ATOM   8318 O  OE1   . GLN B 2 141 ? -10.110 3.680   96.189  1.00 137.17 ? 140  GLN B OE1   1 
ATOM   8319 N  NE2   . GLN B 2 141 ? -11.531 5.417   96.264  1.00 125.26 ? 140  GLN B NE2   1 
ATOM   8320 N  N     . GLY B 2 142 ? -13.017 -1.120  95.116  1.00 137.47 ? 141  GLY B N     1 
ATOM   8321 C  CA    . GLY B 2 142 ? -13.225 -2.147  94.109  1.00 130.07 ? 141  GLY B CA    1 
ATOM   8322 C  C     . GLY B 2 142 ? -14.522 -2.907  94.312  1.00 131.49 ? 141  GLY B C     1 
ATOM   8323 O  O     . GLY B 2 142 ? -15.185 -3.290  93.345  1.00 133.84 ? 141  GLY B O     1 
ATOM   8324 N  N     . LYS B 2 143 ? -14.900 -3.138  95.573  1.00 133.78 ? 142  LYS B N     1 
ATOM   8325 C  CA    . LYS B 2 143 ? -16.168 -3.804  95.855  1.00 129.28 ? 142  LYS B CA    1 
ATOM   8326 C  C     . LYS B 2 143 ? -17.350 -2.957  95.401  1.00 131.28 ? 142  LYS B C     1 
ATOM   8327 O  O     . LYS B 2 143 ? -18.338 -3.486  94.879  1.00 128.71 ? 142  LYS B O     1 
ATOM   8328 C  CB    . LYS B 2 143 ? -16.281 -4.115  97.349  1.00 136.56 ? 142  LYS B CB    1 
ATOM   8329 C  CG    . LYS B 2 143 ? -15.479 -5.319  97.816  1.00 132.04 ? 142  LYS B CG    1 
ATOM   8330 C  CD    . LYS B 2 143 ? -15.996 -6.607  97.195  1.00 123.73 ? 142  LYS B CD    1 
ATOM   8331 C  CE    . LYS B 2 143 ? -15.677 -7.808  98.073  1.00 129.79 ? 142  LYS B CE    1 
ATOM   8332 N  NZ    . LYS B 2 143 ? -14.247 -7.840  98.490  1.00 132.73 ? 142  LYS B NZ    1 
ATOM   8333 N  N     . GLU B 2 144 ? -17.269 -1.638  95.596  1.00 135.39 ? 143  GLU B N     1 
ATOM   8334 C  CA    . GLU B 2 144 ? -18.366 -0.763  95.196  1.00 140.33 ? 143  GLU B CA    1 
ATOM   8335 C  C     . GLU B 2 144 ? -18.501 -0.704  93.679  1.00 142.05 ? 143  GLU B C     1 
ATOM   8336 O  O     . GLU B 2 144 ? -19.617 -0.734  93.149  1.00 148.35 ? 143  GLU B O     1 
ATOM   8337 C  CB    . GLU B 2 144 ? -18.160 0.636   95.776  1.00 146.16 ? 143  GLU B CB    1 
ATOM   8338 C  CG    . GLU B 2 144 ? -19.157 1.667   95.271  1.00 159.43 ? 143  GLU B CG    1 
ATOM   8339 C  CD    . GLU B 2 144 ? -20.595 1.276   95.552  1.00 164.28 ? 143  GLU B CD    1 
ATOM   8340 O  OE1   . GLU B 2 144 ? -20.871 0.770   96.661  1.00 163.19 ? 143  GLU B OE1   1 
ATOM   8341 O  OE2   . GLU B 2 144 ? -21.449 1.470   94.661  1.00 163.95 ? 143  GLU B OE2   1 
ATOM   8342 N  N     . MET B 2 145 ? -17.375 -0.617  92.966  1.00 139.57 ? 144  MET B N     1 
ATOM   8343 C  CA    . MET B 2 145 ? -17.420 -0.642  91.507  1.00 134.42 ? 144  MET B CA    1 
ATOM   8344 C  C     . MET B 2 145 ? -17.934 -1.981  90.994  1.00 131.32 ? 144  MET B C     1 
ATOM   8345 O  O     . MET B 2 145 ? -18.646 -2.034  89.984  1.00 134.68 ? 144  MET B O     1 
ATOM   8346 C  CB    . MET B 2 145 ? -16.033 -0.341  90.936  1.00 129.15 ? 144  MET B CB    1 
ATOM   8347 C  CG    . MET B 2 145 ? -15.905 -0.569  89.436  1.00 133.92 ? 144  MET B CG    1 
ATOM   8348 S  SD    . MET B 2 145 ? -16.836 0.612   88.440  1.00 147.03 ? 144  MET B SD    1 
ATOM   8349 C  CE    . MET B 2 145 ? -15.834 2.084   88.636  1.00 150.58 ? 144  MET B CE    1 
ATOM   8350 N  N     . ALA B 2 146 ? -17.591 -3.074  91.681  1.00 128.07 ? 145  ALA B N     1 
ATOM   8351 C  CA    . ALA B 2 146 ? -18.051 -4.392  91.253  1.00 128.17 ? 145  ALA B CA    1 
ATOM   8352 C  C     . ALA B 2 146 ? -19.558 -4.534  91.424  1.00 129.17 ? 145  ALA B C     1 
ATOM   8353 O  O     . ALA B 2 146 ? -20.239 -5.082  90.549  1.00 130.07 ? 145  ALA B O     1 
ATOM   8354 C  CB    . ALA B 2 146 ? -17.317 -5.482  92.031  1.00 124.46 ? 145  ALA B CB    1 
ATOM   8355 N  N     . THR B 2 147 ? -20.096 -4.054  92.546  1.00 132.50 ? 146  THR B N     1 
ATOM   8356 C  CA    . THR B 2 147 ? -21.539 -4.081  92.747  1.00 133.70 ? 146  THR B CA    1 
ATOM   8357 C  C     . THR B 2 147 ? -22.252 -3.025  91.913  1.00 138.27 ? 146  THR B C     1 
ATOM   8358 O  O     . THR B 2 147 ? -23.469 -3.123  91.721  1.00 141.56 ? 146  THR B O     1 
ATOM   8359 C  CB    . THR B 2 147 ? -21.871 -3.884  94.226  1.00 132.53 ? 146  THR B CB    1 
ATOM   8360 O  OG1   . THR B 2 147 ? -21.319 -2.641  94.679  1.00 136.69 ? 146  THR B OG1   1 
ATOM   8361 C  CG2   . THR B 2 147 ? -21.296 -5.023  95.055  1.00 121.27 ? 146  THR B CG2   1 
ATOM   8362 N  N     . LYS B 2 148 ? -21.523 -2.022  91.419  1.00 143.95 ? 147  LYS B N     1 
ATOM   8363 C  CA    . LYS B 2 148 ? -22.130 -1.008  90.563  1.00 143.92 ? 147  LYS B CA    1 
ATOM   8364 C  C     . LYS B 2 148 ? -22.614 -1.618  89.253  1.00 142.76 ? 147  LYS B C     1 
ATOM   8365 O  O     . LYS B 2 148 ? -23.744 -1.371  88.818  1.00 152.48 ? 147  LYS B O     1 
ATOM   8366 C  CB    . LYS B 2 148 ? -21.127 0.116   90.298  1.00 145.61 ? 147  LYS B CB    1 
ATOM   8367 C  CG    . LYS B 2 148 ? -21.608 1.171   89.315  1.00 145.16 ? 147  LYS B CG    1 
ATOM   8368 C  CD    . LYS B 2 148 ? -20.521 2.201   89.050  1.00 139.10 ? 147  LYS B CD    1 
ATOM   8369 C  CE    . LYS B 2 148 ? -20.049 2.846   90.344  1.00 153.35 ? 147  LYS B CE    1 
ATOM   8370 N  NZ    . LYS B 2 148 ? -18.956 3.831   90.113  1.00 142.86 ? 147  LYS B NZ    1 
ATOM   8371 N  N     . HIS B 2 149 ? -21.769 -2.423  88.612  1.00 136.54 ? 148  HIS B N     1 
ATOM   8372 C  CA    . HIS B 2 149 ? -22.116 -3.092  87.367  1.00 144.14 ? 148  HIS B CA    1 
ATOM   8373 C  C     . HIS B 2 149 ? -22.571 -4.531  87.583  1.00 136.42 ? 148  HIS B C     1 
ATOM   8374 O  O     . HIS B 2 149 ? -22.694 -5.281  86.609  1.00 136.35 ? 148  HIS B O     1 
ATOM   8375 C  CB    . HIS B 2 149 ? -20.929 -3.057  86.400  1.00 141.75 ? 148  HIS B CB    1 
ATOM   8376 C  CG    . HIS B 2 149 ? -20.425 -1.677  86.108  1.00 143.45 ? 148  HIS B CG    1 
ATOM   8377 N  ND1   . HIS B 2 149 ? -21.107 -0.789  85.305  1.00 144.69 ? 148  HIS B ND1   1 
ATOM   8378 C  CD2   . HIS B 2 149 ? -19.300 -1.036  86.506  1.00 144.38 ? 148  HIS B CD2   1 
ATOM   8379 C  CE1   . HIS B 2 149 ? -20.427 0.341   85.224  1.00 144.73 ? 148  HIS B CE1   1 
ATOM   8380 N  NE2   . HIS B 2 149 ? -19.327 0.217   85.943  1.00 144.52 ? 148  HIS B NE2   1 
ATOM   8381 N  N     . ASN B 2 150 ? -22.823 -4.927  88.833  1.00 136.23 ? 149  ASN B N     1 
ATOM   8382 C  CA    . ASN B 2 150 ? -23.269 -6.278  89.177  1.00 136.17 ? 149  ASN B CA    1 
ATOM   8383 C  C     . ASN B 2 150 ? -22.288 -7.325  88.645  1.00 128.96 ? 149  ASN B C     1 
ATOM   8384 O  O     . ASN B 2 150 ? -22.644 -8.238  87.896  1.00 118.53 ? 149  ASN B O     1 
ATOM   8385 C  CB    . ASN B 2 150 ? -24.692 -6.531  88.663  1.00 137.06 ? 149  ASN B CB    1 
ATOM   8386 C  CG    . ASN B 2 150 ? -25.398 -7.642  89.417  1.00 128.74 ? 149  ASN B CG    1 
ATOM   8387 O  OD1   . ASN B 2 150 ? -24.761 -8.516  90.004  1.00 137.49 ? 149  ASN B OD1   1 
ATOM   8388 N  ND2   . ASN B 2 150 ? -26.726 -7.613  89.403  1.00 113.63 ? 149  ASN B ND2   1 
ATOM   8389 N  N     . ILE B 2 151 ? -21.032 -7.174  89.055  1.00 132.77 ? 150  ILE B N     1 
ATOM   8390 C  CA    . ILE B 2 151 ? -19.931 -7.988  88.549  1.00 126.58 ? 150  ILE B CA    1 
ATOM   8391 C  C     . ILE B 2 151 ? -19.195 -8.626  89.722  1.00 117.41 ? 150  ILE B C     1 
ATOM   8392 O  O     . ILE B 2 151 ? -18.994 -7.968  90.753  1.00 116.01 ? 150  ILE B O     1 
ATOM   8393 C  CB    . ILE B 2 151 ? -18.975 -7.142  87.691  1.00 119.16 ? 150  ILE B CB    1 
ATOM   8394 C  CG1   . ILE B 2 151 ? -19.692 -6.608  86.451  1.00 125.18 ? 150  ILE B CG1   1 
ATOM   8395 C  CG2   . ILE B 2 151 ? -17.751 -7.939  87.283  1.00 121.08 ? 150  ILE B CG2   1 
ATOM   8396 C  CD1   . ILE B 2 151 ? -18.788 -5.827  85.525  1.00 142.45 ? 150  ILE B CD1   1 
ATOM   8397 N  N     . PRO B 2 152 ? -18.795 -9.895  89.625  1.00 114.92 ? 151  PRO B N     1 
ATOM   8398 C  CA    . PRO B 2 152 ? -17.942 -10.477 90.668  1.00 108.61 ? 151  PRO B CA    1 
ATOM   8399 C  C     . PRO B 2 152 ? -16.612 -9.744  90.772  1.00 106.65 ? 151  PRO B C     1 
ATOM   8400 O  O     . PRO B 2 152 ? -16.134 -9.132  89.815  1.00 113.20 ? 151  PRO B O     1 
ATOM   8401 C  CB    . PRO B 2 152 ? -17.749 -11.925 90.203  1.00 105.31 ? 151  PRO B CB    1 
ATOM   8402 C  CG    . PRO B 2 152 ? -18.936 -12.202 89.343  1.00 109.37 ? 151  PRO B CG    1 
ATOM   8403 C  CD    . PRO B 2 152 ? -19.247 -10.905 88.653  1.00 111.37 ? 151  PRO B CD    1 
ATOM   8404 N  N     . TYR B 2 153 ? -16.013 -9.817  91.958  1.00 111.14 ? 152  TYR B N     1 
ATOM   8405 C  CA    . TYR B 2 153 ? -14.793 -9.089  92.274  1.00 107.77 ? 152  TYR B CA    1 
ATOM   8406 C  C     . TYR B 2 153 ? -13.741 -10.058 92.789  1.00 105.25 ? 152  TYR B C     1 
ATOM   8407 O  O     . TYR B 2 153 ? -14.060 -11.036 93.469  1.00 114.32 ? 152  TYR B O     1 
ATOM   8408 C  CB    . TYR B 2 153 ? -15.069 -7.993  93.319  1.00 109.71 ? 152  TYR B CB    1 
ATOM   8409 C  CG    . TYR B 2 153 ? -13.857 -7.206  93.769  1.00 112.28 ? 152  TYR B CG    1 
ATOM   8410 C  CD1   . TYR B 2 153 ? -13.332 -6.188  92.982  1.00 108.57 ? 152  TYR B CD1   1 
ATOM   8411 C  CD2   . TYR B 2 153 ? -13.254 -7.463  94.995  1.00 115.58 ? 152  TYR B CD2   1 
ATOM   8412 C  CE1   . TYR B 2 153 ? -12.230 -5.461  93.397  1.00 114.90 ? 152  TYR B CE1   1 
ATOM   8413 C  CE2   . TYR B 2 153 ? -12.154 -6.740  95.418  1.00 114.37 ? 152  TYR B CE2   1 
ATOM   8414 C  CZ    . TYR B 2 153 ? -11.646 -5.741  94.615  1.00 116.38 ? 152  TYR B CZ    1 
ATOM   8415 O  OH    . TYR B 2 153 ? -10.552 -5.016  95.029  1.00 115.93 ? 152  TYR B OH    1 
ATOM   8416 N  N     . ILE B 2 154 ? -12.483 -9.780  92.457  1.00 99.86  ? 153  ILE B N     1 
ATOM   8417 C  CA    . ILE B 2 154 ? -11.374 -10.610 92.912  1.00 100.11 ? 153  ILE B CA    1 
ATOM   8418 C  C     . ILE B 2 154 ? -10.103 -9.774  92.867  1.00 105.54 ? 153  ILE B C     1 
ATOM   8419 O  O     . ILE B 2 154 ? -9.933  -8.923  91.990  1.00 105.42 ? 153  ILE B O     1 
ATOM   8420 C  CB    . ILE B 2 154 ? -11.256 -11.901 92.064  1.00 98.27  ? 153  ILE B CB    1 
ATOM   8421 C  CG1   . ILE B 2 154 ? -10.288 -12.889 92.716  1.00 106.54 ? 153  ILE B CG1   1 
ATOM   8422 C  CG2   . ILE B 2 154 ? -10.823 -11.583 90.639  1.00 108.02 ? 153  ILE B CG2   1 
ATOM   8423 C  CD1   . ILE B 2 154 ? -10.229 -14.221 92.011  1.00 107.99 ? 153  ILE B CD1   1 
ATOM   8424 N  N     . GLU B 2 155 ? -9.223  -10.006 93.837  1.00 105.74 ? 154  GLU B N     1 
ATOM   8425 C  CA    . GLU B 2 155 ? -7.935  -9.330  93.917  1.00 110.36 ? 154  GLU B CA    1 
ATOM   8426 C  C     . GLU B 2 155 ? -6.827  -10.328 93.617  1.00 106.47 ? 154  GLU B C     1 
ATOM   8427 O  O     . GLU B 2 155 ? -6.743  -11.379 94.261  1.00 102.72 ? 154  GLU B O     1 
ATOM   8428 C  CB    . GLU B 2 155 ? -7.719  -8.700  95.295  1.00 108.55 ? 154  GLU B CB    1 
ATOM   8429 C  CG    . GLU B 2 155 ? -8.607  -7.501  95.573  1.00 113.01 ? 154  GLU B CG    1 
ATOM   8430 C  CD    . GLU B 2 155 ? -8.099  -6.654  96.724  1.00 111.69 ? 154  GLU B CD    1 
ATOM   8431 O  OE1   . GLU B 2 155 ? -7.061  -7.015  97.316  1.00 109.98 ? 154  GLU B OE1   1 
ATOM   8432 O  OE2   . GLU B 2 155 ? -8.734  -5.624  97.034  1.00 109.54 ? 154  GLU B OE2   1 
ATOM   8433 N  N     . THR B 2 156 ? -5.984  -9.999  92.640  1.00 101.49 ? 155  THR B N     1 
ATOM   8434 C  CA    . THR B 2 156 ? -4.904  -10.871 92.208  1.00 106.93 ? 155  THR B CA    1 
ATOM   8435 C  C     . THR B 2 156 ? -3.583  -10.115 92.242  1.00 107.72 ? 155  THR B C     1 
ATOM   8436 O  O     . THR B 2 156 ? -3.538  -8.893  92.410  1.00 106.72 ? 155  THR B O     1 
ATOM   8437 C  CB    . THR B 2 156 ? -5.149  -11.417 90.793  1.00 103.39 ? 155  THR B CB    1 
ATOM   8438 O  OG1   . THR B 2 156 ? -5.038  -10.349 89.843  1.00 98.24  ? 155  THR B OG1   1 
ATOM   8439 C  CG2   . THR B 2 156 ? -6.534  -12.042 90.688  1.00 100.43 ? 155  THR B CG2   1 
ATOM   8440 N  N     . SER B 2 157 ? -2.499  -10.869 92.078  1.00 109.74 ? 156  SER B N     1 
ATOM   8441 C  CA    . SER B 2 157 ? -1.160  -10.296 91.955  1.00 112.69 ? 156  SER B CA    1 
ATOM   8442 C  C     . SER B 2 157 ? -0.293  -11.322 91.242  1.00 112.22 ? 156  SER B C     1 
ATOM   8443 O  O     . SER B 2 157 ? -0.013  -12.388 91.801  1.00 119.22 ? 156  SER B O     1 
ATOM   8444 C  CB    . SER B 2 157 ? -0.584  -9.940  93.319  1.00 104.68 ? 156  SER B CB    1 
ATOM   8445 O  OG    . SER B 2 157 ? 0.830   -9.898  93.281  1.00 103.01 ? 156  SER B OG    1 
ATOM   8446 N  N     . ALA B 2 158 ? 0.134   -11.000 90.020  1.00 106.71 ? 157  ALA B N     1 
ATOM   8447 C  CA    . ALA B 2 158 ? 0.877   -11.951 89.198  1.00 109.31 ? 157  ALA B CA    1 
ATOM   8448 C  C     . ALA B 2 158 ? 2.286   -12.211 89.705  1.00 107.82 ? 157  ALA B C     1 
ATOM   8449 O  O     . ALA B 2 158 ? 3.017   -12.965 89.052  1.00 108.70 ? 157  ALA B O     1 
ATOM   8450 C  CB    . ALA B 2 158 ? 0.931   -11.464 87.747  1.00 93.46  ? 157  ALA B CB    1 
ATOM   8451 N  N     . LYS B 2 159 ? 2.676   -11.636 90.843  1.00 103.30 ? 158  LYS B N     1 
ATOM   8452 C  CA    . LYS B 2 159 ? 4.011   -11.815 91.400  1.00 105.65 ? 158  LYS B CA    1 
ATOM   8453 C  C     . LYS B 2 159 ? 4.258   -13.280 91.747  1.00 117.43 ? 158  LYS B C     1 
ATOM   8454 O  O     . LYS B 2 159 ? 3.363   -14.117 91.591  1.00 125.97 ? 158  LYS B O     1 
ATOM   8455 C  CB    . LYS B 2 159 ? 4.186   -10.927 92.633  1.00 114.05 ? 158  LYS B CB    1 
ATOM   8456 C  CG    . LYS B 2 159 ? 5.621   -10.543 92.940  1.00 119.43 ? 158  LYS B CG    1 
ATOM   8457 C  CD    . LYS B 2 159 ? 6.249   -9.808  91.772  1.00 113.30 ? 158  LYS B CD    1 
ATOM   8458 C  CE    . LYS B 2 159 ? 7.681   -9.400  92.077  1.00 119.09 ? 158  LYS B CE    1 
ATOM   8459 N  NZ    . LYS B 2 159 ? 7.757   -8.407  93.182  1.00 107.77 ? 158  LYS B NZ    1 
ATOM   8460 N  N     . ASP B 2 160 ? 5.466   -13.601 92.209  1.00 118.87 ? 159  ASP B N     1 
ATOM   8461 C  CA    . ASP B 2 160 ? 5.802   -14.986 92.531  1.00 131.38 ? 159  ASP B CA    1 
ATOM   8462 C  C     . ASP B 2 160 ? 4.797   -15.657 93.462  1.00 138.25 ? 159  ASP B C     1 
ATOM   8463 O  O     . ASP B 2 160 ? 4.468   -16.830 93.218  1.00 141.84 ? 159  ASP B O     1 
ATOM   8464 C  CB    . ASP B 2 160 ? 7.223   -15.049 93.111  1.00 145.69 ? 159  ASP B CB    1 
ATOM   8465 C  CG    . ASP B 2 160 ? 8.270   -14.547 92.136  1.00 166.05 ? 159  ASP B CG    1 
ATOM   8466 O  OD1   . ASP B 2 160 ? 8.040   -14.640 90.910  1.00 130.89 ? 159  ASP B OD1   1 
ATOM   8467 O  OD2   . ASP B 2 160 ? 9.323   -14.060 92.598  1.00 191.51 ? 159  ASP B OD2   1 
ATOM   8468 N  N     . PRO B 2 161 ? 4.277   -15.015 94.509  1.00 143.29 ? 160  PRO B N     1 
ATOM   8469 C  CA    . PRO B 2 161 ? 3.107   -15.573 95.195  1.00 138.74 ? 160  PRO B CA    1 
ATOM   8470 C  C     . PRO B 2 161 ? 1.899   -15.553 94.278  1.00 137.31 ? 160  PRO B C     1 
ATOM   8471 O  O     . PRO B 2 161 ? 1.535   -14.494 93.744  1.00 128.81 ? 160  PRO B O     1 
ATOM   8472 C  CB    . PRO B 2 161 ? 2.917   -14.635 96.397  1.00 135.73 ? 160  PRO B CB    1 
ATOM   8473 C  CG    . PRO B 2 161 ? 4.255   -14.029 96.615  1.00 130.76 ? 160  PRO B CG    1 
ATOM   8474 C  CD    . PRO B 2 161 ? 4.830   -13.862 95.243  1.00 133.61 ? 160  PRO B CD    1 
ATOM   8475 N  N     . PRO B 2 162 ? 1.243   -16.704 94.077  1.00 155.32 ? 161  PRO B N     1 
ATOM   8476 C  CA    . PRO B 2 162 ? 0.229   -16.814 93.015  1.00 152.39 ? 161  PRO B CA    1 
ATOM   8477 C  C     . PRO B 2 162 ? -0.934  -15.844 93.167  1.00 145.47 ? 161  PRO B C     1 
ATOM   8478 O  O     . PRO B 2 162 ? -1.111  -14.945 92.339  1.00 155.74 ? 161  PRO B O     1 
ATOM   8479 C  CB    . PRO B 2 162 ? -0.242  -18.270 93.134  1.00 169.13 ? 161  PRO B CB    1 
ATOM   8480 C  CG    . PRO B 2 162 ? 0.083   -18.666 94.544  1.00 151.48 ? 161  PRO B CG    1 
ATOM   8481 C  CD    . PRO B 2 162 ? 1.346   -17.934 94.881  1.00 154.99 ? 161  PRO B CD    1 
ATOM   8482 N  N     . LEU B 2 163 ? -1.736  -16.039 94.213  1.00 132.57 ? 162  LEU B N     1 
ATOM   8483 C  CA    . LEU B 2 163 ? -2.848  -15.157 94.556  1.00 128.47 ? 162  LEU B CA    1 
ATOM   8484 C  C     . LEU B 2 163 ? -3.920  -15.108 93.473  1.00 114.86 ? 162  LEU B C     1 
ATOM   8485 O  O     . LEU B 2 163 ? -3.957  -14.175 92.663  1.00 101.24 ? 162  LEU B O     1 
ATOM   8486 C  CB    . LEU B 2 163 ? -2.345  -13.744 94.853  1.00 131.16 ? 162  LEU B CB    1 
ATOM   8487 C  CG    . LEU B 2 163 ? -3.413  -12.816 95.432  1.00 127.15 ? 162  LEU B CG    1 
ATOM   8488 C  CD1   . LEU B 2 163 ? -3.902  -13.322 96.779  1.00 106.22 ? 162  LEU B CD1   1 
ATOM   8489 C  CD2   . LEU B 2 163 ? -2.870  -11.424 95.553  1.00 129.56 ? 162  LEU B CD2   1 
ATOM   8490 N  N     . ASN B 2 164 ? -4.792  -16.116 93.459  1.00 118.83 ? 163  ASN B N     1 
ATOM   8491 C  CA    . ASN B 2 164 ? -6.048  -16.101 92.711  1.00 105.56 ? 163  ASN B CA    1 
ATOM   8492 C  C     . ASN B 2 164 ? -5.853  -15.882 91.214  1.00 110.94 ? 163  ASN B C     1 
ATOM   8493 O  O     . ASN B 2 164 ? -6.764  -15.402 90.530  1.00 104.43 ? 163  ASN B O     1 
ATOM   8494 C  CB    . ASN B 2 164 ? -7.004  -15.045 93.276  1.00 105.55 ? 163  ASN B CB    1 
ATOM   8495 C  CG    . ASN B 2 164 ? -7.249  -15.216 94.765  1.00 111.85 ? 163  ASN B CG    1 
ATOM   8496 O  OD1   . ASN B 2 164 ? -7.271  -16.335 95.283  1.00 109.71 ? 163  ASN B OD1   1 
ATOM   8497 N  ND2   . ASN B 2 164 ? -7.430  -14.102 95.463  1.00 107.82 ? 163  ASN B ND2   1 
ATOM   8498 N  N     . VAL B 2 165 ? -4.682  -16.226 90.678  1.00 111.31 ? 164  VAL B N     1 
ATOM   8499 C  CA    . VAL B 2 165 ? -4.477  -16.124 89.237  1.00 100.98 ? 164  VAL B CA    1 
ATOM   8500 C  C     . VAL B 2 165 ? -5.317  -17.168 88.510  1.00 102.75 ? 164  VAL B C     1 
ATOM   8501 O  O     . VAL B 2 165 ? -6.052  -16.852 87.567  1.00 104.83 ? 164  VAL B O     1 
ATOM   8502 C  CB    . VAL B 2 165 ? -2.983  -16.258 88.892  1.00 102.72 ? 164  VAL B CB    1 
ATOM   8503 C  CG1   . VAL B 2 165 ? -2.806  -16.644 87.438  1.00 92.95  ? 164  VAL B CG1   1 
ATOM   8504 C  CG2   . VAL B 2 165 ? -2.256  -14.955 89.183  1.00 104.26 ? 164  VAL B CG2   1 
ATOM   8505 N  N     . ASP B 2 166 ? -5.227  -18.426 88.945  1.00 104.15 ? 165  ASP B N     1 
ATOM   8506 C  CA    . ASP B 2 166 ? -6.040  -19.474 88.339  1.00 98.53  ? 165  ASP B CA    1 
ATOM   8507 C  C     . ASP B 2 166 ? -7.512  -19.320 88.697  1.00 100.97 ? 165  ASP B C     1 
ATOM   8508 O  O     . ASP B 2 166 ? -8.382  -19.642 87.879  1.00 105.14 ? 165  ASP B O     1 
ATOM   8509 C  CB    . ASP B 2 166 ? -5.531  -20.849 88.769  1.00 91.87  ? 165  ASP B CB    1 
ATOM   8510 C  CG    . ASP B 2 166 ? -4.095  -21.094 88.353  1.00 114.80 ? 165  ASP B CG    1 
ATOM   8511 O  OD1   . ASP B 2 166 ? -3.186  -20.498 88.968  1.00 133.19 ? 165  ASP B OD1   1 
ATOM   8512 O  OD2   . ASP B 2 166 ? -3.873  -21.879 87.407  1.00 121.53 ? 165  ASP B OD2   1 
ATOM   8513 N  N     . LYS B 2 167 ? -7.811  -18.827 89.902  1.00 100.13 ? 166  LYS B N     1 
ATOM   8514 C  CA    . LYS B 2 167 ? -9.202  -18.689 90.321  1.00 98.07  ? 166  LYS B CA    1 
ATOM   8515 C  C     . LYS B 2 167 ? -9.932  -17.642 89.488  1.00 99.65  ? 166  LYS B C     1 
ATOM   8516 O  O     . LYS B 2 167 ? -11.114 -17.812 89.169  1.00 96.87  ? 166  LYS B O     1 
ATOM   8517 C  CB    . LYS B 2 167 ? -9.274  -18.332 91.805  1.00 107.53 ? 166  LYS B CB    1 
ATOM   8518 C  CG    . LYS B 2 167 ? -10.690 -18.281 92.356  1.00 105.78 ? 166  LYS B CG    1 
ATOM   8519 C  CD    . LYS B 2 167 ? -10.770 -17.425 93.607  1.00 114.76 ? 166  LYS B CD    1 
ATOM   8520 C  CE    . LYS B 2 167 ? -12.204 -17.296 94.092  1.00 123.69 ? 166  LYS B CE    1 
ATOM   8521 N  NZ    . LYS B 2 167 ? -12.397 -16.103 94.964  1.00 120.52 ? 166  LYS B NZ    1 
ATOM   8522 N  N     . ALA B 2 168 ? -9.246  -16.554 89.127  1.00 102.24 ? 167  ALA B N     1 
ATOM   8523 C  CA    . ALA B 2 168 ? -9.886  -15.495 88.352  1.00 96.77  ? 167  ALA B CA    1 
ATOM   8524 C  C     . ALA B 2 168 ? -10.359 -16.013 86.999  1.00 98.24  ? 167  ALA B C     1 
ATOM   8525 O  O     . ALA B 2 168 ? -11.489 -15.739 86.578  1.00 101.60 ? 167  ALA B O     1 
ATOM   8526 C  CB    . ALA B 2 168 ? -8.927  -14.318 88.177  1.00 91.42  ? 167  ALA B CB    1 
ATOM   8527 N  N     . PHE B 2 169 ? -9.506  -16.766 86.302  1.00 95.33  ? 168  PHE B N     1 
ATOM   8528 C  CA    . PHE B 2 169 ? -9.921  -17.368 85.038  1.00 97.33  ? 168  PHE B CA    1 
ATOM   8529 C  C     . PHE B 2 169 ? -10.975 -18.443 85.269  1.00 92.74  ? 168  PHE B C     1 
ATOM   8530 O  O     . PHE B 2 169 ? -12.014 -18.463 84.599  1.00 93.89  ? 168  PHE B O     1 
ATOM   8531 C  CB    . PHE B 2 169 ? -8.715  -17.953 84.302  1.00 93.69  ? 168  PHE B CB    1 
ATOM   8532 C  CG    . PHE B 2 169 ? -7.774  -16.919 83.752  1.00 88.63  ? 168  PHE B CG    1 
ATOM   8533 C  CD1   . PHE B 2 169 ? -8.023  -16.315 82.530  1.00 98.07  ? 168  PHE B CD1   1 
ATOM   8534 C  CD2   . PHE B 2 169 ? -6.631  -16.563 84.447  1.00 92.02  ? 168  PHE B CD2   1 
ATOM   8535 C  CE1   . PHE B 2 169 ? -7.155  -15.367 82.018  1.00 92.80  ? 168  PHE B CE1   1 
ATOM   8536 C  CE2   . PHE B 2 169 ? -5.760  -15.617 83.941  1.00 89.78  ? 168  PHE B CE2   1 
ATOM   8537 C  CZ    . PHE B 2 169 ? -6.022  -15.018 82.726  1.00 91.90  ? 168  PHE B CZ    1 
ATOM   8538 N  N     . HIS B 2 170 ? -10.724 -19.347 86.220  1.00 91.89  ? 169  HIS B N     1 
ATOM   8539 C  CA    . HIS B 2 170 ? -11.661 -20.437 86.474  1.00 98.24  ? 169  HIS B CA    1 
ATOM   8540 C  C     . HIS B 2 170 ? -13.028 -19.921 86.904  1.00 101.48 ? 169  HIS B C     1 
ATOM   8541 O  O     . HIS B 2 170 ? -14.050 -20.532 86.573  1.00 101.82 ? 169  HIS B O     1 
ATOM   8542 C  CB    . HIS B 2 170 ? -11.096 -21.387 87.531  1.00 93.89  ? 169  HIS B CB    1 
ATOM   8543 C  CG    . HIS B 2 170 ? -9.951  -22.221 87.046  1.00 92.50  ? 169  HIS B CG    1 
ATOM   8544 N  ND1   . HIS B 2 170 ? -9.640  -23.447 87.593  1.00 92.91  ? 169  HIS B ND1   1 
ATOM   8545 C  CD2   . HIS B 2 170 ? -9.042  -22.005 86.065  1.00 94.35  ? 169  HIS B CD2   1 
ATOM   8546 C  CE1   . HIS B 2 170 ? -8.589  -23.951 86.970  1.00 90.74  ? 169  HIS B CE1   1 
ATOM   8547 N  NE2   . HIS B 2 170 ? -8.207  -23.096 86.039  1.00 98.53  ? 169  HIS B NE2   1 
ATOM   8548 N  N     . ASP B 2 171 ? -13.073 -18.804 87.635  1.00 97.00  ? 170  ASP B N     1 
ATOM   8549 C  CA    . ASP B 2 171 ? -14.363 -18.222 87.991  1.00 92.91  ? 170  ASP B CA    1 
ATOM   8550 C  C     . ASP B 2 171 ? -15.077 -17.670 86.764  1.00 105.03 ? 170  ASP B C     1 
ATOM   8551 O  O     . ASP B 2 171 ? -16.299 -17.808 86.639  1.00 103.07 ? 170  ASP B O     1 
ATOM   8552 C  CB    . ASP B 2 171 ? -14.184 -17.128 89.042  1.00 103.31 ? 170  ASP B CB    1 
ATOM   8553 C  CG    . ASP B 2 171 ? -13.942 -17.686 90.433  1.00 127.53 ? 170  ASP B CG    1 
ATOM   8554 O  OD1   . ASP B 2 171 ? -14.235 -18.880 90.662  1.00 119.21 ? 170  ASP B OD1   1 
ATOM   8555 O  OD2   . ASP B 2 171 ? -13.469 -16.924 91.301  1.00 125.20 ? 170  ASP B OD2   1 
ATOM   8556 N  N     . LEU B 2 172 ? -14.334 -17.043 85.846  1.00 103.75 ? 171  LEU B N     1 
ATOM   8557 C  CA    . LEU B 2 172 ? -14.951 -16.549 84.618  1.00 95.98  ? 171  LEU B CA    1 
ATOM   8558 C  C     . LEU B 2 172 ? -15.490 -17.692 83.771  1.00 97.71  ? 171  LEU B C     1 
ATOM   8559 O  O     . LEU B 2 172 ? -16.523 -17.541 83.109  1.00 102.08 ? 171  LEU B O     1 
ATOM   8560 C  CB    . LEU B 2 172 ? -13.949 -15.713 83.819  1.00 97.77  ? 171  LEU B CB    1 
ATOM   8561 C  CG    . LEU B 2 172 ? -14.484 -15.093 82.524  1.00 94.77  ? 171  LEU B CG    1 
ATOM   8562 C  CD1   . LEU B 2 172 ? -15.732 -14.268 82.799  1.00 99.90  ? 171  LEU B CD1   1 
ATOM   8563 C  CD2   . LEU B 2 172 ? -13.423 -14.246 81.841  1.00 89.59  ? 171  LEU B CD2   1 
ATOM   8564 N  N     . VAL B 2 173 ? -14.811 -18.841 83.780  1.00 98.94  ? 172  VAL B N     1 
ATOM   8565 C  CA    . VAL B 2 173 ? -15.363 -20.023 83.127  1.00 98.87  ? 172  VAL B CA    1 
ATOM   8566 C  C     . VAL B 2 173 ? -16.609 -20.499 83.862  1.00 99.23  ? 172  VAL B C     1 
ATOM   8567 O  O     . VAL B 2 173 ? -17.558 -20.989 83.239  1.00 103.81 ? 172  VAL B O     1 
ATOM   8568 C  CB    . VAL B 2 173 ? -14.295 -21.129 83.033  1.00 97.57  ? 172  VAL B CB    1 
ATOM   8569 C  CG1   . VAL B 2 173 ? -14.874 -22.388 82.404  1.00 96.07  ? 172  VAL B CG1   1 
ATOM   8570 C  CG2   . VAL B 2 173 ? -13.096 -20.641 82.235  1.00 90.70  ? 172  VAL B CG2   1 
ATOM   8571 N  N     . ARG B 2 174 ? -16.639 -20.351 85.190  1.00 96.91  ? 173  ARG B N     1 
ATOM   8572 C  CA    . ARG B 2 174 ? -17.825 -20.737 85.950  1.00 100.15 ? 173  ARG B CA    1 
ATOM   8573 C  C     . ARG B 2 174 ? -18.995 -19.802 85.665  1.00 99.65  ? 173  ARG B C     1 
ATOM   8574 O  O     . ARG B 2 174 ? -20.144 -20.250 85.580  1.00 101.54 ? 173  ARG B O     1 
ATOM   8575 C  CB    . ARG B 2 174 ? -17.510 -20.762 87.447  1.00 99.91  ? 173  ARG B CB    1 
ATOM   8576 C  CG    . ARG B 2 174 ? -16.560 -21.872 87.874  1.00 97.94  ? 173  ARG B CG    1 
ATOM   8577 C  CD    . ARG B 2 174 ? -16.341 -21.870 89.380  1.00 94.55  ? 173  ARG B CD    1 
ATOM   8578 N  NE    . ARG B 2 174 ? -15.418 -22.918 89.803  1.00 94.98  ? 173  ARG B NE    1 
ATOM   8579 C  CZ    . ARG B 2 174 ? -14.143 -22.718 90.107  1.00 94.98  ? 173  ARG B CZ    1 
ATOM   8580 N  NH1   . ARG B 2 174 ? -13.604 -21.511 90.068  1.00 97.79  ? 173  ARG B NH1   1 
ATOM   8581 N  NH2   . ARG B 2 174 ? -13.390 -23.756 90.462  1.00 95.48  ? 173  ARG B NH2   1 
ATOM   8582 N  N     . VAL B 2 175 ? -18.724 -18.502 85.518  1.00 96.89  ? 174  VAL B N     1 
ATOM   8583 C  CA    . VAL B 2 175 ? -19.795 -17.547 85.242  1.00 103.49 ? 174  VAL B CA    1 
ATOM   8584 C  C     . VAL B 2 175 ? -20.464 -17.864 83.910  1.00 111.65 ? 174  VAL B C     1 
ATOM   8585 O  O     . VAL B 2 175 ? -21.693 -17.806 83.786  1.00 118.65 ? 174  VAL B O     1 
ATOM   8586 C  CB    . VAL B 2 175 ? -19.251 -16.106 85.275  1.00 106.51 ? 174  VAL B CB    1 
ATOM   8587 C  CG1   . VAL B 2 175 ? -20.331 -15.117 84.862  1.00 115.02 ? 174  VAL B CG1   1 
ATOM   8588 C  CG2   . VAL B 2 175 ? -18.728 -15.765 86.657  1.00 102.10 ? 174  VAL B CG2   1 
ATOM   8589 N  N     . ILE B 2 176 ? -19.667 -18.214 82.898  1.00 104.85 ? 175  ILE B N     1 
ATOM   8590 C  CA    . ILE B 2 176 ? -20.218 -18.522 81.581  1.00 110.76 ? 175  ILE B CA    1 
ATOM   8591 C  C     . ILE B 2 176 ? -21.086 -19.773 81.642  1.00 110.83 ? 175  ILE B C     1 
ATOM   8592 O  O     . ILE B 2 176 ? -22.119 -19.865 80.966  1.00 114.35 ? 175  ILE B O     1 
ATOM   8593 C  CB    . ILE B 2 176 ? -19.079 -18.664 80.553  1.00 101.20 ? 175  ILE B CB    1 
ATOM   8594 C  CG1   . ILE B 2 176 ? -18.348 -17.330 80.387  1.00 93.71  ? 175  ILE B CG1   1 
ATOM   8595 C  CG2   . ILE B 2 176 ? -19.611 -19.158 79.216  1.00 95.61  ? 175  ILE B CG2   1 
ATOM   8596 C  CD1   . ILE B 2 176 ? -17.041 -17.440 79.644  1.00 100.09 ? 175  ILE B CD1   1 
ATOM   8597 N  N     . ARG B 2 177 ? -20.691 -20.751 82.461  1.00 107.78 ? 176  ARG B N     1 
ATOM   8598 C  CA    . ARG B 2 177 ? -21.457 -21.987 82.570  1.00 109.54 ? 176  ARG B CA    1 
ATOM   8599 C  C     . ARG B 2 177 ? -22.796 -21.788 83.266  1.00 114.37 ? 176  ARG B C     1 
ATOM   8600 O  O     . ARG B 2 177 ? -23.699 -22.612 83.086  1.00 114.01 ? 176  ARG B O     1 
ATOM   8601 C  CB    . ARG B 2 177 ? -20.646 -23.049 83.315  1.00 96.50  ? 176  ARG B CB    1 
ATOM   8602 C  CG    . ARG B 2 177 ? -19.397 -23.515 82.589  1.00 87.16  ? 176  ARG B CG    1 
ATOM   8603 C  CD    . ARG B 2 177 ? -18.667 -24.574 83.395  1.00 88.03  ? 176  ARG B CD    1 
ATOM   8604 N  NE    . ARG B 2 177 ? -17.435 -25.007 82.750  1.00 91.72  ? 176  ARG B NE    1 
ATOM   8605 C  CZ    . ARG B 2 177 ? -16.619 -25.931 83.239  1.00 100.12 ? 176  ARG B CZ    1 
ATOM   8606 N  NH1   . ARG B 2 177 ? -16.873 -26.540 84.386  1.00 108.03 ? 176  ARG B NH1   1 
ATOM   8607 N  NH2   . ARG B 2 177 ? -15.520 -26.252 82.562  1.00 101.46 ? 176  ARG B NH2   1 
ATOM   8608 N  N     . GLN B 2 178 ? -22.949 -20.724 84.056  1.00 123.30 ? 177  GLN B N     1 
ATOM   8609 C  CA    . GLN B 2 178 ? -24.176 -20.487 84.808  1.00 132.33 ? 177  GLN B CA    1 
ATOM   8610 C  C     . GLN B 2 178 ? -24.856 -19.176 84.432  1.00 130.80 ? 177  GLN B C     1 
ATOM   8611 O  O     . GLN B 2 178 ? -25.805 -18.768 85.112  1.00 139.33 ? 177  GLN B O     1 
ATOM   8612 C  CB    . GLN B 2 178 ? -23.893 -20.511 86.315  1.00 124.20 ? 177  GLN B CB    1 
ATOM   8613 C  CG    . GLN B 2 178 ? -23.044 -21.688 86.782  1.00 139.41 ? 177  GLN B CG    1 
ATOM   8614 C  CD    . GLN B 2 178 ? -23.699 -23.034 86.528  1.00 146.86 ? 177  GLN B CD    1 
ATOM   8615 O  OE1   . GLN B 2 178 ? -24.920 -23.133 86.405  1.00 149.02 ? 177  GLN B OE1   1 
ATOM   8616 N  NE2   . GLN B 2 178 ? -22.885 -24.081 86.449  1.00 139.20 ? 177  GLN B NE2   1 
ATOM   8617 N  N     . GLN B 2 179 ? -24.401 -18.508 83.377  1.00 128.05 ? 178  GLN B N     1 
ATOM   8618 C  CA    . GLN B 2 179 ? -25.004 -17.251 82.948  1.00 139.03 ? 178  GLN B CA    1 
ATOM   8619 C  C     . GLN B 2 179 ? -26.351 -17.503 82.277  1.00 144.03 ? 178  GLN B C     1 
ATOM   8620 O  O     . GLN B 2 179 ? -27.245 -16.657 82.301  1.00 141.38 ? 178  GLN B O     1 
ATOM   8621 C  CB    . GLN B 2 179 ? -24.062 -16.500 81.999  1.00 144.25 ? 178  GLN B CB    1 
ATOM   8622 C  CG    . GLN B 2 179 ? -24.525 -15.101 81.613  1.00 152.50 ? 178  GLN B CG    1 
ATOM   8623 C  CD    . GLN B 2 179 ? -25.304 -15.077 80.311  1.00 164.73 ? 178  GLN B CD    1 
ATOM   8624 O  OE1   . GLN B 2 179 ? -25.375 -16.078 79.598  1.00 166.20 ? 178  GLN B OE1   1 
ATOM   8625 N  NE2   . GLN B 2 179 ? -25.891 -13.928 79.993  1.00 154.87 ? 178  GLN B NE2   1 
ATOM   8626 O  OXT   . GLN B 2 179 ? -26.578 -18.567 81.700  1.00 151.72 ? 178  GLN B OXT   1 
HETATM 8627 C  C2    . 5H5 C 3 .   ? -23.354 -15.497 43.263  1.00 108.55 ? 1101 5H5 A C2    1 
HETATM 8628 C  C4    . 5H5 C 3 .   ? -22.229 -16.477 43.428  1.00 102.74 ? 1101 5H5 A C4    1 
HETATM 8629 C  C6    . 5H5 C 3 .   ? -22.340 -17.139 44.796  1.00 97.53  ? 1101 5H5 A C6    1 
HETATM 8630 C  C8    . 5H5 C 3 .   ? -20.338 -15.633 42.115  1.00 97.42  ? 1101 5H5 A C8    1 
HETATM 8631 C  C12   . 5H5 C 3 .   ? -16.677 -13.348 39.933  1.00 89.23  ? 1101 5H5 A C12   1 
HETATM 8632 C  C15   . 5H5 C 3 .   ? -17.051 -14.645 36.557  1.00 92.49  ? 1101 5H5 A C15   1 
HETATM 8633 C  C16   . 5H5 C 3 .   ? -18.240 -15.125 36.078  1.00 95.27  ? 1101 5H5 A C16   1 
HETATM 8634 C  C18   . 5H5 C 3 .   ? -18.446 -15.092 38.214  1.00 95.79  ? 1101 5H5 A C18   1 
HETATM 8635 C  C19   . 5H5 C 3 .   ? -19.066 -15.261 39.576  1.00 93.18  ? 1101 5H5 A C19   1 
HETATM 8636 C  C21   . 5H5 C 3 .   ? -20.960 -16.041 40.928  1.00 98.84  ? 1101 5H5 A C21   1 
HETATM 8637 C  C24   . 5H5 C 3 .   ? -18.320 -15.107 32.484  1.00 101.69 ? 1101 5H5 A C24   1 
HETATM 8638 C  C27   . 5H5 C 3 .   ? -20.580 -16.932 34.648  1.00 100.01 ? 1101 5H5 A C27   1 
HETATM 8639 N  N1    . 5H5 C 3 .   ? -23.195 -14.172 43.754  1.00 102.55 ? 1101 5H5 A N1    1 
HETATM 8640 O  O3    . 5H5 C 3 .   ? -24.388 -15.851 42.712  1.00 108.23 ? 1101 5H5 A O3    1 
HETATM 8641 O  O7    . 5H5 C 3 .   ? -20.964 -15.817 43.323  1.00 103.11 ? 1101 5H5 A O7    1 
HETATM 8642 C  C9    . 5H5 C 3 .   ? -19.073 -15.032 42.076  1.00 92.87  ? 1101 5H5 A C9    1 
HETATM 8643 C  C10   . 5H5 C 3 .   ? -18.406 -14.829 40.860  1.00 92.47  ? 1101 5H5 A C10   1 
HETATM 8644 O  O11   . 5H5 C 3 .   ? -17.175 -14.231 40.927  1.00 91.24  ? 1101 5H5 A O11   1 
HETATM 8645 C  C13   . 5H5 C 3 .   ? -16.132 -14.181 38.784  1.00 89.43  ? 1101 5H5 A C13   1 
HETATM 8646 N  N14   . 5H5 C 3 .   ? -17.199 -14.636 37.890  1.00 93.14  ? 1101 5H5 A N14   1 
HETATM 8647 N  N17   . 5H5 C 3 .   ? -19.097 -15.403 37.061  1.00 96.88  ? 1101 5H5 A N17   1 
HETATM 8648 C  C20   . 5H5 C 3 .   ? -20.339 -15.860 39.684  1.00 92.91  ? 1101 5H5 A C20   1 
HETATM 8649 C  C22   . 5H5 C 3 .   ? -18.522 -15.311 34.621  1.00 101.27 ? 1101 5H5 A C22   1 
HETATM 8650 N  N23   . 5H5 C 3 .   ? -17.782 -14.712 33.669  1.00 102.48 ? 1101 5H5 A N23   1 
HETATM 8651 N  N25   . 5H5 C 3 .   ? -19.373 -15.940 32.716  1.00 98.33  ? 1101 5H5 A N25   1 
HETATM 8652 N  N26   . 5H5 C 3 .   ? -19.491 -16.062 34.108  1.00 98.06  ? 1101 5H5 A N26   1 
HETATM 8653 C  C28   . 5H5 C 3 .   ? -20.101 -18.379 34.613  1.00 99.98  ? 1101 5H5 A C28   1 
HETATM 8654 C  C29   . 5H5 C 3 .   ? -21.902 -16.776 33.897  1.00 114.90 ? 1101 5H5 A C29   1 
HETATM 8655 P  PG    . GNP D 4 .   ? -0.105  -3.724  77.831  1.00 102.17 ? 201  GNP B PG    1 
HETATM 8656 O  O1G   . GNP D 4 .   ? 0.443   -2.329  77.510  1.00 112.54 ? 201  GNP B O1G   1 
HETATM 8657 O  O2G   . GNP D 4 .   ? 0.740   -4.882  77.303  1.00 99.05  ? 201  GNP B O2G   1 
HETATM 8658 O  O3G   . GNP D 4 .   ? -1.608  -3.887  77.580  1.00 94.85  ? 201  GNP B O3G   1 
HETATM 8659 N  N3B   . GNP D 4 .   ? 0.120   -3.783  79.614  1.00 109.88 ? 201  GNP B N3B   1 
HETATM 8660 P  PB    . GNP D 4 .   ? -0.434  -5.047  80.574  1.00 85.90  ? 201  GNP B PB    1 
HETATM 8661 O  O1B   . GNP D 4 .   ? -1.675  -4.697  81.353  1.00 103.29 ? 201  GNP B O1B   1 
HETATM 8662 O  O2B   . GNP D 4 .   ? -0.361  -6.358  79.840  1.00 89.19  ? 201  GNP B O2B   1 
HETATM 8663 O  O3A   . GNP D 4 .   ? 0.781   -5.068  81.740  1.00 106.44 ? 201  GNP B O3A   1 
HETATM 8664 P  PA    . GNP D 4 .   ? 2.082   -6.043  81.752  1.00 103.62 ? 201  GNP B PA    1 
HETATM 8665 O  O1A   . GNP D 4 .   ? 1.707   -7.434  82.155  1.00 97.25  ? 201  GNP B O1A   1 
HETATM 8666 O  O2A   . GNP D 4 .   ? 2.975   -5.776  80.577  1.00 111.99 ? 201  GNP B O2A   1 
HETATM 8667 O  "O5'" . GNP D 4 .   ? 2.779   -5.419  83.122  1.00 112.98 ? 201  GNP B "O5'" 1 
HETATM 8668 C  "C5'" . GNP D 4 .   ? 3.320   -4.126  83.148  1.00 115.51 ? 201  GNP B "C5'" 1 
HETATM 8669 C  "C4'" . GNP D 4 .   ? 4.242   -3.986  84.340  1.00 112.33 ? 201  GNP B "C4'" 1 
HETATM 8670 O  "O4'" . GNP D 4 .   ? 3.535   -4.253  85.557  1.00 111.88 ? 201  GNP B "O4'" 1 
HETATM 8671 C  "C3'" . GNP D 4 .   ? 5.450   -4.926  84.333  1.00 114.71 ? 201  GNP B "C3'" 1 
HETATM 8672 O  "O3'" . GNP D 4 .   ? 6.548   -4.223  84.866  1.00 125.20 ? 201  GNP B "O3'" 1 
HETATM 8673 C  "C2'" . GNP D 4 .   ? 5.001   -6.045  85.269  1.00 107.54 ? 201  GNP B "C2'" 1 
HETATM 8674 O  "O2'" . GNP D 4 .   ? 6.086   -6.729  85.819  1.00 101.25 ? 201  GNP B "O2'" 1 
HETATM 8675 C  "C1'" . GNP D 4 .   ? 4.188   -5.244  86.292  1.00 112.89 ? 201  GNP B "C1'" 1 
HETATM 8676 N  N9    . GNP D 4 .   ? 3.220   -6.037  87.014  1.00 114.38 ? 201  GNP B N9    1 
HETATM 8677 C  C8    . GNP D 4 .   ? 2.113   -6.673  86.504  1.00 107.74 ? 201  GNP B C8    1 
HETATM 8678 N  N7    . GNP D 4 .   ? 1.438   -7.309  87.413  1.00 107.30 ? 201  GNP B N7    1 
HETATM 8679 C  C5    . GNP D 4 .   ? 2.126   -7.089  88.580  1.00 112.42 ? 201  GNP B C5    1 
HETATM 8680 C  C6    . GNP D 4 .   ? 1.868   -7.533  89.910  1.00 107.77 ? 201  GNP B C6    1 
HETATM 8681 O  O6    . GNP D 4 .   ? 0.955   -8.226  90.326  1.00 100.46 ? 201  GNP B O6    1 
HETATM 8682 N  N1    . GNP D 4 .   ? 2.852   -7.055  90.788  1.00 115.28 ? 201  GNP B N1    1 
HETATM 8683 C  C2    . GNP D 4 .   ? 3.921   -6.273  90.454  1.00 116.19 ? 201  GNP B C2    1 
HETATM 8684 N  N2    . GNP D 4 .   ? 4.756   -5.919  91.445  1.00 112.83 ? 201  GNP B N2    1 
HETATM 8685 N  N3    . GNP D 4 .   ? 4.151   -5.869  89.230  1.00 111.21 ? 201  GNP B N3    1 
HETATM 8686 C  C4    . GNP D 4 .   ? 3.237   -6.301  88.349  1.00 112.26 ? 201  GNP B C4    1 
HETATM 8687 MG MG    . MG  E 5 .   ? -0.390  -6.976  77.482  1.00 80.90  ? 202  MG  B MG    1 
HETATM 8688 O  O     . HOH F 6 .   ? 1.370   -40.482 33.128  1.00 111.09 ? 1201 HOH A O     1 
HETATM 8689 O  O     . HOH F 6 .   ? -9.261  -37.905 51.698  1.00 99.68  ? 1202 HOH A O     1 
HETATM 8690 O  O     . HOH F 6 .   ? 1.862   -15.193 33.988  1.00 58.06  ? 1203 HOH A O     1 
HETATM 8691 O  O     . HOH F 6 .   ? -0.371  -15.408 32.367  1.00 72.15  ? 1204 HOH A O     1 
HETATM 8692 O  O     . HOH F 6 .   ? -4.798  -15.682 34.374  1.00 89.46  ? 1205 HOH A O     1 
HETATM 8693 O  O     . HOH F 6 .   ? 4.918   -22.539 42.409  1.00 104.49 ? 1206 HOH A O     1 
HETATM 8694 O  O     . HOH F 6 .   ? -27.595 -4.136  60.499  1.00 87.42  ? 1207 HOH A O     1 
HETATM 8695 O  O     . HOH F 6 .   ? 25.659  -14.568 -9.827  1.00 106.72 ? 1208 HOH A O     1 
HETATM 8696 O  O     . HOH F 6 .   ? 10.635  0.396   2.800   1.00 98.12  ? 1209 HOH A O     1 
HETATM 8697 O  O     . HOH F 6 .   ? -4.640  -31.483 58.580  1.00 79.54  ? 1210 HOH A O     1 
HETATM 8698 O  O     . HOH F 6 .   ? -19.057 -6.503  55.052  1.00 91.78  ? 1211 HOH A O     1 
HETATM 8699 O  O     . HOH F 6 .   ? 14.707  -13.839 54.847  1.00 95.96  ? 1212 HOH A O     1 
HETATM 8700 O  O     . HOH F 6 .   ? 11.889  -22.014 3.539   1.00 79.85  ? 1213 HOH A O     1 
HETATM 8701 O  O     . HOH F 6 .   ? -0.198  -39.676 34.557  1.00 100.29 ? 1214 HOH A O     1 
HETATM 8702 O  O     . HOH F 6 .   ? 17.048  -8.905  47.128  1.00 85.93  ? 1215 HOH A O     1 
HETATM 8703 O  O     . HOH F 6 .   ? 14.569  -17.201 -15.170 1.00 105.81 ? 1216 HOH A O     1 
HETATM 8704 O  O     . HOH F 6 .   ? -2.099  -14.946 49.038  1.00 80.58  ? 1217 HOH A O     1 
HETATM 8705 O  O     . HOH F 6 .   ? -40.380 -5.818  42.682  1.00 112.97 ? 1218 HOH A O     1 
HETATM 8706 O  O     . HOH F 6 .   ? -24.639 -15.554 38.175  1.00 96.52  ? 1219 HOH A O     1 
HETATM 8707 O  O     . HOH F 6 .   ? 4.719   -26.664 44.404  1.00 89.60  ? 1220 HOH A O     1 
HETATM 8708 O  O     . HOH F 6 .   ? -9.386  -17.859 45.629  1.00 76.34  ? 1221 HOH A O     1 
HETATM 8709 O  O     . HOH F 6 .   ? -42.168 -2.539  43.173  1.00 111.82 ? 1222 HOH A O     1 
HETATM 8710 O  O     . HOH F 6 .   ? -38.109 -13.793 43.754  1.00 100.07 ? 1223 HOH A O     1 
HETATM 8711 O  O     . HOH G 6 .   ? -6.586  -16.944 68.880  1.00 80.95  ? 301  HOH B O     1 
HETATM 8712 O  O     . HOH G 6 .   ? -11.066 -26.304 89.813  1.00 100.24 ? 302  HOH B O     1 
HETATM 8713 O  O     . HOH G 6 .   ? -9.997  -22.344 90.935  1.00 95.33  ? 303  HOH B O     1 
HETATM 8714 O  O     . HOH G 6 .   ? 5.410   5.238   79.144  1.00 121.70 ? 304  HOH B O     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     . GLY A 3   ? 2.1750 2.1284 2.0025 0.3375  0.0434  -0.1845 106  GLY A N     
2    C  CA    . GLY A 3   ? 2.1903 2.1843 2.0389 0.3522  0.0460  -0.1728 106  GLY A CA    
3    C  C     . GLY A 3   ? 2.2168 2.2027 2.0754 0.3530  0.0416  -0.1620 106  GLY A C     
4    O  O     . GLY A 3   ? 2.2412 2.1845 2.0845 0.3611  0.0435  -0.1628 106  GLY A O     
5    N  N     . ASN A 4   ? 2.0771 2.1027 1.9601 0.3443  0.0360  -0.1517 107  ASN A N     
6    C  CA    . ASN A 4   ? 2.0370 2.0594 1.9297 0.3449  0.0316  -0.1408 107  ASN A CA    
7    C  C     . ASN A 4   ? 1.9900 1.9747 1.8753 0.3244  0.0253  -0.1421 107  ASN A C     
8    O  O     . ASN A 4   ? 1.8818 1.8700 1.7700 0.3025  0.0201  -0.1461 107  ASN A O     
9    C  CB    . ASN A 4   ? 1.9443 2.0198 1.8637 0.3399  0.0270  -0.1307 107  ASN A CB    
10   C  CG    . ASN A 4   ? 1.9892 2.0675 1.9174 0.3476  0.0239  -0.1190 107  ASN A CG    
11   O  OD1   . ASN A 4   ? 2.0368 2.0756 1.9533 0.3485  0.0231  -0.1173 107  ASN A OD1   
12   N  ND2   . ASN A 4   ? 1.9811 2.1064 1.9297 0.3525  0.0219  -0.1109 107  ASN A ND2   
13   N  N     . ARG A 5   ? 2.1447 2.0938 2.0207 0.3317  0.0262  -0.1381 108  ARG A N     
14   C  CA    . ARG A 5   ? 2.1318 2.0468 2.0027 0.3124  0.0209  -0.1379 108  ARG A CA    
15   C  C     . ARG A 5   ? 2.1475 2.0911 2.0394 0.2945  0.0131  -0.1290 108  ARG A C     
16   O  O     . ARG A 5   ? 2.1452 2.0712 2.0369 0.2743  0.0082  -0.1299 108  ARG A O     
17   C  CB    . ARG A 5   ? 2.1467 2.0176 2.0028 0.3253  0.0248  -0.1343 108  ARG A CB    
18   C  CG    . ARG A 5   ? 2.1795 2.0633 2.0476 0.3330  0.0230  -0.1199 108  ARG A CG    
19   C  CD    . ARG A 5   ? 2.2138 2.1408 2.0941 0.3544  0.0254  -0.1137 108  ARG A CD    
20   N  NE    . ARG A 5   ? 2.3206 2.2371 2.1870 0.3779  0.0339  -0.1195 108  ARG A NE    
21   C  CZ    . ARG A 5   ? 2.2532 2.2062 2.1286 0.3985  0.0375  -0.1161 108  ARG A CZ    
22   N  NH1   . ARG A 5   ? 2.1839 2.1867 2.0824 0.3978  0.0329  -0.1073 108  ARG A NH1   
23   N  NH2   . ARG A 5   ? 2.2615 2.2011 2.1226 0.4204  0.0462  -0.1219 108  ARG A NH2   
24   N  N     . GLU A 6   ? 1.9771 1.9647 1.8869 0.3014  0.0119  -0.1207 109  GLU A N     
25   C  CA    . GLU A 6   ? 1.8745 1.8904 1.8028 0.2842  0.0047  -0.1136 109  GLU A CA    
26   C  C     . GLU A 6   ? 1.7537 1.7902 1.6886 0.2654  0.0014  -0.1197 109  GLU A C     
27   O  O     . GLU A 6   ? 1.6701 1.7110 1.6131 0.2460  -0.0045 -0.1172 109  GLU A O     
28   C  CB    . GLU A 6   ? 1.9191 1.9746 1.8632 0.2967  0.0039  -0.1036 109  GLU A CB    
29   C  CG    . GLU A 6   ? 1.9952 2.0345 1.9324 0.3187  0.0072  -0.0968 109  GLU A CG    
30   C  CD    . GLU A 6   ? 2.0206 2.0231 1.9501 0.3119  0.0051  -0.0914 109  GLU A CD    
31   O  OE1   . GLU A 6   ? 1.9986 2.0043 1.9357 0.2914  -0.0005 -0.0891 109  GLU A OE1   
32   O  OE2   . GLU A 6   ? 2.0860 2.0558 2.0014 0.3274  0.0095  -0.0891 109  GLU A OE2   
33   N  N     . GLU A 7   ? 1.8038 1.8530 1.7346 0.2718  0.0056  -0.1272 110  GLU A N     
34   C  CA    . GLU A 7   ? 1.7685 1.8331 1.7020 0.2550  0.0031  -0.1332 110  GLU A CA    
35   C  C     . GLU A 7   ? 1.6694 1.6966 1.5888 0.2398  0.0003  -0.1412 110  GLU A C     
36   O  O     . GLU A 7   ? 1.6078 1.6436 1.5322 0.2209  -0.0048 -0.1427 110  GLU A O     
37   C  CB    . GLU A 7   ? 1.7263 1.8134 1.6575 0.2669  0.0094  -0.1388 110  GLU A CB    
38   C  CG    . GLU A 7   ? 1.6806 1.7865 1.6140 0.2512  0.0076  -0.1438 110  GLU A CG    
39   C  CD    . GLU A 7   ? 1.6826 1.8126 1.6141 0.2635  0.0149  -0.1481 110  GLU A CD    
40   O  OE1   . GLU A 7   ? 1.6765 1.8111 1.6067 0.2847  0.0213  -0.1471 110  GLU A OE1   
41   O  OE2   . GLU A 7   ? 1.5809 1.7258 1.5121 0.2525  0.0146  -0.1521 110  GLU A OE2   
42   N  N     . LYS A 8   ? 1.6680 1.6535 1.5695 0.2477  0.0035  -0.1464 111  LYS A N     
43   C  CA    . LYS A 8   ? 1.6093 1.5586 1.4982 0.2319  0.0001  -0.1539 111  LYS A CA    
44   C  C     . LYS A 8   ? 1.6010 1.5456 1.5010 0.2144  -0.0064 -0.1466 111  LYS A C     
45   O  O     . LYS A 8   ? 1.5458 1.4835 1.4459 0.1953  -0.0117 -0.1504 111  LYS A O     
46   C  CB    . LYS A 8   ? 1.6031 1.5066 1.4698 0.2441  0.0053  -0.1607 111  LYS A CB    
47   C  CG    . LYS A 8   ? 1.6346 1.5398 1.4885 0.2645  0.0131  -0.1678 111  LYS A CG    
48   C  CD    . LYS A 8   ? 1.5795 1.5035 1.4304 0.2565  0.0122  -0.1766 111  LYS A CD    
49   C  CE    . LYS A 8   ? 1.7199 1.6493 1.5590 0.2779  0.0211  -0.1827 111  LYS A CE    
50   N  NZ    . LYS A 8   ? 1.7258 1.6772 1.5623 0.2710  0.0212  -0.1898 111  LYS A NZ    
51   N  N     . ILE A 9   ? 1.5884 1.5377 1.4975 0.2212  -0.0060 -0.1358 112  ILE A N     
52   C  CA    . ILE A 9   ? 1.5405 1.4887 1.4604 0.2059  -0.0112 -0.1280 112  ILE A CA    
53   C  C     . ILE A 9   ? 1.4906 1.4766 1.4270 0.1918  -0.0164 -0.1251 112  ILE A C     
54   O  O     . ILE A 9   ? 1.5082 1.4911 1.4499 0.1737  -0.0213 -0.1243 112  ILE A O     
55   C  CB    . ILE A 9   ? 1.5222 1.4666 1.4454 0.2184  -0.0091 -0.1170 112  ILE A CB    
56   C  CG1   . ILE A 9   ? 1.5739 1.4745 1.4788 0.2312  -0.0037 -0.1193 112  ILE A CG1   
57   C  CG2   . ILE A 9   ? 1.4302 1.3777 1.3648 0.2034  -0.0138 -0.1084 112  ILE A CG2   
58   C  CD1   . ILE A 9   ? 1.5881 1.4824 1.4936 0.2456  -0.0012 -0.1081 112  ILE A CD1   
59   N  N     . LEU A 10  ? 1.4433 1.4654 1.3881 0.1997  -0.0151 -0.1235 113  LEU A N     
60   C  CA    . LEU A 10  ? 1.3687 1.4246 1.3274 0.1864  -0.0193 -0.1210 113  LEU A CA    
61   C  C     . LEU A 10  ? 1.3699 1.4221 1.3228 0.1729  -0.0216 -0.1297 113  LEU A C     
62   O  O     . LEU A 10  ? 1.3213 1.3842 1.2822 0.1568  -0.0264 -0.1277 113  LEU A O     
63   C  CB    . LEU A 10  ? 1.3195 1.4138 1.2879 0.1975  -0.0168 -0.1177 113  LEU A CB    
64   C  CG    . LEU A 10  ? 1.2091 1.3380 1.1909 0.1843  -0.0202 -0.1151 113  LEU A CG    
65   C  CD1   . LEU A 10  ? 0.9748 1.1079 0.9671 0.1730  -0.0253 -0.1067 113  LEU A CD1   
66   C  CD2   . LEU A 10  ? 1.0976 1.2628 1.0877 0.1947  -0.0168 -0.1136 113  LEU A CD2   
67   N  N     . ASN A 11  ? 1.4412 1.4779 1.3792 0.1799  -0.0181 -0.1393 114  ASN A N     
68   C  CA    . ASN A 11  ? 1.4114 1.4445 1.3414 0.1681  -0.0206 -0.1480 114  ASN A CA    
69   C  C     . ASN A 11  ? 1.4500 1.4589 1.3781 0.1508  -0.0266 -0.1497 114  ASN A C     
70   O  O     . ASN A 11  ? 1.4042 1.4212 1.3339 0.1366  -0.0314 -0.1524 114  ASN A O     
71   C  CB    . ASN A 11  ? 1.4359 1.4536 1.3474 0.1804  -0.0153 -0.1586 114  ASN A CB    
72   C  CG    . ASN A 11  ? 1.3777 1.4276 1.2923 0.1928  -0.0098 -0.1584 114  ASN A CG    
73   O  OD1   . ASN A 11  ? 1.3832 1.4668 1.3144 0.1923  -0.0101 -0.1503 114  ASN A OD1   
74   N  ND2   . ASN A 11  ? 1.3099 1.3495 1.2082 0.2038  -0.0044 -0.1676 114  ASN A ND2   
75   N  N     . ARG A 12  ? 1.6130 1.5930 1.5380 0.1518  -0.0263 -0.1476 115  ARG A N     
76   C  CA    . ARG A 12  ? 1.6319 1.5906 1.5571 0.1346  -0.0315 -0.1486 115  ARG A CA    
77   C  C     . ARG A 12  ? 1.5185 1.4989 1.4620 0.1222  -0.0359 -0.1389 115  ARG A C     
78   O  O     . ARG A 12  ? 1.5364 1.5152 1.4837 0.1061  -0.0412 -0.1400 115  ARG A O     
79   C  CB    . ARG A 12  ? 1.6871 1.6072 1.6030 0.1390  -0.0288 -0.1487 115  ARG A CB    
80   C  CG    . ARG A 12  ? 1.7572 1.6485 1.6521 0.1499  -0.0245 -0.1595 115  ARG A CG    
81   C  CD    . ARG A 12  ? 2.0407 1.8897 1.9253 0.1525  -0.0216 -0.1594 115  ARG A CD    
82   N  NE    . ARG A 12  ? 2.1570 1.9864 2.0433 0.1318  -0.0269 -0.1610 115  ARG A NE    
83   C  CZ    . ARG A 12  ? 2.1296 1.9596 2.0291 0.1222  -0.0287 -0.1513 115  ARG A CZ    
84   N  NH1   . ARG A 12  ? 2.0669 1.9137 1.9774 0.1310  -0.0261 -0.1396 115  ARG A NH1   
85   N  NH2   . ARG A 12  ? 2.1420 1.9563 2.0438 0.1031  -0.0331 -0.1535 115  ARG A NH2   
86   N  N     . GLU A 13  ? 1.3879 1.3888 1.3422 0.1297  -0.0340 -0.1295 116  GLU A N     
87   C  CA    . GLU A 13  ? 1.3762 1.3967 1.3459 0.1188  -0.0376 -0.1208 116  GLU A CA    
88   C  C     . GLU A 13  ? 1.3197 1.3687 1.2952 0.1108  -0.0406 -0.1221 116  GLU A C     
89   O  O     . GLU A 13  ? 1.3343 1.3909 1.3180 0.0974  -0.0447 -0.1189 116  GLU A O     
90   C  CB    . GLU A 13  ? 1.4245 1.4571 1.4018 0.1291  -0.0351 -0.1111 116  GLU A CB    
91   C  CG    . GLU A 13  ? 1.5198 1.5252 1.4893 0.1407  -0.0313 -0.1088 116  GLU A CG    
92   C  CD    . GLU A 13  ? 1.8124 1.7854 1.7780 0.1301  -0.0323 -0.1090 116  GLU A CD    
93   O  OE1   . GLU A 13  ? 1.7593 1.7375 1.7342 0.1157  -0.0357 -0.1049 116  GLU A OE1   
94   O  OE2   . GLU A 13  ? 1.8863 1.8283 1.8393 0.1361  -0.0292 -0.1132 116  GLU A OE2   
95   N  N     . ILE A 14  ? 1.3123 1.3770 1.2835 0.1193  -0.0379 -0.1265 117  ILE A N     
96   C  CA    . ILE A 14  ? 1.2399 1.3297 1.2146 0.1120  -0.0398 -0.1276 117  ILE A CA    
97   C  C     . ILE A 14  ? 1.2421 1.3196 1.2094 0.0999  -0.0442 -0.1345 117  ILE A C     
98   O  O     . ILE A 14  ? 1.1831 1.2743 1.1563 0.0885  -0.0481 -0.1323 117  ILE A O     
99   C  CB    . ILE A 14  ? 1.2605 1.3694 1.2318 0.1242  -0.0348 -0.1304 117  ILE A CB    
100  C  CG1   . ILE A 14  ? 1.1861 1.3148 1.1682 0.1339  -0.0319 -0.1226 117  ILE A CG1   
101  C  CG2   . ILE A 14  ? 1.2044 1.3342 1.1758 0.1163  -0.0359 -0.1324 117  ILE A CG2   
102  C  CD1   . ILE A 14  ? 1.1606 1.3119 1.1425 0.1461  -0.0266 -0.1244 117  ILE A CD1   
103  N  N     . GLY A 15  ? 1.3037 1.3547 1.2574 0.1024  -0.0438 -0.1431 118  GLY A N     
104  C  CA    . GLY A 15  ? 1.2870 1.3260 1.2330 0.0904  -0.0491 -0.1505 118  GLY A CA    
105  C  C     . GLY A 15  ? 1.2311 1.2636 1.1871 0.0757  -0.0547 -0.1460 118  GLY A C     
106  O  O     . GLY A 15  ? 1.1722 1.2098 1.1291 0.0638  -0.0603 -0.1482 118  GLY A O     
107  N  N     . PHE A 16  ? 1.2665 1.2888 1.2302 0.0769  -0.0530 -0.1392 119  PHE A N     
108  C  CA    . PHE A 16  ? 1.2391 1.2563 1.2133 0.0635  -0.0571 -0.1341 119  PHE A CA    
109  C  C     . PHE A 16  ? 1.1718 1.2171 1.1597 0.0571  -0.0593 -0.1260 119  PHE A C     
110  O  O     . PHE A 16  ? 1.1392 1.1877 1.1341 0.0448  -0.0640 -0.1243 119  PHE A O     
111  C  CB    . PHE A 16  ? 1.2398 1.2373 1.2165 0.0674  -0.0535 -0.1285 119  PHE A CB    
112  C  CG    . PHE A 16  ? 1.2365 1.2284 1.2242 0.0542  -0.0562 -0.1227 119  PHE A CG    
113  C  CD1   . PHE A 16  ? 1.2511 1.2212 1.2357 0.0431  -0.0593 -0.1280 119  PHE A CD1   
114  C  CD2   . PHE A 16  ? 1.2513 1.2600 1.2522 0.0525  -0.0556 -0.1121 119  PHE A CD2   
115  C  CE1   . PHE A 16  ? 1.3175 1.2851 1.3140 0.0307  -0.0612 -0.1221 119  PHE A CE1   
116  C  CE2   . PHE A 16  ? 1.2242 1.2288 1.2353 0.0413  -0.0571 -0.1064 119  PHE A CE2   
117  C  CZ    . PHE A 16  ? 1.2922 1.2776 1.3021 0.0304  -0.0597 -0.1111 119  PHE A CZ    
118  N  N     . ALA A 17  ? 1.1664 1.2321 1.1582 0.0654  -0.0561 -0.1211 120  ALA A N     
119  C  CA    . ALA A 17  ? 1.1684 1.2577 1.1712 0.0595  -0.0577 -0.1138 120  ALA A CA    
120  C  C     . ALA A 17  ? 1.1023 1.2050 1.1021 0.0529  -0.0612 -0.1176 120  ALA A C     
121  O  O     . ALA A 17  ? 1.0705 1.1829 1.0775 0.0438  -0.0646 -0.1133 120  ALA A O     
122  C  CB    . ALA A 17  ? 1.1151 1.2216 1.1221 0.0689  -0.0536 -0.1082 120  ALA A CB    
123  N  N     . ILE A 18  ? 1.1660 1.2691 1.1542 0.0583  -0.0600 -0.1254 121  ILE A N     
124  C  CA    . ILE A 18  ? 1.1074 1.2234 1.0904 0.0533  -0.0628 -0.1287 121  ILE A CA    
125  C  C     . ILE A 18  ? 1.1278 1.2298 1.1034 0.0450  -0.0687 -0.1360 121  ILE A C     
126  O  O     . ILE A 18  ? 1.1594 1.2717 1.1309 0.0397  -0.0724 -0.1379 121  ILE A O     
127  C  CB    . ILE A 18  ? 1.1113 1.2377 1.0849 0.0632  -0.0580 -0.1329 121  ILE A CB    
128  C  CG1   . ILE A 18  ? 1.1983 1.3044 1.1576 0.0706  -0.0563 -0.1429 121  ILE A CG1   
129  C  CG2   . ILE A 18  ? 1.1338 1.2757 1.1160 0.0710  -0.0527 -0.1262 121  ILE A CG2   
130  C  CD1   . ILE A 18  ? 1.2801 1.3967 1.2298 0.0816  -0.0505 -0.1472 121  ILE A CD1   
131  N  N     . GLY A 19  ? 1.1579 1.2365 1.1311 0.0432  -0.0700 -0.1401 122  GLY A N     
132  C  CA    . GLY A 19  ? 1.2097 1.2751 1.1774 0.0332  -0.0765 -0.1472 122  GLY A CA    
133  C  C     . GLY A 19  ? 1.2161 1.2669 1.1645 0.0371  -0.0768 -0.1594 122  GLY A C     
134  O  O     . GLY A 19  ? 1.2252 1.2603 1.1672 0.0286  -0.0824 -0.1668 122  GLY A O     
135  N  N     . MET A 20  ? 1.2301 1.2859 1.1689 0.0493  -0.0710 -0.1621 123  MET A N     
136  C  CA    . MET A 20  ? 1.2857 1.3272 1.2043 0.0549  -0.0700 -0.1739 123  MET A CA    
137  C  C     . MET A 20  ? 1.3177 1.3501 1.2305 0.0706  -0.0614 -0.1752 123  MET A C     
138  O  O     . MET A 20  ? 1.3149 1.3645 1.2378 0.0784  -0.0563 -0.1672 123  MET A O     
139  C  CB    . MET A 20  ? 1.3824 1.4429 1.2921 0.0549  -0.0713 -0.1766 123  MET A CB    
140  C  CG    . MET A 20  ? 1.3172 1.4052 1.2351 0.0613  -0.0657 -0.1681 123  MET A CG    
141  S  SD    . MET A 20  ? 1.5560 1.6621 1.4601 0.0620  -0.0655 -0.1713 123  MET A SD    
142  C  CE    . MET A 20  ? 1.3503 1.4350 1.2301 0.0723  -0.0619 -0.1855 123  MET A CE    
143  N  N     . PRO A 21  ? 1.3703 1.3758 1.2665 0.0758  -0.0598 -0.1853 124  PRO A N     
144  C  CA    . PRO A 21  ? 1.4085 1.4040 1.2987 0.0926  -0.0513 -0.1863 124  PRO A CA    
145  C  C     . PRO A 21  ? 1.4462 1.4651 1.3324 0.1049  -0.0451 -0.1862 124  PRO A C     
146  O  O     . PRO A 21  ? 1.4516 1.4838 1.3307 0.1016  -0.0467 -0.1899 124  PRO A O     
147  C  CB    . PRO A 21  ? 1.4337 1.3922 1.3039 0.0936  -0.0517 -0.1984 124  PRO A CB    
148  C  CG    . PRO A 21  ? 1.4729 1.4308 1.3343 0.0800  -0.0597 -0.2062 124  PRO A CG    
149  C  CD    . PRO A 21  ? 1.3961 1.3785 1.2773 0.0668  -0.0659 -0.1966 124  PRO A CD    
150  N  N     . VAL A 22  ? 1.4843 1.5093 1.3755 0.1193  -0.0378 -0.1815 125  VAL A N     
151  C  CA    . VAL A 22  ? 1.4950 1.5449 1.3855 0.1314  -0.0310 -0.1806 125  VAL A CA    
152  C  C     . VAL A 22  ? 1.5803 1.6167 1.4482 0.1407  -0.0268 -0.1924 125  VAL A C     
153  O  O     . VAL A 22  ? 1.5420 1.5997 1.4064 0.1479  -0.0216 -0.1931 125  VAL A O     
154  C  CB    . VAL A 22  ? 1.3726 1.4340 1.2756 0.1445  -0.0251 -0.1724 125  VAL A CB    
155  C  CG1   . VAL A 22  ? 1.3227 1.4190 1.2320 0.1526  -0.0194 -0.1687 125  VAL A CG1   
156  C  CG2   . VAL A 22  ? 1.3778 1.4424 1.2983 0.1357  -0.0296 -0.1624 125  VAL A CG2   
157  N  N     . CYS A 23  ? 1.7725 1.7732 1.6241 0.1402  -0.0286 -0.2018 126  CYS A N     
158  C  CA    . CYS A 23  ? 1.7107 1.6944 1.5379 0.1495  -0.0245 -0.2142 126  CYS A CA    
159  C  C     . CYS A 23  ? 1.6422 1.6394 1.4594 0.1414  -0.0279 -0.2194 126  CYS A C     
160  O  O     . CYS A 23  ? 1.8489 1.8469 1.6490 0.1516  -0.0222 -0.2266 126  CYS A O     
161  C  CB    . CYS A 23  ? 1.6934 1.6328 1.5044 0.1477  -0.0269 -0.2236 126  CYS A CB    
162  S  SG    . CYS A 23  ? 2.4034 2.3207 2.2217 0.1583  -0.0222 -0.2175 126  CYS A SG    
163  N  N     . GLU A 24  ? 1.5761 1.5842 1.4029 0.1242  -0.0367 -0.2155 127  GLU A N     
164  C  CA    . GLU A 24  ? 1.6048 1.6252 1.4213 0.1168  -0.0406 -0.2195 127  GLU A CA    
165  C  C     . GLU A 24  ? 1.6001 1.6540 1.4209 0.1245  -0.0335 -0.2135 127  GLU A C     
166  O  O     . GLU A 24  ? 1.6170 1.6770 1.4218 0.1259  -0.0321 -0.2189 127  GLU A O     
167  C  CB    . GLU A 24  ? 1.5792 1.6046 1.4064 0.0979  -0.0515 -0.2155 127  GLU A CB    
168  C  CG    . GLU A 24  ? 1.5760 1.5709 1.3995 0.0876  -0.0591 -0.2218 127  GLU A CG    
169  C  CD    . GLU A 24  ? 1.6096 1.6132 1.4429 0.0696  -0.0700 -0.2187 127  GLU A CD    
170  O  OE1   . GLU A 24  ? 1.5811 1.6086 1.4156 0.0659  -0.0724 -0.2152 127  GLU A OE1   
171  O  OE2   . GLU A 24  ? 1.6954 1.6822 1.5353 0.0594  -0.0757 -0.2193 127  GLU A OE2   
172  N  N     . PHE A 25  ? 1.5489 1.6246 1.3903 0.1289  -0.0289 -0.2025 128  PHE A N     
173  C  CA    . PHE A 25  ? 1.4980 1.6061 1.3451 0.1350  -0.0218 -0.1966 128  PHE A CA    
174  C  C     . PHE A 25  ? 1.5519 1.6593 1.3855 0.1529  -0.0114 -0.2028 128  PHE A C     
175  O  O     . PHE A 25  ? 1.5874 1.7154 1.4157 0.1570  -0.0055 -0.2025 128  PHE A O     
176  C  CB    . PHE A 25  ? 1.4197 1.5507 1.2924 0.1337  -0.0206 -0.1839 128  PHE A CB    
177  C  CG    . PHE A 25  ? 1.4550 1.5918 1.3408 0.1173  -0.0290 -0.1767 128  PHE A CG    
178  C  CD1   . PHE A 25  ? 1.4015 1.5400 1.2796 0.1061  -0.0347 -0.1784 128  PHE A CD1   
179  C  CD2   . PHE A 25  ? 1.3744 1.5151 1.2794 0.1141  -0.0310 -0.1682 128  PHE A CD2   
180  C  CE1   . PHE A 25  ? 1.4357 1.5800 1.3259 0.0927  -0.0419 -0.1715 128  PHE A CE1   
181  C  CE2   . PHE A 25  ? 1.2961 1.4416 1.2122 0.1002  -0.0378 -0.1617 128  PHE A CE2   
182  C  CZ    . PHE A 25  ? 1.2923 1.4398 1.2015 0.0898  -0.0431 -0.1632 128  PHE A CZ    
183  N  N     . ASP A 26  ? 1.5680 1.6518 1.3954 0.1641  -0.0084 -0.2079 129  ASP A N     
184  C  CA    . ASP A 26  ? 1.5733 1.6540 1.3868 0.1830  0.0020  -0.2141 129  ASP A CA    
185  C  C     . ASP A 26  ? 1.6684 1.7331 1.4536 0.1842  0.0028  -0.2265 129  ASP A C     
186  O  O     . ASP A 26  ? 1.6420 1.7094 1.4142 0.1997  0.0125  -0.2314 129  ASP A O     
187  C  CB    . ASP A 26  ? 1.6136 1.6685 1.4256 0.1952  0.0047  -0.2163 129  ASP A CB    
188  C  CG    . ASP A 26  ? 1.6130 1.6842 1.4508 0.1966  0.0045  -0.2041 129  ASP A CG    
189  O  OD1   . ASP A 26  ? 1.5461 1.6538 1.4012 0.1974  0.0075  -0.1952 129  ASP A OD1   
190  O  OD2   . ASP A 26  ? 1.6330 1.6800 1.4729 0.1965  0.0014  -0.2033 129  ASP A OD2   
191  N  N     . MET A 27  ? 1.7762 1.8257 1.5514 0.1687  -0.0071 -0.2317 130  MET A N     
192  C  CA    . MET A 27  ? 1.6483 1.6816 1.3950 0.1683  -0.0082 -0.2441 130  MET A CA    
193  C  C     . MET A 27  ? 1.5794 1.6395 1.3232 0.1615  -0.0089 -0.2410 130  MET A C     
194  O  O     . MET A 27  ? 1.6643 1.7154 1.3831 0.1628  -0.0088 -0.2505 130  MET A O     
195  C  CB    . MET A 27  ? 1.7445 1.7434 1.4798 0.1554  -0.0194 -0.2530 130  MET A CB    
196  C  CG    . MET A 27  ? 1.8102 1.7788 1.5476 0.1597  -0.0191 -0.2555 130  MET A CG    
197  S  SD    . MET A 27  ? 2.2369 2.1846 1.9540 0.1848  -0.0057 -0.2640 130  MET A SD    
198  C  CE    . MET A 27  ? 2.1460 2.0606 1.8707 0.1863  -0.0071 -0.2627 130  MET A CE    
199  N  N     . VAL A 28  ? 1.5685 1.6594 1.3353 0.1545  -0.0096 -0.2281 131  VAL A N     
200  C  CA    . VAL A 28  ? 1.4903 1.6054 1.2544 0.1480  -0.0095 -0.2237 131  VAL A CA    
201  C  C     . VAL A 28  ? 1.4696 1.6020 1.2248 0.1628  0.0038  -0.2244 131  VAL A C     
202  O  O     . VAL A 28  ? 1.4756 1.6288 1.2479 0.1715  0.0123  -0.2170 131  VAL A O     
203  C  CB    . VAL A 28  ? 1.3610 1.5008 1.1514 0.1365  -0.0133 -0.2098 131  VAL A CB    
204  C  CG1   . VAL A 28  ? 1.2717 1.4319 1.0566 0.1295  -0.0134 -0.2053 131  VAL A CG1   
205  C  CG2   . VAL A 28  ? 1.3504 1.4740 1.1512 0.1237  -0.0250 -0.2087 131  VAL A CG2   
206  N  N     . LYS A 29  ? 1.5806 1.7056 1.3089 0.1658  0.0056  -0.2331 132  LYS A N     
207  C  CA    . LYS A 29  ? 1.5036 1.6436 1.2205 0.1803  0.0190  -0.2345 132  LYS A CA    
208  C  C     . LYS A 29  ? 1.3977 1.5741 1.1260 0.1759  0.0244  -0.2228 132  LYS A C     
209  O  O     . LYS A 29  ? 1.3229 1.5168 1.0456 0.1869  0.0366  -0.2220 132  LYS A O     
210  C  CB    . LYS A 29  ? 1.5284 1.6448 1.2092 0.1854  0.0193  -0.2487 132  LYS A CB    
211  C  CG    . LYS A 29  ? 1.6724 1.7499 1.3378 0.1912  0.0162  -0.2618 132  LYS A CG    
212  C  CD    . LYS A 29  ? 1.9086 1.9633 1.5361 0.1966  0.0172  -0.2766 132  LYS A CD    
213  C  CE    . LYS A 29  ? 1.9575 1.9703 1.5678 0.2024  0.0150  -0.2903 132  LYS A CE    
214  N  NZ    . LYS A 29  ? 1.9137 1.9029 1.4849 0.2088  0.0168  -0.3057 132  LYS A NZ    
215  N  N     . ASP A 30  ? 1.2833 1.4707 1.0270 0.1604  0.0162  -0.2137 133  ASP A N     
216  C  CA    . ASP A 30  ? 1.2186 1.4368 0.9721 0.1548  0.0210  -0.2022 133  ASP A CA    
217  C  C     . ASP A 30  ? 1.2337 1.4788 1.0104 0.1624  0.0318  -0.1939 133  ASP A C     
218  O  O     . ASP A 30  ? 1.2001 1.4473 0.9991 0.1607  0.0287  -0.1893 133  ASP A O     
219  C  CB    . ASP A 30  ? 1.1973 1.4180 0.9631 0.1376  0.0098  -0.1943 133  ASP A CB    
220  C  CG    . ASP A 30  ? 1.1833 1.4288 0.9520 0.1309  0.0140  -0.1837 133  ASP A CG    
221  O  OD1   . ASP A 30  ? 1.2047 1.4680 0.9688 0.1384  0.0260  -0.1817 133  ASP A OD1   
222  O  OD2   . ASP A 30  ? 1.1829 1.4297 0.9583 0.1182  0.0057  -0.1771 133  ASP A OD2   
223  N  N     . PRO A 31  ? 1.2304 1.4975 1.0030 0.1705  0.0444  -0.1916 134  PRO A N     
224  C  CA    . PRO A 31  ? 1.1984 1.4947 0.9949 0.1773  0.0544  -0.1837 134  PRO A CA    
225  C  C     . PRO A 31  ? 1.0775 1.3946 0.9013 0.1636  0.0507  -0.1711 134  PRO A C     
226  O  O     . PRO A 31  ? 1.1284 1.4657 0.9750 0.1673  0.0550  -0.1653 134  PRO A O     
227  C  CB    . PRO A 31  ? 1.1304 1.4463 0.9143 0.1858  0.0683  -0.1836 134  PRO A CB    
228  C  CG    . PRO A 31  ? 1.0393 1.3280 0.7889 0.1901  0.0664  -0.1954 134  PRO A CG    
229  C  CD    . PRO A 31  ? 1.0325 1.2984 0.7774 0.1753  0.0506  -0.1969 134  PRO A CD    
230  N  N     . GLU A 32  ? 1.0474 1.3602 0.8690 0.1483  0.0427  -0.1666 135  GLU A N     
231  C  CA    . GLU A 32  ? 1.0766 1.4043 0.9221 0.1355  0.0388  -0.1554 135  GLU A CA    
232  C  C     . GLU A 32  ? 1.1006 1.4140 0.9610 0.1332  0.0292  -0.1560 135  GLU A C     
233  O  O     . GLU A 32  ? 1.0200 1.3486 0.9034 0.1300  0.0292  -0.1487 135  GLU A O     
234  C  CB    . GLU A 32  ? 1.0694 1.3950 0.9065 0.1216  0.0338  -0.1502 135  GLU A CB    
235  C  CG    . GLU A 32  ? 1.0373 1.3758 0.8960 0.1084  0.0307  -0.1388 135  GLU A CG    
236  C  CD    . GLU A 32  ? 1.0904 1.4271 0.9393 0.0968  0.0277  -0.1327 135  GLU A CD    
237  O  OE1   . GLU A 32  ? 1.3877 1.7153 1.2131 0.0990  0.0278  -0.1370 135  GLU A OE1   
238  O  OE2   . GLU A 32  ? 1.0641 1.4077 0.9275 0.0859  0.0252  -0.1237 135  GLU A OE2   
239  N  N     . VAL A 33  ? 1.1731 1.4571 1.0201 0.1342  0.0209  -0.1646 136  VAL A N     
240  C  CA    . VAL A 33  ? 1.0618 1.3299 0.9211 0.1321  0.0126  -0.1652 136  VAL A CA    
241  C  C     . VAL A 33  ? 1.0620 1.3367 0.9338 0.1452  0.0186  -0.1656 136  VAL A C     
242  O  O     . VAL A 33  ? 1.1725 1.4525 1.0642 0.1428  0.0156  -0.1597 136  VAL A O     
243  C  CB    . VAL A 33  ? 1.0948 1.3303 0.9360 0.1302  0.0035  -0.1750 136  VAL A CB    
244  C  CG1   . VAL A 33  ? 1.1059 1.3232 0.9579 0.1306  -0.0026 -0.1766 136  VAL A CG1   
245  C  CG2   . VAL A 33  ? 1.0775 1.3099 0.9119 0.1163  -0.0047 -0.1725 136  VAL A CG2   
246  N  N     . GLN A 34  ? 1.0920 1.3667 0.9515 0.1600  0.0274  -0.1722 137  GLN A N     
247  C  CA    . GLN A 34  ? 1.1535 1.4350 1.0240 0.1746  0.0335  -0.1724 137  GLN A CA    
248  C  C     . GLN A 34  ? 1.1208 1.4411 1.0145 0.1749  0.0403  -0.1621 137  GLN A C     
249  O  O     . GLN A 34  ? 1.0501 1.3805 0.9622 0.1802  0.0404  -0.1579 137  GLN A O     
250  C  CB    . GLN A 34  ? 1.1907 1.4596 1.0401 0.1917  0.0413  -0.1827 137  GLN A CB    
251  C  CG    . GLN A 34  ? 1.2157 1.4438 1.0415 0.1915  0.0343  -0.1942 137  GLN A CG    
252  C  CD    . GLN A 34  ? 1.3265 1.5324 1.1618 0.1875  0.0252  -0.1940 137  GLN A CD    
253  O  OE1   . GLN A 34  ? 1.3657 1.5804 1.2192 0.1937  0.0269  -0.1885 137  GLN A OE1   
254  N  NE2   . GLN A 34  ? 1.3375 1.5153 1.1603 0.1770  0.0153  -0.1999 137  GLN A NE2   
255  N  N     . ASP A 35  ? 1.0974 1.4399 0.9903 0.1687  0.0459  -0.1577 138  ASP A N     
256  C  CA    . ASP A 35  ? 1.0732 1.4528 0.9886 0.1659  0.0520  -0.1479 138  ASP A CA    
257  C  C     . ASP A 35  ? 1.0135 1.3983 0.9480 0.1505  0.0435  -0.1396 138  ASP A C     
258  O  O     . ASP A 35  ? 1.1150 1.5275 1.0706 0.1481  0.0463  -0.1322 138  ASP A O     
259  C  CB    . ASP A 35  ? 1.0631 1.4632 0.9712 0.1628  0.0613  -0.1452 138  ASP A CB    
260  C  CG    . ASP A 35  ? 1.1330 1.5419 1.0304 0.1804  0.0734  -0.1508 138  ASP A CG    
261  O  OD1   . ASP A 35  ? 1.2415 1.6375 1.1351 0.1955  0.0742  -0.1574 138  ASP A OD1   
262  O  OD2   . ASP A 35  ? 1.2889 1.7170 1.1810 0.1796  0.0828  -0.1482 138  ASP A OD2   
263  N  N     . PHE A 36  ? 1.0204 1.3799 0.9479 0.1401  0.0332  -0.1406 139  PHE A N     
264  C  CA    . PHE A 36  ? 1.0238 1.3851 0.9683 0.1276  0.0254  -0.1333 139  PHE A CA    
265  C  C     . PHE A 36  ? 0.9751 1.3295 0.9317 0.1347  0.0213  -0.1338 139  PHE A C     
266  O  O     . PHE A 36  ? 1.0293 1.4003 1.0050 0.1309  0.0198  -0.1271 139  PHE A O     
267  C  CB    . PHE A 36  ? 1.0055 1.3448 0.9396 0.1149  0.0165  -0.1335 139  PHE A CB    
268  C  CG    . PHE A 36  ? 0.9491 1.2884 0.8987 0.1028  0.0092  -0.1261 139  PHE A CG    
269  C  CD1   . PHE A 36  ? 0.9252 1.2820 0.8833 0.0914  0.0109  -0.1178 139  PHE A CD1   
270  C  CD2   . PHE A 36  ? 0.9726 1.2930 0.9270 0.1030  0.0015  -0.1275 139  PHE A CD2   
271  C  CE1   . PHE A 36  ? 0.9537 1.3086 0.9240 0.0810  0.0046  -0.1117 139  PHE A CE1   
272  C  CE2   . PHE A 36  ? 0.9979 1.3183 0.9652 0.0928  -0.0044 -0.1209 139  PHE A CE2   
273  C  CZ    . PHE A 36  ? 0.9461 1.2834 0.9209 0.0821  -0.0029 -0.1133 139  PHE A CZ    
274  N  N     . ARG A 37  ? 0.9594 1.2883 0.9038 0.1448  0.0193  -0.1418 140  ARG A N     
275  C  CA    . ARG A 37  ? 0.9639 1.2817 0.9171 0.1517  0.0155  -0.1419 140  ARG A CA    
276  C  C     . ARG A 37  ? 1.1247 1.4688 1.0933 0.1641  0.0221  -0.1383 140  ARG A C     
277  O  O     . ARG A 37  ? 1.1107 1.4547 1.0918 0.1671  0.0184  -0.1347 140  ARG A O     
278  C  CB    . ARG A 37  ? 0.8814 1.1645 0.8161 0.1599  0.0134  -0.1516 140  ARG A CB    
279  C  CG    . ARG A 37  ? 0.9911 1.2491 0.9124 0.1473  0.0053  -0.1555 140  ARG A CG    
280  C  CD    . ARG A 37  ? 1.1227 1.3472 1.0247 0.1546  0.0036  -0.1662 140  ARG A CD    
281  N  NE    . ARG A 37  ? 1.1633 1.3707 1.0716 0.1606  0.0012  -0.1661 140  ARG A NE    
282  C  CZ    . ARG A 37  ? 1.2767 1.4556 1.1708 0.1702  0.0019  -0.1744 140  ARG A CZ    
283  N  NH1   . ARG A 37  ? 1.3692 1.5334 1.2415 0.1755  0.0048  -0.1843 140  ARG A NH1   
284  N  NH2   . ARG A 37  ? 1.3183 1.4815 1.2187 0.1748  -0.0001 -0.1726 140  ARG A NH2   
285  N  N     . ARG A 38  ? 0.9798 1.3476 0.9482 0.1715  0.0317  -0.1387 141  ARG A N     
286  C  CA    . ARG A 38  ? 1.0046 1.4030 0.9900 0.1829  0.0379  -0.1345 141  ARG A CA    
287  C  C     . ARG A 38  ? 0.9864 1.4197 0.9925 0.1703  0.0382  -0.1254 141  ARG A C     
288  O  O     . ARG A 38  ? 0.8903 1.3417 0.9151 0.1717  0.0359  -0.1200 141  ARG A O     
289  C  CB    . ARG A 38  ? 1.0426 1.4502 1.0182 0.1993  0.0492  -0.1397 141  ARG A CB    
290  C  CG    . ARG A 38  ? 1.2608 1.6336 1.2154 0.2139  0.0499  -0.1495 141  ARG A CG    
291  C  CD    . ARG A 38  ? 1.4956 1.8804 1.4421 0.2326  0.0622  -0.1540 141  ARG A CD    
292  N  NE    . ARG A 38  ? 1.6183 1.9656 1.5407 0.2457  0.0634  -0.1645 141  ARG A NE    
293  C  CZ    . ARG A 38  ? 1.6353 1.9596 1.5327 0.2437  0.0644  -0.1730 141  ARG A CZ    
294  N  NH1   . ARG A 38  ? 1.4904 1.8251 1.3829 0.2303  0.0647  -0.1717 141  ARG A NH1   
295  N  NH2   . ARG A 38  ? 1.7789 2.0678 1.6545 0.2553  0.0650  -0.1830 141  ARG A NH2   
296  N  N     . ASN A 39  ? 0.9623 1.4043 0.9642 0.1578  0.0409  -0.1235 142  ASN A N     
297  C  CA    . ASN A 39  ? 1.0125 1.4856 1.0321 0.1447  0.0422  -0.1151 142  ASN A CA    
298  C  C     . ASN A 39  ? 0.9592 1.4246 0.9882 0.1300  0.0322  -0.1101 142  ASN A C     
299  O  O     . ASN A 39  ? 0.9165 1.4058 0.9610 0.1192  0.0322  -0.1036 142  ASN A O     
300  C  CB    . ASN A 39  ? 0.9846 1.4653 0.9944 0.1358  0.0487  -0.1141 142  ASN A CB    
301  C  CG    . ASN A 39  ? 0.9476 1.4449 0.9515 0.1494  0.0607  -0.1173 142  ASN A CG    
302  O  OD1   . ASN A 39  ? 0.8918 1.4102 0.9078 0.1627  0.0658  -0.1172 142  ASN A OD1   
303  N  ND2   . ASN A 39  ? 1.0135 1.5021 0.9982 0.1471  0.0655  -0.1199 142  ASN A ND2   
304  N  N     . ILE A 40  ? 1.0003 1.4331 1.0201 0.1289  0.0239  -0.1131 143  ILE A N     
305  C  CA    . ILE A 40  ? 0.9182 1.3428 0.9462 0.1167  0.0150  -0.1083 143  ILE A CA    
306  C  C     . ILE A 40  ? 0.9394 1.3696 0.9812 0.1243  0.0113  -0.1063 143  ILE A C     
307  O  O     . ILE A 40  ? 0.9459 1.3763 0.9968 0.1150  0.0050  -0.1016 143  ILE A O     
308  C  CB    . ILE A 40  ? 0.8706 1.2600 0.8835 0.1107  0.0081  -0.1115 143  ILE A CB    
309  C  CG1   . ILE A 40  ? 0.8944 1.2790 0.9141 0.0954  0.0012  -0.1055 143  ILE A CG1   
310  C  CG2   . ILE A 40  ? 0.9033 1.2680 0.9095 0.1226  0.0049  -0.1171 143  ILE A CG2   
311  C  CD1   . ILE A 40  ? 0.8934 1.2975 0.9179 0.0825  0.0043  -0.0998 143  ILE A CD1   
312  N  N     . LEU A 41  ? 0.9261 1.3607 0.9685 0.1418  0.0152  -0.1095 144  LEU A N     
313  C  CA    . LEU A 41  ? 0.9212 1.3569 0.9736 0.1513  0.0114  -0.1075 144  LEU A CA    
314  C  C     . LEU A 41  ? 0.9912 1.4634 1.0648 0.1477  0.0109  -0.1008 144  LEU A C     
315  O  O     . LEU A 41  ? 1.0127 1.4858 1.0946 0.1513  0.0054  -0.0977 144  LEU A O     
316  C  CB    . LEU A 41  ? 0.9249 1.3530 0.9702 0.1724  0.0163  -0.1126 144  LEU A CB    
317  C  CG    . LEU A 41  ? 1.0064 1.3930 1.0305 0.1762  0.0148  -0.1200 144  LEU A CG    
318  C  CD1   . LEU A 41  ? 1.1446 1.5238 1.1591 0.1970  0.0216  -0.1258 144  LEU A CD1   
319  C  CD2   . LEU A 41  ? 0.9646 1.3245 0.9879 0.1708  0.0059  -0.1183 144  LEU A CD2   
320  N  N     . ASN A 42  ? 0.9181 1.4201 1.0000 0.1403  0.0163  -0.0983 145  ASN A N     
321  C  CA    . ASN A 42  ? 0.9010 1.4378 1.0035 0.1340  0.0148  -0.0923 145  ASN A CA    
322  C  C     . ASN A 42  ? 0.9411 1.4691 1.0462 0.1154  0.0068  -0.0884 145  ASN A C     
323  O  O     . ASN A 42  ? 0.9781 1.5246 1.0972 0.1113  0.0022  -0.0844 145  ASN A O     
324  C  CB    . ASN A 42  ? 0.8843 1.4568 0.9961 0.1307  0.0237  -0.0905 145  ASN A CB    
325  C  CG    . ASN A 42  ? 0.9103 1.4730 1.0108 0.1161  0.0273  -0.0908 145  ASN A CG    
326  O  OD1   . ASN A 42  ? 1.1320 1.6838 1.2182 0.1223  0.0334  -0.0949 145  ASN A OD1   
327  N  ND2   . ASN A 42  ? 0.8766 1.4423 0.9820 0.0971  0.0235  -0.0864 145  ASN A ND2   
328  N  N     . VAL A 43  ? 0.9477 1.4480 1.0388 0.1046  0.0049  -0.0897 146  VAL A N     
329  C  CA    . VAL A 43  ? 0.9511 1.4377 1.0423 0.0898  -0.0025 -0.0864 146  VAL A CA    
330  C  C     . VAL A 43  ? 0.9587 1.4286 1.0503 0.0969  -0.0097 -0.0862 146  VAL A C     
331  O  O     . VAL A 43  ? 0.9565 1.4283 1.0545 0.0889  -0.0155 -0.0826 146  VAL A O     
332  C  CB    . VAL A 43  ? 0.8888 1.3496 0.9646 0.0795  -0.0026 -0.0876 146  VAL A CB    
333  C  CG1   . VAL A 43  ? 0.8549 1.3002 0.9302 0.0661  -0.0095 -0.0840 146  VAL A CG1   
334  C  CG2   . VAL A 43  ? 0.8953 1.3723 0.9693 0.0725  0.0050  -0.0867 146  VAL A CG2   
335  N  N     . CYS A 44  ? 0.9460 1.3982 1.0298 0.1119  -0.0091 -0.0901 147  CYS A N     
336  C  CA    . CYS A 44  ? 1.0294 1.4658 1.1132 0.1200  -0.0147 -0.0893 147  CYS A CA    
337  C  C     . CYS A 44  ? 0.9913 1.4564 1.0900 0.1284  -0.0157 -0.0858 147  CYS A C     
338  O  O     . CYS A 44  ? 0.9637 1.4262 1.0665 0.1273  -0.0220 -0.0823 147  CYS A O     
339  C  CB    . CYS A 44  ? 1.0193 1.4280 1.0899 0.1334  -0.0130 -0.0945 147  CYS A CB    
340  S  SG    . CYS A 44  ? 1.0999 1.4773 1.1529 0.1243  -0.0128 -0.0995 147  CYS A SG    
341  N  N     . LYS A 45  ? 0.9679 1.4619 1.0748 0.1372  -0.0097 -0.0864 148  LYS A N     
342  C  CA    . LYS A 45  ? 0.9466 1.4726 1.0694 0.1460  -0.0109 -0.0828 148  LYS A CA    
343  C  C     . LYS A 45  ? 1.0061 1.5544 1.1415 0.1296  -0.0163 -0.0783 148  LYS A C     
344  O  O     . LYS A 45  ? 0.9817 1.5389 1.1244 0.1320  -0.0226 -0.0751 148  LYS A O     
345  C  CB    . LYS A 45  ? 0.8814 1.4365 1.0115 0.1581  -0.0024 -0.0842 148  LYS A CB    
346  C  CG    . LYS A 45  ? 0.9869 1.5831 1.1368 0.1659  -0.0035 -0.0799 148  LYS A CG    
347  C  CD    . LYS A 45  ? 1.0564 1.6901 1.2178 0.1694  0.0055  -0.0800 148  LYS A CD    
348  C  CE    . LYS A 45  ? 1.1145 1.7936 1.2982 0.1762  0.0037  -0.0755 148  LYS A CE    
349  N  NZ    . LYS A 45  ? 1.1166 1.8083 1.3106 0.1592  -0.0058 -0.0716 148  LYS A NZ    
350  N  N     . GLU A 46  ? 0.9421 1.4983 1.0787 0.1126  -0.0138 -0.0781 149  GLU A N     
351  C  CA    . GLU A 46  ? 0.9434 1.5186 1.0904 0.0956  -0.0182 -0.0745 149  GLU A CA    
352  C  C     . GLU A 46  ? 0.9022 1.4513 1.0419 0.0877  -0.0266 -0.0731 149  GLU A C     
353  O  O     . GLU A 46  ? 0.9086 1.4721 1.0564 0.0804  -0.0324 -0.0705 149  GLU A O     
354  C  CB    . GLU A 46  ? 0.8775 1.4606 1.0243 0.0793  -0.0127 -0.0744 149  GLU A CB    
355  C  CG    . GLU A 46  ? 0.9927 1.6070 1.1485 0.0849  -0.0037 -0.0748 149  GLU A CG    
356  C  CD    . GLU A 46  ? 1.2169 1.8336 1.3690 0.0693  0.0027  -0.0742 149  GLU A CD    
357  O  OE1   . GLU A 46  ? 1.2078 1.8078 1.3537 0.0528  -0.0007 -0.0727 149  GLU A OE1   
358  O  OE2   . GLU A 46  ? 1.1302 1.7646 1.2846 0.0744  0.0116  -0.0749 149  GLU A OE2   
359  N  N     . ALA A 47  ? 0.9616 1.4732 1.0860 0.0891  -0.0272 -0.0750 150  ALA A N     
360  C  CA    . ALA A 47  ? 0.9340 1.4207 1.0514 0.0824  -0.0339 -0.0733 150  ALA A CA    
361  C  C     . ALA A 47  ? 0.9708 1.4551 1.0900 0.0955  -0.0390 -0.0716 150  ALA A C     
362  O  O     . ALA A 47  ? 0.9618 1.4449 1.0820 0.0898  -0.0451 -0.0689 150  ALA A O     
363  C  CB    . ALA A 47  ? 0.9058 1.3566 1.0082 0.0795  -0.0328 -0.0754 150  ALA A CB    
364  N  N     . VAL A 48  ? 0.9687 1.4505 1.0867 0.1134  -0.0362 -0.0731 151  VAL A N     
365  C  CA    . VAL A 48  ? 0.9648 1.4443 1.0837 0.1276  -0.0403 -0.0706 151  VAL A CA    
366  C  C     . VAL A 48  ? 1.0311 1.5487 1.1649 0.1283  -0.0441 -0.0673 151  VAL A C     
367  O  O     . VAL A 48  ? 1.0977 1.6153 1.2319 0.1313  -0.0505 -0.0640 151  VAL A O     
368  C  CB    . VAL A 48  ? 1.0287 1.4963 1.1419 0.1470  -0.0354 -0.0731 151  VAL A CB    
369  C  CG1   . VAL A 48  ? 1.0690 1.5379 1.1838 0.1636  -0.0387 -0.0696 151  VAL A CG1   
370  C  CG2   . VAL A 48  ? 0.9689 1.3964 1.0666 0.1448  -0.0335 -0.0766 151  VAL A CG2   
371  N  N     . ASP A 49  ? 0.9672 1.5188 1.1134 0.1251  -0.0405 -0.0680 152  ASP A N     
372  C  CA    . ASP A 49  ? 0.9391 1.5310 1.1017 0.1237  -0.0446 -0.0651 152  ASP A CA    
373  C  C     . ASP A 49  ? 0.9449 1.5370 1.1077 0.1051  -0.0519 -0.0635 152  ASP A C     
374  O  O     . ASP A 49  ? 1.0310 1.6456 1.2023 0.1054  -0.0586 -0.0611 152  ASP A O     
375  C  CB    . ASP A 49  ? 0.8990 1.5273 1.0756 0.1218  -0.0382 -0.0660 152  ASP A CB    
376  C  CG    . ASP A 49  ? 0.9911 1.6292 1.1705 0.1439  -0.0317 -0.0669 152  ASP A CG    
377  O  OD1   . ASP A 49  ? 1.0147 1.6407 1.1894 0.1615  -0.0339 -0.0658 152  ASP A OD1   
378  O  OD2   . ASP A 49  ? 0.9577 1.6146 1.1431 0.1441  -0.0238 -0.0685 152  ASP A OD2   
379  N  N     . LEU A 50  ? 0.8642 1.4315 1.0170 0.0893  -0.0509 -0.0650 153  LEU A N     
380  C  CA    . LEU A 50  ? 0.9223 1.4842 1.0722 0.0727  -0.0572 -0.0639 153  LEU A CA    
381  C  C     . LEU A 50  ? 1.0476 1.5848 1.1872 0.0791  -0.0633 -0.0620 153  LEU A C     
382  O  O     . LEU A 50  ? 1.0050 1.5484 1.1448 0.0722  -0.0701 -0.0606 153  LEU A O     
383  C  CB    . LEU A 50  ? 0.8716 1.4136 1.0132 0.0557  -0.0535 -0.0654 153  LEU A CB    
384  C  CG    . LEU A 50  ? 0.7987 1.3653 0.9492 0.0383  -0.0516 -0.0656 153  LEU A CG    
385  C  CD1   . LEU A 50  ? 0.8734 1.4749 1.0383 0.0446  -0.0460 -0.0659 153  LEU A CD1   
386  C  CD2   . LEU A 50  ? 0.8783 1.4193 1.0173 0.0241  -0.0477 -0.0663 153  LEU A CD2   
387  N  N     . ARG A 51  ? 1.0559 1.5645 1.1855 0.0916  -0.0608 -0.0621 154  ARG A N     
388  C  CA    . ARG A 51  ? 1.0569 1.5418 1.1767 0.0987  -0.0653 -0.0596 154  ARG A CA    
389  C  C     . ARG A 51  ? 1.1507 1.6550 1.2763 0.1142  -0.0696 -0.0565 154  ARG A C     
390  O  O     . ARG A 51  ? 1.2588 1.7476 1.3763 0.1196  -0.0740 -0.0535 154  ARG A O     
391  C  CB    . ARG A 51  ? 1.0823 1.5312 1.1905 0.1059  -0.0609 -0.0606 154  ARG A CB    
392  C  CG    . ARG A 51  ? 1.0531 1.4774 1.1530 0.0913  -0.0589 -0.0621 154  ARG A CG    
393  C  CD    . ARG A 51  ? 0.9732 1.3810 1.0683 0.0952  -0.0530 -0.0654 154  ARG A CD    
394  N  NE    . ARG A 51  ? 1.0476 1.4366 1.1371 0.1108  -0.0519 -0.0654 154  ARG A NE    
395  C  CZ    . ARG A 51  ? 1.0031 1.3737 1.0864 0.1157  -0.0475 -0.0688 154  ARG A CZ    
396  N  NH1   . ARG A 51  ? 1.0140 1.3833 1.0956 0.1072  -0.0442 -0.0723 154  ARG A NH1   
397  N  NH2   . ARG A 51  ? 1.0098 1.3619 1.0874 0.1293  -0.0466 -0.0688 154  ARG A NH2   
398  N  N     . ASP A 52  ? 1.1873 1.7256 1.3263 0.1222  -0.0682 -0.0568 155  ASP A N     
399  C  CA    . ASP A 52  ? 1.2674 1.8284 1.4133 0.1381  -0.0725 -0.0534 155  ASP A CA    
400  C  C     . ASP A 52  ? 1.3222 1.9251 1.4824 0.1295  -0.0789 -0.0525 155  ASP A C     
401  O  O     . ASP A 52  ? 1.4867 2.1090 1.6517 0.1405  -0.0850 -0.0492 155  ASP A O     
402  C  CB    . ASP A 52  ? 1.4231 1.9926 1.5739 0.1577  -0.0661 -0.0538 155  ASP A CB    
403  C  CG    . ASP A 52  ? 1.5583 2.0855 1.6940 0.1668  -0.0606 -0.0552 155  ASP A CG    
404  O  OD1   . ASP A 52  ? 1.6043 2.1000 1.7274 0.1656  -0.0633 -0.0535 155  ASP A OD1   
405  O  OD2   . ASP A 52  ? 1.5596 2.0852 1.6956 0.1747  -0.0534 -0.0582 155  ASP A OD2   
406  N  N     . LEU A 53  ? 1.1971 1.8142 1.3640 0.1101  -0.0780 -0.0552 156  LEU A N     
407  C  CA    . LEU A 53  ? 1.2431 1.8961 1.4223 0.0977  -0.0847 -0.0550 156  LEU A CA    
408  C  C     . LEU A 53  ? 1.3104 1.9473 1.4781 0.0908  -0.0934 -0.0539 156  LEU A C     
409  O  O     . LEU A 53  ? 1.4483 2.0544 1.6029 0.0778  -0.0927 -0.0555 156  LEU A O     
410  C  CB    . LEU A 53  ? 1.1356 1.8001 1.3216 0.0773  -0.0803 -0.0580 156  LEU A CB    
411  C  CG    . LEU A 53  ? 1.3454 2.0454 1.5443 0.0602  -0.0864 -0.0586 156  LEU A CG    
412  C  CD1   . LEU A 53  ? 1.3890 2.1362 1.6071 0.0723  -0.0902 -0.0564 156  LEU A CD1   
413  C  CD2   . LEU A 53  ? 1.1978 1.9030 1.4014 0.0408  -0.0800 -0.0609 156  LEU A CD2   
414  N  N     . ASN A 54  ? 1.3283 1.9862 1.4999 0.1004  -0.1014 -0.0511 157  ASN A N     
415  C  CA    . ASN A 54  ? 1.4204 2.0612 1.5782 0.0994  -0.1095 -0.0494 157  ASN A CA    
416  C  C     . ASN A 54  ? 1.4485 2.0431 1.5882 0.1102  -0.1053 -0.0474 157  ASN A C     
417  O  O     . ASN A 54  ? 1.3672 1.9290 1.4933 0.0995  -0.1040 -0.0485 157  ASN A O     
418  C  CB    . ASN A 54  ? 1.3596 1.9980 1.5130 0.0750  -0.1139 -0.0528 157  ASN A CB    
419  C  CG    . ASN A 54  ? 1.4036 2.0378 1.5457 0.0740  -0.1239 -0.0516 157  ASN A CG    
420  O  OD1   . ASN A 54  ? 1.4774 2.0926 1.6081 0.0893  -0.1254 -0.0478 157  ASN A OD1   
421  N  ND2   . ASN A 54  ? 1.3323 1.9831 1.4764 0.0556  -0.1305 -0.0548 157  ASN A ND2   
422  N  N     . SER A 55  ? 2.0518 2.6452 2.1922 0.1320  -0.1030 -0.0441 158  SER A N     
423  C  CA    . SER A 55  ? 2.0746 2.6260 2.2004 0.1429  -0.0975 -0.0423 158  SER A CA    
424  C  C     . SER A 55  ? 2.0981 2.6164 2.2063 0.1383  -0.1006 -0.0403 158  SER A C     
425  O  O     . SER A 55  ? 2.1726 2.6557 2.2706 0.1344  -0.0950 -0.0411 158  SER A O     
426  C  CB    . SER A 55  ? 2.0924 2.6491 2.2204 0.1678  -0.0959 -0.0385 158  SER A CB    
427  O  OG    . SER A 55  ? 2.1768 2.7563 2.3185 0.1738  -0.0903 -0.0408 158  SER A OG    
428  N  N     . PRO A 56  ? 1.5256 2.0530 1.6290 0.1389  -0.1089 -0.0375 159  PRO A N     
429  C  CA    . PRO A 56  ? 1.3794 1.8736 1.4646 0.1348  -0.1104 -0.0355 159  PRO A CA    
430  C  C     . PRO A 56  ? 1.2918 1.7657 1.3714 0.1146  -0.1074 -0.0396 159  PRO A C     
431  O  O     . PRO A 56  ? 1.2354 1.6748 1.3048 0.1138  -0.1018 -0.0388 159  PRO A O     
432  C  CB    . PRO A 56  ? 1.2954 1.8118 1.3781 0.1359  -0.1208 -0.0334 159  PRO A CB    
433  C  CG    . PRO A 56  ? 1.4480 2.0015 1.5456 0.1501  -0.1239 -0.0315 159  PRO A CG    
434  C  CD    . PRO A 56  ? 1.4683 2.0361 1.5816 0.1453  -0.1173 -0.0356 159  PRO A CD    
435  N  N     . HIS A 57  ? 1.2181 1.7138 1.3048 0.0981  -0.1107 -0.0437 160  HIS A N     
436  C  CA    . HIS A 57  ? 1.1343 1.6104 1.2136 0.0793  -0.1086 -0.0471 160  HIS A CA    
437  C  C     . HIS A 57  ? 1.0596 1.5231 1.1433 0.0742  -0.1000 -0.0494 160  HIS A C     
438  O  O     . HIS A 57  ? 0.9394 1.3737 1.0134 0.0666  -0.0959 -0.0500 160  HIS A O     
439  C  CB    . HIS A 57  ? 0.9918 1.4928 1.0752 0.0629  -0.1152 -0.0507 160  HIS A CB    
440  C  CG    . HIS A 57  ? 0.9251 1.4029 0.9970 0.0449  -0.1139 -0.0537 160  HIS A CG    
441  N  ND1   . HIS A 57  ? 0.9072 1.3929 0.9849 0.0275  -0.1119 -0.0578 160  HIS A ND1   
442  C  CD2   . HIS A 57  ? 0.9434 1.3894 0.9975 0.0424  -0.1135 -0.0528 160  HIS A CD2   
443  C  CE1   . HIS A 57  ? 0.9093 1.3680 0.9728 0.0156  -0.1106 -0.0595 160  HIS A CE1   
444  N  NE2   . HIS A 57  ? 0.9586 1.3938 1.0081 0.0246  -0.1115 -0.0566 160  HIS A NE2   
445  N  N     . SER A 58  ? 1.1960 1.6820 1.2938 0.0788  -0.0970 -0.0507 161  SER A N     
446  C  CA    . SER A 58  ? 1.1257 1.6029 1.2269 0.0729  -0.0893 -0.0533 161  SER A CA    
447  C  C     . SER A 58  ? 1.0739 1.5171 1.1661 0.0822  -0.0836 -0.0521 161  SER A C     
448  O  O     . SER A 58  ? 0.9508 1.3735 1.0383 0.0737  -0.0790 -0.0538 161  SER A O     
449  C  CB    . SER A 58  ? 1.1179 1.6287 1.2355 0.0767  -0.0870 -0.0548 161  SER A CB    
450  O  OG    . SER A 58  ? 1.1905 1.7089 1.3119 0.0971  -0.0867 -0.0524 161  SER A OG    
451  N  N     . ARG A 59  ? 1.1019 1.5388 1.1916 0.0995  -0.0840 -0.0490 162  ARG A N     
452  C  CA    . ARG A 59  ? 1.0590 1.4619 1.1396 0.1069  -0.0790 -0.0478 162  ARG A CA    
453  C  C     . ARG A 59  ? 1.0654 1.4397 1.1339 0.0978  -0.0793 -0.0463 162  ARG A C     
454  O  O     . ARG A 59  ? 1.0410 1.3902 1.1046 0.0948  -0.0747 -0.0469 162  ARG A O     
455  C  CB    . ARG A 59  ? 1.1958 1.5957 1.2745 0.1268  -0.0794 -0.0441 162  ARG A CB    
456  C  CG    . ARG A 59  ? 1.3327 1.7545 1.4218 0.1391  -0.0770 -0.0455 162  ARG A CG    
457  C  CD    . ARG A 59  ? 1.5360 1.9620 1.6236 0.1590  -0.0792 -0.0409 162  ARG A CD    
458  N  NE    . ARG A 59  ? 1.5108 1.8998 1.5844 0.1663  -0.0773 -0.0373 162  ARG A NE    
459  C  CZ    . ARG A 59  ? 1.4972 1.8807 1.5646 0.1820  -0.0792 -0.0319 162  ARG A CZ    
460  N  NH1   . ARG A 59  ? 1.4472 1.8608 1.5213 0.1933  -0.0839 -0.0293 162  ARG A NH1   
461  N  NH2   . ARG A 59  ? 1.4691 1.8169 1.5237 0.1864  -0.0764 -0.0285 162  ARG A NH2   
462  N  N     . ALA A 60  ? 1.0946 1.4733 1.1579 0.0935  -0.0847 -0.0444 163  ALA A N     
463  C  CA    . ALA A 60  ? 1.0346 1.3874 1.0857 0.0854  -0.0843 -0.0430 163  ALA A CA    
464  C  C     . ALA A 60  ? 0.9112 1.2598 0.9624 0.0687  -0.0821 -0.0465 163  ALA A C     
465  O  O     . ALA A 60  ? 0.9075 1.2310 0.9516 0.0639  -0.0784 -0.0458 163  ALA A O     
466  C  CB    . ALA A 60  ? 1.1775 1.5356 1.2207 0.0864  -0.0907 -0.0405 163  ALA A CB    
467  N  N     . MET A 61  ? 0.9256 1.2989 0.9852 0.0597  -0.0839 -0.0499 164  MET A N     
468  C  CA    . MET A 61  ? 1.0848 1.4536 1.1441 0.0444  -0.0810 -0.0528 164  MET A CA    
469  C  C     . MET A 61  ? 1.0884 1.4447 1.1501 0.0456  -0.0746 -0.0537 164  MET A C     
470  O  O     . MET A 61  ? 1.0842 1.4278 1.1421 0.0352  -0.0715 -0.0546 164  MET A O     
471  C  CB    . MET A 61  ? 1.0231 1.4221 1.0914 0.0344  -0.0838 -0.0558 164  MET A CB    
472  C  CG    . MET A 61  ? 0.9504 1.3591 1.0142 0.0273  -0.0908 -0.0563 164  MET A CG    
473  S  SD    . MET A 61  ? 1.0993 1.4822 1.1483 0.0103  -0.0898 -0.0579 164  MET A SD    
474  C  CE    . MET A 61  ? 1.1059 1.5015 1.1638 -0.0047 -0.0856 -0.0611 164  MET A CE    
475  N  N     . TYR A 62  ? 0.9837 1.3424 1.0505 0.0583  -0.0726 -0.0534 165  TYR A N     
476  C  CA    . TYR A 62  ? 0.8618 1.2081 0.9293 0.0596  -0.0672 -0.0551 165  TYR A CA    
477  C  C     . TYR A 62  ? 0.9150 1.2302 0.9740 0.0620  -0.0652 -0.0530 165  TYR A C     
478  O  O     . TYR A 62  ? 0.9443 1.2453 1.0006 0.0553  -0.0623 -0.0539 165  TYR A O     
479  C  CB    . TYR A 62  ? 0.9322 1.2929 1.0072 0.0720  -0.0655 -0.0565 165  TYR A CB    
480  C  CG    . TYR A 62  ? 0.9901 1.3338 1.0629 0.0760  -0.0606 -0.0586 165  TYR A CG    
481  C  CD1   . TYR A 62  ? 0.8929 1.2348 0.9655 0.0666  -0.0573 -0.0613 165  TYR A CD1   
482  C  CD2   . TYR A 62  ? 0.9574 1.2859 1.0271 0.0891  -0.0593 -0.0580 165  TYR A CD2   
483  C  CE1   . TYR A 62  ? 0.8893 1.2164 0.9588 0.0700  -0.0538 -0.0638 165  TYR A CE1   
484  C  CE2   . TYR A 62  ? 1.0510 1.3631 1.1176 0.0916  -0.0555 -0.0609 165  TYR A CE2   
485  C  CZ    . TYR A 62  ? 0.9611 1.2735 1.0277 0.0820  -0.0532 -0.0640 165  TYR A CZ    
486  O  OH    . TYR A 62  ? 0.9818 1.2786 1.0443 0.0843  -0.0503 -0.0673 165  TYR A OH    
487  N  N     . VAL A 63  ? 0.9626 1.2677 1.0174 0.0716  -0.0668 -0.0497 166  VAL A N     
488  C  CA    . VAL A 63  ? 0.9768 1.2537 1.0249 0.0736  -0.0643 -0.0472 166  VAL A CA    
489  C  C     . VAL A 63  ? 0.9532 1.2177 0.9947 0.0633  -0.0644 -0.0453 166  VAL A C     
490  O  O     . VAL A 63  ? 0.9853 1.2318 1.0245 0.0594  -0.0613 -0.0446 166  VAL A O     
491  C  CB    . VAL A 63  ? 0.9313 1.2000 0.9760 0.0870  -0.0650 -0.0435 166  VAL A CB    
492  C  CG1   . VAL A 63  ? 0.9466 1.1866 0.9858 0.0881  -0.0616 -0.0408 166  VAL A CG1   
493  C  CG2   . VAL A 63  ? 0.9354 1.2168 0.9857 0.0987  -0.0647 -0.0453 166  VAL A CG2   
494  N  N     . TYR A 64  ? 0.9281 1.2024 0.9662 0.0591  -0.0679 -0.0447 167  TYR A N     
495  C  CA    . TYR A 64  ? 0.9293 1.1909 0.9588 0.0504  -0.0677 -0.0433 167  TYR A CA    
496  C  C     . TYR A 64  ? 0.9401 1.2163 0.9704 0.0386  -0.0696 -0.0466 167  TYR A C     
497  O  O     . TYR A 64  ? 0.9990 1.2852 1.0256 0.0356  -0.0738 -0.0471 167  TYR A O     
498  C  CB    . TYR A 64  ? 0.9815 1.2357 1.0022 0.0561  -0.0698 -0.0394 167  TYR A CB    
499  C  CG    . TYR A 64  ? 0.9728 1.2127 0.9924 0.0677  -0.0675 -0.0354 167  TYR A CG    
500  C  CD1   . TYR A 64  ? 0.9642 1.1816 0.9811 0.0670  -0.0628 -0.0327 167  TYR A CD1   
501  C  CD2   . TYR A 64  ? 0.9700 1.2190 0.9915 0.0793  -0.0699 -0.0341 167  TYR A CD2   
502  C  CE1   . TYR A 64  ? 0.9874 1.1907 1.0034 0.0759  -0.0602 -0.0290 167  TYR A CE1   
503  C  CE2   . TYR A 64  ? 0.9865 1.2192 1.0055 0.0896  -0.0672 -0.0301 167  TYR A CE2   
504  C  CZ    . TYR A 64  ? 1.0130 1.2223 1.0292 0.0871  -0.0623 -0.0277 167  TYR A CZ    
505  O  OH    . TYR A 64  ? 1.0615 1.2536 1.0753 0.0957  -0.0592 -0.0237 167  TYR A OH    
506  N  N     . PRO A 65  ? 0.9331 1.2102 0.9672 0.0313  -0.0667 -0.0489 168  PRO A N     
507  C  CA    . PRO A 65  ? 0.8861 1.1757 0.9207 0.0194  -0.0676 -0.0516 168  PRO A CA    
508  C  C     . PRO A 65  ? 0.8367 1.1105 0.8597 0.0109  -0.0675 -0.0509 168  PRO A C     
509  O  O     . PRO A 65  ? 0.7704 1.0225 0.7867 0.0126  -0.0646 -0.0483 168  PRO A O     
510  C  CB    . PRO A 65  ? 0.8720 1.1624 0.9118 0.0160  -0.0634 -0.0531 168  PRO A CB    
511  C  CG    . PRO A 65  ? 0.8739 1.1439 0.9116 0.0223  -0.0606 -0.0510 168  PRO A CG    
512  C  CD    . PRO A 65  ? 0.9230 1.1894 0.9604 0.0332  -0.0625 -0.0490 168  PRO A CD    
513  N  N     . PRO A 66  ? 0.8405 1.1245 0.8606 0.0013  -0.0705 -0.0533 169  PRO A N     
514  C  CA    . PRO A 66  ? 0.8490 1.1153 0.8556 -0.0070 -0.0702 -0.0534 169  PRO A CA    
515  C  C     . PRO A 66  ? 0.8744 1.1219 0.8765 -0.0124 -0.0644 -0.0524 169  PRO A C     
516  O  O     . PRO A 66  ? 1.0271 1.2796 1.0311 -0.0216 -0.0628 -0.0541 169  PRO A O     
517  C  CB    . PRO A 66  ? 0.8537 1.1377 0.8603 -0.0179 -0.0747 -0.0572 169  PRO A CB    
518  C  CG    . PRO A 66  ? 0.9105 1.2228 0.9302 -0.0112 -0.0789 -0.0579 169  PRO A CG    
519  C  CD    . PRO A 66  ? 0.9155 1.2281 0.9445 -0.0018 -0.0747 -0.0560 169  PRO A CD    
520  N  N     . ASN A 67  ? 0.9466 1.1732 0.9430 -0.0066 -0.0612 -0.0491 170  ASN A N     
521  C  CA    . ASN A 67  ? 1.0038 1.2132 0.9957 -0.0102 -0.0561 -0.0474 170  ASN A CA    
522  C  C     . ASN A 67  ? 0.9671 1.1639 0.9457 -0.0199 -0.0551 -0.0486 170  ASN A C     
523  O  O     . ASN A 67  ? 0.9946 1.1736 0.9619 -0.0179 -0.0536 -0.0471 170  ASN A O     
524  C  CB    . ASN A 67  ? 1.0146 1.2084 1.0060 -0.0012 -0.0530 -0.0432 170  ASN A CB    
525  C  CG    . ASN A 67  ? 1.1130 1.2920 1.1014 -0.0034 -0.0482 -0.0408 170  ASN A CG    
526  O  OD1   . ASN A 67  ? 1.1553 1.3175 1.1347 -0.0025 -0.0453 -0.0383 170  ASN A OD1   
527  N  ND2   . ASN A 67  ? 1.2612 1.4469 1.2565 -0.0055 -0.0473 -0.0414 170  ASN A ND2   
528  N  N     . VAL A 68  ? 1.0298 1.2347 1.0087 -0.0304 -0.0555 -0.0514 171  VAL A N     
529  C  CA    . VAL A 68  ? 1.0387 1.2314 1.0044 -0.0415 -0.0549 -0.0535 171  VAL A CA    
530  C  C     . VAL A 68  ? 1.0002 1.1826 0.9632 -0.0477 -0.0496 -0.0520 171  VAL A C     
531  O  O     . VAL A 68  ? 1.0470 1.2366 1.0193 -0.0445 -0.0476 -0.0501 171  VAL A O     
532  C  CB    . VAL A 68  ? 1.0467 1.2578 1.0138 -0.0508 -0.0605 -0.0581 171  VAL A CB    
533  C  CG1   . VAL A 68  ? 0.9650 1.1859 0.9328 -0.0434 -0.0661 -0.0589 171  VAL A CG1   
534  C  CG2   . VAL A 68  ? 0.9406 1.1764 0.9226 -0.0551 -0.0608 -0.0591 171  VAL A CG2   
535  N  N     . GLU A 69  ? 1.0451 1.2088 0.9935 -0.0564 -0.0474 -0.0530 172  GLU A N     
536  C  CA    . GLU A 69  ? 1.0481 1.1997 0.9911 -0.0630 -0.0423 -0.0512 172  GLU A CA    
537  C  C     . GLU A 69  ? 1.0985 1.2658 1.0457 -0.0766 -0.0435 -0.0544 172  GLU A C     
538  O  O     . GLU A 69  ? 1.0814 1.2706 1.0368 -0.0803 -0.0487 -0.0579 172  GLU A O     
539  C  CB    . GLU A 69  ? 1.1328 1.2533 1.0567 -0.0645 -0.0382 -0.0502 172  GLU A CB    
540  C  CG    . GLU A 69  ? 1.2003 1.3070 1.1216 -0.0510 -0.0355 -0.0461 172  GLU A CG    
541  C  CD    . GLU A 69  ? 1.3514 1.4277 1.2545 -0.0506 -0.0299 -0.0441 172  GLU A CD    
542  O  OE1   . GLU A 69  ? 1.3415 1.4045 1.2321 -0.0612 -0.0282 -0.0463 172  GLU A OE1   
543  O  OE2   . GLU A 69  ? 1.4697 1.5354 1.3709 -0.0396 -0.0268 -0.0402 172  GLU A OE2   
544  N  N     . SER A 70  ? 1.3614 1.5180 1.3030 -0.0839 -0.0385 -0.0525 173  SER A N     
545  C  CA    . SER A 70  ? 1.2886 1.4617 1.2361 -0.0965 -0.0382 -0.0542 173  SER A CA    
546  C  C     . SER A 70  ? 1.2250 1.3916 1.1625 -0.1120 -0.0399 -0.0586 173  SER A C     
547  O  O     . SER A 70  ? 1.2956 1.4859 1.2426 -0.1217 -0.0433 -0.0619 173  SER A O     
548  C  CB    . SER A 70  ? 1.2487 1.4135 1.1939 -0.0979 -0.0317 -0.0498 173  SER A CB    
549  O  OG    . SER A 70  ? 1.2386 1.4124 1.1935 -0.0850 -0.0313 -0.0468 173  SER A OG    
550  N  N     . SER A 71  ? 1.1824 1.3175 1.1007 -0.1146 -0.0374 -0.0588 174  SER A N     
551  C  CA    . SER A 71  ? 1.1844 1.3085 1.0901 -0.1305 -0.0386 -0.0635 174  SER A CA    
552  C  C     . SER A 71  ? 1.2875 1.4047 1.1841 -0.1279 -0.0441 -0.0679 174  SER A C     
553  O  O     . SER A 71  ? 1.2634 1.3621 1.1512 -0.1155 -0.0423 -0.0658 174  SER A O     
554  C  CB    . SER A 71  ? 1.1806 1.2701 1.0674 -0.1370 -0.0311 -0.0611 174  SER A CB    
555  O  OG    . SER A 71  ? 1.2169 1.2959 1.0921 -0.1550 -0.0319 -0.0661 174  SER A OG    
556  N  N     . PRO A 72  ? 1.2746 1.4073 1.1728 -0.1393 -0.0507 -0.0739 175  PRO A N     
557  C  CA    . PRO A 72  ? 1.2476 1.3718 1.1337 -0.1373 -0.0562 -0.0783 175  PRO A CA    
558  C  C     . PRO A 72  ? 1.2968 1.3797 1.1562 -0.1412 -0.0519 -0.0801 175  PRO A C     
559  O  O     . PRO A 72  ? 1.3323 1.4008 1.1788 -0.1334 -0.0534 -0.0818 175  PRO A O     
560  C  CB    . PRO A 72  ? 1.1480 1.3009 1.0429 -0.1510 -0.0646 -0.0843 175  PRO A CB    
561  C  CG    . PRO A 72  ? 1.2674 1.4514 1.1851 -0.1538 -0.0636 -0.0816 175  PRO A CG    
562  C  CD    . PRO A 72  ? 1.2429 1.4061 1.1562 -0.1529 -0.0541 -0.0764 175  PRO A CD    
563  N  N     . GLU A 73  ? 1.2376 1.2999 1.0872 -0.1524 -0.0459 -0.0796 176  GLU A N     
564  C  CA    . GLU A 73  ? 1.3390 1.3593 1.1613 -0.1561 -0.0413 -0.0816 176  GLU A CA    
565  C  C     . GLU A 73  ? 1.3478 1.3446 1.1621 -0.1375 -0.0341 -0.0754 176  GLU A C     
566  O  O     . GLU A 73  ? 1.3074 1.3173 1.1369 -0.1255 -0.0317 -0.0690 176  GLU A O     
567  C  CB    . GLU A 73  ? 1.4839 1.4875 1.2974 -0.1737 -0.0365 -0.0823 176  GLU A CB    
568  C  CG    . GLU A 73  ? 1.5029 1.5033 1.3232 -0.1689 -0.0285 -0.0743 176  GLU A CG    
569  C  CD    . GLU A 73  ? 1.6848 1.6684 1.4957 -0.1869 -0.0233 -0.0743 176  GLU A CD    
570  O  OE1   . GLU A 73  ? 1.6968 1.6650 1.4932 -0.2031 -0.0252 -0.0808 176  GLU A OE1   
571  O  OE2   . GLU A 73  ? 1.8670 1.8521 1.6841 -0.1852 -0.0173 -0.0678 176  GLU A OE2   
572  N  N     . LEU A 74  ? 1.3264 1.2883 1.1163 -0.1354 -0.0308 -0.0775 177  LEU A N     
573  C  CA    . LEU A 74  ? 1.3278 1.2672 1.1089 -0.1178 -0.0237 -0.0718 177  LEU A CA    
574  C  C     . LEU A 74  ? 1.3528 1.2543 1.1139 -0.1205 -0.0148 -0.0695 177  LEU A C     
575  O  O     . LEU A 74  ? 1.3321 1.2147 1.0776 -0.1364 -0.0143 -0.0745 177  LEU A O     
576  C  CB    . LEU A 74  ? 1.3153 1.2439 1.0831 -0.1089 -0.0255 -0.0750 177  LEU A CB    
577  C  CG    . LEU A 74  ? 1.3059 1.2649 1.0860 -0.1069 -0.0346 -0.0782 177  LEU A CG    
578  C  CD1   . LEU A 74  ? 1.2828 1.2253 1.0462 -0.0959 -0.0339 -0.0796 177  LEU A CD1   
579  C  CD2   . LEU A 74  ? 1.2645 1.2569 1.0726 -0.0976 -0.0365 -0.0725 177  LEU A CD2   
580  N  N     . PRO A 75  ? 1.3718 1.2615 1.1329 -0.1054 -0.0077 -0.0617 178  PRO A N     
581  C  CA    . PRO A 75  ? 1.3887 1.2388 1.1276 -0.1041 0.0013  -0.0589 178  PRO A CA    
582  C  C     . PRO A 75  ? 1.4519 1.2688 1.1634 -0.1042 0.0034  -0.0647 178  PRO A C     
583  O  O     . PRO A 75  ? 1.4147 1.2389 1.1250 -0.0998 -0.0009 -0.0687 178  PRO A O     
584  C  CB    . PRO A 75  ? 1.3551 1.2076 1.1034 -0.0847 0.0067  -0.0494 178  PRO A CB    
585  C  CG    . PRO A 75  ? 1.3073 1.2014 1.0844 -0.0816 0.0005  -0.0473 178  PRO A CG    
586  C  CD    . PRO A 75  ? 1.2888 1.2022 1.0712 -0.0896 -0.0077 -0.0549 178  PRO A CD    
587  N  N     . LYS A 76  ? 1.4988 1.2770 1.1865 -0.1089 0.0105  -0.0649 179  LYS A N     
588  C  CA    . LYS A 76  ? 1.5075 1.2494 1.1654 -0.1103 0.0131  -0.0714 179  LYS A CA    
589  C  C     . LYS A 76  ? 1.5349 1.2669 1.1865 -0.0885 0.0179  -0.0679 179  LYS A C     
590  O  O     . LYS A 76  ? 1.5973 1.3183 1.2336 -0.0867 0.0165  -0.0740 179  LYS A O     
591  C  CB    . LYS A 76  ? 1.5912 1.2909 1.2241 -0.1197 0.0205  -0.0720 179  LYS A CB    
592  C  CG    . LYS A 76  ? 1.7367 1.4435 1.3735 -0.1439 0.0164  -0.0761 179  LYS A CG    
593  C  CD    . LYS A 76  ? 1.7965 1.4587 1.4079 -0.1530 0.0249  -0.0755 179  LYS A CD    
594  C  CE    . LYS A 76  ? 1.7601 1.4325 1.3784 -0.1777 0.0217  -0.0783 179  LYS A CE    
595  N  NZ    . LYS A 76  ? 1.7371 1.3648 1.3307 -0.1872 0.0307  -0.0768 179  LYS A NZ    
596  N  N     . HIS A 77  ? 1.5135 1.2505 1.1767 -0.0718 0.0237  -0.0579 180  HIS A N     
597  C  CA    . HIS A 77  ? 1.5294 1.2614 1.1902 -0.0511 0.0287  -0.0537 180  HIS A CA    
598  C  C     . HIS A 77  ? 1.5321 1.2990 1.2127 -0.0459 0.0219  -0.0545 180  HIS A C     
599  O  O     . HIS A 77  ? 1.5749 1.3371 1.2503 -0.0321 0.0253  -0.0530 180  HIS A O     
600  C  CB    . HIS A 77  ? 1.5337 1.2640 1.2029 -0.0355 0.0361  -0.0426 180  HIS A CB    
601  C  CG    . HIS A 77  ? 1.5460 1.3173 1.2477 -0.0316 0.0312  -0.0367 180  HIS A CG    
602  N  ND1   . HIS A 77  ? 1.5241 1.3172 1.2411 -0.0450 0.0253  -0.0375 180  HIS A ND1   
603  C  CD2   . HIS A 77  ? 1.5657 1.3593 1.2868 -0.0162 0.0317  -0.0300 180  HIS A CD2   
604  C  CE1   . HIS A 77  ? 1.4519 1.2774 1.1947 -0.0373 0.0222  -0.0322 180  HIS A CE1   
605  N  NE2   . HIS A 77  ? 1.5071 1.3333 1.2531 -0.0206 0.0257  -0.0277 180  HIS A NE2   
606  N  N     . ILE A 78  ? 1.5125 1.3136 1.2149 -0.0560 0.0130  -0.0563 181  ILE A N     
607  C  CA    . ILE A 78  ? 1.5102 1.3417 1.2290 -0.0518 0.0063  -0.0575 181  ILE A CA    
608  C  C     . ILE A 78  ? 1.5108 1.3361 1.2131 -0.0612 0.0007  -0.0670 181  ILE A C     
609  O  O     . ILE A 78  ? 1.5131 1.3433 1.2130 -0.0526 -0.0006 -0.0679 181  ILE A O     
610  C  CB    . ILE A 78  ? 1.5084 1.3784 1.2566 -0.0566 -0.0004 -0.0553 181  ILE A CB    
611  C  CG1   . ILE A 78  ? 1.5496 1.4281 1.3140 -0.0447 0.0043  -0.0459 181  ILE A CG1   
612  C  CG2   . ILE A 78  ? 1.3676 1.2665 1.1297 -0.0550 -0.0081 -0.0578 181  ILE A CG2   
613  N  N     . TYR A 79  ? 1.4804 1.2947 1.1706 -0.0793 -0.0027 -0.0742 182  TYR A N     
614  C  CA    . TYR A 79  ? 1.5218 1.3295 1.1947 -0.0897 -0.0089 -0.0841 182  TYR A CA    
615  C  C     . TYR A 79  ? 1.5909 1.3613 1.2334 -0.0809 -0.0024 -0.0867 182  TYR A C     
616  O  O     . TYR A 79  ? 1.6070 1.3774 1.2380 -0.0802 -0.0067 -0.0923 182  TYR A O     
617  C  CB    . TYR A 79  ? 1.5219 1.3251 1.1889 -0.1125 -0.0135 -0.0911 182  TYR A CB    
618  C  CG    . TYR A 79  ? 1.5850 1.3815 1.2334 -0.1256 -0.0210 -0.1021 182  TYR A CG    
619  C  CD1   . TYR A 79  ? 1.5625 1.3953 1.2263 -0.1324 -0.0324 -0.1062 182  TYR A CD1   
620  C  CD2   . TYR A 79  ? 1.6269 1.3806 1.2416 -0.1307 -0.0169 -0.1086 182  TYR A CD2   
621  C  CE1   . TYR A 79  ? 1.6457 1.4747 1.2926 -0.1443 -0.0404 -0.1163 182  TYR A CE1   
622  C  CE2   . TYR A 79  ? 1.8100 1.5574 1.4063 -0.1434 -0.0246 -0.1195 182  TYR A CE2   
623  C  CZ    . TYR A 79  ? 1.7875 1.5738 1.4005 -0.1503 -0.0368 -0.1232 182  TYR A CZ    
624  O  OH    . TYR A 79  ? 1.7043 1.4865 1.2991 -0.1629 -0.0455 -0.1341 182  TYR A OH    
625  N  N     . ASN A 80  ? 1.6023 1.3406 1.2306 -0.0731 0.0082  -0.0825 183  ASN A N     
626  C  CA    . ASN A 80  ? 1.5643 1.2659 1.1631 -0.0627 0.0160  -0.0844 183  ASN A CA    
627  C  C     . ASN A 80  ? 1.5583 1.2723 1.1641 -0.0427 0.0191  -0.0791 183  ASN A C     
628  O  O     . ASN A 80  ? 1.7449 1.4336 1.3266 -0.0338 0.0246  -0.0815 183  ASN A O     
629  C  CB    . ASN A 80  ? 1.5902 1.2555 1.1735 -0.0576 0.0271  -0.0802 183  ASN A CB    
630  C  CG    . ASN A 80  ? 1.6429 1.2849 1.2106 -0.0779 0.0260  -0.0864 183  ASN A CG    
631  O  OD1   . ASN A 80  ? 1.6286 1.2766 1.1922 -0.0963 0.0172  -0.0956 183  ASN A OD1   
632  N  ND2   . ASN A 80  ? 1.5853 1.2006 1.1441 -0.0748 0.0348  -0.0812 183  ASN A ND2   
633  N  N     . LYS A 81  ? 1.5204 1.2715 1.1574 -0.0358 0.0161  -0.0720 184  LYS A N     
634  C  CA    . LYS A 81  ? 1.5396 1.3061 1.1854 -0.0197 0.0179  -0.0671 184  LYS A CA    
635  C  C     . LYS A 81  ? 1.6030 1.3848 1.2459 -0.0247 0.0091  -0.0734 184  LYS A C     
636  O  O     . LYS A 81  ? 1.6153 1.4130 1.2672 -0.0130 0.0096  -0.0692 184  LYS A O     
637  C  CB    . LYS A 81  ? 1.5339 1.3322 1.2133 -0.0114 0.0180  -0.0575 184  LYS A CB    
638  C  CG    . LYS A 81  ? 1.5921 1.3787 1.2755 -0.0026 0.0268  -0.0497 184  LYS A CG    
639  C  CD    . LYS A 81  ? 1.5134 1.3327 1.2291 0.0054  0.0258  -0.0410 184  LYS A CD    
640  C  CE    . LYS A 81  ? 1.5414 1.3512 1.2607 0.0157  0.0339  -0.0328 184  LYS A CE    
641  N  NZ    . LYS A 81  ? 1.5229 1.3643 1.2726 0.0233  0.0324  -0.0250 184  LYS A NZ    
642  N  N     . LEU A 82  ? 1.6067 1.3844 1.2372 -0.0418 0.0011  -0.0830 185  LEU A N     
643  C  CA    . LEU A 82  ? 1.6257 1.4191 1.2524 -0.0475 -0.0087 -0.0894 185  LEU A CA    
644  C  C     . LEU A 82  ? 1.7871 1.5470 1.3768 -0.0522 -0.0083 -0.0988 185  LEU A C     
645  O  O     . LEU A 82  ? 1.7666 1.4927 1.3350 -0.0582 -0.0032 -0.1029 185  LEU A O     
646  C  CB    . LEU A 82  ? 1.5525 1.3758 1.1982 -0.0644 -0.0204 -0.0932 185  LEU A CB    
647  C  CG    . LEU A 82  ? 1.4375 1.3027 1.1161 -0.0592 -0.0258 -0.0872 185  LEU A CG    
648  C  CD1   . LEU A 82  ? 1.4033 1.2730 1.1003 -0.0453 -0.0174 -0.0768 185  LEU A CD1   
649  C  CD2   . LEU A 82  ? 1.3889 1.2805 1.0849 -0.0756 -0.0353 -0.0908 185  LEU A CD2   
650  N  N     . ASP A 83  ? 1.8897 1.6577 1.4703 -0.0493 -0.0137 -0.1024 186  ASP A N     
651  C  CA    . ASP A 83  ? 1.9280 1.6680 1.4726 -0.0545 -0.0155 -0.1125 186  ASP A CA    
652  C  C     . ASP A 83  ? 1.9265 1.6804 1.4707 -0.0763 -0.0294 -0.1223 186  ASP A C     
653  O  O     . ASP A 83  ? 2.0041 1.7911 1.5624 -0.0787 -0.0398 -0.1229 186  ASP A O     
654  C  CB    . ASP A 83  ? 1.9957 1.7374 1.5290 -0.0393 -0.0139 -0.1107 186  ASP A CB    
655  C  CG    . ASP A 83  ? 2.1307 1.8436 1.6245 -0.0440 -0.0161 -0.1216 186  ASP A CG    
656  O  OD1   . ASP A 83  ? 2.3556 2.0391 1.8277 -0.0565 -0.0158 -0.1301 186  ASP A OD1   
657  O  OD2   . ASP A 83  ? 2.1653 1.8838 1.6485 -0.0353 -0.0181 -0.1218 186  ASP A OD2   
658  N  N     . LYS A 84  ? 1.7919 1.5205 1.3201 -0.0923 -0.0294 -0.1297 187  LYS A N     
659  C  CA    . LYS A 84  ? 1.7809 1.5219 1.3095 -0.1155 -0.0419 -0.1392 187  LYS A CA    
660  C  C     . LYS A 84  ? 1.7463 1.5350 1.3143 -0.1209 -0.0496 -0.1341 187  LYS A C     
661  O  O     . LYS A 84  ? 1.7233 1.5402 1.3000 -0.1327 -0.0621 -0.1393 187  LYS A O     
662  C  CB    . LYS A 84  ? 1.8893 1.6277 1.3936 -0.1204 -0.0513 -0.1492 187  LYS A CB    
663  C  CG    . LYS A 84  ? 1.9059 1.6412 1.3982 -0.1461 -0.0622 -0.1617 187  LYS A CG    
664  C  CD    . LYS A 84  ? 2.0394 1.7759 1.5084 -0.1492 -0.0726 -0.1711 187  LYS A CD    
665  C  CE    . LYS A 84  ? 2.0848 1.8208 1.5429 -0.1763 -0.0847 -0.1840 187  LYS A CE    
666  N  NZ    . LYS A 84  ? 1.9141 1.6525 1.3484 -0.1793 -0.0960 -0.1936 187  LYS A NZ    
667  N  N     . GLY A 85  ? 1.6870 1.4853 1.2786 -0.1114 -0.0423 -0.1239 188  GLY A N     
668  C  CA    . GLY A 85  ? 1.5646 1.4056 1.1922 -0.1139 -0.0480 -0.1187 188  GLY A CA    
669  C  C     . GLY A 85  ? 1.4903 1.3657 1.1337 -0.1036 -0.0550 -0.1156 188  GLY A C     
670  O  O     . GLY A 85  ? 1.4221 1.3335 1.0880 -0.1105 -0.0641 -0.1158 188  GLY A O     
671  N  N     . GLN A 86  ? 1.5280 1.3929 1.1597 -0.0866 -0.0504 -0.1124 189  GLN A N     
672  C  CA    . GLN A 86  ? 1.4407 1.3335 1.0838 -0.0758 -0.0558 -0.1087 189  GLN A CA    
673  C  C     . GLN A 86  ? 1.3592 1.2506 1.0123 -0.0555 -0.0457 -0.0981 189  GLN A C     
674  O  O     . GLN A 86  ? 1.3894 1.2513 1.0265 -0.0467 -0.0350 -0.0958 189  GLN A O     
675  C  CB    . GLN A 86  ? 1.4715 1.3553 1.0872 -0.0769 -0.0621 -0.1162 189  GLN A CB    
676  C  CG    . GLN A 86  ? 1.4827 1.3769 1.0923 -0.0973 -0.0750 -0.1269 189  GLN A CG    
677  C  CD    . GLN A 86  ? 1.4508 1.3363 1.0316 -0.0979 -0.0820 -0.1345 189  GLN A CD    
678  O  OE1   . GLN A 86  ? 1.4515 1.3056 1.0050 -0.0882 -0.0748 -0.1354 189  GLN A OE1   
679  N  NE2   . GLN A 86  ? 1.3864 1.3007 0.9729 -0.1087 -0.0962 -0.1400 189  GLN A NE2   
680  N  N     . ILE A 87  ? 1.3017 1.2252 0.9813 -0.0483 -0.0489 -0.0915 190  ILE A N     
681  C  CA    . ILE A 87  ? 1.3175 1.2443 1.0098 -0.0308 -0.0407 -0.0815 190  ILE A CA    
682  C  C     . ILE A 87  ? 1.3137 1.2482 0.9987 -0.0205 -0.0433 -0.0797 190  ILE A C     
683  O  O     . ILE A 87  ? 1.3146 1.2640 0.9953 -0.0261 -0.0538 -0.0846 190  ILE A O     
684  C  CB    . ILE A 87  ? 1.3738 1.3278 1.0999 -0.0298 -0.0414 -0.0751 190  ILE A CB    
685  C  CG1   . ILE A 87  ? 1.3103 1.2972 1.0520 -0.0375 -0.0534 -0.0780 190  ILE A CG1   
686  C  CG2   . ILE A 87  ? 1.2600 1.2031 0.9914 -0.0365 -0.0363 -0.0747 190  ILE A CG2   
687  C  CD1   . ILE A 87  ? 1.3930 1.4060 1.1658 -0.0360 -0.0540 -0.0726 190  ILE A CD1   
688  N  N     . ILE A 88  ? 1.3045 1.2300 0.9886 -0.0051 -0.0338 -0.0721 191  ILE A N     
689  C  CA    . ILE A 88  ? 1.3945 1.3267 1.0733 0.0063  -0.0342 -0.0682 191  ILE A CA    
690  C  C     . ILE A 88  ? 1.3228 1.2806 1.0321 0.0140  -0.0338 -0.0592 191  ILE A C     
691  O  O     . ILE A 88  ? 1.4072 1.3628 1.1310 0.0206  -0.0252 -0.0524 191  ILE A O     
692  C  CB    . ILE A 88  ? 1.4948 1.3987 1.1496 0.0178  -0.0231 -0.0659 191  ILE A CB    
693  C  CG1   . ILE A 88  ? 1.7778 1.6662 1.4391 0.0231  -0.0110 -0.0609 191  ILE A CG1   
694  C  CG2   . ILE A 88  ? 1.4417 1.3227 1.0614 0.0116  -0.0263 -0.0758 191  ILE A CG2   
695  C  CD1   . ILE A 88  ? 1.6812 1.5427 1.3198 0.0352  0.0011  -0.0584 191  ILE A CD1   
696  N  N     . VAL A 89  ? 1.1728 1.1550 0.8917 0.0131  -0.0434 -0.0594 192  VAL A N     
697  C  CA    . VAL A 89  ? 1.1487 1.1529 0.8933 0.0208  -0.0435 -0.0515 192  VAL A CA    
698  C  C     . VAL A 89  ? 1.2157 1.2183 0.9504 0.0334  -0.0413 -0.0460 192  VAL A C     
699  O  O     . VAL A 89  ? 1.2417 1.2359 0.9522 0.0342  -0.0445 -0.0496 192  VAL A O     
700  C  CB    . VAL A 89  ? 1.1503 1.1831 0.9139 0.0128  -0.0546 -0.0545 192  VAL A CB    
701  C  CG1   . VAL A 89  ? 1.2607 1.2949 1.0344 0.0005  -0.0554 -0.0590 192  VAL A CG1   
702  C  CG2   . VAL A 89  ? 1.1414 1.1837 0.8905 0.0089  -0.0655 -0.0603 192  VAL A CG2   
703  N  N     . VAL A 90  ? 1.2026 1.2123 0.9551 0.0428  -0.0357 -0.0370 193  VAL A N     
704  C  CA    . VAL A 90  ? 1.0931 1.1004 0.8385 0.0550  -0.0318 -0.0300 193  VAL A CA    
705  C  C     . VAL A 90  ? 1.1094 1.1399 0.8738 0.0580  -0.0383 -0.0261 193  VAL A C     
706  O  O     . VAL A 90  ? 1.1457 1.1865 0.9344 0.0583  -0.0364 -0.0224 193  VAL A O     
707  C  CB    . VAL A 90  ? 1.1247 1.1181 0.8735 0.0637  -0.0180 -0.0220 193  VAL A CB    
708  C  CG1   . VAL A 90  ? 1.1545 1.1455 0.8958 0.0753  -0.0133 -0.0141 193  VAL A CG1   
709  C  CG2   . VAL A 90  ? 1.1460 1.1161 0.8758 0.0622  -0.0110 -0.0257 193  VAL A CG2   
710  N  N     . ILE A 91  ? 1.1660 1.2041 0.9183 0.0609  -0.0460 -0.0271 194  ILE A N     
711  C  CA    . ILE A 91  ? 1.1439 1.2028 0.9110 0.0656  -0.0524 -0.0233 194  ILE A CA    
712  C  C     . ILE A 91  ? 1.0649 1.1161 0.8281 0.0787  -0.0450 -0.0132 194  ILE A C     
713  O  O     . ILE A 91  ? 1.1596 1.1961 0.8995 0.0844  -0.0412 -0.0113 194  ILE A O     
714  C  CB    . ILE A 91  ? 1.1094 1.1842 0.8672 0.0617  -0.0658 -0.0295 194  ILE A CB    
715  C  CG1   . ILE A 91  ? 1.1781 1.2633 0.9443 0.0472  -0.0725 -0.0387 194  ILE A CG1   
716  C  CG2   . ILE A 91  ? 0.9881 1.0824 0.7576 0.0702  -0.0713 -0.0241 194  ILE A CG2   
717  C  CD1   . ILE A 91  ? 1.3221 1.4296 1.0862 0.0419  -0.0863 -0.0446 194  ILE A CD1   
718  N  N     . TRP A 92  ? 1.0222 1.0819 0.8070 0.0833  -0.0427 -0.0069 195  TRP A N     
719  C  CA    . TRP A 92  ? 1.0765 1.1289 0.8602 0.0945  -0.0354 0.0032  195  TRP A CA    
720  C  C     . TRP A 92  ? 1.1246 1.1913 0.9125 0.1010  -0.0431 0.0063  195  TRP A C     
721  O  O     . TRP A 92  ? 1.1097 1.1949 0.9095 0.0971  -0.0524 0.0014  195  TRP A O     
722  C  CB    . TRP A 92  ? 1.0839 1.1310 0.8881 0.0947  -0.0253 0.0088  195  TRP A CB    
723  C  CG    . TRP A 92  ? 1.1543 1.1879 0.9549 0.0910  -0.0168 0.0077  195  TRP A CG    
724  C  CD1   . TRP A 92  ? 1.1574 1.1918 0.9637 0.0821  -0.0181 0.0009  195  TRP A CD1   
725  C  CD2   . TRP A 92  ? 1.2085 1.2258 0.9990 0.0971  -0.0049 0.0141  195  TRP A CD2   
726  N  NE1   . TRP A 92  ? 1.1706 1.1897 0.9705 0.0832  -0.0081 0.0028  195  TRP A NE1   
727  C  CE2   . TRP A 92  ? 1.1753 1.1848 0.9661 0.0923  0.0002  0.0107  195  TRP A CE2   
728  C  CE3   . TRP A 92  ? 1.1768 1.1854 0.9577 0.1064  0.0026  0.0230  195  TRP A CE3   
729  C  CZ2   . TRP A 92  ? 1.1647 1.1598 0.9476 0.0974  0.0124  0.0156  195  TRP A CZ2   
730  C  CZ3   . TRP A 92  ? 1.2029 1.1975 0.9762 0.1104  0.0149  0.0279  195  TRP A CZ3   
731  C  CH2   . TRP A 92  ? 1.1914 1.1803 0.9663 0.1062  0.0197  0.0241  195  TRP A CH2   
732  N  N     . VAL A 93  ? 1.1780 1.2359 0.9556 0.1117  -0.0383 0.0149  196  VAL A N     
733  C  CA    . VAL A 93  ? 1.1530 1.2210 0.9308 0.1204  -0.0444 0.0194  196  VAL A CA    
734  C  C     . VAL A 93  ? 1.1820 1.2350 0.9577 0.1303  -0.0340 0.0310  196  VAL A C     
735  O  O     . VAL A 93  ? 1.2183 1.2548 0.9799 0.1330  -0.0247 0.0356  196  VAL A O     
736  C  CB    . VAL A 93  ? 1.0876 1.1633 0.8429 0.1230  -0.0550 0.0156  196  VAL A CB    
737  C  CG1   . VAL A 93  ? 1.1618 1.2191 0.8893 0.1246  -0.0497 0.0161  196  VAL A CG1   
738  C  CG2   . VAL A 93  ? 0.9350 1.0197 0.6883 0.1348  -0.0603 0.0221  196  VAL A CG2   
739  N  N     . ILE A 94  ? 1.2351 1.2933 1.0248 0.1357  -0.0350 0.0359  197  ILE A N     
740  C  CA    . ILE A 94  ? 1.2888 1.3320 1.0760 0.1447  -0.0258 0.0473  197  ILE A CA    
741  C  C     . ILE A 94  ? 1.2531 1.2939 1.0161 0.1563  -0.0294 0.0526  197  ILE A C     
742  O  O     . ILE A 94  ? 1.2170 1.2734 0.9764 0.1599  -0.0410 0.0493  197  ILE A O     
743  C  CB    . ILE A 94  ? 1.2525 1.2987 1.0628 0.1455  -0.0250 0.0498  197  ILE A CB    
744  C  CG1   . ILE A 94  ? 1.1499 1.1979 0.9824 0.1343  -0.0213 0.0449  197  ILE A CG1   
745  C  CG2   . ILE A 94  ? 1.3804 1.4093 1.1867 0.1543  -0.0158 0.0617  197  ILE A CG2   
746  C  CD1   . ILE A 94  ? 1.5181 1.5664 1.3717 0.1340  -0.0198 0.0467  197  ILE A CD1   
747  N  N     . VAL A 95  ? 1.3872 1.4099 1.1334 0.1623  -0.0195 0.0612  198  VAL A N     
748  C  CA    . VAL A 95  ? 1.3707 1.3890 1.0900 0.1734  -0.0220 0.0667  198  VAL A CA    
749  C  C     . VAL A 95  ? 1.5004 1.5057 1.2170 0.1845  -0.0149 0.0797  198  VAL A C     
750  O  O     . VAL A 95  ? 1.5776 1.5844 1.2777 0.1956  -0.0204 0.0845  198  VAL A O     
751  C  CB    . VAL A 95  ? 1.2849 1.2917 0.9796 0.1727  -0.0168 0.0659  198  VAL A CB    
752  C  CG1   . VAL A 95  ? 1.2409 1.2586 0.9331 0.1627  -0.0256 0.0527  198  VAL A CG1   
753  C  CG2   . VAL A 95  ? 1.3491 1.3386 1.0493 0.1705  -0.0005 0.0723  198  VAL A CG2   
754  N  N     . SER A 96  ? 1.7597 1.7522 1.4917 0.1817  -0.0030 0.0858  199  SER A N     
755  C  CA    . SER A 96  ? 1.8275 1.8048 1.5585 0.1900  0.0049  0.0980  199  SER A CA    
756  C  C     . SER A 96  ? 1.8827 1.8615 1.6413 0.1855  0.0054  0.0971  199  SER A C     
757  O  O     . SER A 96  ? 1.7869 1.7755 1.5660 0.1748  0.0034  0.0887  199  SER A O     
758  C  CB    . SER A 96  ? 1.9061 1.8639 1.6281 0.1900  0.0207  0.1073  199  SER A CB    
759  O  OG    . SER A 96  ? 1.8613 1.8177 1.6066 0.1788  0.0287  0.1054  199  SER A OG    
760  N  N     . PRO A 97  ? 1.8119 1.7796 1.5704 0.1938  0.0081  0.1057  200  PRO A N     
761  C  CA    . PRO A 97  ? 1.7770 1.7430 1.5595 0.1897  0.0089  0.1044  200  PRO A CA    
762  C  C     . PRO A 97  ? 1.7514 1.7062 1.5509 0.1785  0.0207  0.1064  200  PRO A C     
763  O  O     . PRO A 97  ? 1.7279 1.6764 1.5447 0.1747  0.0232  0.1068  200  PRO A O     
764  C  CB    . PRO A 97  ? 1.8131 1.7659 1.5851 0.2032  0.0096  0.1141  200  PRO A CB    
765  C  CG    . PRO A 97  ? 1.8491 1.7896 1.5944 0.2116  0.0154  0.1241  200  PRO A CG    
766  C  CD    . PRO A 97  ? 1.8319 1.7878 1.5665 0.2082  0.0095  0.1165  200  PRO A CD    
767  N  N     . ASN A 98  ? 1.7455 1.6981 1.5400 0.1733  0.0279  0.1075  201  ASN A N     
768  C  CA    . ASN A 98  ? 1.7417 1.6880 1.5532 0.1628  0.0388  0.1096  201  ASN A CA    
769  C  C     . ASN A 98  ? 1.6826 1.6446 1.5077 0.1524  0.0355  0.0990  201  ASN A C     
770  O  O     . ASN A 98  ? 1.6574 1.6175 1.4905 0.1456  0.0443  0.1007  201  ASN A O     
771  C  CB    . ASN A 98  ? 1.7803 1.7113 1.5771 0.1660  0.0522  0.1210  201  ASN A CB    
772  C  CG    . ASN A 98  ? 1.8472 1.7612 1.6260 0.1774  0.0557  0.1323  201  ASN A CG    
773  O  OD1   . ASN A 98  ? 1.8253 1.7343 1.6093 0.1809  0.0518  0.1335  201  ASN A OD1   
774  N  ND2   . ASN A 98  ? 1.8997 1.8037 1.6559 0.1841  0.0636  0.1410  201  ASN A ND2   
775  N  N     . ASN A 99  ? 1.6218 1.5996 1.4493 0.1514  0.0231  0.0887  202  ASN A N     
776  C  CA    . ASN A 99  ? 1.5973 1.5891 1.4362 0.1419  0.0188  0.0784  202  ASN A CA    
777  C  C     . ASN A 99  ? 1.5932 1.5835 1.4178 0.1409  0.0234  0.0779  202  ASN A C     
778  O  O     . ASN A 99  ? 1.5671 1.5631 1.4015 0.1331  0.0246  0.0724  202  ASN A O     
779  C  CB    . ASN A 99  ? 1.6317 1.6252 1.4972 0.1319  0.0225  0.0765  202  ASN A CB    
780  C  CG    . ASN A 99  ? 1.5146 1.5108 1.3938 0.1318  0.0165  0.0737  202  ASN A CG    
781  O  OD1   . ASN A 99  ? 1.4897 1.4934 1.3630 0.1375  0.0072  0.0700  202  ASN A OD1   
782  N  ND2   . ASN A 99  ? 1.4712 1.4617 1.3686 0.1253  0.0217  0.0754  202  ASN A ND2   
783  N  N     . ASP A 100 ? 1.6106 1.5921 1.4104 0.1496  0.0261  0.0837  203  ASP A N     
784  C  CA    . ASP A 100 ? 1.5448 1.5238 1.3268 0.1498  0.0294  0.0817  203  ASP A CA    
785  C  C     . ASP A 100 ? 1.4738 1.4655 1.2488 0.1468  0.0166  0.0699  203  ASP A C     
786  O  O     . ASP A 100 ? 1.4637 1.4643 1.2341 0.1501  0.0055  0.0666  203  ASP A O     
787  C  CB    . ASP A 100 ? 1.7717 1.7372 1.5269 0.1603  0.0357  0.0911  203  ASP A CB    
788  C  CG    . ASP A 100 ? 1.9056 1.8577 1.6670 0.1624  0.0493  0.1037  203  ASP A CG    
789  O  OD1   . ASP A 100 ? 1.8572 1.8108 1.6441 0.1553  0.0527  0.1045  203  ASP A OD1   
790  O  OD2   . ASP A 100 ? 1.8101 1.7498 1.5503 0.1708  0.0565  0.1127  203  ASP A OD2   
791  N  N     . LYS A 101 ? 1.4042 1.3968 1.1785 0.1406  0.0185  0.0637  204  LYS A N     
792  C  CA    . LYS A 101 ? 1.3566 1.3599 1.1281 0.1347  0.0075  0.0519  204  LYS A CA    
793  C  C     . LYS A 101 ? 1.2766 1.2715 1.0219 0.1358  0.0091  0.0484  204  LYS A C     
794  O  O     . LYS A 101 ? 1.2898 1.2726 1.0288 0.1374  0.0207  0.0525  204  LYS A O     
795  C  CB    . LYS A 101 ? 1.3618 1.3733 1.1585 0.1245  0.0069  0.0461  204  LYS A CB    
796  C  CG    . LYS A 101 ? 1.4014 1.4047 1.2067 0.1221  0.0195  0.0500  204  LYS A CG    
797  C  CD    . LYS A 101 ? 1.3726 1.3852 1.2040 0.1132  0.0180  0.0455  204  LYS A CD    
798  C  CE    . LYS A 101 ? 1.4666 1.4865 1.3183 0.1121  0.0146  0.0476  204  LYS A CE    
799  N  NZ    . LYS A 101 ? 1.4759 1.4862 1.3298 0.1172  0.0237  0.0584  204  LYS A NZ    
800  N  N     . GLN A 102 ? 1.3119 1.3135 1.0420 0.1348  -0.0026 0.0406  205  GLN A N     
801  C  CA    . GLN A 102 ? 1.3233 1.3172 1.0285 0.1331  -0.0040 0.0340  205  GLN A CA    
802  C  C     . GLN A 102 ? 1.3213 1.3239 1.0352 0.1216  -0.0120 0.0223  205  GLN A C     
803  O  O     . GLN A 102 ? 1.3108 1.3280 1.0478 0.1160  -0.0182 0.0194  205  GLN A O     
804  C  CB    . GLN A 102 ? 1.3759 1.3698 1.0535 0.1400  -0.0116 0.0339  205  GLN A CB    
805  C  CG    . GLN A 102 ? 1.4125 1.3948 1.0757 0.1522  -0.0029 0.0459  205  GLN A CG    
806  C  CD    . GLN A 102 ? 1.4821 1.4651 1.1163 0.1596  -0.0114 0.0457  205  GLN A CD    
807  O  OE1   . GLN A 102 ? 1.5673 1.5408 1.1855 0.1701  -0.0056 0.0554  205  GLN A OE1   
808  N  NE2   . GLN A 102 ? 1.4650 1.4598 1.0919 0.1537  -0.0254 0.0348  205  GLN A NE2   
809  N  N     . LYS A 103 ? 1.2082 1.2003 0.9023 0.1181  -0.0115 0.0155  206  LYS A N     
810  C  CA    . LYS A 103 ? 1.1562 1.1524 0.8556 0.1066  -0.0176 0.0048  206  LYS A CA    
811  C  C     . LYS A 103 ? 1.1874 1.1762 0.8571 0.1034  -0.0243 -0.0041 206  LYS A C     
812  O  O     . LYS A 103 ? 1.2866 1.2619 0.9297 0.1106  -0.0205 -0.0020 206  LYS A O     
813  C  CB    . LYS A 103 ? 1.1868 1.1733 0.8983 0.1034  -0.0067 0.0055  206  LYS A CB    
814  C  CG    . LYS A 103 ? 1.1632 1.1281 0.8508 0.1077  0.0036  0.0058  206  LYS A CG    
815  C  CD    . LYS A 103 ? 1.1575 1.1154 0.8591 0.1061  0.0142  0.0073  206  LYS A CD    
816  C  CE    . LYS A 103 ? 1.2528 1.1891 0.9296 0.1119  0.0251  0.0075  206  LYS A CE    
817  N  NZ    . LYS A 103 ? 1.2825 1.2135 0.9734 0.1123  0.0358  0.0101  206  LYS A NZ    
818  N  N     . TYR A 104 ? 1.2167 1.2141 0.8904 0.0920  -0.0342 -0.0142 207  TYR A N     
819  C  CA    . TYR A 104 ? 1.2218 1.2105 0.8693 0.0853  -0.0406 -0.0244 207  TYR A CA    
820  C  C     . TYR A 104 ? 1.2526 1.2438 0.9120 0.0716  -0.0442 -0.0331 207  TYR A C     
821  O  O     . TYR A 104 ? 1.1636 1.1746 0.8482 0.0659  -0.0503 -0.0339 207  TYR A O     
822  C  CB    . TYR A 104 ? 1.1310 1.1335 0.7644 0.0860  -0.0542 -0.0275 207  TYR A CB    
823  C  CG    . TYR A 104 ? 1.0414 1.0728 0.6999 0.0831  -0.0653 -0.0274 207  TYR A CG    
824  C  CD1   . TYR A 104 ? 1.0461 1.0882 0.7218 0.0930  -0.0631 -0.0174 207  TYR A CD1   
825  C  CD2   . TYR A 104 ? 1.1128 1.1602 0.7765 0.0706  -0.0775 -0.0372 207  TYR A CD2   
826  C  CE1   . TYR A 104 ? 1.1197 1.1870 0.8167 0.0919  -0.0725 -0.0174 207  TYR A CE1   
827  C  CE2   . TYR A 104 ? 1.1490 1.2245 0.8358 0.0689  -0.0869 -0.0368 207  TYR A CE2   
828  C  CZ    . TYR A 104 ? 1.1735 1.2585 0.8764 0.0804  -0.0842 -0.0270 207  TYR A CZ    
829  O  OH    . TYR A 104 ? 1.1874 1.2991 0.9121 0.0802  -0.0928 -0.0266 207  TYR A OH    
830  N  N     . THR A 105 ? 1.2578 1.2275 0.8981 0.0669  -0.0398 -0.0394 208  THR A N     
831  C  CA    . THR A 105 ? 1.1976 1.1633 0.8468 0.0551  -0.0401 -0.0461 208  THR A CA    
832  C  C     . THR A 105 ? 1.2595 1.2297 0.8963 0.0416  -0.0531 -0.0578 208  THR A C     
833  O  O     . THR A 105 ? 1.2430 1.2044 0.8519 0.0412  -0.0579 -0.0631 208  THR A O     
834  C  CB    . THR A 105 ? 1.2340 1.1718 0.8700 0.0584  -0.0267 -0.0456 208  THR A CB    
835  O  OG1   . THR A 105 ? 1.1863 1.1226 0.8339 0.0707  -0.0148 -0.0344 208  THR A OG1   
836  C  CG2   . THR A 105 ? 1.3757 1.3089 1.0231 0.0479  -0.0258 -0.0505 208  THR A CG2   
837  N  N     . LEU A 106 ? 1.2559 1.2404 0.9135 0.0301  -0.0588 -0.0618 209  LEU A N     
838  C  CA    . LEU A 106 ? 1.2310 1.2221 0.8820 0.0147  -0.0704 -0.0726 209  LEU A CA    
839  C  C     . LEU A 106 ? 1.2243 1.1953 0.8717 0.0041  -0.0652 -0.0783 209  LEU A C     
840  O  O     . LEU A 106 ? 1.3142 1.2756 0.9734 0.0083  -0.0547 -0.0731 209  LEU A O     
841  C  CB    . LEU A 106 ? 1.1388 1.1650 0.8170 0.0094  -0.0813 -0.0725 209  LEU A CB    
842  C  CG    . LEU A 106 ? 1.3034 1.3533 0.9845 0.0174  -0.0901 -0.0689 209  LEU A CG    
843  C  CD1   . LEU A 106 ? 1.4141 1.4621 1.1022 0.0343  -0.0815 -0.0572 209  LEU A CD1   
844  C  CD2   . LEU A 106 ? 1.4624 1.5457 1.1687 0.0098  -0.1008 -0.0710 209  LEU A CD2   
845  N  N     . LYS A 107 ? 1.2425 1.2070 0.8729 -0.0099 -0.0729 -0.0890 210  LYS A N     
846  C  CA    . LYS A 107 ? 1.2687 1.2139 0.8946 -0.0222 -0.0694 -0.0951 210  LYS A CA    
847  C  C     . LYS A 107 ? 1.3053 1.2706 0.9399 -0.0404 -0.0822 -0.1032 210  LYS A C     
848  O  O     . LYS A 107 ? 1.3666 1.3325 0.9825 -0.0492 -0.0920 -0.1116 210  LYS A O     
849  C  CB    . LYS A 107 ? 1.3501 1.2568 0.9397 -0.0216 -0.0630 -0.1008 210  LYS A CB    
850  C  CG    . LYS A 107 ? 1.4381 1.3206 1.0213 -0.0329 -0.0580 -0.1062 210  LYS A CG    
851  C  CD    . LYS A 107 ? 1.6724 1.5141 1.2178 -0.0305 -0.0507 -0.1118 210  LYS A CD    
852  C  CE    . LYS A 107 ? 1.7731 1.5881 1.3112 -0.0409 -0.0451 -0.1165 210  LYS A CE    
853  N  NZ    . LYS A 107 ? 2.0804 1.8527 1.5797 -0.0378 -0.0374 -0.1225 210  LYS A NZ    
854  N  N     . ILE A 108 ? 1.4139 1.3966 1.0768 -0.0463 -0.0821 -0.1006 211  ILE A N     
855  C  CA    . ILE A 108 ? 1.3546 1.3624 1.0319 -0.0625 -0.0932 -0.1064 211  ILE A CA    
856  C  C     . ILE A 108 ? 1.2973 1.2939 0.9828 -0.0740 -0.0876 -0.1080 211  ILE A C     
857  O  O     . ILE A 108 ? 1.3140 1.2917 1.0016 -0.0667 -0.0762 -0.1026 211  ILE A O     
858  C  CB    . ILE A 108 ? 1.2882 1.3363 0.9948 -0.0564 -0.0998 -0.1006 211  ILE A CB    
859  C  CG1   . ILE A 108 ? 1.3661 1.4442 1.0835 -0.0717 -0.1130 -0.1072 211  ILE A CG1   
860  C  CG2   . ILE A 108 ? 1.1837 1.2378 0.9165 -0.0489 -0.0911 -0.0920 211  ILE A CG2   
861  C  CD1   . ILE A 108 ? 1.3765 1.4927 1.1144 -0.0634 -0.1212 -0.1025 211  ILE A CD1   
862  N  N     . ASN A 109 ? 1.3402 1.3490 1.0299 -0.0924 -0.0958 -0.1152 212  ASN A N     
863  C  CA    . ASN A 109 ? 1.3747 1.3754 1.0730 -0.1046 -0.0910 -0.1163 212  ASN A CA    
864  C  C     . ASN A 109 ? 1.3261 1.3466 1.0554 -0.0965 -0.0860 -0.1071 212  ASN A C     
865  O  O     . ASN A 109 ? 1.2495 1.2994 0.9984 -0.0875 -0.0900 -0.1023 212  ASN A O     
866  C  CB    . ASN A 109 ? 1.3456 1.3614 1.0459 -0.1266 -0.1014 -0.1251 212  ASN A CB    
867  C  CG    . ASN A 109 ? 1.3446 1.3402 1.0132 -0.1369 -0.1074 -0.1355 212  ASN A CG    
868  O  OD1   . ASN A 109 ? 1.5104 1.5197 1.1712 -0.1334 -0.1164 -0.1382 212  ASN A OD1   
869  N  ND2   . ASN A 109 ? 1.3587 1.3202 1.0073 -0.1496 -0.1027 -0.1415 212  ASN A ND2   
870  N  N     . HIS A 110 ? 1.3920 1.3950 1.1242 -0.0994 -0.0770 -0.1047 213  HIS A N     
871  C  CA    . HIS A 110 ? 1.3292 1.3479 1.0879 -0.0915 -0.0719 -0.0963 213  HIS A CA    
872  C  C     . HIS A 110 ? 1.3254 1.3803 1.1093 -0.1013 -0.0791 -0.0971 213  HIS A C     
873  O  O     . HIS A 110 ? 1.4039 1.4819 1.2109 -0.0924 -0.0787 -0.0911 213  HIS A O     
874  C  CB    . HIS A 110 ? 1.2796 1.2697 1.0328 -0.0910 -0.0608 -0.0932 213  HIS A CB    
875  C  CG    . HIS A 110 ? 1.3403 1.3174 1.0853 -0.1095 -0.0608 -0.0989 213  HIS A CG    
876  N  ND1   . HIS A 110 ? 1.2889 1.2876 1.0540 -0.1206 -0.0631 -0.0984 213  HIS A ND1   
877  C  CD2   . HIS A 110 ? 1.4201 1.3634 1.1383 -0.1190 -0.0582 -0.1049 213  HIS A CD2   
878  C  CE1   . HIS A 110 ? 1.4187 1.3980 1.1704 -0.1369 -0.0618 -0.1035 213  HIS A CE1   
879  N  NE2   . HIS A 110 ? 1.4260 1.3705 1.1488 -0.1364 -0.0590 -0.1078 213  HIS A NE2   
880  N  N     . ASP A 111 ? 1.3074 1.3676 1.0872 -0.1198 -0.0854 -0.1045 214  ASP A N     
881  C  CA    . ASP A 111 ? 1.3159 1.4102 1.1196 -0.1308 -0.0909 -0.1053 214  ASP A CA    
882  C  C     . ASP A 111 ? 1.2863 1.4188 1.1039 -0.1278 -0.1019 -0.1063 214  ASP A C     
883  O  O     . ASP A 111 ? 1.3262 1.4890 1.1609 -0.1389 -0.1081 -0.1086 214  ASP A O     
884  C  CB    . ASP A 111 ? 1.4121 1.4964 1.2066 -0.1533 -0.0923 -0.1124 214  ASP A CB    
885  C  CG    . ASP A 111 ? 1.4214 1.4982 1.1943 -0.1639 -0.1009 -0.1216 214  ASP A CG    
886  O  OD1   . ASP A 111 ? 1.4261 1.4844 1.1794 -0.1532 -0.1008 -0.1225 214  ASP A OD1   
887  O  OD2   . ASP A 111 ? 1.5370 1.6272 1.3124 -0.1833 -0.1077 -0.1280 214  ASP A OD2   
888  N  N     . CYS A 112 ? 1.2712 1.4040 1.0824 -0.1127 -0.1041 -0.1040 215  CYS A N     
889  C  CA    . CYS A 112 ? 1.2945 1.4603 1.1146 -0.1090 -0.1149 -0.1048 215  CYS A CA    
890  C  C     . CYS A 112 ? 1.2342 1.4273 1.0807 -0.0949 -0.1139 -0.0972 215  CYS A C     
891  O  O     . CYS A 112 ? 1.1949 1.3759 1.0468 -0.0832 -0.1051 -0.0908 215  CYS A O     
892  C  CB    . CYS A 112 ? 1.4242 1.5750 1.2205 -0.1002 -0.1181 -0.1064 215  CYS A CB    
893  S  SG    . CYS A 112 ? 1.8110 1.9411 1.6029 -0.0767 -0.1077 -0.0969 215  CYS A SG    
894  N  N     . VAL A 113 ? 1.3013 1.5317 1.1639 -0.0960 -0.1232 -0.0981 216  VAL A N     
895  C  CA    . VAL A 113 ? 1.2269 1.4849 1.1130 -0.0822 -0.1236 -0.0917 216  VAL A CA    
896  C  C     . VAL A 113 ? 1.2405 1.4862 1.1178 -0.0628 -0.1215 -0.0860 216  VAL A C     
897  O  O     . VAL A 113 ? 1.2137 1.4451 1.0696 -0.0609 -0.1246 -0.0881 216  VAL A O     
898  C  CB    . VAL A 113 ? 1.2694 1.5700 1.1719 -0.0873 -0.1346 -0.0942 216  VAL A CB    
899  C  CG1   . VAL A 113 ? 1.2030 1.5310 1.1298 -0.0729 -0.1338 -0.0879 216  VAL A CG1   
900  C  CG2   . VAL A 113 ? 1.3057 1.6167 1.2141 -0.1092 -0.1367 -0.1004 216  VAL A CG2   
901  N  N     . PRO A 114 ? 1.2541 1.5033 1.1459 -0.0488 -0.1158 -0.0790 217  PRO A N     
902  C  CA    . PRO A 114 ? 1.3171 1.5573 1.2020 -0.0311 -0.1142 -0.0732 217  PRO A CA    
903  C  C     . PRO A 114 ? 1.1877 1.4469 1.0673 -0.0255 -0.1244 -0.0737 217  PRO A C     
904  O  O     . PRO A 114 ? 1.1690 1.4134 1.0324 -0.0151 -0.1239 -0.0707 217  PRO A O     
905  C  CB    . PRO A 114 ? 1.1908 1.4395 1.0968 -0.0205 -0.1086 -0.0669 217  PRO A CB    
906  C  CG    . PRO A 114 ? 1.0483 1.2936 0.9635 -0.0315 -0.1033 -0.0689 217  PRO A CG    
907  C  CD    . PRO A 114 ? 1.1151 1.3709 1.0269 -0.0489 -0.1095 -0.0761 217  PRO A CD    
908  N  N     . GLU A 115 ? 1.2603 1.5531 1.1532 -0.0317 -0.1336 -0.0769 218  GLU A N     
909  C  CA    . GLU A 115 ? 1.2751 1.5890 1.1631 -0.0263 -0.1445 -0.0774 218  GLU A CA    
910  C  C     . GLU A 115 ? 1.2167 1.5137 1.0774 -0.0341 -0.1496 -0.0831 218  GLU A C     
911  O  O     . GLU A 115 ? 1.2657 1.5652 1.1130 -0.0249 -0.1555 -0.0817 218  GLU A O     
912  C  CB    . GLU A 115 ? 1.3338 1.6900 1.2437 -0.0326 -0.1531 -0.0799 218  GLU A CB    
913  C  CG    . GLU A 115 ? 1.2084 1.5929 1.1197 -0.0221 -0.1640 -0.0780 218  GLU A CG    
914  C  CD    . GLU A 115 ? 1.3801 1.8096 1.3148 -0.0282 -0.1723 -0.0804 218  GLU A CD    
915  O  OE1   . GLU A 115 ? 1.6749 2.1127 1.6242 -0.0417 -0.1690 -0.0836 218  GLU A OE1   
916  O  OE2   . GLU A 115 ? 1.2195 1.6769 1.1581 -0.0191 -0.1818 -0.0785 218  GLU A OE2   
917  N  N     . GLN A 116 ? 1.2497 1.5279 1.1002 -0.0506 -0.1471 -0.0896 219  GLN A N     
918  C  CA    . GLN A 116 ? 1.1580 1.4146 0.9794 -0.0581 -0.1507 -0.0959 219  GLN A CA    
919  C  C     . GLN A 116 ? 1.2038 1.4243 1.0037 -0.0452 -0.1418 -0.0916 219  GLN A C     
920  O  O     . GLN A 116 ? 1.2683 1.4758 1.0434 -0.0432 -0.1455 -0.0941 219  GLN A O     
921  C  CB    . GLN A 116 ? 1.1963 1.4408 1.0123 -0.0797 -0.1499 -0.1041 219  GLN A CB    
922  C  CG    . GLN A 116 ? 1.1700 1.4504 1.0033 -0.0956 -0.1599 -0.1095 219  GLN A CG    
923  C  CD    . GLN A 116 ? 1.2294 1.4953 1.0589 -0.1174 -0.1572 -0.1164 219  GLN A CD    
924  O  OE1   . GLN A 116 ? 1.2157 1.4519 1.0405 -0.1183 -0.1459 -0.1148 219  GLN A OE1   
925  N  NE2   . GLN A 116 ? 1.1547 1.4417 0.9862 -0.1353 -0.1675 -0.1240 219  GLN A NE2   
926  N  N     . VAL A 117 ? 1.2393 1.4445 1.0483 -0.0366 -0.1301 -0.0851 220  VAL A N     
927  C  CA    . VAL A 117 ? 1.2205 1.3964 1.0134 -0.0233 -0.1212 -0.0796 220  VAL A CA    
928  C  C     . VAL A 117 ? 1.2071 1.3939 0.9962 -0.0075 -0.1253 -0.0739 220  VAL A C     
929  O  O     . VAL A 117 ? 1.3461 1.5134 1.1124 0.0000  -0.1232 -0.0724 220  VAL A O     
930  C  CB    . VAL A 117 ? 1.1919 1.3548 0.9993 -0.0180 -0.1090 -0.0736 220  VAL A CB    
931  C  CG1   . VAL A 117 ? 1.1515 1.2894 0.9462 -0.0039 -0.0998 -0.0670 220  VAL A CG1   
932  C  CG2   . VAL A 117 ? 1.2050 1.3531 1.0116 -0.0323 -0.1043 -0.0785 220  VAL A CG2   
933  N  N     . ILE A 118 ? 1.1659 1.3833 0.9764 -0.0016 -0.1308 -0.0704 221  ILE A N     
934  C  CA    . ILE A 118 ? 1.1387 1.3675 0.9454 0.0138  -0.1354 -0.0646 221  ILE A CA    
935  C  C     . ILE A 118 ? 1.2475 1.4840 1.0335 0.0099  -0.1470 -0.0700 221  ILE A C     
936  O  O     . ILE A 118 ? 1.3097 1.5396 1.0781 0.0218  -0.1486 -0.0660 221  ILE A O     
937  C  CB    . ILE A 118 ? 1.1530 1.4125 0.9871 0.0213  -0.1385 -0.0600 221  ILE A CB    
938  C  CG1   . ILE A 118 ? 1.1945 1.4447 1.0469 0.0237  -0.1274 -0.0559 221  ILE A CG1   
939  C  CG2   . ILE A 118 ? 1.0993 1.3674 0.9284 0.0389  -0.1422 -0.0529 221  ILE A CG2   
940  C  CD1   . ILE A 118 ? 1.0871 1.3644 0.9651 0.0306  -0.1293 -0.0524 221  ILE A CD1   
941  N  N     . ALA A 119 ? 1.2327 1.4830 1.0196 -0.0072 -0.1554 -0.0792 222  ALA A N     
942  C  CA    . ALA A 119 ? 1.2127 1.4702 0.9790 -0.0133 -0.1675 -0.0857 222  ALA A CA    
943  C  C     . ALA A 119 ? 1.2724 1.4920 1.0048 -0.0126 -0.1626 -0.0881 222  ALA A C     
944  O  O     . ALA A 119 ? 1.2643 1.4825 0.9749 -0.0060 -0.1689 -0.0883 222  ALA A O     
945  C  CB    . ALA A 119 ? 1.1830 1.4609 0.9583 -0.0344 -0.1764 -0.0955 222  ALA A CB    
946  N  N     . GLU A 120 ? 1.2963 1.4850 1.0229 -0.0184 -0.1512 -0.0898 223  GLU A N     
947  C  CA    . GLU A 120 ? 1.3134 1.4650 1.0082 -0.0159 -0.1447 -0.0915 223  GLU A CA    
948  C  C     . GLU A 120 ? 1.3342 1.4734 1.0221 0.0045  -0.1365 -0.0811 223  GLU A C     
949  O  O     . GLU A 120 ? 1.4089 1.5261 1.0682 0.0104  -0.1342 -0.0813 223  GLU A O     
950  C  CB    . GLU A 120 ? 1.2745 1.3977 0.9667 -0.0261 -0.1342 -0.0952 223  GLU A CB    
951  C  CG    . GLU A 120 ? 1.4136 1.4977 1.0719 -0.0248 -0.1271 -0.0983 223  GLU A CG    
952  C  CD    . GLU A 120 ? 1.7020 1.7818 1.3324 -0.0356 -0.1380 -0.1091 223  GLU A CD    
953  O  OE1   . GLU A 120 ? 1.6668 1.7704 1.3062 -0.0502 -0.1500 -0.1160 223  GLU A OE1   
954  O  OE2   . GLU A 120 ? 1.6737 1.7269 1.2731 -0.0299 -0.1346 -0.1107 223  GLU A OE2   
955  N  N     . ALA A 121 ? 1.2871 1.4391 0.9997 0.0152  -0.1318 -0.0720 224  ALA A N     
956  C  CA    . ALA A 121 ? 1.3484 1.4897 1.0561 0.0336  -0.1242 -0.0616 224  ALA A CA    
957  C  C     . ALA A 121 ? 1.3184 1.4730 1.0115 0.0433  -0.1337 -0.0592 224  ALA A C     
958  O  O     . ALA A 121 ? 1.2568 1.3933 0.9289 0.0550  -0.1287 -0.0539 224  ALA A O     
959  C  CB    . ALA A 121 ? 1.2055 1.3568 0.9430 0.0409  -0.1177 -0.0534 224  ALA A CB    
960  N  N     . ILE A 122 ? 1.2929 1.4801 0.9968 0.0393  -0.1474 -0.0625 225  ILE A N     
961  C  CA    . ILE A 122 ? 1.3103 1.5133 1.0006 0.0490  -0.1579 -0.0602 225  ILE A CA    
962  C  C     . ILE A 122 ? 1.3251 1.5115 0.9799 0.0437  -0.1628 -0.0674 225  ILE A C     
963  O  O     . ILE A 122 ? 1.4009 1.5812 1.0332 0.0558  -0.1646 -0.0631 225  ILE A O     
964  C  CB    . ILE A 122 ? 1.3324 1.5776 1.0451 0.0458  -0.1715 -0.0622 225  ILE A CB    
965  C  CG1   . ILE A 122 ? 1.2766 1.5354 1.0212 0.0538  -0.1657 -0.0546 225  ILE A CG1   
966  C  CG2   . ILE A 122 ? 1.3443 1.6080 1.0420 0.0556  -0.1839 -0.0601 225  ILE A CG2   
967  C  CD1   . ILE A 122 ? 1.3611 1.6621 1.1292 0.0529  -0.1773 -0.0556 225  ILE A CD1   
968  N  N     . ARG A 123 ? 1.3417 1.5187 0.9893 0.0258  -0.1646 -0.0784 226  ARG A N     
969  C  CA    . ARG A 123 ? 1.3344 1.4904 0.9459 0.0198  -0.1681 -0.0865 226  ARG A CA    
970  C  C     . ARG A 123 ? 1.3676 1.4871 0.9550 0.0328  -0.1542 -0.0806 226  ARG A C     
971  O  O     . ARG A 123 ? 1.4424 1.5507 0.9989 0.0392  -0.1570 -0.0813 226  ARG A O     
972  C  CB    . ARG A 123 ? 1.3816 1.5284 0.9909 -0.0020 -0.1699 -0.0988 226  ARG A CB    
973  C  CG    . ARG A 123 ? 1.3616 1.5017 0.9395 -0.0139 -0.1810 -0.1107 226  ARG A CG    
974  C  CD    . ARG A 123 ? 1.5307 1.6299 1.0701 -0.0070 -0.1723 -0.1119 226  ARG A CD    
975  N  NE    . ARG A 123 ? 1.4991 1.5663 1.0404 -0.0051 -0.1547 -0.1089 226  ARG A NE    
976  C  CZ    . ARG A 123 ? 1.5724 1.6166 1.1067 -0.0193 -0.1501 -0.1173 226  ARG A CZ    
977  N  NH1   . ARG A 123 ? 1.5527 1.5999 1.0774 -0.0382 -0.1612 -0.1298 226  ARG A NH1   
978  N  NH2   . ARG A 123 ? 1.5198 1.5374 1.0568 -0.0145 -0.1340 -0.1129 226  ARG A NH2   
979  N  N     . LYS A 124 ? 1.3761 1.4781 0.9771 0.0369  -0.1391 -0.0746 227  LYS A N     
980  C  CA    . LYS A 124 ? 1.3526 1.4221 0.9339 0.0485  -0.1247 -0.0686 227  LYS A CA    
981  C  C     . LYS A 124 ? 1.4410 1.5154 1.0185 0.0673  -0.1226 -0.0568 227  LYS A C     
982  O  O     . LYS A 124 ? 1.6584 1.7118 1.2082 0.0768  -0.1167 -0.0536 227  LYS A O     
983  C  CB    . LYS A 124 ? 1.2347 1.2883 0.8346 0.0471  -0.1102 -0.0652 227  LYS A CB    
984  C  CG    . LYS A 124 ? 1.2468 1.2659 0.8259 0.0550  -0.0950 -0.0618 227  LYS A CG    
985  C  CD    . LYS A 124 ? 1.4049 1.3999 0.9533 0.0453  -0.0956 -0.0730 227  LYS A CD    
986  C  CE    . LYS A 124 ? 1.3812 1.3425 0.9088 0.0548  -0.0796 -0.0693 227  LYS A CE    
987  N  NZ    . LYS A 124 ? 1.4307 1.3652 0.9255 0.0465  -0.0795 -0.0807 227  LYS A NZ    
988  N  N     . LYS A 125 ? 1.3442 1.4448 0.9481 0.0734  -0.1268 -0.0500 228  LYS A N     
989  C  CA    . LYS A 125 ? 1.3669 1.4696 0.9686 0.0915  -0.1236 -0.0378 228  LYS A CA    
990  C  C     . LYS A 125 ? 1.4358 1.5503 1.0137 0.0979  -0.1363 -0.0383 228  LYS A C     
991  O  O     . LYS A 125 ? 1.5838 1.6861 1.1417 0.1121  -0.1316 -0.0300 228  LYS A O     
992  C  CB    . LYS A 125 ? 1.3933 1.5164 1.0299 0.0965  -0.1229 -0.0305 228  LYS A CB    
993  C  CG    . LYS A 125 ? 1.4386 1.5463 1.0948 0.0965  -0.1080 -0.0257 228  LYS A CG    
994  C  CD    . LYS A 125 ? 1.4462 1.5277 1.0873 0.1088  -0.0941 -0.0160 228  LYS A CD    
995  C  CE    . LYS A 125 ? 1.6515 1.7399 1.2906 0.1247  -0.0951 -0.0050 228  LYS A CE    
996  N  NZ    . LYS A 125 ? 1.3911 1.4973 1.0616 0.1277  -0.0962 -0.0003 228  LYS A NZ    
997  N  N     . THR A 126 ? 1.4112 1.5506 0.9909 0.0875  -0.1523 -0.0474 229  THR A N     
998  C  CA    . THR A 126 ? 1.4902 1.6456 1.0491 0.0931  -0.1664 -0.0482 229  THR A CA    
999  C  C     . THR A 126 ? 1.4920 1.6254 1.0109 0.0885  -0.1687 -0.0563 229  THR A C     
1000 O  O     . THR A 126 ? 1.4763 1.6256 0.9800 0.0826  -0.1842 -0.0640 229  THR A O     
1001 C  CB    . THR A 126 ? 1.3897 1.5852 0.9698 0.0842  -0.1832 -0.0542 229  THR A CB    
1002 O  OG1   . THR A 126 ? 1.3556 1.5511 0.9399 0.0629  -0.1870 -0.0673 229  THR A OG1   
1003 C  CG2   . THR A 126 ? 1.3852 1.6020 1.0019 0.0917  -0.1807 -0.0457 229  THR A CG2   
1004 N  N     . ARG A 127 ? 1.4469 1.5445 0.9479 0.0912  -0.1536 -0.0548 230  ARG A N     
1005 C  CA    . ARG A 127 ? 1.5472 1.6209 1.0069 0.0894  -0.1542 -0.0618 230  ARG A CA    
1006 C  C     . ARG A 127 ? 1.5516 1.6221 0.9843 0.1072  -0.1551 -0.0531 230  ARG A C     
1007 O  O     . ARG A 127 ? 1.5243 1.5938 0.9252 0.1061  -0.1654 -0.0597 230  ARG A O     
1008 C  CB    . ARG A 127 ? 1.5526 1.5897 1.0030 0.0864  -0.1370 -0.0637 230  ARG A CB    
1009 C  CG    . ARG A 127 ? 1.4563 1.4674 0.8654 0.0806  -0.1380 -0.0744 230  ARG A CG    
1010 C  CD    . ARG A 127 ? 1.5343 1.5087 0.9333 0.0820  -0.1192 -0.0741 230  ARG A CD    
1011 N  NE    . ARG A 127 ? 1.5045 1.4525 0.8642 0.0753  -0.1203 -0.0861 230  ARG A NE    
1012 C  CZ    . ARG A 127 ? 1.5030 1.4161 0.8418 0.0794  -0.1049 -0.0866 230  ARG A CZ    
1013 N  NH1   . ARG A 127 ? 1.5113 1.4136 0.8661 0.0895  -0.0873 -0.0757 230  ARG A NH1   
1014 N  NH2   . ARG A 127 ? 1.5492 1.4381 0.8502 0.0732  -0.1072 -0.0986 230  ARG A NH2   
1015 N  N     . SER A 128 ? 1.5432 1.6114 0.9871 0.1232  -0.1445 -0.0385 231  SER A N     
1016 C  CA    . SER A 128 ? 1.4204 1.4861 0.8413 0.1412  -0.1443 -0.0280 231  SER A CA    
1017 C  C     . SER A 128 ? 1.6062 1.7070 1.0359 0.1473  -0.1611 -0.0249 231  SER A C     
1018 O  O     . SER A 128 ? 1.7281 1.8295 1.1437 0.1640  -0.1610 -0.0140 231  SER A O     
1019 C  CB    . SER A 128 ? 1.4206 1.4677 0.8502 0.1549  -0.1251 -0.0132 231  SER A CB    
1020 O  OG    . SER A 128 ? 1.6320 1.6942 1.1021 0.1541  -0.1223 -0.0080 231  SER A OG    
1021 N  N     . MET A 129 ? 1.7792 1.9093 1.2320 0.1346  -0.1750 -0.0335 232  MET A N     
1022 C  CA    . MET A 129 ? 1.6513 1.8186 1.1138 0.1400  -0.1919 -0.0313 232  MET A CA    
1023 C  C     . MET A 129 ? 1.6969 1.8781 1.1323 0.1332  -0.2102 -0.0419 232  MET A C     
1024 O  O     . MET A 129 ? 1.7113 1.9205 1.1448 0.1420  -0.2241 -0.0383 232  MET A O     
1025 C  CB    . MET A 129 ? 1.7595 1.9556 1.2653 0.1311  -0.1965 -0.0337 232  MET A CB    
1026 C  CG    . MET A 129 ? 1.7593 1.9447 1.2935 0.1368  -0.1803 -0.0243 232  MET A CG    
1027 S  SD    . MET A 129 ? 2.1806 2.3721 1.7222 0.1615  -0.1762 -0.0062 232  MET A SD    
1028 C  CE    . MET A 129 ? 1.6515 1.8930 1.2156 0.1622  -0.1964 -0.0085 232  MET A CE    
1029 N  N     . LEU A 130 ? 1.6756 1.8375 1.0896 0.1181  -0.2105 -0.0548 233  LEU A N     
1030 C  CA    . LEU A 130 ? 1.6667 1.8370 1.0516 0.1091  -0.2276 -0.0668 233  LEU A CA    
1031 C  C     . LEU A 130 ? 1.6697 1.8865 1.0790 0.0992  -0.2478 -0.0728 233  LEU A C     
1032 O  O     . LEU A 130 ? 1.6491 1.8920 1.0478 0.1058  -0.2636 -0.0717 233  LEU A O     
1033 C  CB    . LEU A 130 ? 1.6558 1.8153 1.0008 0.1265  -0.2294 -0.0602 233  LEU A CB    
1034 C  CG    . LEU A 130 ? 1.6566 1.7724 0.9602 0.1279  -0.2174 -0.0635 233  LEU A CG    
1035 C  CD1   . LEU A 130 ? 1.6870 1.7955 0.9676 0.1078  -0.2279 -0.0823 233  LEU A CD1   
1036 C  CD2   . LEU A 130 ? 1.5579 1.6425 0.8738 0.1307  -0.1938 -0.0571 233  LEU A CD2   
1037 N  N     . LEU A 131 ? 1.6991 1.9270 1.1416 0.0835  -0.2469 -0.0787 234  LEU A N     
1038 C  CA    . LEU A 131 ? 1.6323 1.9047 1.1028 0.0720  -0.2636 -0.0845 234  LEU A CA    
1039 C  C     . LEU A 131 ? 1.6049 1.8777 1.0638 0.0468  -0.2744 -0.1022 234  LEU A C     
1040 O  O     . LEU A 131 ? 1.6329 1.8699 1.0757 0.0356  -0.2648 -0.1100 234  LEU A O     
1041 C  CB    . LEU A 131 ? 1.6290 1.9157 1.1447 0.0707  -0.2555 -0.0792 234  LEU A CB    
1042 C  CG    . LEU A 131 ? 1.6082 1.9236 1.1487 0.0898  -0.2571 -0.0656 234  LEU A CG    
1043 C  CD1   . LEU A 131 ? 1.6288 1.9211 1.1479 0.1133  -0.2474 -0.0520 234  LEU A CD1   
1044 C  CD2   . LEU A 131 ? 1.6569 1.9807 1.2385 0.0864  -0.2478 -0.0625 234  LEU A CD2   
1045 N  N     . SER A 132 ? 1.6092 1.9231 1.0766 0.0380  -0.2945 -0.1085 235  SER A N     
1046 C  CA    . SER A 132 ? 1.6587 1.9774 1.1176 0.0122  -0.3067 -0.1255 235  SER A CA    
1047 C  C     . SER A 132 ? 1.7221 2.0483 1.2170 -0.0066 -0.3019 -0.1307 235  SER A C     
1048 O  O     . SER A 132 ? 1.7076 2.0360 1.2327 0.0009  -0.2898 -0.1214 235  SER A O     
1049 C  CB    . SER A 132 ? 1.6476 2.0102 1.1028 0.0093  -0.3307 -0.1300 235  SER A CB    
1050 O  OG    . SER A 132 ? 1.5906 2.0014 1.0866 0.0151  -0.3377 -0.1224 235  SER A OG    
1051 N  N     . SER A 133 ? 1.7820 2.1112 1.2723 -0.0320 -0.3115 -0.1458 236  SER A N     
1052 C  CA    . SER A 133 ? 1.8117 2.1466 1.3332 -0.0515 -0.3071 -0.1511 236  SER A CA    
1053 C  C     . SER A 133 ? 1.8163 2.2041 1.3831 -0.0495 -0.3142 -0.1447 236  SER A C     
1054 O  O     . SER A 133 ? 1.7398 2.1299 1.3376 -0.0508 -0.3031 -0.1400 236  SER A O     
1055 C  CB    . SER A 133 ? 1.8415 2.1676 1.3459 -0.0799 -0.3166 -0.1687 236  SER A CB    
1056 O  OG    . SER A 133 ? 1.9987 2.3623 1.4973 -0.0873 -0.3387 -0.1753 236  SER A OG    
1057 N  N     . GLU A 134 ? 2.0019 2.4329 1.5723 -0.0457 -0.3324 -0.1442 237  GLU A N     
1058 C  CA    . GLU A 134 ? 1.9289 2.4118 1.5415 -0.0406 -0.3388 -0.1371 237  GLU A CA    
1059 C  C     . GLU A 134 ? 1.9633 2.4439 1.5899 -0.0125 -0.3264 -0.1205 237  GLU A C     
1060 O  O     . GLU A 134 ? 2.0261 2.5308 1.6896 -0.0088 -0.3220 -0.1143 237  GLU A O     
1061 C  CB    . GLU A 134 ? 1.8707 2.4021 1.4831 -0.0427 -0.3621 -0.1407 237  GLU A CB    
1062 C  CG    . GLU A 134 ? 2.0564 2.6015 1.6650 -0.0736 -0.3765 -0.1574 237  GLU A CG    
1063 C  CD    . GLU A 134 ? 2.2573 2.7615 1.8172 -0.0829 -0.3796 -0.1685 237  GLU A CD    
1064 O  OE1   . GLU A 134 ? 2.2054 2.6784 1.7342 -0.0634 -0.3732 -0.1626 237  GLU A OE1   
1065 O  OE2   . GLU A 134 ? 2.3124 2.8148 1.8644 -0.1100 -0.3881 -0.1833 237  GLU A OE2   
1066 N  N     . GLN A 135 ? 1.6947 2.1459 1.2915 0.0070  -0.3203 -0.1132 238  GLN A N     
1067 C  CA    . GLN A 135 ? 1.6368 2.0817 1.2445 0.0326  -0.3079 -0.0974 238  GLN A CA    
1068 C  C     . GLN A 135 ? 1.6619 2.0776 1.2869 0.0306  -0.2879 -0.0943 238  GLN A C     
1069 O  O     . GLN A 135 ? 1.5969 2.0213 1.2474 0.0444  -0.2797 -0.0838 238  GLN A O     
1070 C  CB    . GLN A 135 ? 1.6009 2.0191 1.1708 0.0521  -0.3054 -0.0904 238  GLN A CB    
1071 C  CG    . GLN A 135 ? 1.5767 2.0285 1.1346 0.0637  -0.3237 -0.0875 238  GLN A CG    
1072 C  CD    . GLN A 135 ? 1.5006 1.9240 1.0211 0.0847  -0.3190 -0.0788 238  GLN A CD    
1073 O  OE1   . GLN A 135 ? 1.5096 1.8892 1.0008 0.0824  -0.3083 -0.0816 238  GLN A OE1   
1074 N  NE2   . GLN A 135 ? 1.4975 1.9454 1.0185 0.1060  -0.3264 -0.0675 238  GLN A NE2   
1075 N  N     . LEU A 136 ? 1.6455 2.0260 1.2561 0.0141  -0.2798 -0.1034 239  LEU A N     
1076 C  CA    . LEU A 136 ? 1.5651 1.9192 1.1917 0.0118  -0.2616 -0.1007 239  LEU A CA    
1077 C  C     . LEU A 136 ? 1.5672 1.9530 1.2354 0.0017  -0.2627 -0.1016 239  LEU A C     
1078 O  O     . LEU A 136 ? 1.5611 1.9397 1.2509 0.0084  -0.2497 -0.0945 239  LEU A O     
1079 C  CB    . LEU A 136 ? 1.5134 1.8245 1.1146 -0.0033 -0.2538 -0.1104 239  LEU A CB    
1080 C  CG    . LEU A 136 ? 1.4452 1.7232 1.0560 -0.0027 -0.2340 -0.1066 239  LEU A CG    
1081 C  CD1   . LEU A 136 ? 1.3848 1.6473 0.9944 0.0213  -0.2216 -0.0925 239  LEU A CD1   
1082 C  CD2   . LEU A 136 ? 1.3162 1.5531 0.8997 -0.0166 -0.2274 -0.1165 239  LEU A CD2   
1083 N  N     . LYS A 137 ? 1.5620 1.9838 1.2416 -0.0146 -0.2780 -0.1101 240  LYS A N     
1084 C  CA    . LYS A 137 ? 1.5269 1.9820 1.2462 -0.0240 -0.2788 -0.1106 240  LYS A CA    
1085 C  C     . LYS A 137 ? 1.5273 2.0143 1.2731 -0.0028 -0.2790 -0.0984 240  LYS A C     
1086 O  O     . LYS A 137 ? 1.5075 2.0069 1.2841 -0.0028 -0.2717 -0.0948 240  LYS A O     
1087 C  CB    . LYS A 137 ? 1.4681 1.9562 1.1934 -0.0471 -0.2953 -0.1224 240  LYS A CB    
1088 C  CG    . LYS A 137 ? 1.4742 1.9301 1.1764 -0.0712 -0.2947 -0.1356 240  LYS A CG    
1089 C  CD    . LYS A 137 ? 1.5255 2.0162 1.2375 -0.0960 -0.3108 -0.1470 240  LYS A CD    
1090 C  CE    . LYS A 137 ? 1.6049 2.1326 1.3087 -0.0903 -0.3305 -0.1479 240  LYS A CE    
1091 N  NZ    . LYS A 137 ? 1.3986 1.9636 1.1138 -0.1157 -0.3471 -0.1593 240  LYS A NZ    
1092 N  N     . LEU A 138 ? 1.5232 2.0225 1.2563 0.0161  -0.2868 -0.0917 241  LEU A N     
1093 C  CA    . LEU A 138 ? 1.5445 2.0726 1.3004 0.0376  -0.2872 -0.0799 241  LEU A CA    
1094 C  C     . LEU A 138 ? 1.5048 2.0018 1.2670 0.0528  -0.2684 -0.0698 241  LEU A C     
1095 O  O     . LEU A 138 ? 1.4752 1.9884 1.2673 0.0581  -0.2629 -0.0649 241  LEU A O     
1096 C  CB    . LEU A 138 ? 1.5764 2.1210 1.3133 0.0548  -0.2998 -0.0746 241  LEU A CB    
1097 C  CG    . LEU A 138 ? 1.5377 2.1090 1.2933 0.0801  -0.3005 -0.0614 241  LEU A CG    
1098 C  CD1   . LEU A 138 ? 1.4536 2.0782 1.2470 0.0746  -0.3095 -0.0632 241  LEU A CD1   
1099 C  CD2   . LEU A 138 ? 1.6881 2.2637 1.4173 0.0990  -0.3102 -0.0548 241  LEU A CD2   
1100 N  N     . CYS A 139 ? 1.5526 2.0053 1.2867 0.0597  -0.2584 -0.0668 242  CYS A N     
1101 C  CA    . CYS A 139 ? 1.5390 1.9627 1.2784 0.0737  -0.2411 -0.0571 242  CYS A CA    
1102 C  C     . CYS A 139 ? 1.5067 1.9191 1.2676 0.0602  -0.2297 -0.0609 242  CYS A C     
1103 O  O     . CYS A 139 ? 1.4597 1.8664 1.2389 0.0700  -0.2189 -0.0536 242  CYS A O     
1104 C  CB    . CYS A 139 ? 1.4881 1.8690 1.1929 0.0823  -0.2327 -0.0533 242  CYS A CB    
1105 S  SG    . CYS A 139 ? 1.8114 2.1557 1.4903 0.0612  -0.2283 -0.0655 242  CYS A SG    
1106 N  N     . VAL A 140 ? 1.5105 1.9183 1.2685 0.0377  -0.2320 -0.0722 243  VAL A N     
1107 C  CA    . VAL A 140 ? 1.5233 1.9221 1.3011 0.0245  -0.2220 -0.0757 243  VAL A CA    
1108 C  C     . VAL A 140 ? 1.4265 1.8656 1.2406 0.0242  -0.2254 -0.0740 243  VAL A C     
1109 O  O     . VAL A 140 ? 1.4161 1.8524 1.2491 0.0336  -0.2153 -0.0674 243  VAL A O     
1110 C  CB    . VAL A 140 ? 1.4780 1.8613 1.2419 0.0007  -0.2239 -0.0880 243  VAL A CB    
1111 C  CG1   . VAL A 140 ? 1.3345 1.7161 1.1214 -0.0136 -0.2158 -0.0913 243  VAL A CG1   
1112 C  CG2   . VAL A 140 ? 1.4191 1.7567 1.1485 0.0031  -0.2162 -0.0888 243  VAL A CG2   
1113 N  N     . LEU A 141 ? 1.4189 1.8970 1.2429 0.0138  -0.2398 -0.0799 244  LEU A N     
1114 C  CA    . LEU A 141 ? 1.3517 1.8717 1.2107 0.0129  -0.2431 -0.0787 244  LEU A CA    
1115 C  C     . LEU A 141 ? 1.3979 1.9323 1.2704 0.0384  -0.2405 -0.0671 244  LEU A C     
1116 O  O     . LEU A 141 ? 1.5770 2.1375 1.4783 0.0414  -0.2385 -0.0645 244  LEU A O     
1117 C  CB    . LEU A 141 ? 1.3543 1.9166 1.2201 -0.0013 -0.2601 -0.0863 244  LEU A CB    
1118 C  CG    . LEU A 141 ? 1.3577 1.9071 1.2106 -0.0288 -0.2636 -0.0987 244  LEU A CG    
1119 C  CD1   . LEU A 141 ? 1.3125 1.9074 1.1745 -0.0433 -0.2813 -0.1060 244  LEU A CD1   
1120 C  CD2   . LEU A 141 ? 1.3555 1.8868 1.2225 -0.0428 -0.2507 -0.1014 244  LEU A CD2   
1121 N  N     . GLU A 142 ? 1.3955 1.9123 1.2469 0.0570  -0.2400 -0.0599 245  GLU A N     
1122 C  CA    . GLU A 142 ? 1.4302 1.9522 1.2911 0.0815  -0.2356 -0.0483 245  GLU A CA    
1123 C  C     . GLU A 142 ? 1.4517 1.9370 1.3157 0.0876  -0.2181 -0.0431 245  GLU A C     
1124 O  O     . GLU A 142 ? 1.4612 1.9538 1.3432 0.1015  -0.2125 -0.0363 245  GLU A O     
1125 C  CB    . GLU A 142 ? 1.4705 1.9895 1.3068 0.0989  -0.2426 -0.0419 245  GLU A CB    
1126 C  CG    . GLU A 142 ? 1.5180 2.0351 1.3587 0.1253  -0.2371 -0.0291 245  GLU A CG    
1127 C  CD    . GLU A 142 ? 1.6036 2.0734 1.4196 0.1362  -0.2253 -0.0221 245  GLU A CD    
1128 O  OE1   . GLU A 142 ? 1.5434 1.9837 1.3394 0.1242  -0.2211 -0.0271 245  GLU A OE1   
1129 O  OE2   . GLU A 142 ? 1.6367 2.0985 1.4529 0.1567  -0.2197 -0.0114 245  GLU A OE2   
1130 N  N     . TYR A 143 ? 1.4304 1.8770 1.2774 0.0776  -0.2094 -0.0465 246  TYR A N     
1131 C  CA    . TYR A 143 ? 1.4431 1.8558 1.2926 0.0824  -0.1935 -0.0417 246  TYR A CA    
1132 C  C     . TYR A 143 ? 1.4416 1.8438 1.3028 0.0640  -0.1862 -0.0486 246  TYR A C     
1133 O  O     . TYR A 143 ? 1.4406 1.8270 1.3133 0.0676  -0.1747 -0.0450 246  TYR A O     
1134 C  CB    . TYR A 143 ? 1.5729 1.9466 1.3932 0.0903  -0.1868 -0.0372 246  TYR A CB    
1135 C  CG    . TYR A 143 ? 1.5910 1.9632 1.4031 0.1131  -0.1867 -0.0262 246  TYR A CG    
1136 C  CD1   . TYR A 143 ? 1.5563 1.9465 1.3890 0.1272  -0.1860 -0.0195 246  TYR A CD1   
1137 C  CD2   . TYR A 143 ? 1.7036 2.0546 1.4860 0.1212  -0.1868 -0.0223 246  TYR A CD2   
1138 C  CE1   . TYR A 143 ? 1.6765 2.0623 1.5003 0.1485  -0.1854 -0.0090 246  TYR A CE1   
1139 C  CE2   . TYR A 143 ? 1.7299 2.0778 1.5036 0.1421  -0.1861 -0.0114 246  TYR A CE2   
1140 C  CZ    . TYR A 143 ? 1.7882 2.1529 1.5826 0.1556  -0.1854 -0.0047 246  TYR A CZ    
1141 O  OH    . TYR A 143 ? 1.9264 2.2851 1.7107 0.1768  -0.1843 0.0066  246  TYR A OH    
1142 N  N     . GLN A 144 ? 1.3930 1.8025 1.2508 0.0443  -0.1925 -0.0583 247  GLN A N     
1143 C  CA    . GLN A 144 ? 1.2972 1.6983 1.1660 0.0267  -0.1860 -0.0644 247  GLN A CA    
1144 C  C     . GLN A 144 ? 1.3589 1.7907 1.2596 0.0270  -0.1855 -0.0632 247  GLN A C     
1145 O  O     . GLN A 144 ? 1.4280 1.8974 1.3428 0.0211  -0.1955 -0.0665 247  GLN A O     
1146 C  CB    . GLN A 144 ? 1.2549 1.6571 1.1114 0.0055  -0.1936 -0.0750 247  GLN A CB    
1147 C  CG    . GLN A 144 ? 1.1674 1.5483 1.0259 -0.0119 -0.1852 -0.0807 247  GLN A CG    
1148 C  CD    . GLN A 144 ? 1.2303 1.6190 1.0820 -0.0344 -0.1938 -0.0913 247  GLN A CD    
1149 O  OE1   . GLN A 144 ? 1.3135 1.7319 1.1657 -0.0385 -0.2071 -0.0949 247  GLN A OE1   
1150 N  NE2   . GLN A 144 ? 1.2371 1.5992 1.0824 -0.0492 -0.1864 -0.0964 247  GLN A NE2   
1151 N  N     . GLY A 145 ? 1.2612 1.6779 1.1733 0.0339  -0.1737 -0.0584 248  GLY A N     
1152 C  CA    . GLY A 145 ? 1.2293 1.6714 1.1690 0.0379  -0.1717 -0.0564 248  GLY A CA    
1153 C  C     . GLY A 145 ? 1.2183 1.6592 1.1639 0.0603  -0.1674 -0.0474 248  GLY A C     
1154 O  O     . GLY A 145 ? 1.1953 1.6563 1.1623 0.0660  -0.1655 -0.0456 248  GLY A O     
1155 N  N     . LYS A 146 ? 1.2090 1.6263 1.1357 0.0733  -0.1654 -0.0416 249  LYS A N     
1156 C  CA    . LYS A 146 ? 1.1802 1.5895 1.1099 0.0937  -0.1599 -0.0327 249  LYS A CA    
1157 C  C     . LYS A 146 ? 1.1457 1.5136 1.0655 0.0963  -0.1473 -0.0290 249  LYS A C     
1158 O  O     . LYS A 146 ? 1.1202 1.4749 1.0390 0.1117  -0.1418 -0.0215 249  LYS A O     
1159 C  CB    . LYS A 146 ? 1.2515 1.6713 1.1687 0.1093  -0.1681 -0.0271 249  LYS A CB    
1160 C  CG    . LYS A 146 ? 1.2460 1.7114 1.1757 0.1097  -0.1811 -0.0295 249  LYS A CG    
1161 C  CD    . LYS A 146 ? 1.3511 1.8273 1.2700 0.1289  -0.1886 -0.0223 249  LYS A CD    
1162 C  CE    . LYS A 146 ? 1.3896 1.9153 1.3244 0.1310  -0.2015 -0.0239 249  LYS A CE    
1163 N  NZ    . LYS A 146 ? 1.5746 2.1122 1.4978 0.1507  -0.2097 -0.0164 249  LYS A NZ    
1164 N  N     . TYR A 147 ? 1.1578 1.5051 1.0705 0.0815  -0.1426 -0.0338 250  TYR A N     
1165 C  CA    . TYR A 147 ? 1.1720 1.4836 1.0775 0.0825  -0.1308 -0.0306 250  TYR A CA    
1166 C  C     . TYR A 147 ? 1.1177 1.4232 1.0340 0.0676  -0.1252 -0.0361 250  TYR A C     
1167 O  O     . TYR A 147 ? 1.0742 1.3980 0.9979 0.0546  -0.1301 -0.0427 250  TYR A O     
1168 C  CB    . TYR A 147 ? 1.1667 1.4535 1.0459 0.0830  -0.1296 -0.0292 250  TYR A CB    
1169 C  CG    . TYR A 147 ? 1.1743 1.4590 1.0404 0.0999  -0.1321 -0.0215 250  TYR A CG    
1170 C  CD1   . TYR A 147 ? 1.2446 1.5521 1.1030 0.1036  -0.1440 -0.0224 250  TYR A CD1   
1171 C  CD2   . TYR A 147 ? 1.1793 1.4395 1.0404 0.1118  -0.1226 -0.0131 250  TYR A CD2   
1172 C  CE1   . TYR A 147 ? 1.3026 1.6077 1.1475 0.1201  -0.1462 -0.0147 250  TYR A CE1   
1173 C  CE2   . TYR A 147 ? 1.2722 1.5284 1.1200 0.1274  -0.1240 -0.0053 250  TYR A CE2   
1174 C  CZ    . TYR A 147 ? 1.3137 1.5920 1.1527 0.1321  -0.1358 -0.0059 250  TYR A CZ    
1175 O  OH    . TYR A 147 ? 1.3416 1.6155 1.1659 0.1486  -0.1373 0.0027  250  TYR A OH    
1176 N  N     . ILE A 148 ? 1.1217 1.4015 1.0386 0.0695  -0.1147 -0.0329 251  ILE A N     
1177 C  CA    . ILE A 148 ? 1.1220 1.3941 1.0488 0.0581  -0.1085 -0.0365 251  ILE A CA    
1178 C  C     . ILE A 148 ? 1.1338 1.3733 1.0474 0.0563  -0.0999 -0.0345 251  ILE A C     
1179 O  O     . ILE A 148 ? 1.1295 1.3524 1.0350 0.0668  -0.0954 -0.0283 251  ILE A O     
1180 C  CB    . ILE A 148 ? 1.0548 1.3356 1.0021 0.0636  -0.1046 -0.0347 251  ILE A CB    
1181 C  CG1   . ILE A 148 ? 1.0417 1.3572 1.0039 0.0635  -0.1121 -0.0376 251  ILE A CG1   
1182 C  CG2   . ILE A 148 ? 1.0651 1.3325 1.0194 0.0543  -0.0972 -0.0369 251  ILE A CG2   
1183 C  CD1   . ILE A 148 ? 1.1410 1.4722 1.1071 0.0465  -0.1163 -0.0449 251  ILE A CD1   
1184 N  N     . LEU A 149 ? 1.0958 1.3262 1.0071 0.0433  -0.0973 -0.0393 252  LEU A N     
1185 C  CA    . LEU A 149 ? 1.0632 1.2650 0.9648 0.0419  -0.0884 -0.0374 252  LEU A CA    
1186 C  C     . LEU A 149 ? 1.1250 1.3198 1.0419 0.0455  -0.0806 -0.0336 252  LEU A C     
1187 O  O     . LEU A 149 ? 0.9874 1.1960 0.9206 0.0422  -0.0814 -0.0357 252  LEU A O     
1188 C  CB    . LEU A 149 ? 1.0305 1.2238 0.9232 0.0277  -0.0882 -0.0437 252  LEU A CB    
1189 C  CG    . LEU A 149 ? 1.1190 1.3143 0.9936 0.0214  -0.0955 -0.0489 252  LEU A CG    
1190 C  CD1   . LEU A 149 ? 1.1145 1.2977 0.9809 0.0066  -0.0940 -0.0553 252  LEU A CD1   
1191 C  CD2   . LEU A 149 ? 1.0719 1.2510 0.9262 0.0311  -0.0942 -0.0450 252  LEU A CD2   
1192 N  N     . LYS A 150 ? 1.1182 1.2920 1.0294 0.0520  -0.0731 -0.0280 253  LYS A N     
1193 C  CA    . LYS A 150 ? 1.0081 1.1740 0.9326 0.0546  -0.0661 -0.0244 253  LYS A CA    
1194 C  C     . LYS A 150 ? 1.0315 1.1751 0.9482 0.0527  -0.0579 -0.0220 253  LYS A C     
1195 O  O     . LYS A 150 ? 1.0704 1.2011 0.9712 0.0564  -0.0555 -0.0193 253  LYS A O     
1196 C  CB    . LYS A 150 ? 1.0003 1.1665 0.9305 0.0665  -0.0649 -0.0185 253  LYS A CB    
1197 C  CG    . LYS A 150 ? 1.0061 1.1597 0.9466 0.0687  -0.0572 -0.0145 253  LYS A CG    
1198 C  CD    . LYS A 150 ? 1.0014 1.1501 0.9434 0.0799  -0.0554 -0.0083 253  LYS A CD    
1199 C  CE    . LYS A 150 ? 1.0425 1.1714 0.9848 0.0816  -0.0466 -0.0023 253  LYS A CE    
1200 N  NZ    . LYS A 150 ? 1.0880 1.2155 1.0468 0.0794  -0.0435 -0.0026 253  LYS A NZ    
1201 N  N     . VAL A 151 ? 1.0627 1.2028 0.9902 0.0477  -0.0536 -0.0226 254  VAL A N     
1202 C  CA    . VAL A 151 ? 1.0501 1.1718 0.9732 0.0474  -0.0455 -0.0194 254  VAL A CA    
1203 C  C     . VAL A 151 ? 1.0548 1.1674 0.9793 0.0566  -0.0400 -0.0121 254  VAL A C     
1204 O  O     . VAL A 151 ? 1.0627 1.1810 0.9989 0.0609  -0.0406 -0.0097 254  VAL A O     
1205 C  CB    . VAL A 151 ? 1.1046 1.2272 1.0401 0.0412  -0.0430 -0.0211 254  VAL A CB    
1206 C  CG1   . VAL A 151 ? 1.0812 1.1871 1.0126 0.0417  -0.0350 -0.0175 254  VAL A CG1   
1207 C  CG2   . VAL A 151 ? 1.0662 1.1981 1.0008 0.0317  -0.0480 -0.0278 254  VAL A CG2   
1208 N  N     . CYS A 152 ? 1.1005 1.1978 1.0123 0.0595  -0.0340 -0.0084 255  CYS A N     
1209 C  CA    . CYS A 152 ? 1.2006 1.2886 1.1129 0.0673  -0.0274 -0.0006 255  CYS A CA    
1210 C  C     . CYS A 152 ? 1.1911 1.2765 1.1200 0.0657  -0.0214 0.0026  255  CYS A C     
1211 O  O     . CYS A 152 ? 1.1764 1.2564 1.1053 0.0624  -0.0170 0.0024  255  CYS A O     
1212 C  CB    . CYS A 152 ? 1.2638 1.3376 1.1559 0.0714  -0.0225 0.0024  255  CYS A CB    
1213 S  SG    . CYS A 152 ? 1.1837 1.2600 1.0537 0.0740  -0.0303 -0.0009 255  CYS A SG    
1214 N  N     . GLY A 153 ? 1.1527 1.2420 1.0953 0.0680  -0.0213 0.0054  256  GLY A N     
1215 C  CA    . GLY A 153 ? 1.1860 1.2739 1.1447 0.0657  -0.0166 0.0081  256  GLY A CA    
1216 C  C     . GLY A 153 ? 1.2270 1.3251 1.2012 0.0624  -0.0214 0.0042  256  GLY A C     
1217 O  O     . GLY A 153 ? 1.1894 1.2856 1.1754 0.0627  -0.0191 0.0070  256  GLY A O     
1218 N  N     . CYS A 154 ? 1.1294 1.2378 1.1034 0.0587  -0.0278 -0.0023 257  CYS A N     
1219 C  CA    . CYS A 154 ? 1.2224 1.3412 1.2094 0.0559  -0.0320 -0.0066 257  CYS A CA    
1220 C  C     . CYS A 154 ? 1.2235 1.3528 1.2076 0.0588  -0.0384 -0.0101 257  CYS A C     
1221 O  O     . CYS A 154 ? 1.1354 1.2643 1.1085 0.0631  -0.0401 -0.0088 257  CYS A O     
1222 C  CB    . CYS A 154 ? 1.0862 1.2099 1.0777 0.0486  -0.0326 -0.0105 257  CYS A CB    
1223 S  SG    . CYS A 154 ? 1.0951 1.2215 1.0730 0.0438  -0.0356 -0.0150 257  CYS A SG    
1224 N  N     . ASP A 155 ? 1.2188 1.3588 1.2130 0.0569  -0.0420 -0.0145 258  ASP A N     
1225 C  CA    . ASP A 155 ? 1.1209 1.2740 1.1155 0.0604  -0.0475 -0.0177 258  ASP A CA    
1226 C  C     . ASP A 155 ? 1.1088 1.2765 1.1028 0.0538  -0.0519 -0.0234 258  ASP A C     
1227 O  O     . ASP A 155 ? 1.1379 1.3199 1.1390 0.0536  -0.0553 -0.0272 258  ASP A O     
1228 C  CB    . ASP A 155 ? 1.0908 1.2456 1.0959 0.0641  -0.0478 -0.0188 258  ASP A CB    
1229 C  CG    . ASP A 155 ? 1.3467 1.4866 1.3512 0.0707  -0.0440 -0.0133 258  ASP A CG    
1230 O  OD1   . ASP A 155 ? 1.3462 1.4758 1.3428 0.0725  -0.0407 -0.0081 258  ASP A OD1   
1231 O  OD2   . ASP A 155 ? 1.3538 1.4911 1.3647 0.0739  -0.0438 -0.0141 258  ASP A OD2   
1232 N  N     . GLU A 156 ? 1.0441 1.2078 1.0294 0.0480  -0.0513 -0.0239 259  GLU A N     
1233 C  CA    . GLU A 156 ? 1.0272 1.2019 1.0103 0.0401  -0.0549 -0.0291 259  GLU A CA    
1234 C  C     . GLU A 156 ? 0.9476 1.1298 0.9209 0.0412  -0.0600 -0.0303 259  GLU A C     
1235 O  O     . GLU A 156 ? 1.0105 1.1824 0.9724 0.0454  -0.0590 -0.0272 259  GLU A O     
1236 C  CB    . GLU A 156 ? 1.0142 1.1777 0.9919 0.0327  -0.0512 -0.0294 259  GLU A CB    
1237 C  CG    . GLU A 156 ? 1.0390 1.2104 1.0138 0.0231  -0.0540 -0.0345 259  GLU A CG    
1238 C  CD    . GLU A 156 ? 1.2673 1.4255 1.2372 0.0171  -0.0495 -0.0342 259  GLU A CD    
1239 O  OE1   . GLU A 156 ? 1.3828 1.5303 1.3556 0.0206  -0.0448 -0.0303 259  GLU A OE1   
1240 O  OE2   . GLU A 156 ? 1.2481 1.4065 1.2114 0.0088  -0.0508 -0.0377 259  GLU A OE2   
1241 N  N     . TYR A 157 ? 0.8962 1.0977 0.8740 0.0374  -0.0654 -0.0348 260  TYR A N     
1242 C  CA    . TYR A 157 ? 0.8516 1.0657 0.8229 0.0381  -0.0717 -0.0364 260  TYR A CA    
1243 C  C     . TYR A 157 ? 0.8710 1.0950 0.8401 0.0256  -0.0751 -0.0420 260  TYR A C     
1244 O  O     . TYR A 157 ? 0.9905 1.2128 0.9641 0.0175  -0.0723 -0.0441 260  TYR A O     
1245 C  CB    . TYR A 157 ? 0.8902 1.1227 0.8711 0.0471  -0.0757 -0.0358 260  TYR A CB    
1246 C  CG    . TYR A 157 ? 1.0149 1.2355 0.9950 0.0596  -0.0727 -0.0301 260  TYR A CG    
1247 C  CD1   . TYR A 157 ? 1.0438 1.2535 1.0319 0.0622  -0.0673 -0.0282 260  TYR A CD1   
1248 C  CD2   . TYR A 157 ? 0.9926 1.2121 0.9630 0.0682  -0.0755 -0.0264 260  TYR A CD2   
1249 C  CE1   . TYR A 157 ? 1.0843 1.2814 1.0715 0.0721  -0.0643 -0.0231 260  TYR A CE1   
1250 C  CE2   . TYR A 157 ? 1.0528 1.2593 1.0215 0.0792  -0.0720 -0.0205 260  TYR A CE2   
1251 C  CZ    . TYR A 157 ? 1.1578 1.3526 1.1351 0.0806  -0.0662 -0.0190 260  TYR A CZ    
1252 O  OH    . TYR A 157 ? 1.2642 1.4445 1.2397 0.0900  -0.0624 -0.0132 260  TYR A OH    
1253 N  N     . PHE A 158 ? 0.9224 1.1567 0.8839 0.0237  -0.0815 -0.0442 261  PHE A N     
1254 C  CA    . PHE A 158 ? 0.8618 1.1064 0.8202 0.0106  -0.0858 -0.0499 261  PHE A CA    
1255 C  C     . PHE A 158 ? 0.9295 1.2050 0.8979 0.0120  -0.0936 -0.0518 261  PHE A C     
1256 O  O     . PHE A 158 ? 1.0811 1.3651 1.0417 0.0130  -0.1002 -0.0528 261  PHE A O     
1257 C  CB    . PHE A 158 ? 0.8986 1.1256 0.8363 0.0056  -0.0868 -0.0515 261  PHE A CB    
1258 C  CG    . PHE A 158 ? 0.9374 1.1355 0.8653 0.0048  -0.0786 -0.0495 261  PHE A CG    
1259 C  CD1   . PHE A 158 ? 1.0754 1.2591 1.0031 0.0157  -0.0728 -0.0437 261  PHE A CD1   
1260 C  CD2   . PHE A 158 ? 0.9679 1.1532 0.8867 -0.0068 -0.0765 -0.0533 261  PHE A CD2   
1261 C  CE1   . PHE A 158 ? 1.1274 1.2881 1.0481 0.0155  -0.0653 -0.0414 261  PHE A CE1   
1262 C  CE2   . PHE A 158 ? 1.0293 1.1890 0.9392 -0.0058 -0.0688 -0.0509 261  PHE A CE2   
1263 C  CZ    . PHE A 158 ? 1.0215 1.1707 0.9333 0.0056  -0.0633 -0.0449 261  PHE A CZ    
1264 N  N     . LEU A 159 ? 0.9259 1.2192 0.9113 0.0124  -0.0929 -0.0524 262  LEU A N     
1265 C  CA    . LEU A 159 ? 0.8285 1.1531 0.8263 0.0168  -0.0989 -0.0531 262  LEU A CA    
1266 C  C     . LEU A 159 ? 0.8427 1.1910 0.8479 0.0029  -0.1030 -0.0582 262  LEU A C     
1267 O  O     . LEU A 159 ? 0.9158 1.2943 0.9339 0.0058  -0.1076 -0.0589 262  LEU A O     
1268 C  CB    . LEU A 159 ? 0.8695 1.2001 0.8811 0.0281  -0.0950 -0.0504 262  LEU A CB    
1269 C  CG    . LEU A 159 ? 0.9238 1.2368 0.9310 0.0430  -0.0920 -0.0452 262  LEU A CG    
1270 C  CD1   . LEU A 159 ? 0.9634 1.2805 0.9833 0.0517  -0.0881 -0.0441 262  LEU A CD1   
1271 C  CD2   . LEU A 159 ? 1.0631 1.3838 1.0636 0.0525  -0.0981 -0.0426 262  LEU A CD2   
1272 N  N     . GLU A 160 ? 0.8374 1.1733 0.8351 -0.0120 -0.1011 -0.0616 263  GLU A N     
1273 C  CA    . GLU A 160 ? 1.1333 1.4894 1.1383 -0.0271 -0.1038 -0.0661 263  GLU A CA    
1274 C  C     . GLU A 160 ? 1.0029 1.3455 0.9913 -0.0412 -0.1069 -0.0703 263  GLU A C     
1275 O  O     . GLU A 160 ? 0.9760 1.2880 0.9475 -0.0406 -0.1036 -0.0697 263  GLU A O     
1276 C  CB    . GLU A 160 ? 1.0610 1.4154 1.0755 -0.0328 -0.0965 -0.0661 263  GLU A CB    
1277 C  CG    . GLU A 160 ? 1.0348 1.4124 1.0592 -0.0480 -0.0979 -0.0697 263  GLU A CG    
1278 C  CD    . GLU A 160 ? 1.2235 1.6407 1.2661 -0.0433 -0.1028 -0.0699 263  GLU A CD    
1279 O  OE1   . GLU A 160 ? 1.2972 1.7218 1.3465 -0.0267 -0.1028 -0.0668 263  GLU A OE1   
1280 O  OE2   . GLU A 160 ? 1.3090 1.7502 1.3594 -0.0562 -0.1064 -0.0731 263  GLU A OE2   
1281 N  N     . LYS A 161 ? 1.0272 1.3931 1.0208 -0.0542 -0.1130 -0.0748 264  LYS A N     
1282 C  CA    . LYS A 161 ? 0.9949 1.3493 0.9727 -0.0698 -0.1168 -0.0801 264  LYS A CA    
1283 C  C     . LYS A 161 ? 1.0843 1.4107 1.0530 -0.0820 -0.1090 -0.0814 264  LYS A C     
1284 O  O     . LYS A 161 ? 1.2501 1.5805 1.2183 -0.0994 -0.1101 -0.0858 264  LYS A O     
1285 C  CB    . LYS A 161 ? 1.0282 1.4179 1.0165 -0.0821 -0.1256 -0.0846 264  LYS A CB    
1286 C  CG    . LYS A 161 ? 1.1884 1.6070 1.1831 -0.0710 -0.1351 -0.0836 264  LYS A CG    
1287 C  CD    . LYS A 161 ? 1.2612 1.7112 1.2621 -0.0861 -0.1452 -0.0891 264  LYS A CD    
1288 C  CE    . LYS A 161 ? 1.3105 1.7362 1.2894 -0.1036 -0.1479 -0.0955 264  LYS A CE    
1289 N  NZ    . LYS A 161 ? 1.3314 1.7870 1.3157 -0.1206 -0.1585 -0.1016 264  LYS A NZ    
1290 N  N     . TYR A 162 ? 1.0592 1.3575 1.0210 -0.0731 -0.1010 -0.0775 265  TYR A N     
1291 C  CA    . TYR A 162 ? 1.1622 1.4324 1.1127 -0.0833 -0.0941 -0.0784 265  TYR A CA    
1292 C  C     . TYR A 162 ? 1.1157 1.3565 1.0415 -0.0868 -0.0947 -0.0812 265  TYR A C     
1293 O  O     . TYR A 162 ? 1.0639 1.2993 0.9810 -0.0763 -0.0975 -0.0802 265  TYR A O     
1294 C  CB    . TYR A 162 ? 1.0598 1.3145 1.0143 -0.0732 -0.0853 -0.0730 265  TYR A CB    
1295 C  CG    . TYR A 162 ? 1.0701 1.3454 1.0441 -0.0730 -0.0824 -0.0711 265  TYR A CG    
1296 C  CD1   . TYR A 162 ? 1.1821 1.4578 1.1584 -0.0864 -0.0787 -0.0724 265  TYR A CD1   
1297 C  CD2   . TYR A 162 ? 1.0160 1.3079 1.0042 -0.0590 -0.0827 -0.0680 265  TYR A CD2   
1298 C  CE1   . TYR A 162 ? 0.8977 1.1918 0.8900 -0.0857 -0.0754 -0.0705 265  TYR A CE1   
1299 C  CE2   . TYR A 162 ? 1.0187 1.3279 1.0225 -0.0581 -0.0796 -0.0668 265  TYR A CE2   
1300 C  CZ    . TYR A 162 ? 1.0321 1.3432 1.0379 -0.0713 -0.0760 -0.0681 265  TYR A CZ    
1301 O  OH    . TYR A 162 ? 1.1452 1.4735 1.1651 -0.0699 -0.0723 -0.0668 265  TYR A OH    
1302 N  N     . PRO A 163 ? 1.1156 1.3358 1.0286 -0.1009 -0.0918 -0.0846 266  PRO A N     
1303 C  CA    . PRO A 163 ? 1.1071 1.2927 0.9944 -0.1017 -0.0898 -0.0868 266  PRO A CA    
1304 C  C     . PRO A 163 ? 1.1335 1.2991 1.0160 -0.0843 -0.0832 -0.0808 266  PRO A C     
1305 O  O     . PRO A 163 ? 1.1704 1.3341 1.0638 -0.0778 -0.0768 -0.0757 266  PRO A O     
1306 C  CB    . PRO A 163 ? 1.0661 1.2308 0.9440 -0.1173 -0.0847 -0.0894 266  PRO A CB    
1307 C  CG    . PRO A 163 ? 1.1007 1.2962 0.9968 -0.1304 -0.0885 -0.0916 266  PRO A CG    
1308 C  CD    . PRO A 163 ? 1.2053 1.4325 1.1251 -0.1174 -0.0900 -0.0869 266  PRO A CD    
1309 N  N     . LEU A 164 ? 1.1973 1.3491 1.0634 -0.0771 -0.0848 -0.0813 267  LEU A N     
1310 C  CA    . LEU A 164 ? 1.1486 1.2865 1.0125 -0.0603 -0.0789 -0.0751 267  LEU A CA    
1311 C  C     . LEU A 164 ? 1.0336 1.1463 0.8940 -0.0584 -0.0688 -0.0715 267  LEU A C     
1312 O  O     . LEU A 164 ? 1.1015 1.2136 0.9720 -0.0469 -0.0637 -0.0655 267  LEU A O     
1313 C  CB    . LEU A 164 ? 1.2999 1.4242 1.1432 -0.0546 -0.0812 -0.0765 267  LEU A CB    
1314 C  CG    . LEU A 164 ? 1.2228 1.3352 1.0639 -0.0375 -0.0752 -0.0696 267  LEU A CG    
1315 C  CD1   . LEU A 164 ? 1.3118 1.4493 1.1740 -0.0272 -0.0776 -0.0645 267  LEU A CD1   
1316 C  CD2   . LEU A 164 ? 1.2155 1.3111 1.0326 -0.0331 -0.0761 -0.0712 267  LEU A CD2   
1317 N  N     . SER A 165 ? 0.9819 1.0735 0.8278 -0.0696 -0.0659 -0.0752 268  SER A N     
1318 C  CA    . SER A 165 ? 1.0964 1.1637 0.9376 -0.0670 -0.0563 -0.0714 268  SER A CA    
1319 C  C     . SER A 165 ? 1.1758 1.2572 1.0370 -0.0683 -0.0538 -0.0677 268  SER A C     
1320 O  O     . SER A 165 ? 1.0850 1.1509 0.9455 -0.0634 -0.0465 -0.0633 268  SER A O     
1321 C  CB    . SER A 165 ? 1.0803 1.1188 0.8983 -0.0783 -0.0537 -0.0764 268  SER A CB    
1322 O  OG    . SER A 165 ? 1.0239 1.0743 0.8429 -0.0954 -0.0600 -0.0826 268  SER A OG    
1323 N  N     . GLN A 166 ? 1.0892 1.2002 0.9675 -0.0739 -0.0595 -0.0694 269  GLN A N     
1324 C  CA    . GLN A 166 ? 1.1221 1.2468 1.0180 -0.0746 -0.0568 -0.0662 269  GLN A CA    
1325 C  C     . GLN A 166 ? 1.1521 1.2873 1.0628 -0.0595 -0.0553 -0.0607 269  GLN A C     
1326 O  O     . GLN A 166 ? 1.1626 1.2995 1.0828 -0.0570 -0.0512 -0.0573 269  GLN A O     
1327 C  CB    . GLN A 166 ? 1.2168 1.3697 1.1252 -0.0863 -0.0625 -0.0700 269  GLN A CB    
1328 C  CG    . GLN A 166 ? 1.0915 1.2560 1.0142 -0.0896 -0.0588 -0.0674 269  GLN A CG    
1329 C  CD    . GLN A 166 ? 1.2585 1.4477 1.1910 -0.1036 -0.0627 -0.0712 269  GLN A CD    
1330 O  OE1   . GLN A 166 ? 1.2252 1.4237 1.1545 -0.1119 -0.0690 -0.0760 269  GLN A OE1   
1331 N  NE2   . GLN A 166 ? 1.2707 1.4718 1.2152 -0.1066 -0.0591 -0.0689 269  GLN A NE2   
1332 N  N     . TYR A 167 ? 1.0152 1.1566 0.9272 -0.0498 -0.0585 -0.0599 270  TYR A N     
1333 C  CA    . TYR A 167 ? 1.0022 1.1486 0.9259 -0.0362 -0.0564 -0.0548 270  TYR A CA    
1334 C  C     . TYR A 167 ? 1.0622 1.1854 0.9801 -0.0305 -0.0488 -0.0503 270  TYR A C     
1335 O  O     . TYR A 167 ? 0.9912 1.0919 0.8924 -0.0314 -0.0454 -0.0505 270  TYR A O     
1336 C  CB    . TYR A 167 ? 0.9595 1.1119 0.8819 -0.0272 -0.0603 -0.0541 270  TYR A CB    
1337 C  CG    . TYR A 167 ? 0.8938 1.0745 0.8275 -0.0280 -0.0678 -0.0565 270  TYR A CG    
1338 C  CD1   . TYR A 167 ? 0.9283 1.1194 0.8565 -0.0379 -0.0741 -0.0618 270  TYR A CD1   
1339 C  CD2   . TYR A 167 ? 0.8501 1.0471 0.7996 -0.0186 -0.0686 -0.0537 270  TYR A CD2   
1340 C  CE1   . TYR A 167 ? 0.8934 1.1134 0.8333 -0.0376 -0.0811 -0.0635 270  TYR A CE1   
1341 C  CE2   . TYR A 167 ? 0.7802 1.0031 0.7398 -0.0173 -0.0749 -0.0554 270  TYR A CE2   
1342 C  CZ    . TYR A 167 ? 0.8437 1.0796 0.7993 -0.0264 -0.0812 -0.0600 270  TYR A CZ    
1343 O  OH    . TYR A 167 ? 0.8246 1.0894 0.7917 -0.0244 -0.0876 -0.0612 270  TYR A OH    
1344 N  N     . LYS A 168 ? 1.0612 1.1905 0.9930 -0.0242 -0.0462 -0.0463 271  LYS A N     
1345 C  CA    . LYS A 168 ? 1.0630 1.1749 0.9922 -0.0194 -0.0397 -0.0418 271  LYS A CA    
1346 C  C     . LYS A 168 ? 0.9636 1.0608 0.8848 -0.0103 -0.0364 -0.0386 271  LYS A C     
1347 O  O     . LYS A 168 ? 0.9698 1.0474 0.8803 -0.0085 -0.0309 -0.0364 271  LYS A O     
1348 C  CB    . LYS A 168 ? 1.1482 1.2723 1.0942 -0.0151 -0.0390 -0.0389 271  LYS A CB    
1349 C  CG    . LYS A 168 ? 1.1072 1.2408 1.0581 -0.0232 -0.0396 -0.0408 271  LYS A CG    
1350 C  CD    . LYS A 168 ? 1.1659 1.3083 1.1301 -0.0182 -0.0387 -0.0381 271  LYS A CD    
1351 C  CE    . LYS A 168 ? 1.1871 1.3373 1.1537 -0.0257 -0.0383 -0.0394 271  LYS A CE    
1352 N  NZ    . LYS A 168 ? 1.1746 1.3330 1.1519 -0.0207 -0.0379 -0.0374 271  LYS A NZ    
1353 N  N     . TYR A 169 ? 1.0210 1.1269 0.9466 -0.0039 -0.0390 -0.0378 272  TYR A N     
1354 C  CA    . TYR A 169 ? 1.0096 1.1023 0.9275 0.0047  -0.0351 -0.0341 272  TYR A CA    
1355 C  C     . TYR A 169 ? 0.9799 1.0542 0.8760 0.0018  -0.0336 -0.0367 272  TYR A C     
1356 O  O     . TYR A 169 ? 0.9103 0.9665 0.7966 0.0071  -0.0271 -0.0336 272  TYR A O     
1357 C  CB    . TYR A 169 ? 0.9944 1.0988 0.9192 0.0115  -0.0383 -0.0326 272  TYR A CB    
1358 C  CG    . TYR A 169 ? 1.0618 1.1528 0.9763 0.0195  -0.0341 -0.0287 272  TYR A CG    
1359 C  CD1   . TYR A 169 ? 1.0241 1.1083 0.9447 0.0266  -0.0276 -0.0227 272  TYR A CD1   
1360 C  CD2   . TYR A 169 ? 1.1313 1.2178 1.0299 0.0198  -0.0366 -0.0310 272  TYR A CD2   
1361 C  CE1   . TYR A 169 ? 1.1517 1.2247 1.0633 0.0338  -0.0226 -0.0185 272  TYR A CE1   
1362 C  CE2   . TYR A 169 ? 1.0842 1.1580 0.9717 0.0276  -0.0320 -0.0272 272  TYR A CE2   
1363 C  CZ    . TYR A 169 ? 1.1243 1.1914 1.0187 0.0347  -0.0245 -0.0207 272  TYR A CZ    
1364 O  OH    . TYR A 169 ? 1.2023 1.2578 1.0861 0.0424  -0.0189 -0.0163 272  TYR A OH    
1365 N  N     . ILE A 170 ? 0.9288 1.0078 0.8170 -0.0065 -0.0394 -0.0426 273  ILE A N     
1366 C  CA    . ILE A 170 ? 1.0096 1.0701 0.8750 -0.0106 -0.0389 -0.0464 273  ILE A CA    
1367 C  C     . ILE A 170 ? 0.9935 1.0325 0.8484 -0.0149 -0.0329 -0.0467 273  ILE A C     
1368 O  O     . ILE A 170 ? 1.0702 1.0864 0.9079 -0.0110 -0.0273 -0.0461 273  ILE A O     
1369 C  CB    . ILE A 170 ? 1.0436 1.1170 0.9048 -0.0202 -0.0477 -0.0531 273  ILE A CB    
1370 C  CG1   . ILE A 170 ? 1.0205 1.1150 0.8915 -0.0137 -0.0535 -0.0518 273  ILE A CG1   
1371 C  CG2   . ILE A 170 ? 1.0584 1.1112 0.8943 -0.0257 -0.0479 -0.0581 273  ILE A CG2   
1372 C  CD1   . ILE A 170 ? 1.0083 1.0922 0.8697 -0.0021 -0.0505 -0.0478 273  ILE A CD1   
1373 N  N     . ARG A 171 ? 1.0858 1.1309 0.9497 -0.0223 -0.0334 -0.0474 274  ARG A N     
1374 C  CA    . ARG A 171 ? 1.0676 1.0912 0.9206 -0.0262 -0.0275 -0.0471 274  ARG A CA    
1375 C  C     . ARG A 171 ? 1.0230 1.0358 0.8789 -0.0144 -0.0198 -0.0400 274  ARG A C     
1376 O  O     . ARG A 171 ? 1.0582 1.0477 0.8996 -0.0127 -0.0136 -0.0388 274  ARG A O     
1377 C  CB    . ARG A 171 ? 1.1161 1.1495 0.9775 -0.0371 -0.0297 -0.0488 274  ARG A CB    
1378 C  CG    . ARG A 171 ? 1.1706 1.1790 1.0164 -0.0434 -0.0243 -0.0493 274  ARG A CG    
1379 C  CD    . ARG A 171 ? 1.2190 1.2371 1.0723 -0.0550 -0.0258 -0.0505 274  ARG A CD    
1380 N  NE    . ARG A 171 ? 1.2746 1.3104 1.1313 -0.0670 -0.0330 -0.0566 274  ARG A NE    
1381 C  CZ    . ARG A 171 ? 1.3130 1.3571 1.1737 -0.0800 -0.0344 -0.0589 274  ARG A CZ    
1382 N  NH1   . ARG A 171 ? 1.2227 1.2566 1.0822 -0.0828 -0.0290 -0.0555 274  ARG A NH1   
1383 N  NH2   . ARG A 171 ? 1.3714 1.4354 1.2374 -0.0902 -0.0413 -0.0643 274  ARG A NH2   
1384 N  N     . SER A 172 ? 0.9567 0.9862 0.8311 -0.0063 -0.0201 -0.0354 275  SER A N     
1385 C  CA    . SER A 172 ? 1.0021 1.0249 0.8810 0.0046  -0.0134 -0.0286 275  SER A CA    
1386 C  C     . SER A 172 ? 1.1844 1.1909 1.0490 0.0124  -0.0083 -0.0270 275  SER A C     
1387 O  O     . SER A 172 ? 1.2391 1.2312 1.0982 0.0197  -0.0009 -0.0227 275  SER A O     
1388 C  CB    . SER A 172 ? 1.0137 1.0580 0.9154 0.0096  -0.0155 -0.0248 275  SER A CB    
1389 O  OG    . SER A 172 ? 1.1547 1.1957 1.0633 0.0181  -0.0099 -0.0185 275  SER A OG    
1390 N  N     . CYS A 173 ? 1.1198 1.1288 0.9774 0.0119  -0.0119 -0.0302 276  CYS A N     
1391 C  CA    . CYS A 173 ? 1.0499 1.0420 0.8900 0.0188  -0.0069 -0.0294 276  CYS A CA    
1392 C  C     . CYS A 173 ? 1.1332 1.0988 0.9491 0.0152  -0.0032 -0.0333 276  CYS A C     
1393 O  O     . CYS A 173 ? 1.1925 1.1394 0.9956 0.0235  0.0048  -0.0305 276  CYS A O     
1394 C  CB    . CYS A 173 ? 1.0005 1.0013 0.8364 0.0186  -0.0126 -0.0321 276  CYS A CB    
1395 S  SG    . CYS A 173 ? 0.9241 0.9472 0.7822 0.0266  -0.0141 -0.0261 276  CYS A SG    
1396 N  N     . ILE A 174 ? 1.0515 1.0149 0.8608 0.0027  -0.0083 -0.0397 277  ILE A N     
1397 C  CA    . ILE A 174 ? 1.0714 1.0070 0.8562 -0.0028 -0.0051 -0.0443 277  ILE A CA    
1398 C  C     . ILE A 174 ? 1.2640 1.1825 1.0465 0.0037  0.0038  -0.0390 277  ILE A C     
1399 O  O     . ILE A 174 ? 1.3346 1.2271 1.0972 0.0096  0.0111  -0.0387 277  ILE A O     
1400 C  CB    . ILE A 174 ? 1.1420 1.0816 0.9237 -0.0192 -0.0126 -0.0516 277  ILE A CB    
1401 C  CG1   . ILE A 174 ? 1.1100 1.0661 0.8914 -0.0245 -0.0217 -0.0570 277  ILE A CG1   
1402 C  CG2   . ILE A 174 ? 1.2315 1.1396 0.9886 -0.0262 -0.0086 -0.0560 277  ILE A CG2   
1403 C  CD1   . ILE A 174 ? 1.0755 1.0433 0.8593 -0.0409 -0.0297 -0.0636 277  ILE A CD1   
1404 N  N     . MET A 175 ? 1.4378 1.3705 1.2399 0.0034  0.0034  -0.0347 278  MET A N     
1405 C  CA    . MET A 175 ? 1.3412 1.2601 1.1419 0.0099  0.0109  -0.0291 278  MET A CA    
1406 C  C     . MET A 175 ? 1.3160 1.2318 1.1192 0.0256  0.0184  -0.0223 278  MET A C     
1407 O  O     . MET A 175 ? 1.3634 1.2582 1.1540 0.0332  0.0264  -0.0191 278  MET A O     
1408 C  CB    . MET A 175 ? 1.4096 1.3474 1.2307 0.0064  0.0078  -0.0260 278  MET A CB    
1409 C  CG    . MET A 175 ? 1.4861 1.4278 1.3058 -0.0090 0.0019  -0.0318 278  MET A CG    
1410 S  SD    . MET A 175 ? 1.4771 1.4440 1.3208 -0.0118 -0.0016 -0.0283 278  MET A SD    
1411 C  CE    . MET A 175 ? 1.5391 1.5063 1.3762 -0.0303 -0.0063 -0.0352 278  MET A CE    
1412 N  N     . LEU A 176 ? 1.2786 1.2151 1.0980 0.0308  0.0164  -0.0195 279  LEU A N     
1413 C  CA    . LEU A 176 ? 1.3363 1.2735 1.1608 0.0445  0.0237  -0.0126 279  LEU A CA    
1414 C  C     . LEU A 176 ? 1.3692 1.2879 1.1720 0.0500  0.0289  -0.0143 279  LEU A C     
1415 O  O     . LEU A 176 ? 1.3795 1.2981 1.1849 0.0616  0.0361  -0.0084 279  LEU A O     
1416 C  CB    . LEU A 176 ? 1.3005 1.2657 1.1508 0.0467  0.0200  -0.0086 279  LEU A CB    
1417 C  CG    . LEU A 176 ? 1.3981 1.3821 1.2702 0.0434  0.0157  -0.0064 279  LEU A CG    
1418 C  CD1   . LEU A 176 ? 1.4471 1.4553 1.3407 0.0433  0.0109  -0.0048 279  LEU A CD1   
1419 C  CD2   . LEU A 176 ? 1.4358 1.4162 1.3129 0.0516  0.0219  0.0003  279  LEU A CD2   
1420 N  N     . GLY A 177 ? 1.3746 1.2786 1.1561 0.0417  0.0254  -0.0223 280  GLY A N     
1421 C  CA    . GLY A 177 ? 1.3282 1.2136 1.0862 0.0465  0.0296  -0.0249 280  GLY A CA    
1422 C  C     . GLY A 177 ? 1.3205 1.2211 1.0847 0.0511  0.0280  -0.0230 280  GLY A C     
1423 O  O     . GLY A 177 ? 1.3827 1.2698 1.1298 0.0588  0.0338  -0.0225 280  GLY A O     
1424 N  N     . ARG A 178 ? 1.2962 1.2232 1.0830 0.0473  0.0208  -0.0216 281  ARG A N     
1425 C  CA    . ARG A 178 ? 1.2706 1.2115 1.0641 0.0519  0.0193  -0.0189 281  ARG A CA    
1426 C  C     . ARG A 178 ? 1.2470 1.1921 1.0303 0.0436  0.0098  -0.0261 281  ARG A C     
1427 O  O     . ARG A 178 ? 1.1211 1.0622 0.8959 0.0329  0.0036  -0.0333 281  ARG A O     
1428 C  CB    . ARG A 178 ? 1.2441 1.2096 1.0679 0.0540  0.0179  -0.0126 281  ARG A CB    
1429 C  CG    . ARG A 178 ? 1.2955 1.2618 1.1320 0.0626  0.0266  -0.0047 281  ARG A CG    
1430 C  CD    . ARG A 178 ? 1.4435 1.4300 1.3034 0.0668  0.0271  0.0019  281  ARG A CD    
1431 N  NE    . ARG A 178 ? 1.5399 1.5446 1.4151 0.0592  0.0175  -0.0008 281  ARG A NE    
1432 C  CZ    . ARG A 178 ? 1.6290 1.6471 1.5230 0.0552  0.0137  -0.0003 281  ARG A CZ    
1433 N  NH1   . ARG A 178 ? 1.5143 1.5315 1.4154 0.0577  0.0178  0.0031  281  ARG A NH1   
1434 N  NH2   . ARG A 178 ? 1.5684 1.6014 1.4738 0.0493  0.0057  -0.0033 281  ARG A NH2   
1435 N  N     . MET A 179 ? 1.3535 1.3078 1.1380 0.0486  0.0086  -0.0235 282  MET A N     
1436 C  CA    . MET A 179 ? 1.2442 1.2053 1.0198 0.0433  -0.0006 -0.0290 282  MET A CA    
1437 C  C     . MET A 179 ? 1.0919 1.0793 0.8917 0.0416  -0.0077 -0.0268 282  MET A C     
1438 O  O     . MET A 179 ? 1.0232 1.0198 0.8399 0.0485  -0.0037 -0.0196 282  MET A O     
1439 C  CB    . MET A 179 ? 1.2017 1.1515 0.9564 0.0515  0.0031  -0.0277 282  MET A CB    
1440 C  CG    . MET A 179 ? 1.4210 1.3443 1.1443 0.0503  0.0060  -0.0340 282  MET A CG    
1441 S  SD    . MET A 179 ? 1.3576 1.2675 1.0537 0.0605  0.0105  -0.0327 282  MET A SD    
1442 C  CE    . MET A 179 ? 1.2855 1.1899 0.9910 0.0752  0.0265  -0.0214 282  MET A CE    
1443 N  N     . PRO A 180 ? 1.0010 1.0011 0.8031 0.0323  -0.0179 -0.0328 283  PRO A N     
1444 C  CA    . PRO A 180 ? 1.0255 1.0499 0.8487 0.0323  -0.0243 -0.0309 283  PRO A CA    
1445 C  C     . PRO A 180 ? 1.1120 1.1404 0.9320 0.0413  -0.0244 -0.0265 283  PRO A C     
1446 O  O     . PRO A 180 ? 1.1550 1.1743 0.9538 0.0434  -0.0254 -0.0284 283  PRO A O     
1447 C  CB    . PRO A 180 ? 1.0761 1.1119 0.8982 0.0208  -0.0344 -0.0388 283  PRO A CB    
1448 C  CG    . PRO A 180 ? 1.1157 1.1330 0.9228 0.0127  -0.0321 -0.0440 283  PRO A CG    
1449 C  CD    . PRO A 180 ? 1.0427 1.0358 0.8304 0.0208  -0.0234 -0.0416 283  PRO A CD    
1450 N  N     . ASN A 181 ? 1.0448 1.0857 0.8846 0.0465  -0.0233 -0.0206 284  ASN A N     
1451 C  CA    . ASN A 181 ? 1.0599 1.1047 0.8990 0.0551  -0.0231 -0.0153 284  ASN A CA    
1452 C  C     . ASN A 181 ? 1.1019 1.1673 0.9550 0.0535  -0.0321 -0.0167 284  ASN A C     
1453 O  O     . ASN A 181 ? 1.1517 1.2270 1.0253 0.0535  -0.0319 -0.0145 284  ASN A O     
1454 C  CB    . ASN A 181 ? 1.1293 1.1689 0.9788 0.0627  -0.0133 -0.0066 284  ASN A CB    
1455 C  CG    . ASN A 181 ? 1.1828 1.2036 1.0159 0.0677  -0.0036 -0.0038 284  ASN A CG    
1456 O  OD1   . ASN A 181 ? 1.1398 1.1486 0.9512 0.0660  -0.0042 -0.0087 284  ASN A OD1   
1457 N  ND2   . ASN A 181 ? 1.2526 1.2709 1.0957 0.0737  0.0055  0.0041  284  ASN A ND2   
1458 N  N     . LEU A 182 ? 1.1212 1.1934 0.9627 0.0524  -0.0402 -0.0207 285  LEU A N     
1459 C  CA    . LEU A 182 ? 1.1427 1.2363 0.9959 0.0516  -0.0492 -0.0225 285  LEU A CA    
1460 C  C     . LEU A 182 ? 1.0963 1.1928 0.9415 0.0615  -0.0516 -0.0180 285  LEU A C     
1461 O  O     . LEU A 182 ? 1.1750 1.2573 1.0026 0.0673  -0.0474 -0.0147 285  LEU A O     
1462 C  CB    . LEU A 182 ? 1.1184 1.2226 0.9676 0.0408  -0.0580 -0.0312 285  LEU A CB    
1463 C  CG    . LEU A 182 ? 1.0611 1.1571 0.9108 0.0303  -0.0552 -0.0359 285  LEU A CG    
1464 C  CD1   . LEU A 182 ? 0.9721 1.0781 0.8168 0.0185  -0.0638 -0.0442 285  LEU A CD1   
1465 C  CD2   . LEU A 182 ? 1.2361 1.3376 1.1080 0.0298  -0.0513 -0.0332 285  LEU A CD2   
1466 N  N     . MET A 183 ? 1.0731 1.1879 0.9307 0.0643  -0.0580 -0.0175 286  MET A N     
1467 C  CA    . MET A 183 ? 1.0379 1.1572 0.8881 0.0744  -0.0615 -0.0131 286  MET A CA    
1468 C  C     . MET A 183 ? 1.0363 1.1804 0.8953 0.0736  -0.0722 -0.0169 286  MET A C     
1469 O  O     . MET A 183 ? 1.0815 1.2392 0.9562 0.0663  -0.0752 -0.0216 286  MET A O     
1470 C  CB    . MET A 183 ? 1.1082 1.2188 0.9664 0.0841  -0.0538 -0.0041 286  MET A CB    
1471 C  CG    . MET A 183 ? 1.2262 1.3503 1.1050 0.0868  -0.0564 -0.0031 286  MET A CG    
1472 S  SD    . MET A 183 ? 1.6169 1.7289 1.4987 0.0990  -0.0494 0.0074  286  MET A SD    
1473 C  CE    . MET A 183 ? 1.5391 1.6683 1.4406 0.1018  -0.0549 0.0057  286  MET A CE    
1474 N  N     . LEU A 184 ? 1.1352 1.2862 0.9838 0.0819  -0.0779 -0.0144 287  LEU A N     
1475 C  CA    . LEU A 184 ? 1.1012 1.2784 0.9574 0.0832  -0.0885 -0.0171 287  LEU A CA    
1476 C  C     . LEU A 184 ? 1.1595 1.3425 1.0284 0.0953  -0.0872 -0.0105 287  LEU A C     
1477 O  O     . LEU A 184 ? 1.1877 1.3539 1.0512 0.1047  -0.0805 -0.0028 287  LEU A O     
1478 C  CB    . LEU A 184 ? 1.0681 1.2522 0.9042 0.0849  -0.0972 -0.0190 287  LEU A CB    
1479 C  CG    . LEU A 184 ? 1.0435 1.2340 0.8711 0.0708  -0.1040 -0.0286 287  LEU A CG    
1480 C  CD1   . LEU A 184 ? 1.0326 1.1966 0.8473 0.0633  -0.0958 -0.0310 287  LEU A CD1   
1481 C  CD2   . LEU A 184 ? 1.0624 1.2652 0.8729 0.0734  -0.1148 -0.0305 287  LEU A CD2   
1482 N  N     . MET A 185 ? 1.2455 1.4518 1.1311 0.0950  -0.0932 -0.0134 288  MET A N     
1483 C  CA    . MET A 185 ? 1.2690 1.4814 1.1664 0.1070  -0.0925 -0.0082 288  MET A CA    
1484 C  C     . MET A 185 ? 1.1768 1.4205 1.0834 0.1091  -0.1026 -0.0115 288  MET A C     
1485 O  O     . MET A 185 ? 1.1779 1.4392 1.0941 0.0979  -0.1070 -0.0186 288  MET A O     
1486 C  CB    . MET A 185 ? 1.2319 1.4348 1.1458 0.1044  -0.0845 -0.0079 288  MET A CB    
1487 C  CG    . MET A 185 ? 1.2539 1.4576 1.1777 0.1165  -0.0827 -0.0031 288  MET A CG    
1488 S  SD    . MET A 185 ? 1.5919 1.7788 1.5303 0.1128  -0.0731 -0.0027 288  MET A SD    
1489 C  CE    . MET A 185 ? 1.5290 1.7184 1.4754 0.1274  -0.0730 0.0013  288  MET A CE    
1490 N  N     . ALA A 186 ? 1.2158 1.4669 1.1198 0.1236  -0.1060 -0.0059 289  ALA A N     
1491 C  CA    . ALA A 186 ? 1.2840 1.5675 1.1970 0.1280  -0.1158 -0.0080 289  ALA A CA    
1492 C  C     . ALA A 186 ? 1.2153 1.5133 1.1513 0.1266  -0.1141 -0.0110 289  ALA A C     
1493 O  O     . ALA A 186 ? 1.2299 1.5113 1.1727 0.1304  -0.1060 -0.0085 289  ALA A O     
1494 C  CB    . ALA A 186 ? 1.2711 1.5567 1.1749 0.1463  -0.1190 0.0000  289  ALA A CB    
1495 N  N     . LYS A 187 ? 1.1590 1.4885 1.1067 0.1205  -0.1217 -0.0167 290  LYS A N     
1496 C  CA    . LYS A 187 ? 1.1512 1.4974 1.1200 0.1194  -0.1200 -0.0197 290  LYS A CA    
1497 C  C     . LYS A 187 ? 1.2221 1.5676 1.1968 0.1378  -0.1171 -0.0139 290  LYS A C     
1498 O  O     . LYS A 187 ? 1.2975 1.6355 1.2829 0.1392  -0.1104 -0.0145 290  LYS A O     
1499 C  CB    . LYS A 187 ? 1.0803 1.4639 1.0605 0.1111  -0.1289 -0.0256 290  LYS A CB    
1500 C  CG    . LYS A 187 ? 1.0390 1.4225 1.0161 0.0906  -0.1306 -0.0326 290  LYS A CG    
1501 C  CD    . LYS A 187 ? 1.0342 1.4561 1.0237 0.0818  -0.1395 -0.0380 290  LYS A CD    
1502 C  CE    . LYS A 187 ? 1.0778 1.4966 1.0646 0.0602  -0.1400 -0.0452 290  LYS A CE    
1503 N  NZ    . LYS A 187 ? 1.1250 1.5200 1.0886 0.0546  -0.1416 -0.0462 290  LYS A NZ    
1504 N  N     . GLU A 188 ? 1.2513 1.6035 1.2179 0.1524  -0.1221 -0.0082 291  GLU A N     
1505 C  CA    . GLU A 188 ? 1.3159 1.6670 1.2866 0.1713  -0.1195 -0.0023 291  GLU A CA    
1506 C  C     . GLU A 188 ? 1.3855 1.6979 1.3496 0.1759  -0.1088 0.0023  291  GLU A C     
1507 O  O     . GLU A 188 ? 1.3249 1.6309 1.2958 0.1862  -0.1040 0.0043  291  GLU A O     
1508 C  CB    . GLU A 188 ? 1.3505 1.7158 1.3116 0.1866  -0.1274 0.0037  291  GLU A CB    
1509 C  CG    . GLU A 188 ? 1.4346 1.7777 1.3724 0.1883  -0.1279 0.0088  291  GLU A CG    
1510 C  CD    . GLU A 188 ? 1.5907 1.9471 1.5207 0.1740  -0.1360 0.0033  291  GLU A CD    
1511 O  OE1   . GLU A 188 ? 1.5704 1.9382 1.5110 0.1573  -0.1371 -0.0048 291  GLU A OE1   
1512 O  OE2   . GLU A 188 ? 1.7767 2.1307 1.6885 0.1795  -0.1411 0.0071  291  GLU A OE2   
1513 N  N     . SER A 189 ? 1.3320 1.6185 1.2827 0.1683  -0.1048 0.0038  292  SER A N     
1514 C  CA    . SER A 189 ? 1.3491 1.6013 1.2959 0.1703  -0.0945 0.0079  292  SER A CA    
1515 C  C     . SER A 189 ? 1.3778 1.6250 1.3389 0.1591  -0.0890 0.0019  292  SER A C     
1516 O  O     . SER A 189 ? 1.3737 1.6010 1.3378 0.1630  -0.0820 0.0039  292  SER A O     
1517 C  CB    . SER A 189 ? 1.2664 1.4952 1.1956 0.1662  -0.0913 0.0118  292  SER A CB    
1518 O  OG    . SER A 189 ? 1.2594 1.4923 1.1880 0.1500  -0.0927 0.0056  292  SER A OG    
1519 N  N     . LEU A 190 ? 1.3107 1.5747 1.2796 0.1450  -0.0921 -0.0053 293  LEU A N     
1520 C  CA    . LEU A 190 ? 1.3329 1.5945 1.3145 0.1350  -0.0875 -0.0107 293  LEU A CA    
1521 C  C     . LEU A 190 ? 1.2962 1.5776 1.2924 0.1414  -0.0886 -0.0135 293  LEU A C     
1522 O  O     . LEU A 190 ? 1.2409 1.5121 1.2443 0.1410  -0.0831 -0.0154 293  LEU A O     
1523 C  CB    . LEU A 190 ? 1.3416 1.6109 1.3241 0.1179  -0.0895 -0.0166 293  LEU A CB    
1524 C  CG    . LEU A 190 ? 1.2209 1.4841 1.2127 0.1059  -0.0845 -0.0214 293  LEU A CG    
1525 C  CD1   . LEU A 190 ? 1.2165 1.5053 1.2232 0.1030  -0.0869 -0.0267 293  LEU A CD1   
1526 C  CD2   . LEU A 190 ? 1.2269 1.4641 1.2192 0.1095  -0.0767 -0.0183 293  LEU A CD2   
1527 N  N     . TYR A 191 ? 1.2086 1.5191 1.2088 0.1475  -0.0958 -0.0139 294  TYR A N     
1528 C  CA    . TYR A 191 ? 1.1518 1.4838 1.1663 0.1550  -0.0962 -0.0162 294  TYR A CA    
1529 C  C     . TYR A 191 ? 1.2503 1.5655 1.2622 0.1727  -0.0916 -0.0113 294  TYR A C     
1530 O  O     . TYR A 191 ? 1.3588 1.6766 1.3799 0.1773  -0.0879 -0.0139 294  TYR A O     
1531 C  CB    . TYR A 191 ? 1.0719 1.4421 1.0927 0.1575  -0.1053 -0.0172 294  TYR A CB    
1532 C  CG    . TYR A 191 ? 1.0678 1.4569 1.0932 0.1388  -0.1099 -0.0232 294  TYR A CG    
1533 C  CD1   . TYR A 191 ? 1.1464 1.5202 1.1719 0.1228  -0.1051 -0.0274 294  TYR A CD1   
1534 C  CD2   . TYR A 191 ? 1.0877 1.5098 1.1170 0.1370  -0.1191 -0.0244 294  TYR A CD2   
1535 C  CE1   . TYR A 191 ? 1.1354 1.5230 1.1633 0.1060  -0.1087 -0.0326 294  TYR A CE1   
1536 C  CE2   . TYR A 191 ? 1.0970 1.5340 1.1295 0.1187  -0.1231 -0.0302 294  TYR A CE2   
1537 C  CZ    . TYR A 191 ? 1.1428 1.5609 1.1739 0.1033  -0.1175 -0.0342 294  TYR A CZ    
1538 O  OH    . TYR A 191 ? 1.2254 1.6551 1.2581 0.0852  -0.1209 -0.0397 294  TYR A OH    
1539 N  N     . SER A 192 ? 1.2849 1.5814 1.2830 0.1827  -0.0912 -0.0042 295  SER A N     
1540 C  CA    . SER A 192 ? 1.3342 1.6107 1.3276 0.1993  -0.0863 0.0011  295  SER A CA    
1541 C  C     . SER A 192 ? 1.2590 1.5039 1.2524 0.1939  -0.0775 -0.0005 295  SER A C     
1542 O  O     . SER A 192 ? 1.1979 1.4287 1.1912 0.2048  -0.0729 0.0007  295  SER A O     
1543 C  CB    . SER A 192 ? 1.3118 1.5750 1.2888 0.2106  -0.0877 0.0099  295  SER A CB    
1544 O  OG    . SER A 192 ? 1.3685 1.6100 1.3348 0.1998  -0.0851 0.0117  295  SER A OG    
1545 N  N     . GLN A 193 ? 1.2270 1.4606 1.2200 0.1775  -0.0752 -0.0032 296  GLN A N     
1546 C  CA    . GLN A 193 ? 1.3972 1.6049 1.3918 0.1707  -0.0679 -0.0051 296  GLN A CA    
1547 C  C     . GLN A 193 ? 1.3727 1.5923 1.3803 0.1640  -0.0671 -0.0131 296  GLN A C     
1548 O  O     . GLN A 193 ? 1.3481 1.5486 1.3575 0.1586  -0.0620 -0.0156 296  GLN A O     
1549 C  CB    . GLN A 193 ? 1.4063 1.5980 1.3952 0.1575  -0.0656 -0.0038 296  GLN A CB    
1550 C  CG    . GLN A 193 ? 1.4858 1.6624 1.4603 0.1638  -0.0649 0.0045  296  GLN A CG    
1551 C  CD    . GLN A 193 ? 1.6872 1.8581 1.6559 0.1516  -0.0641 0.0051  296  GLN A CD    
1552 O  OE1   . GLN A 193 ? 1.7780 1.9567 1.7533 0.1387  -0.0647 -0.0006 296  GLN A OE1   
1553 N  NE2   . GLN A 193 ? 1.6471 1.8032 1.6020 0.1564  -0.0623 0.0123  296  GLN A NE2   
1554 N  N     . LEU A 194 ? 1.3547 1.6058 1.3711 0.1638  -0.0718 -0.0170 297  LEU A N     
1555 C  CA    . LEU A 194 ? 1.3425 1.6066 1.3704 0.1581  -0.0704 -0.0240 297  LEU A CA    
1556 C  C     . LEU A 194 ? 1.4019 1.6650 1.4323 0.1732  -0.0675 -0.0247 297  LEU A C     
1557 O  O     . LEU A 194 ? 1.4219 1.7031 1.4540 0.1866  -0.0704 -0.0223 297  LEU A O     
1558 C  CB    . LEU A 194 ? 1.3188 1.6173 1.3554 0.1505  -0.0759 -0.0275 297  LEU A CB    
1559 C  CG    . LEU A 194 ? 1.2409 1.5414 1.2740 0.1352  -0.0789 -0.0280 297  LEU A CG    
1560 C  CD1   . LEU A 194 ? 1.1622 1.4975 1.2032 0.1294  -0.0850 -0.0311 297  LEU A CD1   
1561 C  CD2   . LEU A 194 ? 1.1295 1.4124 1.1629 0.1215  -0.0743 -0.0313 297  LEU A CD2   
1562 N  N     . PRO A 195 ? 1.4635 1.7059 1.4936 0.1722  -0.0620 -0.0280 298  PRO A N     
1563 C  CA    . PRO A 195 ? 1.4797 1.7189 1.5102 0.1867  -0.0587 -0.0297 298  PRO A CA    
1564 C  C     . PRO A 195 ? 1.5295 1.8018 1.5717 0.1881  -0.0599 -0.0349 298  PRO A C     
1565 O  O     . PRO A 195 ? 1.5105 1.8016 1.5602 0.1746  -0.0618 -0.0385 298  PRO A O     
1566 C  CB    . PRO A 195 ? 1.5158 1.7230 1.5418 0.1810  -0.0532 -0.0331 298  PRO A CB    
1567 C  CG    . PRO A 195 ? 1.4569 1.6490 1.4797 0.1668  -0.0535 -0.0305 298  PRO A CG    
1568 C  CD    . PRO A 195 ? 1.4460 1.6650 1.4738 0.1586  -0.0586 -0.0301 298  PRO A CD    
1569 N  N     . MET A 196 ? 1.6089 1.8874 1.6519 0.2053  -0.0581 -0.0347 299  MET A N     
1570 C  CA    . MET A 196 ? 1.6715 1.9825 1.7260 0.2092  -0.0579 -0.0389 299  MET A CA    
1571 C  C     . MET A 196 ? 1.7550 2.0556 1.8100 0.2033  -0.0525 -0.0462 299  MET A C     
1572 O  O     . MET A 196 ? 1.7221 1.9911 1.7678 0.2077  -0.0480 -0.0480 299  MET A O     
1573 C  CB    . MET A 196 ? 1.6745 1.9972 1.7297 0.2318  -0.0575 -0.0355 299  MET A CB    
1574 C  CG    . MET A 196 ? 1.6914 2.0511 1.7599 0.2374  -0.0567 -0.0390 299  MET A CG    
1575 S  SD    . MET A 196 ? 1.8495 2.2133 1.9166 0.2668  -0.0529 -0.0363 299  MET A SD    
1576 C  CE    . MET A 196 ? 1.5918 1.9048 1.6431 0.2706  -0.0443 -0.0410 299  MET A CE    
1577 N  N     . ASP A 197 ? 1.9556 2.2821 2.0206 0.1928  -0.0529 -0.0505 300  ASP A N     
1578 C  CA    . ASP A 197 ? 1.9350 2.2561 2.0000 0.1884  -0.0478 -0.0573 300  ASP A CA    
1579 C  C     . ASP A 197 ? 1.9450 2.2780 2.0122 0.2061  -0.0434 -0.0596 300  ASP A C     
1580 O  O     . ASP A 197 ? 1.9598 2.3241 2.0364 0.2157  -0.0449 -0.0569 300  ASP A O     
1581 C  CB    . ASP A 197 ? 1.8001 2.1426 1.8733 0.1707  -0.0491 -0.0602 300  ASP A CB    
1582 C  CG    . ASP A 197 ? 1.8918 2.2757 1.9780 0.1708  -0.0522 -0.0584 300  ASP A CG    
1583 O  OD1   . ASP A 197 ? 1.8022 2.2092 1.8959 0.1794  -0.0491 -0.0604 300  ASP A OD1   
1584 O  OD2   . ASP A 197 ? 1.9339 2.3277 2.0228 0.1619  -0.0577 -0.0551 300  ASP A OD2   
1585 N  N     . CYS A 198 ? 1.9202 2.2284 1.9785 0.2106  -0.0380 -0.0647 301  CYS A N     
1586 C  CA    . CYS A 198 ? 1.8759 2.1876 1.9325 0.2290  -0.0325 -0.0674 301  CYS A CA    
1587 C  C     . CYS A 198 ? 1.8264 2.1347 1.8801 0.2229  -0.0276 -0.0755 301  CYS A C     
1588 O  O     . CYS A 198 ? 1.9622 2.2384 2.0033 0.2255  -0.0241 -0.0804 301  CYS A O     
1589 C  CB    . CYS A 198 ? 2.0252 2.3024 2.0686 0.2447  -0.0303 -0.0654 301  CYS A CB    
1590 S  SG    . CYS A 198 ? 2.1495 2.3771 2.1788 0.2317  -0.0306 -0.0666 301  CYS A SG    
1591 N  N     . PHE A 199 ? 1.6549 1.9960 1.7197 0.2142  -0.0275 -0.0770 302  PHE A N     
1592 C  CA    . PHE A 199 ? 1.5093 1.8518 1.5714 0.2090  -0.0226 -0.0838 302  PHE A CA    
1593 C  C     . PHE A 199 ? 1.4393 1.7973 1.5025 0.2277  -0.0160 -0.0864 302  PHE A C     
1594 O  O     . PHE A 199 ? 1.4335 1.8257 1.5096 0.2367  -0.0159 -0.0825 302  PHE A O     
1595 C  CB    . PHE A 199 ? 1.3423 1.7106 1.4144 0.1906  -0.0245 -0.0835 302  PHE A CB    
1596 C  CG    . PHE A 199 ? 1.3090 1.6862 1.3794 0.1874  -0.0187 -0.0892 302  PHE A CG    
1597 C  CD1   . PHE A 199 ? 1.2592 1.6087 1.3167 0.1798  -0.0174 -0.0946 302  PHE A CD1   
1598 C  CD2   . PHE A 199 ? 1.2605 1.6749 1.3423 0.1920  -0.0146 -0.0889 302  PHE A CD2   
1599 C  CE1   . PHE A 199 ? 1.2467 1.6038 1.3006 0.1774  -0.0122 -0.0996 302  PHE A CE1   
1600 C  CE2   . PHE A 199 ? 1.2724 1.6945 1.3513 0.1894  -0.0085 -0.0936 302  PHE A CE2   
1601 C  CZ    . PHE A 199 ? 1.3713 1.7638 1.4352 0.1824  -0.0073 -0.0990 302  PHE A CZ    
1602 N  N     . THR A 200 ? 1.4037 1.7371 1.4534 0.2337  -0.0105 -0.0932 303  THR A N     
1603 C  CA    . THR A 200 ? 1.3682 1.7125 1.4160 0.2517  -0.0029 -0.0967 303  THR A CA    
1604 C  C     . THR A 200 ? 1.3085 1.6500 1.3489 0.2442  0.0019  -0.1043 303  THR A C     
1605 O  O     . THR A 200 ? 1.3170 1.6328 1.3472 0.2303  -0.0004 -0.1083 303  THR A O     
1606 C  CB    . THR A 200 ? 1.3641 1.6762 1.3981 0.2716  0.0002  -0.0980 303  THR A CB    
1607 O  OG1   . THR A 200 ? 1.2702 1.5901 1.3002 0.2892  0.0086  -0.1025 303  THR A OG1   
1608 C  CG2   . THR A 200 ? 1.4233 1.6872 1.4397 0.2628  -0.0013 -0.1028 303  THR A CG2   
1609 N  N     . MET A 201 ? 1.2808 1.6507 1.3266 0.2539  0.0087  -0.1060 304  MET A N     
1610 C  CA    . MET A 201 ? 1.2693 1.6377 1.3062 0.2492  0.0144  -0.1129 304  MET A CA    
1611 C  C     . MET A 201 ? 1.2356 1.5598 1.2496 0.2572  0.0172  -0.1211 304  MET A C     
1612 O  O     . MET A 201 ? 1.2087 1.5186 1.2158 0.2765  0.0208  -0.1221 304  MET A O     
1613 C  CB    . MET A 201 ? 1.3470 1.7557 1.3945 0.2598  0.0222  -0.1124 304  MET A CB    
1614 C  CG    . MET A 201 ? 1.4185 1.8722 1.4886 0.2482  0.0197  -0.1054 304  MET A CG    
1615 S  SD    . MET A 201 ? 1.2955 1.7506 1.3653 0.2199  0.0168  -0.1060 304  MET A SD    
1616 C  CE    . MET A 201 ? 1.3433 1.8089 1.4047 0.2247  0.0280  -0.1119 304  MET A CE    
1617 N  N     . PRO A 202 ? 1.2747 1.5759 1.2758 0.2432  0.0156  -0.1269 305  PRO A N     
1618 C  CA    . PRO A 202 ? 1.3699 1.6279 1.3487 0.2484  0.0171  -0.1354 305  PRO A CA    
1619 C  C     . PRO A 202 ? 1.4142 1.6715 1.3808 0.2661  0.0267  -0.1424 305  PRO A C     
1620 O  O     . PRO A 202 ? 1.3564 1.6494 1.3331 0.2745  0.0328  -0.1402 305  PRO A O     
1621 C  CB    . PRO A 202 ? 1.3027 1.5461 1.2745 0.2270  0.0119  -0.1390 305  PRO A CB    
1622 C  CG    . PRO A 202 ? 1.2843 1.5661 1.2703 0.2159  0.0121  -0.1344 305  PRO A CG    
1623 C  CD    . PRO A 202 ? 1.2391 1.5521 1.2453 0.2215  0.0117  -0.1257 305  PRO A CD    
1624 N  N     . SER A 203 ? 1.4435 1.6599 1.3879 0.2714  0.0282  -0.1511 306  SER A N     
1625 C  CA    . SER A 203 ? 1.5332 1.7429 1.4624 0.2899  0.0378  -0.1587 306  SER A CA    
1626 C  C     . SER A 203 ? 1.4943 1.7242 1.4195 0.2841  0.0424  -0.1632 306  SER A C     
1627 O  O     . SER A 203 ? 1.5389 1.7863 1.4617 0.2998  0.0518  -0.1653 306  SER A O     
1628 C  CB    . SER A 203 ? 1.6747 1.8315 1.5790 0.2948  0.0377  -0.1677 306  SER A CB    
1629 O  OG    . SER A 203 ? 1.7153 1.8520 1.6220 0.3016  0.0349  -0.1628 306  SER A OG    
1630 N  N     . TYR A 204 ? 1.4609 1.6891 1.3848 0.2628  0.0363  -0.1641 307  TYR A N     
1631 C  CA    . TYR A 204 ? 1.4378 1.6837 1.3563 0.2566  0.0404  -0.1675 307  TYR A CA    
1632 C  C     . TYR A 204 ? 1.4725 1.7680 1.4133 0.2540  0.0440  -0.1588 307  TYR A C     
1633 O  O     . TYR A 204 ? 1.4845 1.7976 1.4224 0.2482  0.0482  -0.1599 307  TYR A O     
1634 C  CB    . TYR A 204 ? 1.3443 1.5708 1.2528 0.2355  0.0324  -0.1711 307  TYR A CB    
1635 C  CG    . TYR A 204 ? 1.2664 1.5009 1.1922 0.2175  0.0231  -0.1627 307  TYR A CG    
1636 C  CD1   . TYR A 204 ? 1.2262 1.4948 1.1675 0.2060  0.0227  -0.1554 307  TYR A CD1   
1637 C  CD2   . TYR A 204 ? 1.2915 1.4983 1.2173 0.2118  0.0154  -0.1620 307  TYR A CD2   
1638 C  CE1   . TYR A 204 ? 1.1860 1.4597 1.1412 0.1904  0.0148  -0.1483 307  TYR A CE1   
1639 C  CE2   . TYR A 204 ? 1.2192 1.4330 1.1597 0.1963  0.0078  -0.1544 307  TYR A CE2   
1640 C  CZ    . TYR A 204 ? 1.1645 1.4112 1.1191 0.1861  0.0075  -0.1479 307  TYR A CZ    
1641 O  OH    . TYR A 204 ? 1.1311 1.3828 1.0985 0.1716  0.0004  -0.1408 307  TYR A OH    
1642 N  N     . SER A 205 ? 1.4911 1.8093 1.4533 0.2576  0.0423  -0.1501 308  SER A N     
1643 C  CA    . SER A 205 ? 1.5218 1.8881 1.5061 0.2546  0.0455  -0.1422 308  SER A CA    
1644 C  C     . SER A 205 ? 1.5131 1.9045 1.4972 0.2718  0.0575  -0.1441 308  SER A C     
1645 O  O     . SER A 205 ? 1.4985 1.9288 1.4970 0.2667  0.0620  -0.1393 308  SER A O     
1646 C  CB    . SER A 205 ? 1.4114 1.7952 1.4170 0.2555  0.0400  -0.1334 308  SER A CB    
1647 O  OG    . SER A 205 ? 1.4328 1.8085 1.4369 0.2772  0.0429  -0.1336 308  SER A OG    
1648 N  N     . ARG A 206 ? 1.6461 2.0156 1.6141 0.2918  0.0635  -0.1507 309  ARG A N     
1649 C  CA    . ARG A 206 ? 1.8395 2.2284 1.8038 0.3101  0.0760  -0.1536 309  ARG A CA    
1650 C  C     . ARG A 206 ? 1.8392 2.2037 1.7766 0.3080  0.0805  -0.1636 309  ARG A C     
1651 O  O     . ARG A 206 ? 1.8503 2.1705 1.7660 0.3059  0.0760  -0.1715 309  ARG A O     
1652 C  CB    . ARG A 206 ? 1.8619 2.2422 1.8241 0.3362  0.0807  -0.1544 309  ARG A CB    
1653 C  CG    . ARG A 206 ? 1.9548 2.3627 1.9429 0.3410  0.0765  -0.1441 309  ARG A CG    
1654 C  CD    . ARG A 206 ? 2.0923 2.4876 2.0756 0.3682  0.0810  -0.1446 309  ARG A CD    
1655 N  NE    . ARG A 206 ? 2.1278 2.4670 2.0887 0.3700  0.0764  -0.1505 309  ARG A NE    
1656 C  CZ    . ARG A 206 ? 2.1879 2.5093 2.1532 0.3650  0.0672  -0.1458 309  ARG A CZ    
1657 N  NH1   . ARG A 206 ? 2.1748 2.5286 2.1645 0.3584  0.0610  -0.1358 309  ARG A NH1   
1658 N  NH2   . ARG A 206 ? 2.1381 2.4077 2.0821 0.3662  0.0644  -0.1515 309  ARG A NH2   
1659 N  N     . ARG A 207 ? 1.7693 2.1631 1.7081 0.3079  0.0894  -0.1633 310  ARG A N     
1660 C  CA    . ARG A 207 ? 1.8145 2.1895 1.7272 0.3056  0.0939  -0.1721 310  ARG A CA    
1661 C  C     . ARG A 207 ? 1.7923 2.1328 1.6788 0.3265  0.1001  -0.1830 310  ARG A C     
1662 O  O     . ARG A 207 ? 1.7027 2.0029 1.5633 0.3219  0.0962  -0.1925 310  ARG A O     
1663 C  CB    . ARG A 207 ? 1.8083 2.2246 1.7287 0.3035  0.1040  -0.1682 310  ARG A CB    
1664 C  CG    . ARG A 207 ? 1.8524 2.2522 1.7445 0.3028  0.1098  -0.1766 310  ARG A CG    
1665 C  CD    . ARG A 207 ? 1.8871 2.3291 1.7878 0.3004  0.1206  -0.1712 310  ARG A CD    
1666 N  NE    . ARG A 207 ? 1.8329 2.3028 1.7571 0.2791  0.1151  -0.1608 310  ARG A NE    
1667 C  CZ    . ARG A 207 ? 1.8048 2.2646 1.7216 0.2586  0.1086  -0.1598 310  ARG A CZ    
1668 N  NH1   . ARG A 207 ? 1.8137 2.2390 1.7015 0.2557  0.1060  -0.1683 310  ARG A NH1   
1669 N  NH2   . ARG A 207 ? 1.7598 2.2442 1.6981 0.2407  0.1045  -0.1501 310  ARG A NH2   
1670 N  N     . THR A 221 ? 1.2527 1.9613 1.0415 0.1982  0.2820  -0.0888 324  THR A N     
1671 C  CA    . THR A 221 ? 1.3344 2.0119 1.1085 0.1802  0.2681  -0.0857 324  THR A CA    
1672 C  C     . THR A 221 ? 1.2977 1.9903 1.0704 0.1630  0.2790  -0.0713 324  THR A C     
1673 O  O     . THR A 221 ? 1.3008 2.0319 1.0936 0.1604  0.2952  -0.0627 324  THR A O     
1674 C  CB    . THR A 221 ? 1.3057 1.9746 1.1062 0.1680  0.2495  -0.0855 324  THR A CB    
1675 O  OG1   . THR A 221 ? 1.3307 2.0381 1.1707 0.1561  0.2550  -0.0752 324  THR A OG1   
1676 C  CG2   . THR A 221 ? 1.2881 1.9403 1.0898 0.1843  0.2391  -0.0988 324  THR A CG2   
1677 N  N     . LYS A 222 ? 1.2958 1.9582 1.0449 0.1514  0.2703  -0.0684 325  LYS A N     
1678 C  CA    . LYS A 222 ? 1.3200 1.9889 1.0630 0.1349  0.2793  -0.0545 325  LYS A CA    
1679 C  C     . LYS A 222 ? 1.3227 1.9763 1.0784 0.1138  0.2647  -0.0477 325  LYS A C     
1680 O  O     . LYS A 222 ? 1.2584 1.8819 1.0070 0.1139  0.2466  -0.0546 325  LYS A O     
1681 C  CB    . LYS A 222 ? 1.3416 1.9877 1.0387 0.1420  0.2846  -0.0557 325  LYS A CB    
1682 C  CG    . LYS A 222 ? 1.4474 2.1091 1.1281 0.1619  0.3021  -0.0608 325  LYS A CG    
1683 C  CD    . LYS A 222 ? 1.5597 2.1972 1.1926 0.1680  0.3064  -0.0619 325  LYS A CD    
1684 C  CE    . LYS A 222 ? 1.7417 2.3976 1.3582 0.1865  0.3268  -0.0650 325  LYS A CE    
1685 N  NZ    . LYS A 222 ? 1.7084 2.4086 1.3516 0.1798  0.3477  -0.0516 325  LYS A NZ    
1686 N  N     . SER A 223 ? 1.2891 1.9634 1.0636 0.0958  0.2732  -0.0341 326  SER A N     
1687 C  CA    . SER A 223 ? 1.2298 1.8889 1.0147 0.0755  0.2614  -0.0270 326  SER A CA    
1688 C  C     . SER A 223 ? 1.2227 1.8432 0.9707 0.0727  0.2539  -0.0251 326  SER A C     
1689 O  O     . SER A 223 ? 1.3795 1.9919 1.0954 0.0812  0.2622  -0.0248 326  SER A O     
1690 C  CB    . SER A 223 ? 1.2065 1.8949 1.0166 0.0563  0.2738  -0.0130 326  SER A CB    
1691 O  OG    . SER A 223 ? 1.1698 1.8393 0.9850 0.0368  0.2636  -0.0060 326  SER A OG    
1692 N  N     . LEU A 224 ? 1.2512 1.8484 1.0037 0.0614  0.2377  -0.0238 327  LEU A N     
1693 C  CA    . LEU A 224 ? 1.3052 1.8682 1.0263 0.0579  0.2299  -0.0204 327  LEU A CA    
1694 C  C     . LEU A 224 ? 1.3313 1.8976 1.0385 0.0467  0.2445  -0.0057 327  LEU A C     
1695 O  O     . LEU A 224 ? 1.3120 1.8564 0.9848 0.0500  0.2445  -0.0027 327  LEU A O     
1696 C  CB    . LEU A 224 ? 1.3048 1.8460 1.0377 0.0477  0.2112  -0.0208 327  LEU A CB    
1697 C  CG    . LEU A 224 ? 1.3137 1.8203 1.0182 0.0445  0.2007  -0.0172 327  LEU A CG    
1698 C  CD1   . LEU A 224 ? 1.3234 1.8093 1.0018 0.0608  0.1896  -0.0296 327  LEU A CD1   
1699 C  CD2   . LEU A 224 ? 1.1940 1.6868 0.9164 0.0304  0.1881  -0.0129 327  LEU A CD2   
1700 N  N     . TRP A 225 ? 1.3780 1.9718 1.1111 0.0335  0.2572  0.0037  328  TRP A N     
1701 C  CA    . TRP A 225 ? 1.3850 1.9814 1.1093 0.0194  0.2713  0.0189  328  TRP A CA    
1702 C  C     . TRP A 225 ? 1.3476 1.9639 1.0556 0.0278  0.2918  0.0224  328  TRP A C     
1703 O  O     . TRP A 225 ? 1.3712 1.9952 1.0749 0.0159  0.3067  0.0356  328  TRP A O     
1704 C  CB    . TRP A 225 ? 1.3546 1.9697 1.1148 -0.0015 0.2745  0.0272  328  TRP A CB    
1705 C  CG    . TRP A 225 ? 1.3916 1.9831 1.1626 -0.0118 0.2563  0.0262  328  TRP A CG    
1706 C  CD1   . TRP A 225 ? 1.3993 1.9586 1.1540 -0.0041 0.2386  0.0193  328  TRP A CD1   
1707 C  CD2   . TRP A 225 ? 1.4740 2.0727 1.2739 -0.0317 0.2544  0.0322  328  TRP A CD2   
1708 N  NE1   . TRP A 225 ? 1.3094 1.8557 1.0812 -0.0170 0.2266  0.0211  328  TRP A NE1   
1709 C  CE2   . TRP A 225 ? 1.3527 1.9215 1.1511 -0.0340 0.2358  0.0286  328  TRP A CE2   
1710 C  CE3   . TRP A 225 ? 1.4517 2.0798 1.2785 -0.0483 0.2665  0.0401  328  TRP A CE3   
1711 C  CZ2   . TRP A 225 ? 1.3839 1.9493 1.2047 -0.0512 0.2294  0.0322  328  TRP A CZ2   
1712 C  CZ3   . TRP A 225 ? 1.3937 2.0184 1.2429 -0.0666 0.2592  0.0432  328  TRP A CZ3   
1713 C  CH2   . TRP A 225 ? 1.4246 2.0172 1.2696 -0.0675 0.2410  0.0392  328  TRP A CH2   
1714 N  N     . VAL A 226 ? 1.3740 1.9979 1.0723 0.0480  0.2936  0.0109  329  VAL A N     
1715 C  CA    . VAL A 226 ? 1.3475 1.9869 1.0252 0.0590  0.3127  0.0129  329  VAL A CA    
1716 C  C     . VAL A 226 ? 1.3495 1.9582 0.9802 0.0736  0.3084  0.0075  329  VAL A C     
1717 O  O     . VAL A 226 ? 1.4592 2.0752 1.0656 0.0826  0.3240  0.0099  329  VAL A O     
1718 C  CB    . VAL A 226 ? 1.2867 1.9614 0.9870 0.0723  0.3219  0.0047  329  VAL A CB    
1719 C  CG1   . VAL A 226 ? 1.2725 1.9302 0.9564 0.0940  0.3104  -0.0124 329  VAL A CG1   
1720 C  CG2   . VAL A 226 ? 1.5525 2.2564 1.2471 0.0752  0.3470  0.0127  329  VAL A CG2   
1721 N  N     . ILE A 227 ? 1.3690 1.9449 0.9862 0.0758  0.2878  0.0006  330  ILE A N     
1722 C  CA    . ILE A 227 ? 1.4401 1.9876 1.0143 0.0893  0.2807  -0.0061 330  ILE A CA    
1723 C  C     . ILE A 227 ? 1.4453 1.9745 0.9921 0.0799  0.2839  0.0079  330  ILE A C     
1724 O  O     . ILE A 227 ? 1.4519 1.9628 1.0032 0.0677  0.2725  0.0142  330  ILE A O     
1725 C  CB    . ILE A 227 ? 1.3990 1.9220 0.9729 0.0950  0.2570  -0.0195 330  ILE A CB    
1726 C  CG1   . ILE A 227 ? 1.2806 1.8211 0.8874 0.1010  0.2536  -0.0307 330  ILE A CG1   
1727 C  CG2   . ILE A 227 ? 1.4945 1.9932 1.0255 0.1101  0.2502  -0.0289 330  ILE A CG2   
1728 C  CD1   . ILE A 227 ? 1.2938 1.8540 0.8951 0.1181  0.2677  -0.0386 330  ILE A CD1   
1729 N  N     . ASN A 228 ? 1.5137 2.0470 1.0308 0.0867  0.2999  0.0131  331  ASN A N     
1730 C  CA    . ASN A 228 ? 1.5594 2.0758 1.0471 0.0795  0.3053  0.0276  331  ASN A CA    
1731 C  C     . ASN A 228 ? 1.4998 1.9855 0.9450 0.0924  0.2913  0.0205  331  ASN A C     
1732 O  O     . ASN A 228 ? 1.5342 2.0182 0.9455 0.1058  0.2992  0.0173  331  ASN A O     
1733 C  CB    . ASN A 228 ? 1.4834 2.0223 0.9627 0.0785  0.3314  0.0387  331  ASN A CB    
1734 C  CG    . ASN A 228 ? 1.5213 2.0447 0.9777 0.0671  0.3391  0.0567  331  ASN A CG    
1735 O  OD1   . ASN A 228 ? 1.4400 1.9335 0.8794 0.0638  0.3246  0.0600  331  ASN A OD1   
1736 N  ND2   . ASN A 228 ? 1.6797 2.2235 1.1354 0.0614  0.3625  0.0690  331  ASN A ND2   
1737 N  N     . SER A 229 ? 1.5119 1.9739 0.9589 0.0882  0.2703  0.0179  332  SER A N     
1738 C  CA    . SER A 229 ? 1.4462 1.8801 0.8571 0.0979  0.2541  0.0119  332  SER A CA    
1739 C  C     . SER A 229 ? 1.4871 1.9018 0.9123 0.0883  0.2342  0.0137  332  SER A C     
1740 O  O     . SER A 229 ? 1.4786 1.9009 0.9406 0.0766  0.2320  0.0161  332  SER A O     
1741 C  CB    . SER A 229 ? 1.4500 1.8823 0.8479 0.1151  0.2467  -0.0075 332  SER A CB    
1742 O  OG    . SER A 229 ? 1.4860 1.9209 0.9168 0.1142  0.2337  -0.0192 332  SER A OG    
1743 N  N     . ALA A 230 ? 1.4566 1.8471 0.8520 0.0939  0.2195  0.0124  333  ALA A N     
1744 C  CA    . ALA A 230 ? 1.3481 1.7201 0.7536 0.0874  0.1999  0.0135  333  ALA A CA    
1745 C  C     . ALA A 230 ? 1.4549 1.8217 0.8693 0.0949  0.1808  -0.0049 333  ALA A C     
1746 O  O     . ALA A 230 ? 1.5378 1.9092 0.9413 0.1065  0.1813  -0.0184 333  ALA A O     
1747 C  CB    . ALA A 230 ? 1.3578 1.7083 0.7278 0.0890  0.1943  0.0241  333  ALA A CB    
1748 N  N     . LEU A 231 ? 1.3964 1.7521 0.8302 0.0880  0.1645  -0.0051 334  LEU A N     
1749 C  CA    . LEU A 231 ? 1.3589 1.7085 0.8034 0.0931  0.1461  -0.0210 334  LEU A CA    
1750 C  C     . LEU A 231 ? 1.3779 1.7112 0.7860 0.1035  0.1326  -0.0285 334  LEU A C     
1751 O  O     . LEU A 231 ? 1.4332 1.7537 0.8206 0.1027  0.1265  -0.0192 334  LEU A O     
1752 C  CB    . LEU A 231 ? 1.3357 1.6791 0.8111 0.0824  0.1338  -0.0179 334  LEU A CB    
1753 C  CG    . LEU A 231 ? 1.2867 1.6226 0.7757 0.0855  0.1144  -0.0323 334  LEU A CG    
1754 C  CD1   . LEU A 231 ? 1.2512 1.6001 0.7580 0.0905  0.1183  -0.0460 334  LEU A CD1   
1755 C  CD2   . LEU A 231 ? 1.2251 1.5540 0.7405 0.0750  0.1039  -0.0264 334  LEU A CD2   
1756 N  N     . ARG A 232 ? 1.2971 1.6304 0.6966 0.1136  0.1278  -0.0453 335  ARG A N     
1757 C  CA    . ARG A 232 ? 1.3722 1.6906 0.7384 0.1227  0.1134  -0.0552 335  ARG A CA    
1758 C  C     . ARG A 232 ? 1.3586 1.6718 0.7386 0.1257  0.0987  -0.0734 335  ARG A C     
1759 O  O     . ARG A 232 ? 1.3868 1.7081 0.7797 0.1299  0.1061  -0.0831 335  ARG A O     
1760 C  CB    . ARG A 232 ? 1.5362 1.8562 0.8633 0.1337  0.1256  -0.0574 335  ARG A CB    
1761 C  CG    . ARG A 232 ? 1.5174 1.8388 0.8231 0.1317  0.1388  -0.0393 335  ARG A CG    
1762 C  CD    . ARG A 232 ? 1.5865 1.9095 0.8525 0.1435  0.1509  -0.0425 335  ARG A CD    
1763 N  NE    . ARG A 232 ? 1.6739 2.0000 0.9214 0.1414  0.1672  -0.0243 335  ARG A NE    
1764 C  CZ    . ARG A 232 ? 1.6629 1.9930 0.8780 0.1501  0.1825  -0.0226 335  ARG A CZ    
1765 N  NH1   . ARG A 232 ? 1.5149 1.8461 0.7110 0.1622  0.1839  -0.0385 335  ARG A NH1   
1766 N  NH2   . ARG A 232 ? 1.6957 2.0276 0.8959 0.1467  0.1974  -0.0045 335  ARG A NH2   
1767 N  N     . ILE A 233 ? 1.3732 1.6731 0.7503 0.1239  0.0782  -0.0775 336  ILE A N     
1768 C  CA    . ILE A 233 ? 1.4238 1.7161 0.8121 0.1252  0.0627  -0.0942 336  ILE A CA    
1769 C  C     . ILE A 233 ? 1.4630 1.7421 0.8153 0.1318  0.0483  -0.1044 336  ILE A C     
1770 O  O     . ILE A 233 ? 1.4962 1.7707 0.8278 0.1314  0.0413  -0.0961 336  ILE A O     
1771 C  CB    . ILE A 233 ? 1.3505 1.6411 0.7744 0.1150  0.0504  -0.0905 336  ILE A CB    
1772 C  CG1   . ILE A 233 ? 1.3414 1.6450 0.7989 0.1078  0.0642  -0.0804 336  ILE A CG1   
1773 C  CG2   . ILE A 233 ? 1.2604 1.5427 0.6956 0.1159  0.0353  -0.1072 336  ILE A CG2   
1774 C  CD1   . ILE A 233 ? 1.1834 1.4849 0.6733 0.0979  0.0540  -0.0752 336  ILE A CD1   
1775 N  N     . LYS A 234 ? 1.4258 1.6980 0.7695 0.1381  0.0439  -0.1225 337  LYS A N     
1776 C  CA    . LYS A 234 ? 1.4881 1.7472 0.7963 0.1439  0.0304  -0.1350 337  LYS A CA    
1777 C  C     . LYS A 234 ? 1.4466 1.6959 0.7705 0.1380  0.0087  -0.1455 337  LYS A C     
1778 O  O     . LYS A 234 ? 1.4839 1.7310 0.8336 0.1358  0.0076  -0.1543 337  LYS A O     
1779 C  CB    . LYS A 234 ? 1.5565 1.8117 0.8396 0.1551  0.0411  -0.1489 337  LYS A CB    
1780 C  CG    . LYS A 234 ? 1.5381 1.7777 0.7814 0.1610  0.0277  -0.1638 337  LYS A CG    
1781 C  CD    . LYS A 234 ? 1.5668 1.8004 0.7872 0.1726  0.0396  -0.1784 337  LYS A CD    
1782 C  CE    . LYS A 234 ? 1.6329 1.8480 0.8139 0.1774  0.0251  -0.1958 337  LYS A CE    
1783 N  NZ    . LYS A 234 ? 1.8261 2.0321 0.9848 0.1894  0.0368  -0.2112 337  LYS A NZ    
1784 N  N     . ILE A 235 ? 1.4519 1.6962 0.7607 0.1354  -0.0083 -0.1440 338  ILE A N     
1785 C  CA    . ILE A 235 ? 1.4272 1.6633 0.7452 0.1299  -0.0300 -0.1550 338  ILE A CA    
1786 C  C     . ILE A 235 ? 1.5320 1.7557 0.8129 0.1357  -0.0388 -0.1727 338  ILE A C     
1787 O  O     . ILE A 235 ? 1.5355 1.7585 0.7794 0.1419  -0.0380 -0.1711 338  ILE A O     
1788 C  CB    . ILE A 235 ? 1.3675 1.6082 0.6942 0.1235  -0.0441 -0.1425 338  ILE A CB    
1789 C  CG1   . ILE A 235 ? 1.5310 1.7789 0.9006 0.1157  -0.0401 -0.1304 338  ILE A CG1   
1790 C  CG2   . ILE A 235 ? 1.3979 1.6321 0.7185 0.1200  -0.0674 -0.1547 338  ILE A CG2   
1791 C  CD1   . ILE A 235 ? 1.5094 1.7657 0.8841 0.1163  -0.0207 -0.1136 338  ILE A CD1   
1792 N  N     . LEU A 236 ? 1.5416 1.7542 0.8307 0.1337  -0.0471 -0.1898 339  LEU A N     
1793 C  CA    . LEU A 236 ? 1.6141 1.8118 0.8681 0.1386  -0.0547 -0.2087 339  LEU A CA    
1794 C  C     . LEU A 236 ? 1.7169 1.9092 0.9654 0.1309  -0.0798 -0.2162 339  LEU A C     
1795 O  O     . LEU A 236 ? 1.7823 1.9781 1.0045 0.1321  -0.0891 -0.2127 339  LEU A O     
1796 C  CB    . LEU A 236 ? 1.6292 1.8148 0.8904 0.1422  -0.0470 -0.2241 339  LEU A CB    
1797 C  CG    . LEU A 236 ? 1.7114 1.8989 0.9586 0.1541  -0.0237 -0.2241 339  LEU A CG    
1798 C  CD1   . LEU A 236 ? 1.5308 1.7377 0.8078 0.1533  -0.0069 -0.2052 339  LEU A CD1   
1799 C  CD2   . LEU A 236 ? 1.7979 1.9694 1.0445 0.1596  -0.0195 -0.2421 339  LEU A CD2   
1800 N  N     . CYS A 237 ? 1.7478 1.9324 1.0209 0.1231  -0.0907 -0.2264 340  CYS A N     
1801 C  CA    . CYS A 237 ? 1.8902 2.0708 1.1618 0.1143  -0.1144 -0.2349 340  CYS A CA    
1802 C  C     . CYS A 237 ? 1.8852 2.0697 1.2026 0.1037  -0.1215 -0.2312 340  CYS A C     
1803 O  O     . CYS A 237 ? 1.7704 1.9600 1.1176 0.1038  -0.1086 -0.2221 340  CYS A O     
1804 C  CB    . CYS A 237 ? 1.9401 2.1003 1.1812 0.1155  -0.1221 -0.2579 340  CYS A CB    
1805 S  SG    . CYS A 237 ? 1.9423 2.0828 1.1987 0.1168  -0.1117 -0.2730 340  CYS A SG    
1806 N  N     . ALA A 238 ? 1.9723 2.1552 1.2950 0.0944  -0.1422 -0.2382 341  ALA A N     
1807 C  CA    . ALA A 238 ? 1.9661 2.1529 1.3305 0.0840  -0.1501 -0.2352 341  ALA A CA    
1808 C  C     . ALA A 238 ? 2.0826 2.2578 1.4444 0.0746  -0.1688 -0.2528 341  ALA A C     
1809 O  O     . ALA A 238 ? 2.1921 2.3688 1.5295 0.0722  -0.1841 -0.2591 341  ALA A O     
1810 C  CB    . ALA A 238 ? 1.8671 2.0741 1.2515 0.0808  -0.1557 -0.2161 341  ALA A CB    
1811 N  N     . THR A 239 ? 2.0027 2.1663 1.3890 0.0689  -0.1677 -0.2604 342  THR A N     
1812 C  CA    . THR A 239 ? 2.0583 2.2090 1.4468 0.0581  -0.1840 -0.2764 342  THR A CA    
1813 C  C     . THR A 239 ? 2.1460 2.3078 1.5769 0.0468  -0.1930 -0.2683 342  THR A C     
1814 O  O     . THR A 239 ? 2.1098 2.2859 1.5679 0.0484  -0.1851 -0.2517 342  THR A O     
1815 C  CB    . THR A 239 ? 2.0548 2.1789 1.4338 0.0608  -0.1755 -0.2931 342  THR A CB    
1816 O  OG1   . THR A 239 ? 2.1512 2.2613 1.5378 0.0483  -0.1905 -0.3070 342  THR A OG1   
1817 C  CG2   . THR A 239 ? 1.9848 2.1088 1.3908 0.0666  -0.1566 -0.2844 342  THR A CG2   
1818 N  N     . TYR A 240 ? 2.4625 2.6174 1.8981 0.0349  -0.2097 -0.2804 343  TYR A N     
1819 C  CA    . TYR A 240 ? 2.5016 2.6668 1.9758 0.0230  -0.2198 -0.2747 343  TYR A CA    
1820 C  C     . TYR A 240 ? 2.4453 2.6388 1.9349 0.0229  -0.2260 -0.2564 343  TYR A C     
1821 O  O     . TYR A 240 ? 2.3987 2.6036 1.9235 0.0167  -0.2288 -0.2468 343  TYR A O     
1822 C  CB    . TYR A 240 ? 2.4601 2.6162 1.9654 0.0227  -0.2067 -0.2712 343  TYR A CB    
1823 C  CG    . TYR A 240 ? 2.6469 2.7741 2.1431 0.0215  -0.2026 -0.2887 343  TYR A CG    
1824 C  CD1   . TYR A 240 ? 2.6364 2.7511 2.1435 0.0083  -0.2148 -0.3001 343  TYR A CD1   
1825 C  CD2   . TYR A 240 ? 2.7272 2.8394 2.2042 0.0337  -0.1860 -0.2933 343  TYR A CD2   
1826 C  CE1   . TYR A 240 ? 2.7688 2.8537 2.2658 0.0075  -0.2105 -0.3157 343  TYR A CE1   
1827 C  CE2   . TYR A 240 ? 2.8415 2.9259 2.3091 0.0344  -0.1816 -0.3089 343  TYR A CE2   
1828 C  CZ    . TYR A 240 ? 2.8861 2.9554 2.3629 0.0213  -0.1939 -0.3200 343  TYR A CZ    
1829 O  OH    . TYR A 240 ? 2.9089 2.9472 2.3747 0.0223  -0.1891 -0.3352 343  TYR A OH    
1830 N  N     . VAL A 241 ? 2.2163 2.4204 1.6789 0.0305  -0.2277 -0.2511 344  VAL A N     
1831 C  CA    . VAL A 241 ? 2.1569 2.3858 1.6313 0.0325  -0.2323 -0.2329 344  VAL A CA    
1832 C  C     . VAL A 241 ? 2.2296 2.4734 1.7179 0.0214  -0.2543 -0.2348 344  VAL A C     
1833 O  O     . VAL A 241 ? 2.1572 2.4193 1.6745 0.0191  -0.2580 -0.2209 344  VAL A O     
1834 C  CB    . VAL A 241 ? 2.0923 2.3264 1.5316 0.0443  -0.2273 -0.2262 344  VAL A CB    
1835 C  CG1   . VAL A 241 ? 2.1336 2.3581 1.5322 0.0444  -0.2378 -0.2432 344  VAL A CG1   
1836 C  CG2   . VAL A 241 ? 2.0147 2.2721 1.4629 0.0469  -0.2334 -0.2076 344  VAL A CG2   
1837 N  N     . ASN A 242 ? 2.3072 2.5436 1.7754 0.0142  -0.2689 -0.2522 345  ASN A N     
1838 C  CA    . ASN A 242 ? 2.2665 2.5181 1.7471 0.0019  -0.2910 -0.2563 345  ASN A CA    
1839 C  C     . ASN A 242 ? 2.2431 2.5240 1.7262 0.0065  -0.3005 -0.2402 345  ASN A C     
1840 O  O     . ASN A 242 ? 2.1992 2.4982 1.7161 0.0043  -0.3026 -0.2267 345  ASN A O     
1841 C  CB    . ASN A 242 ? 2.2517 2.5023 1.7741 -0.0099 -0.2923 -0.2567 345  ASN A CB    
1842 C  CG    . ASN A 242 ? 2.2866 2.5512 1.8221 -0.0248 -0.3145 -0.2637 345  ASN A CG    
1843 O  OD1   . ASN A 242 ? 2.3640 2.6135 1.8881 -0.0354 -0.3237 -0.2821 345  ASN A OD1   
1844 N  ND2   . ASN A 242 ? 2.2429 2.5366 1.8027 -0.0257 -0.3230 -0.2491 345  ASN A ND2   
1845 N  N     . LYS A 250 ? 1.9777 2.3468 1.2889 0.1078  -0.2896 -0.1134 353  LYS A N     
1846 C  CA    . LYS A 250 ? 1.9347 2.2824 1.2372 0.1025  -0.2772 -0.1294 353  LYS A CA    
1847 C  C     . LYS A 250 ? 1.8641 2.1998 1.1973 0.1000  -0.2564 -0.1232 353  LYS A C     
1848 O  O     . LYS A 250 ? 1.8043 2.1483 1.1722 0.0980  -0.2558 -0.1118 353  LYS A O     
1849 C  CB    . LYS A 250 ? 1.8887 2.2247 1.1417 0.1118  -0.2692 -0.1316 353  LYS A CB    
1850 C  CG    . LYS A 250 ? 1.8765 2.2144 1.1110 0.1251  -0.2585 -0.1095 353  LYS A CG    
1851 C  CD    . LYS A 250 ? 2.0697 2.3995 1.2521 0.1341  -0.2551 -0.1126 353  LYS A CD    
1852 C  CE    . LYS A 250 ? 1.9668 2.3071 1.1242 0.1326  -0.2796 -0.1264 353  LYS A CE    
1853 N  NZ    . LYS A 250 ? 1.8065 2.1379 0.9105 0.1417  -0.2763 -0.1305 353  LYS A NZ    
1854 N  N     . ILE A 251 ? 1.8489 2.1659 1.1692 0.1005  -0.2394 -0.1308 354  ILE A N     
1855 C  CA    . ILE A 251 ? 1.8571 2.1636 1.2059 0.0973  -0.2206 -0.1275 354  ILE A CA    
1856 C  C     . ILE A 251 ? 1.7575 2.0510 1.0824 0.1051  -0.1986 -0.1223 354  ILE A C     
1857 O  O     . ILE A 251 ? 1.8128 2.1001 1.0999 0.1104  -0.1971 -0.1296 354  ILE A O     
1858 C  CB    . ILE A 251 ? 1.7400 2.0384 1.1103 0.0862  -0.2237 -0.1462 354  ILE A CB    
1859 N  N     . TYR A 252 ? 1.6609 1.9508 1.0083 0.1054  -0.1814 -0.1098 355  TYR A N     
1860 C  CA    . TYR A 252 ? 1.5853 1.8649 0.9181 0.1105  -0.1590 -0.1043 355  TYR A CA    
1861 C  C     . TYR A 252 ? 1.6662 1.9412 1.0354 0.1046  -0.1449 -0.1027 355  TYR A C     
1862 O  O     . TYR A 252 ? 1.6341 1.9129 1.0373 0.0977  -0.1521 -0.1036 355  TYR A O     
1863 C  CB    . TYR A 252 ? 1.6232 1.9053 0.9355 0.1193  -0.1515 -0.0842 355  TYR A CB    
1864 C  CG    . TYR A 252 ? 1.7157 2.0035 1.0554 0.1186  -0.1517 -0.0663 355  TYR A CG    
1865 C  CD1   . TYR A 252 ? 1.7451 2.0268 1.1063 0.1163  -0.1337 -0.0556 355  TYR A CD1   
1866 C  CD2   . TYR A 252 ? 1.7926 2.0921 1.1362 0.1205  -0.1698 -0.0605 355  TYR A CD2   
1867 C  CE1   . TYR A 252 ? 1.6990 1.9832 1.0829 0.1159  -0.1334 -0.0401 355  TYR A CE1   
1868 C  CE2   . TYR A 252 ? 1.8801 2.1837 1.2475 0.1214  -0.1691 -0.0442 355  TYR A CE2   
1869 C  CZ    . TYR A 252 ? 1.8482 2.1425 1.2346 0.1191  -0.1506 -0.0344 355  TYR A CZ    
1870 O  OH    . TYR A 252 ? 1.7587 2.0543 1.1665 0.1201  -0.1496 -0.0190 355  TYR A OH    
1871 N  N     . VAL A 253 ? 1.6370 1.9047 0.9989 0.1074  -0.1247 -0.1001 356  VAL A N     
1872 C  CA    . VAL A 253 ? 1.5421 1.8067 0.9356 0.1025  -0.1103 -0.0983 356  VAL A CA    
1873 C  C     . VAL A 253 ? 1.5544 1.8196 0.9497 0.1049  -0.0941 -0.0788 356  VAL A C     
1874 O  O     . VAL A 253 ? 1.5163 1.7794 0.8830 0.1110  -0.0831 -0.0726 356  VAL A O     
1875 C  CB    . VAL A 253 ? 1.4871 1.7443 0.8751 0.1029  -0.1002 -0.1135 356  VAL A CB    
1876 C  CG1   . VAL A 253 ? 1.2709 1.5277 0.6889 0.0994  -0.0836 -0.1089 356  VAL A CG1   
1877 C  CG2   . VAL A 253 ? 1.5104 1.7633 0.9012 0.0988  -0.1158 -0.1330 356  VAL A CG2   
1878 N  N     . ARG A 254 ? 1.5405 1.8075 0.9684 0.0997  -0.0923 -0.0691 357  ARG A N     
1879 C  CA    . ARG A 254 ? 1.4749 1.7399 0.9081 0.0999  -0.0773 -0.0512 357  ARG A CA    
1880 C  C     . ARG A 254 ? 1.4099 1.6733 0.8682 0.0941  -0.0620 -0.0533 357  ARG A C     
1881 O  O     . ARG A 254 ? 1.4900 1.7544 0.9769 0.0886  -0.0668 -0.0614 357  ARG A O     
1882 C  CB    . ARG A 254 ? 1.4578 1.7246 0.9075 0.0989  -0.0859 -0.0382 357  ARG A CB    
1883 C  CG    . ARG A 254 ? 1.4836 1.7448 0.9323 0.0998  -0.0717 -0.0190 357  ARG A CG    
1884 C  CD    . ARG A 254 ? 1.5135 1.7750 0.9721 0.1016  -0.0815 -0.0067 357  ARG A CD    
1885 N  NE    . ARG A 254 ? 1.4975 1.7517 0.9351 0.1072  -0.0727 0.0116  357  ARG A NE    
1886 C  CZ    . ARG A 254 ? 1.5128 1.7575 0.9594 0.1038  -0.0577 0.0242  357  ARG A CZ    
1887 N  NH1   . ARG A 254 ? 1.5541 1.7972 1.0304 0.0950  -0.0500 0.0207  357  ARG A NH1   
1888 N  NH2   . ARG A 254 ? 1.4055 1.6412 0.8296 0.1091  -0.0503 0.0407  357  ARG A NH2   
1889 N  N     . THR A 255 ? 1.3807 1.6426 0.8285 0.0953  -0.0437 -0.0457 358  THR A N     
1890 C  CA    . THR A 255 ? 1.4578 1.7213 0.9276 0.0902  -0.0284 -0.0471 358  THR A CA    
1891 C  C     . THR A 255 ? 1.4490 1.7107 0.9318 0.0854  -0.0166 -0.0298 358  THR A C     
1892 O  O     . THR A 255 ? 1.4275 1.6844 0.9005 0.0869  -0.0192 -0.0167 358  THR A O     
1893 C  CB    . THR A 255 ? 1.4125 1.6783 0.8619 0.0947  -0.0157 -0.0544 358  THR A CB    
1894 O  OG1   . THR A 255 ? 1.4596 1.7243 0.8806 0.0987  -0.0050 -0.0420 358  THR A OG1   
1895 C  CG2   . THR A 255 ? 1.4130 1.6770 0.8450 0.0997  -0.0275 -0.0720 358  THR A CG2   
1896 N  N     . GLY A 256 ? 1.3669 1.6321 0.8714 0.0796  -0.0035 -0.0301 359  GLY A N     
1897 C  CA    . GLY A 256 ? 1.1703 1.4334 0.6879 0.0732  0.0087  -0.0155 359  GLY A CA    
1898 C  C     . GLY A 256 ? 1.2652 1.5357 0.8090 0.0666  0.0204  -0.0194 359  GLY A C     
1899 O  O     . GLY A 256 ? 1.3678 1.6429 0.9291 0.0664  0.0151  -0.0324 359  GLY A O     
1900 N  N     . ILE A 257 ? 1.2514 1.5232 0.7981 0.0610  0.0362  -0.0082 360  ILE A N     
1901 C  CA    . ILE A 257 ? 1.2505 1.5322 0.8228 0.0540  0.0477  -0.0104 360  ILE A CA    
1902 C  C     . ILE A 257 ? 1.2972 1.5729 0.8913 0.0444  0.0488  -0.0002 360  ILE A C     
1903 O  O     . ILE A 257 ? 1.2723 1.5399 0.8563 0.0405  0.0563  0.0137  360  ILE A O     
1904 C  CB    . ILE A 257 ? 1.1787 1.4700 0.7382 0.0541  0.0660  -0.0068 360  ILE A CB    
1905 C  CG1   . ILE A 257 ? 1.3805 1.6744 0.9118 0.0651  0.0650  -0.0160 360  ILE A CG1   
1906 C  CG2   . ILE A 257 ? 1.0924 1.3982 0.6806 0.0479  0.0762  -0.0106 360  ILE A CG2   
1907 C  CD1   . ILE A 257 ? 1.2966 1.5945 0.8378 0.0703  0.0555  -0.0337 360  ILE A CD1   
1908 N  N     . TYR A 258 ? 1.3319 1.6097 0.9545 0.0406  0.0418  -0.0070 361  TYR A N     
1909 C  CA    . TYR A 258 ? 1.2849 1.5562 0.9285 0.0320  0.0415  0.0007  361  TYR A CA    
1910 C  C     . TYR A 258 ? 1.1908 1.4736 0.8611 0.0241  0.0501  -0.0026 361  TYR A C     
1911 O  O     . TYR A 258 ? 1.1105 1.4060 0.7895 0.0271  0.0511  -0.0134 361  TYR A O     
1912 C  CB    . TYR A 258 ? 1.2526 1.5161 0.9069 0.0343  0.0248  -0.0030 361  TYR A CB    
1913 C  CG    . TYR A 258 ? 1.4556 1.7091 1.0873 0.0411  0.0154  0.0025  361  TYR A CG    
1914 C  CD1   . TYR A 258 ? 1.3474 1.6042 0.9601 0.0496  0.0071  -0.0053 361  TYR A CD1   
1915 C  CD2   . TYR A 258 ? 1.3704 1.6113 0.9990 0.0395  0.0148  0.0155  361  TYR A CD2   
1916 C  CE1   . TYR A 258 ? 1.3410 1.5914 0.9335 0.0559  -0.0025 -0.0001 361  TYR A CE1   
1917 C  CE2   . TYR A 258 ? 1.3715 1.6052 0.9800 0.0471  0.0060  0.0213  361  TYR A CE2   
1918 C  CZ    . TYR A 258 ? 1.4377 1.6775 1.0288 0.0551  -0.0030 0.0136  361  TYR A CZ    
1919 O  OH    . TYR A 258 ? 1.4795 1.7147 1.0510 0.0628  -0.0128 0.0194  361  TYR A OH    
1920 N  N     . HIS A 259 ? 1.3164 1.5942 0.9985 0.0143  0.0561  0.0069  362  HIS A N     
1921 C  CA    . HIS A 259 ? 1.3201 1.6081 1.0298 0.0054  0.0615  0.0044  362  HIS A CA    
1922 C  C     . HIS A 259 ? 1.2811 1.5586 1.0090 0.0016  0.0515  0.0045  362  HIS A C     
1923 O  O     . HIS A 259 ? 1.3500 1.6198 1.0859 -0.0076 0.0557  0.0123  362  HIS A O     
1924 C  CB    . HIS A 259 ? 1.2808 1.5730 0.9894 -0.0047 0.0777  0.0145  362  HIS A CB    
1925 C  CG    . HIS A 259 ? 1.3359 1.6418 1.0727 -0.0146 0.0831  0.0121  362  HIS A CG    
1926 N  ND1   . HIS A 259 ? 1.3233 1.6205 1.0734 -0.0259 0.0840  0.0182  362  HIS A ND1   
1927 C  CD2   . HIS A 259 ? 1.3192 1.6472 1.0727 -0.0142 0.0877  0.0041  362  HIS A CD2   
1928 C  CE1   . HIS A 259 ? 1.2108 1.5252 0.9848 -0.0330 0.0880  0.0139  362  HIS A CE1   
1929 N  NE2   . HIS A 259 ? 1.1842 1.5184 0.9614 -0.0256 0.0904  0.0058  362  HIS A NE2   
1930 N  N     . GLY A 260 ? 1.3199 1.5958 1.0530 0.0087  0.0382  -0.0044 363  GLY A N     
1931 C  CA    . GLY A 260 ? 1.2978 1.5649 1.0476 0.0066  0.0284  -0.0048 363  GLY A CA    
1932 C  C     . GLY A 260 ? 1.3403 1.5896 1.0781 0.0069  0.0248  0.0059  363  GLY A C     
1933 O  O     . GLY A 260 ? 1.5121 1.7517 1.2580 -0.0001 0.0278  0.0129  363  GLY A O     
1934 N  N     . GLY A 261 ? 1.2632 1.5078 0.9809 0.0153  0.0182  0.0072  364  GLY A N     
1935 C  CA    . GLY A 261 ? 1.2787 1.5082 0.9844 0.0182  0.0137  0.0174  364  GLY A CA    
1936 C  C     . GLY A 261 ? 1.3048 1.5247 0.9872 0.0172  0.0242  0.0302  364  GLY A C     
1937 O  O     . GLY A 261 ? 1.2881 1.4963 0.9543 0.0229  0.0200  0.0387  364  GLY A O     
1938 N  N     . GLU A 262 ? 1.3611 1.5861 1.0417 0.0101  0.0379  0.0324  365  GLU A N     
1939 C  CA    . GLU A 262 ? 1.4326 1.6483 1.0905 0.0081  0.0494  0.0448  365  GLU A CA    
1940 C  C     . GLU A 262 ? 1.5157 1.7415 1.1522 0.0150  0.0525  0.0423  365  GLU A C     
1941 O  O     . GLU A 262 ? 1.4091 1.6515 1.0533 0.0139  0.0570  0.0334  365  GLU A O     
1942 C  CB    . GLU A 262 ? 1.5239 1.7392 1.1926 -0.0054 0.0635  0.0497  365  GLU A CB    
1943 C  CG    . GLU A 262 ? 1.8533 2.0543 1.5375 -0.0130 0.0620  0.0536  365  GLU A CG    
1944 C  CD    . GLU A 262 ? 1.8623 2.0666 1.5605 -0.0278 0.0741  0.0554  365  GLU A CD    
1945 O  OE1   . GLU A 262 ? 1.6377 1.8633 1.3480 -0.0313 0.0790  0.0482  365  GLU A OE1   
1946 O  OE2   . GLU A 262 ? 1.7569 1.9428 1.4538 -0.0358 0.0787  0.0638  365  GLU A OE2   
1947 N  N     . PRO A 263 ? 1.4063 1.6230 1.0154 0.0231  0.0502  0.0497  366  PRO A N     
1948 C  CA    . PRO A 263 ? 1.3596 1.5852 0.9454 0.0301  0.0530  0.0469  366  PRO A CA    
1949 C  C     . PRO A 263 ? 1.3496 1.5800 0.9285 0.0232  0.0716  0.0526  366  PRO A C     
1950 O  O     . PRO A 263 ? 1.3393 1.5573 0.9107 0.0167  0.0819  0.0657  366  PRO A O     
1951 C  CB    . PRO A 263 ? 1.3615 1.5743 0.9200 0.0396  0.0459  0.0559  366  PRO A CB    
1952 C  CG    . PRO A 263 ? 1.3549 1.5567 0.9276 0.0399  0.0355  0.0593  366  PRO A CG    
1953 C  CD    . PRO A 263 ? 1.3840 1.5827 0.9816 0.0278  0.0437  0.0602  366  PRO A CD    
1954 N  N     . LEU A 264 ? 1.3272 1.5753 0.9088 0.0245  0.0762  0.0427  367  LEU A N     
1955 C  CA    . LEU A 264 ? 1.3559 1.6130 0.9323 0.0187  0.0943  0.0475  367  LEU A CA    
1956 C  C     . LEU A 264 ? 1.3653 1.6166 0.9055 0.0254  0.1010  0.0560  367  LEU A C     
1957 O  O     . LEU A 264 ? 1.3540 1.6022 0.8841 0.0190  0.1163  0.0676  367  LEU A O     
1958 C  CB    . LEU A 264 ? 1.3320 1.6113 0.9252 0.0193  0.0976  0.0342  367  LEU A CB    
1959 C  CG    . LEU A 264 ? 1.2311 1.5186 0.8604 0.0115  0.0946  0.0274  367  LEU A CG    
1960 C  CD1   . LEU A 264 ? 1.1272 1.4355 0.7698 0.0157  0.0963  0.0141  367  LEU A CD1   
1961 C  CD2   . LEU A 264 ? 1.2024 1.4884 0.8449 -0.0029 0.1065  0.0380  367  LEU A CD2   
1962 N  N     . CYS A 265 ? 1.3954 1.6451 0.9152 0.0377  0.0896  0.0505  368  CYS A N     
1963 C  CA    . CYS A 265 ? 1.4717 1.7148 0.9543 0.0457  0.0932  0.0583  368  CYS A CA    
1964 C  C     . CYS A 265 ? 1.5334 1.7667 1.0012 0.0559  0.0749  0.0573  368  CYS A C     
1965 O  O     . CYS A 265 ? 1.4704 1.7046 0.9574 0.0568  0.0602  0.0489  368  CYS A O     
1966 C  CB    . CYS A 265 ? 1.4481 1.7064 0.9162 0.0512  0.1014  0.0504  368  CYS A CB    
1967 S  SG    . CYS A 265 ? 1.4881 1.7584 0.9637 0.0602  0.0864  0.0283  368  CYS A SG    
1968 N  N     . ASP A 266 ? 1.5463 1.7711 0.9798 0.0636  0.0758  0.0665  369  ASP A N     
1969 C  CA    . ASP A 266 ? 1.5636 1.7814 0.9813 0.0738  0.0584  0.0670  369  ASP A CA    
1970 C  C     . ASP A 266 ? 1.5629 1.7931 0.9801 0.0807  0.0441  0.0491  369  ASP A C     
1971 O  O     . ASP A 266 ? 1.6534 1.8934 1.0613 0.0829  0.0501  0.0399  369  ASP A O     
1972 C  CB    . ASP A 266 ? 1.6622 1.8690 1.0411 0.0812  0.0633  0.0814  369  ASP A CB    
1973 C  CG    . ASP A 266 ? 1.8198 2.0094 1.1966 0.0748  0.0759  0.0999  369  ASP A CG    
1974 O  OD1   . ASP A 266 ? 1.8632 2.0537 1.2546 0.0634  0.0917  0.1028  369  ASP A OD1   
1975 O  OD2   . ASP A 266 ? 1.9440 2.1190 1.3046 0.0812  0.0700  0.1117  369  ASP A OD2   
1976 N  N     . ASN A 267 ? 1.5611 1.7905 0.9884 0.0840  0.0257  0.0440  370  ASN A N     
1977 C  CA    . ASN A 267 ? 1.5164 1.7554 0.9441 0.0890  0.0108  0.0270  370  ASN A CA    
1978 C  C     . ASN A 267 ? 1.5457 1.7855 0.9344 0.0992  0.0066  0.0258  370  ASN A C     
1979 O  O     . ASN A 267 ? 1.5276 1.7600 0.8924 0.1049  0.0054  0.0387  370  ASN A O     
1980 C  CB    . ASN A 267 ? 1.4658 1.7046 0.9144 0.0890  -0.0075 0.0235  370  ASN A CB    
1981 C  CG    . ASN A 267 ? 1.5427 1.7787 1.0266 0.0799  -0.0036 0.0263  370  ASN A CG    
1982 O  OD1   . ASN A 267 ? 1.6951 1.9249 1.1897 0.0798  -0.0106 0.0339  370  ASN A OD1   
1983 N  ND2   . ASN A 267 ? 1.4990 1.7400 1.0004 0.0727  0.0078  0.0204  370  ASN A ND2   
1984 N  N     . VAL A 268 ? 1.5601 1.8078 0.9409 0.1020  0.0045  0.0102  371  VAL A N     
1985 C  CA    . VAL A 268 ? 1.6139 1.8623 0.9567 0.1114  -0.0004 0.0062  371  VAL A CA    
1986 C  C     . VAL A 268 ? 1.6192 1.8719 0.9641 0.1142  -0.0217 -0.0100 371  VAL A C     
1987 O  O     . VAL A 268 ? 1.5370 1.7931 0.9117 0.1087  -0.0284 -0.0209 371  VAL A O     
1988 C  CB    . VAL A 268 ? 1.5847 1.8366 0.9092 0.1134  0.0166  0.0017  371  VAL A CB    
1989 C  CG1   . VAL A 268 ? 1.5683 1.8182 0.8973 0.1079  0.0382  0.0171  371  VAL A CG1   
1990 C  CG2   . VAL A 268 ? 1.5220 1.7811 0.8650 0.1113  0.0157  -0.0172 371  VAL A CG2   
1991 N  N     . ASN A 269 ? 1.6419 1.8945 0.9541 0.1223  -0.0325 -0.0114 372  ASN A N     
1992 C  CA    . ASN A 269 ? 1.6494 1.9064 0.9596 0.1242  -0.0541 -0.0259 372  ASN A CA    
1993 C  C     . ASN A 269 ? 1.6565 1.9136 0.9322 0.1303  -0.0553 -0.0390 372  ASN A C     
1994 O  O     . ASN A 269 ? 1.6072 1.8615 0.8506 0.1366  -0.0442 -0.0323 372  ASN A O     
1995 C  CB    . ASN A 269 ? 1.7409 1.9996 1.0453 0.1283  -0.0705 -0.0161 372  ASN A CB    
1996 C  CG    . ASN A 269 ? 1.8654 2.1238 1.2055 0.1230  -0.0725 -0.0063 372  ASN A CG    
1997 O  OD1   . ASN A 269 ? 1.6945 1.9583 1.0613 0.1184  -0.0855 -0.0149 372  ASN A OD1   
1998 N  ND2   . ASN A 269 ? 1.9849 2.2358 1.3246 0.1233  -0.0591 0.0116  372  ASN A ND2   
1999 N  N     . THR A 270 ? 1.6021 1.8611 0.8836 0.1284  -0.0686 -0.0579 373  THR A N     
2000 C  CA    . THR A 270 ? 1.6058 1.8626 0.8540 0.1339  -0.0722 -0.0729 373  THR A CA    
2001 C  C     . THR A 270 ? 1.7300 1.9893 0.9479 0.1397  -0.0902 -0.0717 373  THR A C     
2002 O  O     . THR A 270 ? 1.7161 1.9797 0.9396 0.1404  -0.0990 -0.0585 373  THR A O     
2003 C  CB    . THR A 270 ? 1.5884 1.8433 0.8538 0.1290  -0.0789 -0.0938 373  THR A CB    
2004 O  OG1   . THR A 270 ? 1.6192 1.8778 0.9046 0.1235  -0.1000 -0.0988 373  THR A OG1   
2005 C  CG2   . THR A 270 ? 1.6227 1.8771 0.9201 0.1240  -0.0624 -0.0939 373  THR A CG2   
2006 N  N     . GLN A 271 ? 1.7699 2.0264 0.9545 0.1444  -0.0960 -0.0859 374  GLN A N     
2007 C  CA    . GLN A 271 ? 1.7873 2.0473 0.9410 0.1496  -0.1146 -0.0871 374  GLN A CA    
2008 C  C     . GLN A 271 ? 1.8209 2.0886 0.9991 0.1429  -0.1384 -0.0945 374  GLN A C     
2009 O  O     . GLN A 271 ? 1.6687 1.9363 0.8823 0.1344  -0.1408 -0.1030 374  GLN A O     
2010 C  CB    . GLN A 271 ? 1.8213 2.0751 0.9331 0.1554  -0.1150 -0.1028 374  GLN A CB    
2011 C  CG    . GLN A 271 ? 1.8863 2.1341 0.9713 0.1628  -0.0910 -0.0962 374  GLN A CG    
2012 C  CD    . GLN A 271 ? 1.8453 2.0950 0.9037 0.1705  -0.0859 -0.0755 374  GLN A CD    
2013 O  OE1   . GLN A 271 ? 1.8240 2.0753 0.9016 0.1688  -0.0768 -0.0570 374  GLN A OE1   
2014 N  NE2   . GLN A 271 ? 1.9125 2.1603 0.9245 0.1791  -0.0915 -0.0787 374  GLN A NE2   
2015 N  N     . ARG A 272 ? 2.0381 2.3137 1.1970 0.1471  -0.1561 -0.0906 375  ARG A N     
2016 C  CA    . ARG A 272 ? 1.9919 2.2787 1.1716 0.1413  -0.1800 -0.0965 375  ARG A CA    
2017 C  C     . ARG A 272 ? 1.9403 2.2256 1.0980 0.1387  -0.1957 -0.1192 375  ARG A C     
2018 O  O     . ARG A 272 ? 2.0543 2.3422 1.1736 0.1450  -0.2055 -0.1214 375  ARG A O     
2019 C  CB    . ARG A 272 ? 2.0166 2.3152 1.1902 0.1477  -0.1908 -0.0787 375  ARG A CB    
2020 C  CG    . ARG A 272 ? 2.1384 2.4343 1.3271 0.1513  -0.1745 -0.0558 375  ARG A CG    
2021 C  CD    . ARG A 272 ? 2.1721 2.4774 1.3490 0.1601  -0.1849 -0.0382 375  ARG A CD    
2022 N  NE    . ARG A 272 ? 2.2527 2.5514 1.4408 0.1636  -0.1688 -0.0164 375  ARG A NE    
2023 C  CZ    . ARG A 272 ? 2.1758 2.4777 1.4013 0.1599  -0.1696 -0.0076 375  ARG A CZ    
2024 N  NH1   . ARG A 272 ? 2.0117 2.3248 1.2691 0.1528  -0.1851 -0.0176 375  ARG A NH1   
2025 N  NH2   . ARG A 272 ? 2.2385 2.5311 1.4687 0.1633  -0.1540 0.0116  375  ARG A NH2   
2026 N  N     . VAL A 273 ? 1.9474 2.2272 1.1281 0.1292  -0.1980 -0.1361 376  VAL A N     
2027 C  CA    . VAL A 273 ? 1.9365 2.2106 1.0976 0.1252  -0.2116 -0.1592 376  VAL A CA    
2028 C  C     . VAL A 273 ? 1.9578 2.2421 1.1482 0.1141  -0.2340 -0.1674 376  VAL A C     
2029 O  O     . VAL A 273 ? 1.9892 2.2799 1.2215 0.1084  -0.2331 -0.1596 376  VAL A O     
2030 C  CB    . VAL A 273 ? 1.8824 2.1385 1.0406 0.1241  -0.1955 -0.1738 376  VAL A CB    
2031 C  CG1   . VAL A 273 ? 1.8005 2.0501 0.9342 0.1346  -0.1719 -0.1639 376  VAL A CG1   
2032 C  CG2   . VAL A 273 ? 1.8473 2.1010 1.0532 0.1150  -0.1901 -0.1757 376  VAL A CG2   
2033 N  N     . PRO A 274 ? 2.0253 2.3121 1.1951 0.1104  -0.2542 -0.1828 377  PRO A N     
2034 C  CA    . PRO A 274 ? 2.0687 2.3655 1.2676 0.0979  -0.2751 -0.1922 377  PRO A CA    
2035 C  C     . PRO A 274 ? 2.1545 2.4352 1.3753 0.0877  -0.2702 -0.2090 377  PRO A C     
2036 O  O     . PRO A 274 ? 2.1965 2.4582 1.4045 0.0909  -0.2534 -0.2166 377  PRO A O     
2037 C  CB    . PRO A 274 ? 2.0860 2.3895 1.2493 0.0975  -0.2971 -0.2038 377  PRO A CB    
2038 C  CG    . PRO A 274 ? 2.1462 2.4326 1.2614 0.1071  -0.2852 -0.2103 377  PRO A CG    
2039 C  CD    . PRO A 274 ? 2.0884 2.3708 1.2062 0.1175  -0.2599 -0.1911 377  PRO A CD    
2040 N  N     . CYS A 275 ? 2.2135 2.5026 1.4681 0.0756  -0.2849 -0.2143 378  CYS A N     
2041 C  CA    . CYS A 275 ? 2.3095 2.5837 1.5883 0.0650  -0.2819 -0.2287 378  CYS A CA    
2042 C  C     . CYS A 275 ? 2.4914 2.7477 1.7410 0.0595  -0.2904 -0.2535 378  CYS A C     
2043 O  O     . CYS A 275 ? 2.5730 2.8131 1.8379 0.0512  -0.2877 -0.2668 378  CYS A O     
2044 C  CB    . CYS A 275 ? 2.2366 2.5261 1.5612 0.0536  -0.2942 -0.2247 378  CYS A CB    
2045 S  SG    . CYS A 275 ? 2.4190 2.6916 1.7819 0.0424  -0.2856 -0.2348 378  CYS A SG    
2046 N  N     . SER A 276 ? 2.5011 2.7584 1.7078 0.0641  -0.3003 -0.2599 379  SER A N     
2047 C  CA    . SER A 276 ? 2.7068 2.9452 1.8820 0.0588  -0.3092 -0.2844 379  SER A CA    
2048 C  C     . SER A 276 ? 2.8356 3.0456 2.0003 0.0633  -0.2880 -0.2947 379  SER A C     
2049 O  O     . SER A 276 ? 2.8551 3.0473 2.0310 0.0543  -0.2890 -0.3104 379  SER A O     
2050 C  CB    . SER A 276 ? 2.7035 2.9477 1.8304 0.0657  -0.3206 -0.2874 379  SER A CB    
2051 O  OG    . SER A 276 ? 2.7202 2.9602 1.8197 0.0816  -0.3017 -0.2759 379  SER A OG    
2052 N  N     . ASN A 277 ? 2.7702 2.9758 1.9136 0.0776  -0.2683 -0.2854 380  ASN A N     
2053 C  CA    . ASN A 277 ? 2.7201 2.9035 1.8560 0.0842  -0.2460 -0.2920 380  ASN A CA    
2054 C  C     . ASN A 277 ? 2.6126 2.8056 1.7718 0.0923  -0.2248 -0.2703 380  ASN A C     
2055 O  O     . ASN A 277 ? 2.6646 2.8615 1.8000 0.1038  -0.2125 -0.2594 380  ASN A O     
2056 C  CB    . ASN A 277 ? 2.7448 2.9121 1.8262 0.0935  -0.2418 -0.3050 380  ASN A CB    
2057 C  CG    . ASN A 277 ? 2.6617 2.8068 1.7356 0.1011  -0.2191 -0.3130 380  ASN A CG    
2058 O  OD1   . ASN A 277 ? 2.6849 2.8212 1.7908 0.0963  -0.2120 -0.3162 380  ASN A OD1   
2059 N  ND2   . ASN A 277 ? 2.5477 2.6844 1.5789 0.1138  -0.2072 -0.3158 380  ASN A ND2   
2060 N  N     . PRO A 278 ? 2.5517 2.7484 1.7571 0.0860  -0.2200 -0.2634 381  PRO A N     
2061 C  CA    . PRO A 278 ? 2.4161 2.6215 1.6448 0.0921  -0.2006 -0.2435 381  PRO A CA    
2062 C  C     . PRO A 278 ? 2.4285 2.6216 1.6376 0.1030  -0.1772 -0.2446 381  PRO A C     
2063 O  O     . PRO A 278 ? 2.4987 2.6777 1.7182 0.1027  -0.1672 -0.2546 381  PRO A O     
2064 C  CB    . PRO A 278 ? 2.2617 2.4680 1.5391 0.0822  -0.2015 -0.2421 381  PRO A CB    
2065 C  CG    . PRO A 278 ? 2.3804 2.5879 1.6635 0.0703  -0.2252 -0.2544 381  PRO A CG    
2066 C  CD    . PRO A 278 ? 2.5295 2.7234 1.7673 0.0721  -0.2330 -0.2728 381  PRO A CD    
2067 N  N     . ARG A 279 ? 2.1779 2.3770 1.3586 0.1132  -0.1682 -0.2340 382  ARG A N     
2068 C  CA    . ARG A 279 ? 2.0247 2.2158 1.1850 0.1240  -0.1454 -0.2336 382  ARG A CA    
2069 C  C     . ARG A 279 ? 1.8754 2.0804 1.0308 0.1310  -0.1330 -0.2113 382  ARG A C     
2070 O  O     . ARG A 279 ? 1.8663 2.0811 1.0071 0.1321  -0.1439 -0.2020 382  ARG A O     
2071 C  CB    . ARG A 279 ? 2.0971 2.2727 1.2088 0.1303  -0.1475 -0.2518 382  ARG A CB    
2072 C  CG    . ARG A 279 ? 2.0393 2.1951 1.1483 0.1328  -0.1363 -0.2691 382  ARG A CG    
2073 C  CD    . ARG A 279 ? 2.1721 2.3144 1.2937 0.1217  -0.1537 -0.2873 382  ARG A CD    
2074 N  NE    . ARG A 279 ? 2.1926 2.3127 1.3074 0.1255  -0.1431 -0.3041 382  ARG A NE    
2075 N  N     . TRP A 280 ? 1.7783 1.9842 0.9460 0.1357  -0.1103 -0.2026 383  TRP A N     
2076 C  CA    . TRP A 280 ? 1.7252 1.9416 0.8872 0.1415  -0.0956 -0.1819 383  TRP A CA    
2077 C  C     . TRP A 280 ? 1.6602 1.8718 0.7961 0.1516  -0.0735 -0.1834 383  TRP A C     
2078 O  O     . TRP A 280 ? 1.7482 1.9616 0.8491 0.1593  -0.0679 -0.1764 383  TRP A O     
2079 C  CB    . TRP A 280 ? 1.7037 1.9300 0.9114 0.1353  -0.0889 -0.1658 383  TRP A CB    
2080 C  CG    . TRP A 280 ? 1.6626 1.8965 0.8920 0.1277  -0.1082 -0.1594 383  TRP A CG    
2081 C  CD1   . TRP A 280 ? 1.6489 1.8920 0.8716 0.1292  -0.1146 -0.1435 383  TRP A CD1   
2082 C  CD2   . TRP A 280 ? 1.7214 1.9548 0.9827 0.1181  -0.1229 -0.1682 383  TRP A CD2   
2083 N  NE1   . TRP A 280 ? 1.6289 1.8788 0.8782 0.1219  -0.1323 -0.1420 383  TRP A NE1   
2084 C  CE2   . TRP A 280 ? 1.6909 1.9354 0.9645 0.1144  -0.1375 -0.1570 383  TRP A CE2   
2085 C  CE3   . TRP A 280 ? 1.8131 2.0372 1.0933 0.1128  -0.1244 -0.1839 383  TRP A CE3   
2086 C  CZ2   . TRP A 280 ? 1.6971 1.9457 1.0021 0.1051  -0.1532 -0.1610 383  TRP A CZ2   
2087 C  CZ3   . TRP A 280 ? 1.8244 2.0505 1.1346 0.1030  -0.1401 -0.1877 383  TRP A CZ3   
2088 C  CH2   . TRP A 280 ? 1.7503 1.9895 1.0732 0.0989  -0.1541 -0.1764 383  TRP A CH2   
2089 N  N     . ASN A 281 ? 1.6479 1.8541 0.8006 0.1524  -0.0606 -0.1919 384  ASN A N     
2090 C  CA    . ASN A 281 ? 1.6131 1.8156 0.7434 0.1628  -0.0396 -0.1959 384  ASN A CA    
2091 C  C     . ASN A 281 ? 1.6099 1.8243 0.7304 0.1678  -0.0217 -0.1759 384  ASN A C     
2092 O  O     . ASN A 281 ? 1.8318 2.0444 0.9162 0.1774  -0.0098 -0.1765 384  ASN A O     
2093 C  CB    . ASN A 281 ? 1.6681 1.8554 0.7526 0.1696  -0.0464 -0.2151 384  ASN A CB    
2094 C  CG    . ASN A 281 ? 1.7070 1.8798 0.7990 0.1633  -0.0641 -0.2354 384  ASN A CG    
2095 O  OD1   . ASN A 281 ? 1.8790 2.0514 1.0100 0.1564  -0.0655 -0.2371 384  ASN A OD1   
2096 N  ND2   . ASN A 281 ? 1.6454 1.8055 0.6991 0.1652  -0.0777 -0.2510 384  ASN A ND2   
2097 N  N     . GLU A 282 ? 1.6278 1.8535 0.7798 0.1611  -0.0194 -0.1579 385  GLU A N     
2098 C  CA    . GLU A 282 ? 1.7192 1.9543 0.8641 0.1636  -0.0039 -0.1374 385  GLU A CA    
2099 C  C     . GLU A 282 ? 1.6532 1.8982 0.8396 0.1579  0.0119  -0.1257 385  GLU A C     
2100 O  O     . GLU A 282 ? 1.4964 1.7428 0.7206 0.1498  0.0044  -0.1270 385  GLU A O     
2101 C  CB    . GLU A 282 ? 1.7159 1.9531 0.8507 0.1613  -0.0180 -0.1243 385  GLU A CB    
2102 C  CG    . GLU A 282 ? 1.7428 1.9820 0.9126 0.1517  -0.0365 -0.1233 385  GLU A CG    
2103 C  CD    . GLU A 282 ? 1.7459 1.9896 0.9101 0.1509  -0.0464 -0.1067 385  GLU A CD    
2104 O  OE1   . GLU A 282 ? 1.7620 2.0086 0.9185 0.1534  -0.0323 -0.0890 385  GLU A OE1   
2105 O  OE2   . GLU A 282 ? 1.7479 1.9922 0.9152 0.1478  -0.0680 -0.1112 385  GLU A OE2   
2106 N  N     . TRP A 283 ? 1.7112 1.9636 0.8898 0.1617  0.0338  -0.1144 386  TRP A N     
2107 C  CA    . TRP A 283 ? 1.6480 1.9116 0.8628 0.1554  0.0494  -0.1012 386  TRP A CA    
2108 C  C     . TRP A 283 ? 1.6303 1.8960 0.8526 0.1488  0.0472  -0.0811 386  TRP A C     
2109 O  O     . TRP A 283 ? 1.6341 1.8959 0.8248 0.1528  0.0443  -0.0727 386  TRP A O     
2110 C  CB    . TRP A 283 ? 1.6276 1.9000 0.8324 0.1615  0.0745  -0.0980 386  TRP A CB    
2111 C  CG    . TRP A 283 ? 1.5975 1.8695 0.8040 0.1681  0.0801  -0.1159 386  TRP A CG    
2112 C  CD1   . TRP A 283 ? 1.6857 1.9471 0.8580 0.1781  0.0763  -0.1324 386  TRP A CD1   
2113 C  CD2   . TRP A 283 ? 1.6409 1.9226 0.8842 0.1661  0.0904  -0.1190 386  TRP A CD2   
2114 N  NE1   . TRP A 283 ? 1.6350 1.8972 0.8201 0.1830  0.0844  -0.1455 386  TRP A NE1   
2115 C  CE2   . TRP A 283 ? 1.6405 1.9163 0.8697 0.1761  0.0930  -0.1372 386  TRP A CE2   
2116 C  CE3   . TRP A 283 ? 1.6306 1.9251 0.9165 0.1570  0.0975  -0.1083 386  TRP A CE3   
2117 C  CZ2   . TRP A 283 ? 1.6505 1.9335 0.9073 0.1785  0.1025  -0.1441 386  TRP A CZ2   
2118 C  CZ3   . TRP A 283 ? 1.6021 1.9053 0.9155 0.1585  0.1061  -0.1155 386  TRP A CZ3   
2119 C  CH2   . TRP A 283 ? 1.6366 1.9344 0.9358 0.1697  0.1087  -0.1328 386  TRP A CH2   
2120 N  N     . LEU A 284 ? 1.5376 1.8084 0.8006 0.1394  0.0484  -0.0735 387  LEU A N     
2121 C  CA    . LEU A 284 ? 1.4842 1.7549 0.7578 0.1328  0.0477  -0.0547 387  LEU A CA    
2122 C  C     . LEU A 284 ? 1.4485 1.7280 0.7387 0.1277  0.0702  -0.0413 387  LEU A C     
2123 O  O     . LEU A 284 ? 1.4627 1.7503 0.7853 0.1227  0.0772  -0.0453 387  LEU A O     
2124 C  CB    . LEU A 284 ? 1.4649 1.7331 0.7710 0.1253  0.0303  -0.0563 387  LEU A CB    
2125 C  CG    . LEU A 284 ? 1.5113 1.7730 0.8069 0.1279  0.0068  -0.0689 387  LEU A CG    
2126 C  CD1   . LEU A 284 ? 1.4716 1.7332 0.8029 0.1198  -0.0074 -0.0682 387  LEU A CD1   
2127 C  CD2   . LEU A 284 ? 1.6298 1.8874 0.8859 0.1345  -0.0005 -0.0625 387  LEU A CD2   
2128 N  N     . ASN A 285 ? 1.4660 1.7442 0.7338 0.1287  0.0815  -0.0254 388  ASN A N     
2129 C  CA    . ASN A 285 ? 1.4766 1.7625 0.7588 0.1219  0.1027  -0.0111 388  ASN A CA    
2130 C  C     . ASN A 285 ? 1.4597 1.7408 0.7685 0.1114  0.0986  0.0021  388  ASN A C     
2131 O  O     . ASN A 285 ? 1.4632 1.7331 0.7589 0.1124  0.0875  0.0104  388  ASN A O     
2132 C  CB    . ASN A 285 ? 1.4956 1.7808 0.7402 0.1273  0.1184  0.0004  388  ASN A CB    
2133 C  CG    . ASN A 285 ? 1.5809 1.8524 0.7956 0.1309  0.1085  0.0117  388  ASN A CG    
2134 O  OD1   . ASN A 285 ? 1.6368 1.9025 0.8230 0.1398  0.0945  0.0037  388  ASN A OD1   
2135 N  ND2   . ASN A 285 ? 1.5660 1.8320 0.7864 0.1239  0.1156  0.0305  388  ASN A ND2   
2136 N  N     . TYR A 286 ? 1.4726 1.7621 0.8180 0.1019  0.1073  0.0037  389  TYR A N     
2137 C  CA    . TYR A 286 ? 1.5163 1.8006 0.8886 0.0912  0.1044  0.0146  389  TYR A CA    
2138 C  C     . TYR A 286 ? 1.5315 1.8177 0.9051 0.0830  0.1247  0.0317  389  TYR A C     
2139 O  O     . TYR A 286 ? 1.5455 1.8437 0.9152 0.0829  0.1421  0.0324  389  TYR A O     
2140 C  CB    . TYR A 286 ? 1.3983 1.6895 0.8115 0.0852  0.0978  0.0039  389  TYR A CB    
2141 C  CG    . TYR A 286 ? 1.3755 1.6635 0.7903 0.0913  0.0781  -0.0125 389  TYR A CG    
2142 C  CD1   . TYR A 286 ? 1.4776 1.7557 0.8983 0.0902  0.0600  -0.0118 389  TYR A CD1   
2143 C  CD2   . TYR A 286 ? 1.3271 1.6217 0.7374 0.0982  0.0782  -0.0286 389  TYR A CD2   
2144 C  CE1   . TYR A 286 ? 1.4653 1.7413 0.8885 0.0942  0.0423  -0.0266 389  TYR A CE1   
2145 C  CE2   . TYR A 286 ? 1.3036 1.5929 0.7143 0.1024  0.0606  -0.0438 389  TYR A CE2   
2146 C  CZ    . TYR A 286 ? 1.4235 1.7042 0.8413 0.0997  0.0425  -0.0427 389  TYR A CZ    
2147 O  OH    . TYR A 286 ? 1.5449 1.8213 0.9645 0.1024  0.0252  -0.0575 389  TYR A OH    
2148 N  N     . ASP A 287 ? 1.5488 1.8224 0.9277 0.0762  0.1226  0.0455  390  ASP A N     
2149 C  CA    . ASP A 287 ? 1.5323 1.8031 0.9121 0.0665  0.1407  0.0625  390  ASP A CA    
2150 C  C     . ASP A 287 ? 1.5441 1.8261 0.9650 0.0534  0.1482  0.0610  390  ASP A C     
2151 O  O     . ASP A 287 ? 1.5354 1.8083 0.9741 0.0432  0.1479  0.0695  390  ASP A O     
2152 C  CB    . ASP A 287 ? 1.5031 1.7525 0.8677 0.0658  0.1354  0.0777  390  ASP A CB    
2153 C  CG    . ASP A 287 ? 1.5573 1.7990 0.9158 0.0563  0.1547  0.0961  390  ASP A CG    
2154 O  OD1   . ASP A 287 ? 1.5797 1.8346 0.9407 0.0511  0.1726  0.0976  390  ASP A OD1   
2155 O  OD2   . ASP A 287 ? 1.6003 1.8226 0.9517 0.0539  0.1522  0.1093  390  ASP A OD2   
2156 N  N     . ILE A 288 ? 1.5012 1.8031 0.9361 0.0543  0.1550  0.0498  391  ILE A N     
2157 C  CA    . ILE A 288 ? 1.5776 1.8944 1.0513 0.0433  0.1618  0.0473  391  ILE A CA    
2158 C  C     . ILE A 288 ? 1.5249 1.8650 1.0014 0.0462  0.1769  0.0413  391  ILE A C     
2159 O  O     . ILE A 288 ? 1.4067 1.7523 0.8700 0.0585  0.1734  0.0290  391  ILE A O     
2160 C  CB    . ILE A 288 ? 1.4906 1.8068 0.9929 0.0427  0.1443  0.0352  391  ILE A CB    
2161 C  CG1   . ILE A 288 ? 1.3770 1.7118 0.9171 0.0335  0.1513  0.0310  391  ILE A CG1   
2162 C  CG2   . ILE A 288 ? 1.5379 1.8536 1.0279 0.0562  0.1302  0.0197  391  ILE A CG2   
2163 N  N     . TYR A 289 ? 1.7135 2.0671 1.2068 0.0348  0.1941  0.0500  392  TYR A N     
2164 C  CA    . TYR A 289 ? 1.6778 2.0579 1.1805 0.0366  0.2095  0.0453  392  TYR A CA    
2165 C  C     . TYR A 289 ? 1.5700 1.9649 1.1037 0.0397  0.2010  0.0296  392  TYR A C     
2166 O  O     . TYR A 289 ? 1.5895 1.9814 1.1504 0.0319  0.1909  0.0277  392  TYR A O     
2167 C  CB    . TYR A 289 ? 1.7653 2.1576 1.2823 0.0213  0.2287  0.0593  392  TYR A CB    
2168 C  CG    . TYR A 289 ? 1.6667 2.0834 1.1786 0.0240  0.2494  0.0610  392  TYR A CG    
2169 C  CD1   . TYR A 289 ? 1.7891 2.2113 1.2771 0.0408  0.2514  0.0519  392  TYR A CD1   
2170 C  CD2   . TYR A 289 ? 1.8007 2.2353 1.3318 0.0093  0.2673  0.0718  392  TYR A CD2   
2171 C  CE1   . TYR A 289 ? 1.7898 2.2349 1.2728 0.0443  0.2714  0.0538  392  TYR A CE1   
2172 C  CE2   . TYR A 289 ? 1.8796 2.3392 1.4080 0.0117  0.2870  0.0741  392  TYR A CE2   
2173 C  CZ    . TYR A 289 ? 1.7437 2.2085 1.2478 0.0299  0.2894  0.0652  392  TYR A CZ    
2174 O  OH    . TYR A 289 ? 1.6543 2.1445 1.1554 0.0334  0.3100  0.0677  392  TYR A OH    
2175 N  N     . ILE A 290 ? 1.4297 1.8391 0.9575 0.0520  0.2055  0.0185  393  ILE A N     
2176 C  CA    . ILE A 290 ? 1.3756 1.7979 0.9303 0.0568  0.1985  0.0038  393  ILE A CA    
2177 C  C     . ILE A 290 ? 1.4015 1.8439 0.9973 0.0440  0.2047  0.0074  393  ILE A C     
2178 O  O     . ILE A 290 ? 1.4194 1.8596 1.0399 0.0411  0.1919  0.0009  393  ILE A O     
2179 C  CB    . ILE A 290 ? 1.3955 1.8292 0.9342 0.0727  0.2055  -0.0075 393  ILE A CB    
2180 C  CG1   . ILE A 290 ? 1.4075 1.8189 0.9145 0.0855  0.1905  -0.0182 393  ILE A CG1   
2181 C  CG2   . ILE A 290 ? 1.3637 1.8188 0.9348 0.0759  0.2072  -0.0179 393  ILE A CG2   
2182 C  CD1   . ILE A 290 ? 1.4268 1.8290 0.9508 0.0882  0.1712  -0.0316 393  ILE A CD1   
2183 N  N     . PRO A 291 ? 1.4261 1.8889 1.0312 0.0355  0.2235  0.0174  394  PRO A N     
2184 C  CA    . PRO A 291 ? 1.3912 1.8750 1.0368 0.0225  0.2276  0.0199  394  PRO A CA    
2185 C  C     . PRO A 291 ? 1.3818 1.8488 1.0416 0.0072  0.2176  0.0267  394  PRO A C     
2186 O  O     . PRO A 291 ? 1.4721 1.9520 1.1651 -0.0019 0.2150  0.0250  394  PRO A O     
2187 C  CB    . PRO A 291 ? 1.4358 1.9437 1.0829 0.0159  0.2504  0.0304  394  PRO A CB    
2188 C  CG    . PRO A 291 ? 1.4382 1.9282 1.0449 0.0200  0.2569  0.0385  394  PRO A CG    
2189 C  CD    . PRO A 291 ? 1.4471 1.9174 1.0279 0.0372  0.2422  0.0265  394  PRO A CD    
2190 N  N     . ASP A 292 ? 1.3350 1.7737 0.9702 0.0049  0.2119  0.0342  395  ASP A N     
2191 C  CA    . ASP A 292 ? 1.3872 1.8073 1.0327 -0.0083 0.2035  0.0413  395  ASP A CA    
2192 C  C     . ASP A 292 ? 1.3893 1.7936 1.0422 -0.0028 0.1824  0.0313  395  ASP A C     
2193 O  O     . ASP A 292 ? 1.3407 1.7271 0.9994 -0.0113 0.1742  0.0364  395  ASP A O     
2194 C  CB    . ASP A 292 ? 1.4088 1.8058 1.0246 -0.0129 0.2086  0.0557  395  ASP A CB    
2195 C  CG    . ASP A 292 ? 1.4436 1.8519 1.0623 -0.0269 0.2289  0.0691  395  ASP A CG    
2196 O  OD1   . ASP A 292 ? 1.5477 1.9824 1.1710 -0.0248 0.2429  0.0678  395  ASP A OD1   
2197 O  OD2   . ASP A 292 ? 1.3626 1.7531 0.9787 -0.0400 0.2313  0.0809  395  ASP A OD2   
2198 N  N     . LEU A 293 ? 1.3512 1.7609 1.0037 0.0111  0.1742  0.0175  396  LEU A N     
2199 C  CA    . LEU A 293 ? 1.2764 1.6733 0.9389 0.0152  0.1551  0.0079  396  LEU A CA    
2200 C  C     . LEU A 293 ? 1.2017 1.6103 0.9017 0.0055  0.1525  0.0057  396  LEU A C     
2201 O  O     . LEU A 293 ? 1.1859 1.6197 0.9058 0.0030  0.1625  0.0040  396  LEU A O     
2202 C  CB    . LEU A 293 ? 1.2377 1.6362 0.8897 0.0314  0.1480  -0.0066 396  LEU A CB    
2203 C  CG    . LEU A 293 ? 1.2813 1.6613 0.8967 0.0419  0.1413  -0.0084 396  LEU A CG    
2204 C  CD1   . LEU A 293 ? 1.2883 1.6705 0.8960 0.0561  0.1350  -0.0244 396  LEU A CD1   
2205 C  CD2   . LEU A 293 ? 1.2337 1.5902 0.8439 0.0384  0.1261  -0.0043 396  LEU A CD2   
2206 N  N     . PRO A 294 ? 1.1867 1.5788 0.8969 0.0003  0.1394  0.0058  397  PRO A N     
2207 C  CA    . PRO A 294 ? 1.1742 1.5760 0.9178 -0.0081 0.1356  0.0030  397  PRO A CA    
2208 C  C     . PRO A 294 ? 1.1199 1.5312 0.8777 0.0027  0.1269  -0.0112 397  PRO A C     
2209 O  O     . PRO A 294 ? 1.0865 1.4926 0.8281 0.0158  0.1219  -0.0195 397  PRO A O     
2210 C  CB    . PRO A 294 ? 1.1579 1.5348 0.9011 -0.0154 0.1250  0.0085  397  PRO A CB    
2211 C  CG    . PRO A 294 ? 1.1999 1.5567 0.9146 -0.0047 0.1166  0.0078  397  PRO A CG    
2212 C  CD    . PRO A 294 ? 1.1808 1.5453 0.8717 0.0018  0.1281  0.0098  397  PRO A CD    
2213 N  N     . ARG A 295 ? 1.1128 1.5372 0.9006 -0.0033 0.1250  -0.0140 398  ARG A N     
2214 C  CA    . ARG A 295 ? 1.0618 1.4952 0.8648 0.0067  0.1178  -0.0263 398  ARG A CA    
2215 C  C     . ARG A 295 ? 1.0388 1.4485 0.8346 0.0132  0.1011  -0.0331 398  ARG A C     
2216 O  O     . ARG A 295 ? 1.0372 1.4458 0.8295 0.0251  0.0955  -0.0437 398  ARG A O     
2217 C  CB    . ARG A 295 ? 1.0144 1.4672 0.8503 -0.0016 0.1190  -0.0263 398  ARG A CB    
2218 C  CG    . ARG A 295 ? 1.0078 1.4693 0.8602 0.0088  0.1118  -0.0378 398  ARG A CG    
2219 C  CD    . ARG A 295 ? 1.0106 1.4842 0.8529 0.0238  0.1185  -0.0451 398  ARG A CD    
2220 N  NE    . ARG A 295 ? 0.9724 1.4510 0.8283 0.0349  0.1121  -0.0558 398  ARG A NE    
2221 C  CZ    . ARG A 295 ? 0.9246 1.3821 0.7717 0.0433  0.0999  -0.0643 398  ARG A CZ    
2222 N  NH1   . ARG A 295 ? 0.8998 1.3322 0.7264 0.0422  0.0917  -0.0638 398  ARG A NH1   
2223 N  NH2   . ARG A 295 ? 0.9330 1.3949 0.7923 0.0532  0.0958  -0.0733 398  ARG A NH2   
2224 N  N     . ALA A 296 ? 1.0573 1.4477 0.8508 0.0055  0.0935  -0.0270 399  ALA A N     
2225 C  CA    . ALA A 296 ? 1.0884 1.4585 0.8776 0.0103  0.0779  -0.0320 399  ALA A CA    
2226 C  C     . ALA A 296 ? 1.1297 1.4832 0.8891 0.0167  0.0738  -0.0307 399  ALA A C     
2227 O  O     . ALA A 296 ? 1.1140 1.4501 0.8685 0.0171  0.0622  -0.0301 399  ALA A O     
2228 C  CB    . ALA A 296 ? 1.0942 1.4536 0.8985 -0.0001 0.0716  -0.0266 399  ALA A CB    
2229 N  N     . ALA A 297 ? 1.2618 1.6214 1.0009 0.0220  0.0830  -0.0301 400  ALA A N     
2230 C  CA    . ALA A 297 ? 1.2485 1.5937 0.9572 0.0283  0.0790  -0.0286 400  ALA A CA    
2231 C  C     . ALA A 297 ? 1.1349 1.4717 0.8369 0.0385  0.0652  -0.0411 400  ALA A C     
2232 O  O     . ALA A 297 ? 1.2395 1.5844 0.9499 0.0447  0.0648  -0.0520 400  ALA A O     
2233 C  CB    . ALA A 297 ? 1.1531 1.5077 0.8410 0.0317  0.0933  -0.0250 400  ALA A CB    
2234 N  N     . ARG A 298 ? 0.9903 1.3107 0.6772 0.0402  0.0540  -0.0394 401  ARG A N     
2235 C  CA    . ARG A 298 ? 1.1787 1.4905 0.8593 0.0476  0.0396  -0.0506 401  ARG A CA    
2236 C  C     . ARG A 298 ? 1.3147 1.6172 0.9631 0.0533  0.0348  -0.0492 401  ARG A C     
2237 O  O     . ARG A 298 ? 1.2805 1.5785 0.9151 0.0508  0.0388  -0.0373 401  ARG A O     
2238 C  CB    . ARG A 298 ? 1.1394 1.4425 0.8403 0.0432  0.0266  -0.0512 401  ARG A CB    
2239 C  CG    . ARG A 298 ? 1.2844 1.5954 1.0159 0.0379  0.0294  -0.0530 401  ARG A CG    
2240 C  CD    . ARG A 298 ? 1.1929 1.4945 0.9420 0.0343  0.0171  -0.0534 401  ARG A CD    
2241 N  NE    . ARG A 298 ? 1.1885 1.4800 0.9328 0.0295  0.0143  -0.0421 401  ARG A NE    
2242 C  CZ    . ARG A 298 ? 1.3230 1.6039 1.0582 0.0322  0.0027  -0.0413 401  ARG A CZ    
2243 N  NH1   . ARG A 298 ? 1.4282 1.7072 1.1588 0.0380  -0.0079 -0.0515 401  ARG A NH1   
2244 N  NH2   . ARG A 298 ? 1.2731 1.5452 1.0038 0.0291  0.0018  -0.0299 401  ARG A NH2   
2245 N  N     . LEU A 299 ? 1.1488 1.4478 0.7846 0.0611  0.0262  -0.0614 402  LEU A N     
2246 C  CA    . LEU A 299 ? 1.2242 1.5148 0.8303 0.0667  0.0180  -0.0624 402  LEU A CA    
2247 C  C     . LEU A 299 ? 1.1748 1.4563 0.7884 0.0653  -0.0001 -0.0657 402  LEU A C     
2248 O  O     . LEU A 299 ? 1.1701 1.4502 0.7997 0.0651  -0.0079 -0.0763 402  LEU A O     
2249 C  CB    . LEU A 299 ? 1.2548 1.5466 0.8387 0.0756  0.0202  -0.0747 402  LEU A CB    
2250 C  CG    . LEU A 299 ? 1.2609 1.5436 0.8146 0.0814  0.0082  -0.0798 402  LEU A CG    
2251 C  CD1   . LEU A 299 ? 1.2861 1.5672 0.8164 0.0820  0.0117  -0.0661 402  LEU A CD1   
2252 C  CD2   . LEU A 299 ? 1.3311 1.6127 0.8647 0.0899  0.0101  -0.0944 402  LEU A CD2   
2253 N  N     . CYS A 300 ? 1.1646 1.4404 0.7671 0.0646  -0.0064 -0.0559 403  CYS A N     
2254 C  CA    . CYS A 300 ? 1.2735 1.5436 0.8827 0.0638  -0.0233 -0.0572 403  CYS A CA    
2255 C  C     . CYS A 300 ? 1.3382 1.6056 0.9174 0.0701  -0.0332 -0.0599 403  CYS A C     
2256 O  O     . CYS A 300 ? 1.3962 1.6621 0.9537 0.0730  -0.0297 -0.0495 403  CYS A O     
2257 C  CB    . CYS A 300 ? 1.3101 1.5768 0.9338 0.0586  -0.0231 -0.0431 403  CYS A CB    
2258 S  SG    . CYS A 300 ? 1.3283 1.5978 0.9858 0.0501  -0.0128 -0.0402 403  CYS A SG    
2259 N  N     . LEU A 301 ? 1.3309 1.5970 0.9080 0.0720  -0.0456 -0.0739 404  LEU A N     
2260 C  CA    . LEU A 301 ? 1.5388 1.8032 1.0876 0.0772  -0.0567 -0.0792 404  LEU A CA    
2261 C  C     . LEU A 301 ? 1.4255 1.6895 0.9859 0.0745  -0.0758 -0.0839 404  LEU A C     
2262 O  O     . LEU A 301 ? 1.3391 1.6032 0.9287 0.0691  -0.0795 -0.0854 404  LEU A O     
2263 C  CB    . LEU A 301 ? 1.4488 1.7112 0.9774 0.0821  -0.0531 -0.0936 404  LEU A CB    
2264 C  CG    . LEU A 301 ? 1.5264 1.7866 1.0735 0.0805  -0.0511 -0.1072 404  LEU A CG    
2265 C  CD1   . LEU A 301 ? 1.4727 1.7276 1.0291 0.0773  -0.0685 -0.1191 404  LEU A CD1   
2266 C  CD2   . LEU A 301 ? 1.4396 1.6987 0.9650 0.0874  -0.0400 -0.1161 404  LEU A CD2   
2267 N  N     . SER A 302 ? 1.4765 1.7414 1.0135 0.0782  -0.0879 -0.0863 405  SER A N     
2268 C  CA    . SER A 302 ? 1.4833 1.7512 1.0295 0.0754  -0.1069 -0.0909 405  SER A CA    
2269 C  C     . SER A 302 ? 1.5008 1.7700 1.0148 0.0798  -0.1187 -0.0977 405  SER A C     
2270 O  O     . SER A 302 ? 1.5240 1.7923 1.0083 0.0862  -0.1123 -0.0935 405  SER A O     
2271 C  CB    . SER A 302 ? 1.4551 1.7276 1.0193 0.0740  -0.1109 -0.0758 405  SER A CB    
2272 O  OG    . SER A 302 ? 1.5005 1.7742 1.0416 0.0801  -0.1086 -0.0626 405  SER A OG    
2273 N  N     . ILE A 303 ? 1.5642 1.8359 1.0841 0.0760  -0.1359 -0.1082 406  ILE A N     
2274 C  CA    . ILE A 303 ? 1.5299 1.8046 1.0223 0.0784  -0.1507 -0.1154 406  ILE A CA    
2275 C  C     . ILE A 303 ? 1.5795 1.8665 1.0796 0.0788  -0.1642 -0.1040 406  ILE A C     
2276 O  O     . ILE A 303 ? 1.6245 1.9175 1.1527 0.0727  -0.1742 -0.1050 406  ILE A O     
2277 C  CB    . ILE A 303 ? 1.4857 1.7548 0.9779 0.0729  -0.1614 -0.1358 406  ILE A CB    
2278 C  CG1   . ILE A 303 ? 1.4835 1.7398 0.9658 0.0750  -0.1472 -0.1466 406  ILE A CG1   
2279 C  CG2   . ILE A 303 ? 1.5402 1.8138 1.0052 0.0739  -0.1789 -0.1434 406  ILE A CG2   
2280 C  CD1   . ILE A 303 ? 1.5230 1.7691 1.0019 0.0704  -0.1560 -0.1670 406  ILE A CD1   
2281 N  N     . CYS A 304 ? 1.6233 1.9143 1.0986 0.0865  -0.1640 -0.0926 407  CYS A N     
2282 C  CA    . CYS A 304 ? 1.6922 1.9948 1.1725 0.0895  -0.1748 -0.0794 407  CYS A CA    
2283 C  C     . CYS A 304 ? 1.7693 2.0813 1.2236 0.0927  -0.1930 -0.0850 407  CYS A C     
2284 O  O     . CYS A 304 ? 1.7865 2.0934 1.2099 0.0950  -0.1936 -0.0953 407  CYS A O     
2285 C  CB    . CYS A 304 ? 1.6866 1.9858 1.1590 0.0966  -0.1609 -0.0595 407  CYS A CB    
2286 S  SG    . CYS A 304 ? 1.5954 1.8836 1.0937 0.0922  -0.1390 -0.0527 407  CYS A SG    
2287 N  N     . SER A 305 ? 1.7803 2.1070 1.2474 0.0932  -0.2080 -0.0783 408  SER A N     
2288 C  CA    . SER A 305 ? 1.8249 2.1650 1.2713 0.0962  -0.2273 -0.0815 408  SER A CA    
2289 C  C     . SER A 305 ? 1.8517 2.1989 1.2823 0.1079  -0.2275 -0.0618 408  SER A C     
2290 O  O     . SER A 305 ? 1.8703 2.2120 1.3112 0.1121  -0.2143 -0.0459 408  SER A O     
2291 C  CB    . SER A 305 ? 1.8801 2.2353 1.3546 0.0874  -0.2464 -0.0899 408  SER A CB    
2292 O  OG    . SER A 305 ? 1.9147 2.2780 1.4235 0.0872  -0.2451 -0.0768 408  SER A OG    
2293 N  N     . VAL A 306 ? 1.9129 2.2713 1.3169 0.1131  -0.2429 -0.0631 409  VAL A N     
2294 C  CA    . VAL A 306 ? 1.9774 2.3425 1.3617 0.1257  -0.2445 -0.0446 409  VAL A CA    
2295 C  C     . VAL A 306 ? 2.0524 2.4379 1.4218 0.1286  -0.2685 -0.0487 409  VAL A C     
2296 O  O     . VAL A 306 ? 1.9715 2.3575 1.3178 0.1252  -0.2780 -0.0645 409  VAL A O     
2297 C  CB    . VAL A 306 ? 1.9151 2.2632 1.2635 0.1338  -0.2265 -0.0371 409  VAL A CB    
2298 C  CG1   . VAL A 306 ? 1.8950 2.2348 1.2155 0.1307  -0.2256 -0.0552 409  VAL A CG1   
2299 C  CG2   . VAL A 306 ? 1.9387 2.2925 1.2601 0.1473  -0.2304 -0.0195 409  VAL A CG2   
2300 N  N     . LYS A 307 ? 2.1069 2.5097 1.4893 0.1350  -0.2787 -0.0347 410  LYS A N     
2301 C  CA    . LYS A 307 ? 2.0810 2.5074 1.4514 0.1388  -0.3021 -0.0361 410  LYS A CA    
2302 C  C     . LYS A 307 ? 2.1351 2.5669 1.4839 0.1556  -0.3021 -0.0145 410  LYS A C     
2303 O  O     . LYS A 307 ? 2.2036 2.6284 1.5649 0.1624  -0.2893 0.0030  410  LYS A O     
2304 C  CB    . LYS A 307 ? 2.1293 2.5783 1.5404 0.1301  -0.3189 -0.0413 410  LYS A CB    
2305 C  CG    . LYS A 307 ? 2.1175 2.5650 1.5429 0.1134  -0.3260 -0.0647 410  LYS A CG    
2306 C  CD    . LYS A 307 ? 2.0879 2.5162 1.5406 0.1051  -0.3078 -0.0683 410  LYS A CD    
2307 C  CE    . LYS A 307 ? 2.0833 2.5081 1.5487 0.0895  -0.3146 -0.0908 410  LYS A CE    
2308 N  NZ    . LYS A 307 ? 2.1570 2.6070 1.6479 0.0811  -0.3363 -0.0964 410  LYS A NZ    
2309 N  N     . GLU A 314 ? 1.8939 2.2378 1.2407 0.1885  -0.2080 0.0737  417  GLU A N     
2310 C  CA    . GLU A 314 ? 1.9853 2.3563 1.3519 0.1862  -0.2312 0.0631  417  GLU A CA    
2311 C  C     . GLU A 314 ? 2.0671 2.4415 1.4770 0.1722  -0.2311 0.0504  417  GLU A C     
2312 O  O     . GLU A 314 ? 2.0845 2.4451 1.5158 0.1692  -0.2165 0.0567  417  GLU A O     
2313 C  CB    . GLU A 314 ? 2.0410 2.4239 1.3798 0.1850  -0.2457 0.0487  417  GLU A CB    
2314 C  CG    . GLU A 314 ? 2.0138 2.3810 1.3372 0.1755  -0.2344 0.0335  417  GLU A CG    
2315 C  CD    . GLU A 314 ? 1.8809 2.2278 1.1664 0.1830  -0.2164 0.0443  417  GLU A CD    
2316 O  OE1   . GLU A 314 ? 1.8780 2.2236 1.1417 0.1961  -0.2163 0.0621  417  GLU A OE1   
2317 O  OE2   . GLU A 314 ? 1.8081 2.1405 1.0859 0.1760  -0.2020 0.0355  417  GLU A OE2   
2318 N  N     . GLU A 315 ? 2.1337 2.5255 1.5551 0.1633  -0.2474 0.0324  418  GLU A N     
2319 C  CA    . GLU A 315 ? 2.2567 2.6539 1.7189 0.1503  -0.2497 0.0206  418  GLU A CA    
2320 C  C     . GLU A 315 ? 2.1725 2.5518 1.6337 0.1387  -0.2371 0.0055  418  GLU A C     
2321 O  O     . GLU A 315 ? 2.2108 2.5942 1.6668 0.1307  -0.2456 -0.0124 418  GLU A O     
2322 C  CB    . GLU A 315 ? 2.3266 2.7517 1.8037 0.1461  -0.2738 0.0101  418  GLU A CB    
2323 C  CG    . GLU A 315 ? 2.3468 2.7940 1.8212 0.1590  -0.2882 0.0244  418  GLU A CG    
2324 C  CD    . GLU A 315 ? 2.3794 2.8258 1.8791 0.1666  -0.2800 0.0422  418  GLU A CD    
2325 O  OE1   . GLU A 315 ? 2.1958 2.6355 1.7273 0.1581  -0.2715 0.0390  418  GLU A OE1   
2326 O  OE2   . GLU A 315 ? 2.4926 2.9438 1.9786 0.1818  -0.2820 0.0595  418  GLU A OE2   
2327 N  N     . HIS A 316 ? 2.0102 2.3693 1.4764 0.1380  -0.2164 0.0130  419  HIS A N     
2328 C  CA    . HIS A 316 ? 1.9482 2.2921 1.4185 0.1280  -0.2028 0.0010  419  HIS A CA    
2329 C  C     . HIS A 316 ? 1.9464 2.2926 1.4587 0.1177  -0.2029 -0.0061 419  HIS A C     
2330 O  O     . HIS A 316 ? 1.9106 2.2537 1.4450 0.1190  -0.1964 0.0053  419  HIS A O     
2331 C  CB    . HIS A 316 ? 1.9101 2.2333 1.3644 0.1315  -0.1806 0.0125  419  HIS A CB    
2332 C  CG    . HIS A 316 ? 1.9484 2.2668 1.3596 0.1404  -0.1777 0.0183  419  HIS A CG    
2333 N  ND1   . HIS A 316 ? 1.9102 2.2246 1.2965 0.1382  -0.1748 0.0058  419  HIS A ND1   
2334 C  CD2   . HIS A 316 ? 1.9189 2.2351 1.3061 0.1523  -0.1766 0.0356  419  HIS A CD2   
2335 C  CE1   . HIS A 316 ? 1.9198 2.2304 1.2687 0.1479  -0.1721 0.0151  419  HIS A CE1   
2336 N  NE2   . HIS A 316 ? 1.9193 2.2306 1.2678 0.1564  -0.1732 0.0334  419  HIS A NE2   
2337 N  N     . CYS A 317 ? 1.9843 2.3340 1.5057 0.1079  -0.2100 -0.0247 420  CYS A N     
2338 C  CA    . CYS A 317 ? 1.9734 2.3258 1.5328 0.0979  -0.2117 -0.0324 420  CYS A CA    
2339 C  C     . CYS A 317 ? 1.8760 2.2149 1.4366 0.0891  -0.2026 -0.0479 420  CYS A C     
2340 O  O     . CYS A 317 ? 2.0065 2.3438 1.5455 0.0872  -0.2077 -0.0612 420  CYS A O     
2341 C  CB    . CYS A 317 ? 1.9569 2.3308 1.5317 0.0941  -0.2333 -0.0394 420  CYS A CB    
2342 S  SG    . CYS A 317 ? 2.1570 2.5346 1.7773 0.0811  -0.2361 -0.0492 420  CYS A SG    
2343 N  N     . PRO A 318 ? 1.8096 2.1384 1.3938 0.0842  -0.1894 -0.0467 421  PRO A N     
2344 C  CA    . PRO A 318 ? 1.7719 2.0893 1.3591 0.0770  -0.1811 -0.0609 421  PRO A CA    
2345 C  C     . PRO A 318 ? 1.7556 2.0784 1.3593 0.0681  -0.1944 -0.0772 421  PRO A C     
2346 O  O     . PRO A 318 ? 1.7313 2.0663 1.3579 0.0647  -0.2060 -0.0758 421  PRO A O     
2347 C  CB    . PRO A 318 ? 1.7366 2.0445 1.3463 0.0750  -0.1648 -0.0526 421  PRO A CB    
2348 C  CG    . PRO A 318 ? 1.7449 2.0609 1.3742 0.0774  -0.1700 -0.0395 421  PRO A CG    
2349 C  CD    . PRO A 318 ? 1.8439 2.1703 1.4509 0.0859  -0.1810 -0.0321 421  PRO A CD    
2350 N  N     . LEU A 319 ? 1.6845 1.9977 1.2761 0.0643  -0.1920 -0.0925 422  LEU A N     
2351 C  CA    . LEU A 319 ? 1.6464 1.9599 1.2491 0.0553  -0.2032 -0.1094 422  LEU A CA    
2352 C  C     . LEU A 319 ? 1.5597 1.8596 1.1803 0.0496  -0.1920 -0.1175 422  LEU A C     
2353 O  O     . LEU A 319 ? 1.5892 1.8898 1.2343 0.0417  -0.1984 -0.1243 422  LEU A O     
2354 C  CB    . LEU A 319 ? 1.6536 1.9656 1.2233 0.0558  -0.2129 -0.1229 422  LEU A CB    
2355 C  CG    . LEU A 319 ? 1.7298 2.0552 1.2758 0.0624  -0.2247 -0.1160 422  LEU A CG    
2356 C  CD1   . LEU A 319 ? 1.7365 2.0579 1.2478 0.0625  -0.2334 -0.1311 422  LEU A CD1   
2357 C  CD2   . LEU A 319 ? 1.7436 2.0885 1.3133 0.0594  -0.2407 -0.1100 422  LEU A CD2   
2358 N  N     . ALA A 320 ? 1.5100 1.7986 1.1194 0.0538  -0.1754 -0.1166 423  ALA A N     
2359 C  CA    . ALA A 320 ? 1.4750 1.7524 1.1010 0.0501  -0.1640 -0.1230 423  ALA A CA    
2360 C  C     . ALA A 320 ? 1.4496 1.7217 1.0672 0.0559  -0.1452 -0.1147 423  ALA A C     
2361 O  O     . ALA A 320 ? 1.4577 1.7298 1.0474 0.0621  -0.1407 -0.1114 423  ALA A O     
2362 C  CB    . ALA A 320 ? 1.5328 1.8001 1.1484 0.0465  -0.1686 -0.1423 423  ALA A CB    
2363 N  N     . TRP A 321 ? 1.3633 1.6318 1.0050 0.0534  -0.1343 -0.1113 424  TRP A N     
2364 C  CA    . TRP A 321 ? 1.3278 1.5937 0.9675 0.0568  -0.1167 -0.1025 424  TRP A CA    
2365 C  C     . TRP A 321 ? 1.2762 1.5350 0.9224 0.0559  -0.1065 -0.1125 424  TRP A C     
2366 O  O     . TRP A 321 ? 1.2556 1.5093 0.9110 0.0527  -0.1125 -0.1247 424  TRP A O     
2367 C  CB    . TRP A 321 ? 1.3684 1.6375 1.0304 0.0550  -0.1122 -0.0874 424  TRP A CB    
2368 C  CG    . TRP A 321 ? 1.3543 1.6221 1.0482 0.0490  -0.1137 -0.0903 424  TRP A CG    
2369 C  CD1   . TRP A 321 ? 1.3380 1.6091 1.0493 0.0447  -0.1266 -0.0935 424  TRP A CD1   
2370 C  CD2   . TRP A 321 ? 1.3348 1.5985 1.0468 0.0466  -0.1017 -0.0899 424  TRP A CD2   
2371 N  NE1   . TRP A 321 ? 1.4070 1.6747 1.1448 0.0402  -0.1227 -0.0948 424  TRP A NE1   
2372 C  CE2   . TRP A 321 ? 1.3700 1.6332 1.1083 0.0415  -0.1080 -0.0928 424  TRP A CE2   
2373 C  CE3   . TRP A 321 ? 1.3224 1.5845 1.0314 0.0481  -0.0863 -0.0871 424  TRP A CE3   
2374 C  CZ2   . TRP A 321 ? 1.3093 1.5692 1.0689 0.0387  -0.0999 -0.0931 424  TRP A CZ2   
2375 C  CZ3   . TRP A 321 ? 1.3627 1.6234 1.0945 0.0449  -0.0790 -0.0877 424  TRP A CZ3   
2376 C  CH2   . TRP A 321 ? 1.3425 1.6014 1.0983 0.0406  -0.0859 -0.0906 424  TRP A CH2   
2377 N  N     . GLY A 322 ? 1.2632 1.5222 0.9050 0.0590  -0.0907 -0.1066 425  GLY A N     
2378 C  CA    . GLY A 322 ? 1.2732 1.5288 0.9220 0.0597  -0.0796 -0.1140 425  GLY A CA    
2379 C  C     . GLY A 322 ? 1.3062 1.5664 0.9538 0.0618  -0.0624 -0.1043 425  GLY A C     
2380 O  O     . GLY A 322 ? 1.3440 1.6069 0.9717 0.0647  -0.0576 -0.0960 425  GLY A O     
2381 N  N     . ASN A 323 ? 1.2749 1.5367 0.9436 0.0599  -0.0532 -0.1048 426  ASN A N     
2382 C  CA    . ASN A 323 ? 1.2672 1.5358 0.9392 0.0601  -0.0371 -0.0960 426  ASN A CA    
2383 C  C     . ASN A 323 ? 1.2615 1.5328 0.9371 0.0638  -0.0274 -0.1052 426  ASN A C     
2384 O  O     . ASN A 323 ? 1.2842 1.5503 0.9689 0.0648  -0.0327 -0.1162 426  ASN A O     
2385 C  CB    . ASN A 323 ? 1.2630 1.5339 0.9603 0.0534  -0.0348 -0.0847 426  ASN A CB    
2386 C  CG    . ASN A 323 ? 1.2845 1.5524 0.9781 0.0514  -0.0426 -0.0742 426  ASN A CG    
2387 O  OD1   . ASN A 323 ? 1.2580 1.5250 0.9279 0.0549  -0.0452 -0.0711 426  ASN A OD1   
2388 N  ND2   . ASN A 323 ? 1.3152 1.5815 1.0313 0.0465  -0.0461 -0.0686 426  ASN A ND2   
2389 N  N     . ILE A 324 ? 1.2208 1.5005 0.8896 0.0660  -0.0128 -0.1000 427  ILE A N     
2390 C  CA    . ILE A 324 ? 1.2386 1.5245 0.9106 0.0710  -0.0018 -0.1071 427  ILE A CA    
2391 C  C     . ILE A 324 ? 1.2010 1.5007 0.8806 0.0685  0.0139  -0.0960 427  ILE A C     
2392 O  O     . ILE A 324 ? 1.2276 1.5296 0.8933 0.0665  0.0192  -0.0860 427  ILE A O     
2393 C  CB    . ILE A 324 ? 1.2121 1.4931 0.8550 0.0799  -0.0012 -0.1184 427  ILE A CB    
2394 C  CG1   . ILE A 324 ? 1.2009 1.4906 0.8456 0.0868  0.0132  -0.1235 427  ILE A CG1   
2395 C  CG2   . ILE A 324 ? 1.2271 1.5076 0.8411 0.0815  -0.0006 -0.1123 427  ILE A CG2   
2396 C  CD1   . ILE A 324 ? 1.2754 1.5589 0.8905 0.0968  0.0155  -0.1351 427  ILE A CD1   
2397 N  N     . ASN A 325 ? 1.0677 1.3768 0.7696 0.0682  0.0212  -0.0976 428  ASN A N     
2398 C  CA    . ASN A 325 ? 1.0854 1.4105 0.7974 0.0648  0.0360  -0.0884 428  ASN A CA    
2399 C  C     . ASN A 325 ? 1.2683 1.6024 0.9601 0.0724  0.0487  -0.0905 428  ASN A C     
2400 O  O     . ASN A 325 ? 1.3038 1.6362 0.9864 0.0818  0.0492  -0.1021 428  ASN A O     
2401 C  CB    . ASN A 325 ? 1.2018 1.5366 0.9444 0.0627  0.0386  -0.0900 428  ASN A CB    
2402 C  CG    . ASN A 325 ? 1.1438 1.4682 0.9046 0.0573  0.0258  -0.0905 428  ASN A CG    
2403 O  OD1   . ASN A 325 ? 1.0486 1.3649 0.8084 0.0510  0.0193  -0.0833 428  ASN A OD1   
2404 N  ND2   . ASN A 325 ? 0.9242 1.2487 0.7012 0.0607  0.0226  -0.0984 428  ASN A ND2   
2405 N  N     . LEU A 326 ? 1.2767 1.6193 0.9608 0.0683  0.0597  -0.0792 429  LEU A N     
2406 C  CA    . LEU A 326 ? 1.1572 1.5107 0.8237 0.0749  0.0740  -0.0795 429  LEU A CA    
2407 C  C     . LEU A 326 ? 1.1547 1.5278 0.8414 0.0783  0.0855  -0.0829 429  LEU A C     
2408 O  O     . LEU A 326 ? 1.2711 1.6542 0.9449 0.0865  0.0971  -0.0859 429  LEU A O     
2409 C  CB    . LEU A 326 ? 1.1440 1.5010 0.7980 0.0686  0.0834  -0.0653 429  LEU A CB    
2410 C  CG    . LEU A 326 ? 1.1716 1.5110 0.8000 0.0682  0.0741  -0.0608 429  LEU A CG    
2411 C  CD1   . LEU A 326 ? 1.1256 1.4673 0.7416 0.0624  0.0853  -0.0456 429  LEU A CD1   
2412 C  CD2   . LEU A 326 ? 1.1798 1.5104 0.7793 0.0794  0.0681  -0.0721 429  LEU A CD2   
2413 N  N     . PHE A 327 ? 1.2289 1.6086 0.9462 0.0729  0.0828  -0.0822 430  PHE A N     
2414 C  CA    . PHE A 327 ? 1.1856 1.5847 0.9243 0.0770  0.0913  -0.0858 430  PHE A CA    
2415 C  C     . PHE A 327 ? 1.1256 1.5160 0.8802 0.0808  0.0798  -0.0954 430  PHE A C     
2416 O  O     . PHE A 327 ? 1.1227 1.4987 0.8841 0.0744  0.0672  -0.0947 430  PHE A O     
2417 C  CB    . PHE A 327 ? 1.0823 1.5019 0.8448 0.0658  0.1008  -0.0743 430  PHE A CB    
2418 C  CG    . PHE A 327 ? 1.1431 1.5739 0.8927 0.0618  0.1150  -0.0645 430  PHE A CG    
2419 C  CD1   . PHE A 327 ? 1.1972 1.6496 0.9457 0.0685  0.1301  -0.0652 430  PHE A CD1   
2420 C  CD2   . PHE A 327 ? 1.1119 1.5314 0.8503 0.0516  0.1140  -0.0539 430  PHE A CD2   
2421 C  CE1   . PHE A 327 ? 1.1193 1.5824 0.8561 0.0642  0.1441  -0.0556 430  PHE A CE1   
2422 C  CE2   . PHE A 327 ? 1.0085 1.4364 0.7340 0.0475  0.1277  -0.0441 430  PHE A CE2   
2423 C  CZ    . PHE A 327 ? 1.1041 1.5541 0.8290 0.0533  0.1430  -0.0448 430  PHE A CZ    
2424 N  N     . ASP A 328 ? 1.1628 1.5617 0.9229 0.0917  0.0847  -0.1039 431  ASP A N     
2425 C  CA    . ASP A 328 ? 1.1646 1.5553 0.9397 0.0961  0.0755  -0.1124 431  ASP A CA    
2426 C  C     . ASP A 328 ? 1.2678 1.6782 1.0759 0.0908  0.0787  -0.1064 431  ASP A C     
2427 O  O     . ASP A 328 ? 1.2345 1.6632 1.0534 0.0820  0.0867  -0.0963 431  ASP A O     
2428 C  CB    . ASP A 328 ? 1.2045 1.5895 0.9653 0.1118  0.0784  -0.1251 431  ASP A CB    
2429 C  CG    . ASP A 328 ? 1.2330 1.6435 1.0018 0.1207  0.0943  -0.1243 431  ASP A CG    
2430 O  OD1   . ASP A 328 ? 1.3761 1.8092 1.1556 0.1138  0.1042  -0.1139 431  ASP A OD1   
2431 O  OD2   . ASP A 328 ? 1.2322 1.6400 0.9964 0.1345  0.0973  -0.1341 431  ASP A OD2   
2432 N  N     . TYR A 329 ? 1.2270 1.6336 1.0508 0.0956  0.0724  -0.1126 432  TYR A N     
2433 C  CA    . TYR A 329 ? 1.0935 1.5174 0.9476 0.0905  0.0731  -0.1073 432  TYR A CA    
2434 C  C     . TYR A 329 ? 1.1374 1.5923 1.0047 0.0960  0.0870  -0.1050 432  TYR A C     
2435 O  O     . TYR A 329 ? 1.1262 1.6001 1.0190 0.0907  0.0882  -0.0998 432  TYR A O     
2436 C  CB    . TYR A 329 ? 1.0259 1.4355 0.8907 0.0949  0.0623  -0.1141 432  TYR A CB    
2437 C  CG    . TYR A 329 ? 0.9836 1.3916 0.8444 0.1114  0.0655  -0.1242 432  TYR A CG    
2438 C  CD1   . TYR A 329 ? 1.1226 1.5092 0.9578 0.1202  0.0633  -0.1341 432  TYR A CD1   
2439 C  CD2   . TYR A 329 ? 0.9470 1.3741 0.8290 0.1184  0.0704  -0.1240 432  TYR A CD2   
2440 C  CE1   . TYR A 329 ? 1.1378 1.5193 0.9673 0.1357  0.0668  -0.1437 432  TYR A CE1   
2441 C  CE2   . TYR A 329 ? 0.9848 1.4088 0.8623 0.1350  0.0739  -0.1327 432  TYR A CE2   
2442 C  CZ    . TYR A 329 ? 1.0418 1.4415 0.8925 0.1436  0.0725  -0.1426 432  TYR A CZ    
2443 O  OH    . TYR A 329 ? 1.0680 1.4613 0.9123 0.1605  0.0765  -0.1516 432  TYR A OH    
2444 N  N     . THR A 330 ? 1.1554 1.6171 1.0063 0.1065  0.0976  -0.1086 433  THR A N     
2445 C  CA    . THR A 330 ? 1.1601 1.6540 1.0235 0.1125  0.1121  -0.1058 433  THR A CA    
2446 C  C     . THR A 330 ? 1.1994 1.7105 1.0576 0.1035  0.1237  -0.0963 433  THR A C     
2447 O  O     . THR A 330 ? 1.2256 1.7625 1.0878 0.1095  0.1377  -0.0944 433  THR A O     
2448 C  CB    . THR A 330 ? 1.1700 1.6618 1.0200 0.1323  0.1180  -0.1162 433  THR A CB    
2449 O  OG1   . THR A 330 ? 1.3711 1.8490 1.1891 0.1363  0.1221  -0.1197 433  THR A OG1   
2450 C  CG2   . THR A 330 ? 1.0914 1.5593 0.9416 0.1404  0.1063  -0.1259 433  THR A CG2   
2451 N  N     . ASP A 331 ? 1.3283 1.8253 1.1774 0.0898  0.1188  -0.0897 434  ASP A N     
2452 C  CA    . ASP A 331 ? 1.3300 1.8374 1.1706 0.0803  0.1293  -0.0798 434  ASP A CA    
2453 C  C     . ASP A 331 ? 1.3727 1.8794 1.1853 0.0915  0.1395  -0.0831 434  ASP A C     
2454 O  O     . ASP A 331 ? 1.4622 1.9875 1.2717 0.0885  0.1534  -0.0758 434  ASP A O     
2455 C  CB    . ASP A 331 ? 1.2972 1.8382 1.1657 0.0710  0.1394  -0.0709 434  ASP A CB    
2456 C  CG    . ASP A 331 ? 1.3928 1.9334 1.2856 0.0579  0.1296  -0.0669 434  ASP A CG    
2457 O  OD1   . ASP A 331 ? 1.2894 1.8052 1.1793 0.0578  0.1157  -0.0712 434  ASP A OD1   
2458 O  OD2   . ASP A 331 ? 1.4073 1.9728 1.3220 0.0472  0.1359  -0.0596 434  ASP A OD2   
2459 N  N     . THR A 332 ? 1.2412 1.7257 1.0323 0.1039  0.1329  -0.0942 435  THR A N     
2460 C  CA    . THR A 332 ? 1.2718 1.7516 1.0326 0.1156  0.1411  -0.0992 435  THR A CA    
2461 C  C     . THR A 332 ? 1.2271 1.6821 0.9589 0.1102  0.1339  -0.0975 435  THR A C     
2462 O  O     . THR A 332 ? 1.1826 1.6152 0.9122 0.1055  0.1186  -0.1002 435  THR A O     
2463 C  CB    . THR A 332 ? 1.3370 1.8066 1.0895 0.1331  0.1387  -0.1134 435  THR A CB    
2464 O  OG1   . THR A 332 ? 1.3649 1.8582 1.1447 0.1397  0.1451  -0.1141 435  THR A OG1   
2465 C  CG2   . THR A 332 ? 1.1843 1.6483 0.9033 0.1455  0.1478  -0.1193 435  THR A CG2   
2466 N  N     . LEU A 333 ? 1.2872 1.7473 0.9970 0.1112  0.1452  -0.0926 436  LEU A N     
2467 C  CA    . LEU A 333 ? 1.2206 1.6584 0.8995 0.1084  0.1390  -0.0911 436  LEU A CA    
2468 C  C     . LEU A 333 ? 1.1610 1.5759 0.8142 0.1208  0.1296  -0.1056 436  LEU A C     
2469 O  O     . LEU A 333 ? 1.1967 1.6148 0.8432 0.1343  0.1358  -0.1153 436  LEU A O     
2470 C  CB    . LEU A 333 ? 1.2063 1.6560 0.8672 0.1070  0.1546  -0.0815 436  LEU A CB    
2471 C  CG    . LEU A 333 ? 1.2851 1.7146 0.9154 0.1027  0.1494  -0.0762 436  LEU A CG    
2472 C  CD1   . LEU A 333 ? 1.0874 1.5078 0.7321 0.0876  0.1393  -0.0666 436  LEU A CD1   
2473 C  CD2   . LEU A 333 ? 1.2572 1.6979 0.8663 0.1042  0.1667  -0.0677 436  LEU A CD2   
2474 N  N     . VAL A 334 ? 1.1298 1.5211 0.7683 0.1162  0.1145  -0.1071 437  VAL A N     
2475 C  CA    . VAL A 334 ? 1.2840 1.6525 0.8990 0.1252  0.1034  -0.1212 437  VAL A CA    
2476 C  C     . VAL A 334 ? 1.4613 1.8276 1.0400 0.1355  0.1124  -0.1252 437  VAL A C     
2477 O  O     . VAL A 334 ? 1.5274 1.9003 1.0912 0.1323  0.1205  -0.1152 437  VAL A O     
2478 C  CB    . VAL A 334 ? 1.2969 1.6450 0.9079 0.1166  0.0848  -0.1207 437  VAL A CB    
2479 C  CG1   . VAL A 334 ? 1.3797 1.7267 1.0240 0.1095  0.0753  -0.1205 437  VAL A CG1   
2480 C  CG2   . VAL A 334 ? 1.2733 1.6229 0.8736 0.1079  0.0863  -0.1070 437  VAL A CG2   
2481 N  N     . SER A 335 ? 1.5474 1.9028 1.1102 0.1482  0.1114  -0.1400 438  SER A N     
2482 C  CA    . SER A 335 ? 1.5017 1.8519 1.0270 0.1593  0.1192  -0.1461 438  SER A CA    
2483 C  C     . SER A 335 ? 1.5168 1.8435 1.0238 0.1694  0.1097  -0.1645 438  SER A C     
2484 O  O     . SER A 335 ? 1.5379 1.8617 1.0640 0.1734  0.1074  -0.1720 438  SER A O     
2485 C  CB    . SER A 335 ? 1.5122 1.8874 1.0407 0.1674  0.1414  -0.1414 438  SER A CB    
2486 O  OG    . SER A 335 ? 1.6408 2.0251 1.1922 0.1754  0.1463  -0.1480 438  SER A OG    
2487 N  N     . GLY A 336 ? 1.4768 1.7861 0.9461 0.1731  0.1040  -0.1715 439  GLY A N     
2488 C  CA    . GLY A 336 ? 1.4823 1.7667 0.9288 0.1814  0.0948  -0.1897 439  GLY A CA    
2489 C  C     . GLY A 336 ? 1.4918 1.7554 0.9300 0.1717  0.0727  -0.1943 439  GLY A C     
2490 O  O     . GLY A 336 ? 1.4476 1.7161 0.8964 0.1601  0.0647  -0.1830 439  GLY A O     
2491 N  N     . LYS A 337 ? 1.5227 1.7627 0.9414 0.1770  0.0633  -0.2113 440  LYS A N     
2492 C  CA    . LYS A 337 ? 1.5699 1.7904 0.9787 0.1683  0.0420  -0.2180 440  LYS A CA    
2493 C  C     . LYS A 337 ? 1.6382 1.8548 1.0830 0.1591  0.0308  -0.2178 440  LYS A C     
2494 O  O     . LYS A 337 ? 1.7328 1.9502 1.1988 0.1636  0.0371  -0.2208 440  LYS A O     
2495 C  CB    . LYS A 337 ? 1.7493 1.9451 1.1205 0.1763  0.0366  -0.2371 440  LYS A CB    
2496 C  CG    . LYS A 337 ? 1.7236 1.9052 1.0710 0.1685  0.0173  -0.2424 440  LYS A CG    
2497 C  CD    . LYS A 337 ? 1.7259 1.8840 1.0317 0.1769  0.0141  -0.2615 440  LYS A CD    
2498 C  CE    . LYS A 337 ? 1.7366 1.9008 1.0142 0.1914  0.0335  -0.2618 440  LYS A CE    
2499 N  NZ    . LYS A 337 ? 1.7401 1.8792 0.9746 0.2004  0.0310  -0.2813 440  LYS A NZ    
2500 N  N     . MET A 338 ? 1.6792 1.8921 1.1306 0.1471  0.0144  -0.2138 441  MET A N     
2501 C  CA    . MET A 338 ? 1.5663 1.7762 1.0512 0.1379  0.0038  -0.2124 441  MET A CA    
2502 C  C     . MET A 338 ? 1.5925 1.7931 1.0725 0.1273  -0.0162 -0.2136 441  MET A C     
2503 O  O     . MET A 338 ? 1.5859 1.7935 1.0524 0.1240  -0.0200 -0.2057 441  MET A O     
2504 C  CB    . MET A 338 ? 1.5454 1.7769 1.0653 0.1330  0.0123  -0.1959 441  MET A CB    
2505 C  CG    . MET A 338 ? 1.7857 2.0145 1.3402 0.1261  0.0047  -0.1953 441  MET A CG    
2506 S  SD    . MET A 338 ? 1.9355 2.1826 1.5222 0.1140  0.0036  -0.1759 441  MET A SD    
2507 C  CE    . MET A 338 ? 1.6308 1.8712 1.1978 0.1065  -0.0121 -0.1730 441  MET A CE    
2508 N  N     . ALA A 339 ? 1.5362 1.7217 1.0278 0.1221  -0.0286 -0.2231 442  ALA A N     
2509 C  CA    . ALA A 339 ? 1.5190 1.6986 1.0134 0.1110  -0.0478 -0.2239 442  ALA A CA    
2510 C  C     . ALA A 339 ? 1.5643 1.7551 1.0974 0.1019  -0.0511 -0.2112 442  ALA A C     
2511 O  O     . ALA A 339 ? 1.5461 1.7397 1.1043 0.1031  -0.0433 -0.2087 442  ALA A O     
2512 C  CB    . ALA A 339 ? 1.4853 1.6411 0.9685 0.1092  -0.0596 -0.2421 442  ALA A CB    
2513 N  N     . LEU A 340 ? 1.5389 1.7363 1.0758 0.0937  -0.0627 -0.2031 443  LEU A N     
2514 C  CA    . LEU A 340 ? 1.4374 1.6455 1.0077 0.0857  -0.0655 -0.1900 443  LEU A CA    
2515 C  C     . LEU A 340 ? 1.4581 1.6610 1.0347 0.0764  -0.0845 -0.1930 443  LEU A C     
2516 O  O     . LEU A 340 ? 1.5014 1.7089 1.0637 0.0741  -0.0939 -0.1896 443  LEU A O     
2517 C  CB    . LEU A 340 ? 1.4125 1.6371 0.9833 0.0860  -0.0573 -0.1733 443  LEU A CB    
2518 C  CG    . LEU A 340 ? 1.4541 1.6899 1.0576 0.0807  -0.0523 -0.1590 443  LEU A CG    
2519 C  CD1   . LEU A 340 ? 1.5122 1.7607 1.1094 0.0826  -0.0400 -0.1450 443  LEU A CD1   
2520 C  CD2   . LEU A 340 ? 1.4765 1.7119 1.0978 0.0720  -0.0669 -0.1544 443  LEU A CD2   
2521 N  N     . ASN A 341 ? 1.5508 1.7451 1.1491 0.0714  -0.0900 -0.1987 444  ASN A N     
2522 C  CA    . ASN A 341 ? 1.5866 1.7784 1.1962 0.0615  -0.1069 -0.2005 444  ASN A CA    
2523 C  C     . ASN A 341 ? 1.4895 1.6975 1.1202 0.0567  -0.1092 -0.1838 444  ASN A C     
2524 O  O     . ASN A 341 ? 1.4172 1.6310 1.0722 0.0562  -0.1008 -0.1746 444  ASN A O     
2525 C  CB    . ASN A 341 ? 1.5657 1.7435 1.1937 0.0574  -0.1098 -0.2095 444  ASN A CB    
2526 C  CG    . ASN A 341 ? 1.6647 1.8219 1.2690 0.0605  -0.1115 -0.2276 444  ASN A CG    
2527 O  OD1   . ASN A 341 ? 1.7029 1.8495 1.2995 0.0534  -0.1252 -0.2379 444  ASN A OD1   
2528 N  ND2   . ASN A 341 ? 1.6543 1.8059 1.2468 0.0710  -0.0974 -0.2318 444  ASN A ND2   
2529 N  N     . LEU A 342 ? 1.5179 1.7330 1.1385 0.0537  -0.1206 -0.1800 445  LEU A N     
2530 C  CA    . LEU A 342 ? 1.4542 1.6835 1.0903 0.0513  -0.1222 -0.1638 445  LEU A CA    
2531 C  C     . LEU A 342 ? 1.5033 1.7343 1.1710 0.0431  -0.1306 -0.1613 445  LEU A C     
2532 O  O     . LEU A 342 ? 1.5333 1.7549 1.2096 0.0383  -0.1368 -0.1722 445  LEU A O     
2533 C  CB    . LEU A 342 ? 1.4363 1.6732 1.0495 0.0528  -0.1313 -0.1599 445  LEU A CB    
2534 C  CG    . LEU A 342 ? 1.3843 1.6213 0.9651 0.0612  -0.1223 -0.1589 445  LEU A CG    
2535 C  CD1   . LEU A 342 ? 1.4212 1.6679 0.9854 0.0630  -0.1300 -0.1492 445  LEU A CD1   
2536 C  CD2   . LEU A 342 ? 1.3158 1.5548 0.9035 0.0656  -0.1030 -0.1505 445  LEU A CD2   
2537 N  N     . TRP A 343 ? 1.5497 1.7917 1.2339 0.0418  -0.1300 -0.1466 446  TRP A N     
2538 C  CA    . TRP A 343 ? 1.3843 1.6296 1.0984 0.0353  -0.1360 -0.1419 446  TRP A CA    
2539 C  C     . TRP A 343 ? 1.4410 1.6977 1.1561 0.0327  -0.1497 -0.1358 446  TRP A C     
2540 O  O     . TRP A 343 ? 1.4858 1.7495 1.1834 0.0375  -0.1502 -0.1283 446  TRP A O     
2541 C  CB    . TRP A 343 ? 1.3553 1.6037 1.0899 0.0362  -0.1237 -0.1297 446  TRP A CB    
2542 C  CG    . TRP A 343 ? 1.3867 1.6275 1.1265 0.0383  -0.1115 -0.1347 446  TRP A CG    
2543 C  CD1   . TRP A 343 ? 1.3785 1.6191 1.1043 0.0442  -0.0989 -0.1345 446  TRP A CD1   
2544 C  CD2   . TRP A 343 ? 1.4453 1.6790 1.2060 0.0351  -0.1106 -0.1401 446  TRP A CD2   
2545 N  NE1   . TRP A 343 ? 1.4024 1.6378 1.1401 0.0453  -0.0907 -0.1395 446  TRP A NE1   
2546 C  CE2   . TRP A 343 ? 1.5061 1.7362 1.2644 0.0401  -0.0977 -0.1429 446  TRP A CE2   
2547 C  CE3   . TRP A 343 ? 1.3928 1.6234 1.1740 0.0287  -0.1191 -0.1423 446  TRP A CE3   
2548 C  CZ2   . TRP A 343 ? 1.4704 1.6934 1.2451 0.0399  -0.0937 -0.1477 446  TRP A CZ2   
2549 C  CZ3   . TRP A 343 ? 1.4594 1.6813 1.2559 0.0277  -0.1144 -0.1469 446  TRP A CZ3   
2550 C  CH2   . TRP A 343 ? 1.4336 1.6515 1.2264 0.0337  -0.1022 -0.1495 446  TRP A CH2   
2551 N  N     . PRO A 344 ? 1.4535 1.7130 1.1888 0.0256  -0.1606 -0.1383 447  PRO A N     
2552 C  CA    . PRO A 344 ? 1.4108 1.6847 1.1502 0.0237  -0.1737 -0.1318 447  PRO A CA    
2553 C  C     . PRO A 344 ? 1.4273 1.7100 1.1771 0.0282  -0.1676 -0.1142 447  PRO A C     
2554 O  O     . PRO A 344 ? 1.3944 1.6728 1.1605 0.0285  -0.1566 -0.1078 447  PRO A O     
2555 C  CB    . PRO A 344 ? 1.3432 1.6177 1.1063 0.0143  -0.1836 -0.1384 447  PRO A CB    
2556 C  CG    . PRO A 344 ? 1.3073 1.5684 1.0852 0.0128  -0.1724 -0.1417 447  PRO A CG    
2557 C  CD    . PRO A 344 ? 1.4187 1.6689 1.1738 0.0193  -0.1612 -0.1467 447  PRO A CD    
2558 N  N     . VAL A 345 ? 1.4942 1.7883 1.2332 0.0320  -0.1751 -0.1064 448  VAL A N     
2559 C  CA    . VAL A 345 ? 1.5948 1.8948 1.3397 0.0375  -0.1695 -0.0893 448  VAL A CA    
2560 C  C     . VAL A 345 ? 1.7105 2.0176 1.4868 0.0337  -0.1736 -0.0835 448  VAL A C     
2561 O  O     . VAL A 345 ? 1.6953 2.0116 1.4830 0.0285  -0.1866 -0.0891 448  VAL A O     
2562 C  CB    . VAL A 345 ? 1.5060 1.8151 1.2277 0.0442  -0.1763 -0.0824 448  VAL A CB    
2563 C  CG1   . VAL A 345 ? 1.5398 1.8508 1.2646 0.0507  -0.1689 -0.0645 448  VAL A CG1   
2564 C  CG2   . VAL A 345 ? 1.5341 1.8359 1.2231 0.0478  -0.1724 -0.0892 448  VAL A CG2   
2565 N  N     . PRO A 346 ? 1.9305 2.2340 1.7213 0.0356  -0.1629 -0.0726 449  PRO A N     
2566 C  CA    . PRO A 346 ? 1.9004 2.2102 1.7198 0.0329  -0.1658 -0.0669 449  PRO A CA    
2567 C  C     . PRO A 346 ? 2.0888 2.4134 1.9102 0.0380  -0.1747 -0.0561 449  PRO A C     
2568 O  O     . PRO A 346 ? 2.1008 2.4316 1.9011 0.0431  -0.1806 -0.0540 449  PRO A O     
2569 C  CB    . PRO A 346 ? 1.8658 2.1645 1.6946 0.0340  -0.1506 -0.0596 449  PRO A CB    
2570 N  N     . HIS A 347 ? 1.9220 2.2530 1.7680 0.0376  -0.1755 -0.0489 450  HIS A N     
2571 C  CA    . HIS A 347 ? 1.8390 2.1857 1.6897 0.0437  -0.1834 -0.0380 450  HIS A CA    
2572 C  C     . HIS A 347 ? 1.8586 2.1986 1.6917 0.0540  -0.1748 -0.0242 450  HIS A C     
2573 O  O     . HIS A 347 ? 1.8015 2.1264 1.6343 0.0549  -0.1611 -0.0192 450  HIS A O     
2574 C  CB    . HIS A 347 ? 1.6651 2.0195 1.5470 0.0414  -0.1843 -0.0336 450  HIS A CB    
2575 N  N     . GLY A 348 ? 1.8832 2.2343 1.7012 0.0613  -0.1831 -0.0181 451  GLY A N     
2576 C  CA    . GLY A 348 ? 1.9120 2.2554 1.7100 0.0714  -0.1756 -0.0047 451  GLY A CA    
2577 C  C     . GLY A 348 ? 2.0597 2.3935 1.8266 0.0724  -0.1715 -0.0084 451  GLY A C     
2578 O  O     . GLY A 348 ? 2.0882 2.4120 1.8516 0.0658  -0.1653 -0.0187 451  GLY A O     
2579 N  N     . LEU A 349 ? 2.1292 2.4662 1.8731 0.0816  -0.1746 0.0004  452  LEU A N     
2580 C  CA    . LEU A 349 ? 2.1068 2.4361 1.8186 0.0838  -0.1710 -0.0017 452  LEU A CA    
2581 C  C     . LEU A 349 ? 2.1602 2.4728 1.8571 0.0900  -0.1556 0.0124  452  LEU A C     
2582 O  O     . LEU A 349 ? 2.1348 2.4483 1.8212 0.0997  -0.1568 0.0260  452  LEU A O     
2583 C  CB    . LEU A 349 ? 1.9847 2.3298 1.6781 0.0890  -0.1865 -0.0030 452  LEU A CB    
2584 N  N     . GLU A 350 ? 2.2434 2.5406 1.9391 0.0843  -0.1413 0.0093  453  GLU A N     
2585 C  CA    . GLU A 350 ? 2.2820 2.5625 1.9633 0.0875  -0.1259 0.0214  453  GLU A CA    
2586 C  C     . GLU A 350 ? 2.2811 2.5573 1.9303 0.0898  -0.1214 0.0208  453  GLU A C     
2587 O  O     . GLU A 350 ? 2.2055 2.4921 1.8381 0.0938  -0.1324 0.0167  453  GLU A O     
2588 C  CB    . GLU A 350 ? 2.2878 2.5561 1.9871 0.0795  -0.1127 0.0194  453  GLU A CB    
2589 C  CG    . GLU A 350 ? 2.3495 2.6198 2.0784 0.0776  -0.1153 0.0209  453  GLU A CG    
2590 C  CD    . GLU A 350 ? 2.4961 2.7543 2.2403 0.0699  -0.1029 0.0188  453  GLU A CD    
2591 O  OE1   . GLU A 350 ? 2.5577 2.8085 2.2920 0.0654  -0.0929 0.0156  453  GLU A OE1   
2592 O  OE2   . GLU A 350 ? 2.3483 2.6058 2.1147 0.0685  -0.1031 0.0205  453  GLU A OE2   
2593 N  N     . ASP A 351 ? 2.3775 2.6392 2.0176 0.0870  -0.1053 0.0247  454  ASP A N     
2594 C  CA    . ASP A 351 ? 2.3538 2.6117 1.9645 0.0886  -0.0988 0.0240  454  ASP A CA    
2595 C  C     . ASP A 351 ? 2.2669 2.5342 1.8752 0.0848  -0.1051 0.0067  454  ASP A C     
2596 O  O     . ASP A 351 ? 2.2771 2.5490 1.9084 0.0784  -0.1093 -0.0047 454  ASP A O     
2597 C  CB    . ASP A 351 ? 2.4250 2.6681 2.0321 0.0841  -0.0796 0.0304  454  ASP A CB    
2598 C  CG    . ASP A 351 ? 2.5426 2.7719 2.1437 0.0882  -0.0722 0.0480  454  ASP A CG    
2599 O  OD1   . ASP A 351 ? 2.5750 2.8049 2.1598 0.0978  -0.0789 0.0574  454  ASP A OD1   
2600 O  OD2   . ASP A 351 ? 2.6275 2.8449 2.2395 0.0820  -0.0599 0.0523  454  ASP A OD2   
2601 N  N     . LEU A 352 ? 1.9561 2.2246 1.5346 0.0891  -0.1054 0.0049  455  LEU A N     
2602 C  CA    . LEU A 352 ? 1.7670 2.0426 1.3377 0.0871  -0.1128 -0.0117 455  LEU A CA    
2603 C  C     . LEU A 352 ? 1.6512 1.9224 1.2342 0.0798  -0.1022 -0.0227 455  LEU A C     
2604 O  O     . LEU A 352 ? 1.5770 1.8521 1.1616 0.0771  -0.1088 -0.0379 455  LEU A O     
2605 C  CB    . LEU A 352 ? 1.7271 2.0031 1.2599 0.0942  -0.1137 -0.0103 455  LEU A CB    
2606 C  CG    . LEU A 352 ? 1.7890 2.0707 1.3065 0.1031  -0.1249 0.0009  455  LEU A CG    
2607 C  CD1   . LEU A 352 ? 1.7689 2.0513 1.2472 0.1100  -0.1267 0.0007  455  LEU A CD1   
2608 C  CD2   . LEU A 352 ? 1.8301 2.1259 1.3681 0.1019  -0.1441 -0.0050 455  LEU A CD2   
2609 N  N     . LEU A 353 ? 1.5694 1.8326 1.1608 0.0765  -0.0864 -0.0155 456  LEU A N     
2610 C  CA    . LEU A 353 ? 1.4793 1.7408 1.0855 0.0701  -0.0764 -0.0245 456  LEU A CA    
2611 C  C     . LEU A 353 ? 1.5189 1.7790 1.1586 0.0641  -0.0760 -0.0233 456  LEU A C     
2612 O  O     . LEU A 353 ? 1.5412 1.7994 1.1906 0.0650  -0.0798 -0.0136 456  LEU A O     
2613 C  CB    . LEU A 353 ? 1.4007 1.6572 0.9922 0.0699  -0.0585 -0.0182 456  LEU A CB    
2614 C  CG    . LEU A 353 ? 1.4482 1.7062 1.0062 0.0757  -0.0563 -0.0212 456  LEU A CG    
2615 C  CD1   . LEU A 353 ? 1.4273 1.6819 0.9739 0.0745  -0.0371 -0.0139 456  LEU A CD1   
2616 C  CD2   . LEU A 353 ? 1.4252 1.6882 0.9813 0.0761  -0.0638 -0.0394 456  LEU A CD2   
2617 N  N     . ASN A 354 ? 1.4147 1.6755 1.0711 0.0589  -0.0712 -0.0332 457  ASN A N     
2618 C  CA    . ASN A 354 ? 1.4325 1.6921 1.1197 0.0532  -0.0710 -0.0340 457  ASN A CA    
2619 C  C     . ASN A 354 ? 1.3468 1.6050 1.0436 0.0486  -0.0567 -0.0359 457  ASN A C     
2620 O  O     . ASN A 354 ? 1.2924 1.5533 1.0014 0.0465  -0.0568 -0.0471 457  ASN A O     
2621 C  CB    . ASN A 354 ? 1.4126 1.6768 1.1146 0.0517  -0.0846 -0.0460 457  ASN A CB    
2622 C  CG    . ASN A 354 ? 1.3528 1.6158 1.0852 0.0466  -0.0851 -0.0455 457  ASN A CG    
2623 O  OD1   . ASN A 354 ? 1.3796 1.6428 1.1267 0.0432  -0.0859 -0.0557 457  ASN A OD1   
2624 N  ND2   . ASN A 354 ? 1.3650 1.6252 1.1055 0.0469  -0.0841 -0.0335 457  ASN A ND2   
2625 N  N     . PRO A 355 ? 1.3659 1.6200 1.0577 0.0469  -0.0442 -0.0248 458  PRO A N     
2626 C  CA    . PRO A 355 ? 1.4069 1.6628 1.1092 0.0416  -0.0309 -0.0262 458  PRO A CA    
2627 C  C     . PRO A 355 ? 1.5636 1.8197 1.2954 0.0362  -0.0320 -0.0296 458  PRO A C     
2628 O  O     . PRO A 355 ? 1.5236 1.7852 1.2668 0.0337  -0.0262 -0.0365 458  PRO A O     
2629 C  CB    . PRO A 355 ? 1.3743 1.6243 1.0648 0.0395  -0.0191 -0.0120 458  PRO A CB    
2630 C  CG    . PRO A 355 ? 1.4194 1.6647 1.0855 0.0462  -0.0250 -0.0050 458  PRO A CG    
2631 C  CD    . PRO A 355 ? 1.3919 1.6394 1.0667 0.0496  -0.0415 -0.0104 458  PRO A CD    
2632 N  N     . ILE A 356 ? 1.9083 2.1593 1.6523 0.0353  -0.0392 -0.0246 459  ILE A N     
2633 C  CA    . ILE A 356 ? 1.9087 2.1587 1.6789 0.0304  -0.0398 -0.0269 459  ILE A CA    
2634 C  C     . ILE A 356 ? 1.9028 2.1581 1.6855 0.0311  -0.0475 -0.0402 459  ILE A C     
2635 O  O     . ILE A 356 ? 1.9195 2.1755 1.7221 0.0275  -0.0458 -0.0440 459  ILE A O     
2636 C  CB    . ILE A 356 ? 2.0214 2.2640 1.7991 0.0305  -0.0447 -0.0178 459  ILE A CB    
2637 C  CG1   . ILE A 356 ? 2.0954 2.3296 1.8548 0.0318  -0.0383 -0.0045 459  ILE A CG1   
2638 C  CG2   . ILE A 356 ? 1.8986 2.1381 1.6996 0.0249  -0.0418 -0.0177 459  ILE A CG2   
2639 C  CD1   . ILE A 356 ? 2.1417 2.3669 1.9058 0.0337  -0.0419 0.0052  459  ILE A CD1   
2640 N  N     . GLY A 357 ? 1.5317 1.7896 1.3022 0.0354  -0.0561 -0.0475 460  GLY A N     
2641 C  CA    . GLY A 357 ? 1.4149 1.6747 1.1951 0.0354  -0.0635 -0.0603 460  GLY A CA    
2642 C  C     . GLY A 357 ? 1.3483 1.6104 1.1325 0.0351  -0.0549 -0.0682 460  GLY A C     
2643 O  O     . GLY A 357 ? 1.3826 1.6480 1.1608 0.0350  -0.0435 -0.0648 460  GLY A O     
2644 N  N     . VAL A 358 ? 1.2261 1.4868 1.0212 0.0351  -0.0605 -0.0789 461  VAL A N     
2645 C  CA    . VAL A 358 ? 1.2491 1.5116 1.0488 0.0366  -0.0533 -0.0869 461  VAL A CA    
2646 C  C     . VAL A 358 ? 1.3134 1.5775 1.0894 0.0420  -0.0493 -0.0930 461  VAL A C     
2647 O  O     . VAL A 358 ? 1.3241 1.5860 1.0809 0.0443  -0.0559 -0.0949 461  VAL A O     
2648 C  CB    . VAL A 358 ? 1.2272 1.4845 1.0425 0.0358  -0.0603 -0.0961 461  VAL A CB    
2649 C  CG1   . VAL A 358 ? 1.2070 1.4587 1.0087 0.0379  -0.0704 -0.1066 461  VAL A CG1   
2650 C  CG2   . VAL A 358 ? 1.2299 1.4894 1.0558 0.0377  -0.0517 -0.1008 461  VAL A CG2   
2651 N  N     . THR A 359 ? 1.2966 1.5658 1.0736 0.0445  -0.0385 -0.0960 462  THR A N     
2652 C  CA    . THR A 359 ? 1.2655 1.5368 1.0212 0.0507  -0.0328 -0.1024 462  THR A CA    
2653 C  C     . THR A 359 ? 1.3409 1.6071 1.0990 0.0553  -0.0347 -0.1160 462  THR A C     
2654 O  O     . THR A 359 ? 1.3295 1.5960 1.1080 0.0546  -0.0331 -0.1179 462  THR A O     
2655 C  CB    . THR A 359 ? 1.2060 1.4885 0.9603 0.0512  -0.0176 -0.0955 462  THR A CB    
2656 O  OG1   . THR A 359 ? 1.2028 1.4919 0.9767 0.0517  -0.0110 -0.0985 462  THR A OG1   
2657 C  CG2   . THR A 359 ? 1.1956 1.4801 0.9536 0.0448  -0.0149 -0.0813 462  THR A CG2   
2658 N  N     . GLY A 360 ? 1.5689 1.8288 1.3045 0.0604  -0.0381 -0.1256 463  GLY A N     
2659 C  CA    . GLY A 360 ? 1.5363 1.7874 1.2698 0.0652  -0.0397 -0.1392 463  GLY A CA    
2660 C  C     . GLY A 360 ? 1.5809 1.8187 1.2995 0.0644  -0.0531 -0.1493 463  GLY A C     
2661 O  O     . GLY A 360 ? 1.4354 1.6728 1.1531 0.0590  -0.0635 -0.1451 463  GLY A O     
2662 N  N     . SER A 361 ? 1.5633 1.7903 1.2702 0.0698  -0.0532 -0.1626 464  SER A N     
2663 C  CA    . SER A 361 ? 1.5696 1.7827 1.2598 0.0681  -0.0658 -0.1739 464  SER A CA    
2664 C  C     . SER A 361 ? 1.4875 1.6928 1.1983 0.0602  -0.0774 -0.1758 464  SER A C     
2665 O  O     . SER A 361 ? 1.3431 1.5479 1.0771 0.0590  -0.0741 -0.1732 464  SER A O     
2666 C  CB    . SER A 361 ? 1.5057 1.7064 1.1752 0.0764  -0.0613 -0.1882 464  SER A CB    
2667 O  OG    . SER A 361 ? 1.4969 1.6832 1.1465 0.0739  -0.0737 -0.1999 464  SER A OG    
2668 N  N     . ASN A 362 ? 1.5064 1.7068 1.2085 0.0546  -0.0912 -0.1801 465  ASN A N     
2669 C  CA    . ASN A 362 ? 1.4735 1.6675 1.1940 0.0462  -0.1026 -0.1825 465  ASN A CA    
2670 C  C     . ASN A 362 ? 1.5196 1.6947 1.2391 0.0473  -0.1026 -0.1961 465  ASN A C     
2671 O  O     . ASN A 362 ? 1.6112 1.7746 1.3062 0.0515  -0.1027 -0.2081 465  ASN A O     
2672 C  CB    . ASN A 362 ? 1.4892 1.6860 1.2002 0.0398  -0.1175 -0.1837 465  ASN A CB    
2673 C  CG    . ASN A 362 ? 1.5099 1.7068 1.2446 0.0302  -0.1286 -0.1821 465  ASN A CG    
2674 O  OD1   . ASN A 362 ? 1.5606 1.7465 1.3096 0.0273  -0.1285 -0.1874 465  ASN A OD1   
2675 N  ND2   . ASN A 362 ? 1.4432 1.6528 1.1819 0.0259  -0.1378 -0.1744 465  ASN A ND2   
2676 N  N     . PRO A 363 ? 1.4809 1.6509 1.2244 0.0443  -0.1018 -0.1945 466  PRO A N     
2677 C  CA    . PRO A 363 ? 1.5058 1.6548 1.2470 0.0452  -0.1022 -0.2070 466  PRO A CA    
2678 C  C     . PRO A 363 ? 1.5619 1.6967 1.2895 0.0377  -0.1157 -0.2190 466  PRO A C     
2679 O  O     . PRO A 363 ? 1.5959 1.7110 1.3055 0.0407  -0.1153 -0.2325 466  PRO A O     
2680 C  CB    . PRO A 363 ? 1.5494 1.6986 1.3205 0.0421  -0.1002 -0.2000 466  PRO A CB    
2681 C  CG    . PRO A 363 ? 1.4678 1.6379 1.2531 0.0434  -0.0938 -0.1852 466  PRO A CG    
2682 C  CD    . PRO A 363 ? 1.5371 1.7188 1.3086 0.0412  -0.0989 -0.1813 466  PRO A CD    
2683 N  N     . ASN A 364 ? 1.5891 1.7334 1.3247 0.0280  -0.1277 -0.2146 467  ASN A N     
2684 C  CA    . ASN A 364 ? 1.6665 1.8016 1.3902 0.0194  -0.1419 -0.2256 467  ASN A CA    
2685 C  C     . ASN A 364 ? 1.7600 1.8940 1.4500 0.0243  -0.1437 -0.2334 467  ASN A C     
2686 O  O     . ASN A 364 ? 1.8446 1.9959 1.5275 0.0271  -0.1437 -0.2251 467  ASN A O     
2687 C  CB    . ASN A 364 ? 1.6395 1.7904 1.3827 0.0090  -0.1537 -0.2173 467  ASN A CB    
2688 C  CG    . ASN A 364 ? 1.7927 1.9351 1.5320 -0.0026 -0.1688 -0.2283 467  ASN A CG    
2689 O  OD1   . ASN A 364 ? 1.9225 2.0488 1.6374 -0.0029 -0.1725 -0.2426 467  ASN A OD1   
2690 N  ND2   . ASN A 364 ? 1.8604 2.0139 1.6237 -0.0124 -0.1775 -0.2220 467  ASN A ND2   
2691 N  N     . LYS A 365 ? 1.7720 1.8842 1.4399 0.0255  -0.1449 -0.2492 468  LYS A N     
2692 C  CA    . LYS A 365 ? 1.8090 1.9174 1.4419 0.0313  -0.1455 -0.2580 468  LYS A CA    
2693 C  C     . LYS A 365 ? 1.8946 2.0068 1.5139 0.0218  -0.1628 -0.2638 468  LYS A C     
2694 O  O     . LYS A 365 ? 2.0685 2.1785 1.6567 0.0260  -0.1649 -0.2709 468  LYS A O     
2695 C  CB    . LYS A 365 ? 1.8505 1.9322 1.4626 0.0384  -0.1382 -0.2730 468  LYS A CB    
2696 C  CG    . LYS A 365 ? 1.7457 1.8270 1.3674 0.0506  -0.1205 -0.2676 468  LYS A CG    
2697 C  CD    . LYS A 365 ? 1.6799 1.7855 1.3017 0.0585  -0.1106 -0.2545 468  LYS A CD    
2698 C  CE    . LYS A 365 ? 1.6243 1.7335 1.2590 0.0691  -0.0939 -0.2485 468  LYS A CE    
2699 N  NZ    . LYS A 365 ? 1.5740 1.7076 1.2121 0.0742  -0.0846 -0.2349 468  LYS A NZ    
2700 N  N     . GLU A 366 ? 1.8819 2.0009 1.5232 0.0093  -0.1752 -0.2609 469  GLU A N     
2701 C  CA    . GLU A 366 ? 1.9538 2.0820 1.5855 0.0002  -0.1925 -0.2648 469  GLU A CA    
2702 C  C     . GLU A 366 ? 1.9339 2.0883 1.5629 0.0049  -0.1940 -0.2512 469  GLU A C     
2703 O  O     . GLU A 366 ? 2.0086 2.1712 1.6201 0.0019  -0.2064 -0.2546 469  GLU A O     
2704 C  CB    . GLU A 366 ? 1.9470 2.0771 1.6057 -0.0145 -0.2045 -0.2651 469  GLU A CB    
2705 C  CG    . GLU A 366 ? 2.1180 2.2419 1.7620 -0.0266 -0.2221 -0.2794 469  GLU A CG    
2706 C  CD    . GLU A 366 ? 2.0725 2.2217 1.7087 -0.0286 -0.2352 -0.2745 469  GLU A CD    
2707 O  OE1   . GLU A 366 ? 2.0798 2.2531 1.7351 -0.0257 -0.2341 -0.2580 469  GLU A OE1   
2708 O  OE2   . GLU A 366 ? 1.9578 2.1019 1.5674 -0.0326 -0.2466 -0.2872 469  GLU A OE2   
2709 N  N     . THR A 367 ? 1.8729 2.0394 1.5175 0.0122  -0.1817 -0.2360 470  THR A N     
2710 C  CA    . THR A 367 ? 1.8146 2.0024 1.4556 0.0172  -0.1811 -0.2222 470  THR A CA    
2711 C  C     . THR A 367 ? 1.7724 1.9572 1.3756 0.0259  -0.1779 -0.2274 470  THR A C     
2712 O  O     . THR A 367 ? 1.8108 1.9780 1.3943 0.0308  -0.1710 -0.2392 470  THR A O     
2713 C  CB    . THR A 367 ? 1.6724 1.8689 1.3360 0.0225  -0.1670 -0.2067 470  THR A CB    
2714 O  OG1   . THR A 367 ? 1.6699 1.8855 1.3341 0.0253  -0.1679 -0.1921 470  THR A OG1   
2715 C  CG2   . THR A 367 ? 1.6193 1.8058 1.2710 0.0323  -0.1503 -0.2091 470  THR A CG2   
2716 N  N     . PRO A 368 ? 1.7646 1.9658 1.3558 0.0286  -0.1827 -0.2187 471  PRO A N     
2717 C  CA    . PRO A 368 ? 1.8188 2.0181 1.3734 0.0378  -0.1781 -0.2215 471  PRO A CA    
2718 C  C     . PRO A 368 ? 1.7476 1.9412 1.2978 0.0478  -0.1576 -0.2180 471  PRO A C     
2719 O  O     . PRO A 368 ? 1.6647 1.8658 1.2387 0.0494  -0.1471 -0.2056 471  PRO A O     
2720 C  CB    . PRO A 368 ? 1.7535 1.9733 1.3045 0.0394  -0.1846 -0.2075 471  PRO A CB    
2721 C  CG    . PRO A 368 ? 1.7556 1.9856 1.3320 0.0291  -0.2002 -0.2055 471  PRO A CG    
2722 C  CD    . PRO A 368 ? 1.7394 1.9604 1.3467 0.0233  -0.1950 -0.2078 471  PRO A CD    
2723 N  N     . CYS A 369 ? 1.7351 1.9161 1.2544 0.0546  -0.1520 -0.2295 472  CYS A N     
2724 C  CA    . CYS A 369 ? 1.7204 1.8984 1.2323 0.0651  -0.1325 -0.2272 472  CYS A CA    
2725 C  C     . CYS A 369 ? 1.6630 1.8525 1.1508 0.0727  -0.1262 -0.2178 472  CYS A C     
2726 O  O     . CYS A 369 ? 1.7622 1.9601 1.2365 0.0709  -0.1373 -0.2139 472  CYS A O     
2727 C  CB    . CYS A 369 ? 1.7007 1.8569 1.1936 0.0695  -0.1280 -0.2451 472  CYS A CB    
2728 S  SG    . CYS A 369 ? 2.0960 2.2335 1.6123 0.0610  -0.1346 -0.2568 472  CYS A SG    
2729 N  N     . LEU A 370 ? 1.6000 1.7908 1.0826 0.0815  -0.1078 -0.2136 473  LEU A N     
2730 C  CA    . LEU A 370 ? 1.5900 1.7901 1.0484 0.0890  -0.0990 -0.2047 473  LEU A CA    
2731 C  C     . LEU A 370 ? 1.5677 1.7635 1.0145 0.0988  -0.0801 -0.2086 473  LEU A C     
2732 O  O     . LEU A 370 ? 1.4870 1.6862 0.9587 0.0999  -0.0683 -0.2043 473  LEU A O     
2733 C  CB    . LEU A 370 ? 1.5366 1.7534 1.0146 0.0866  -0.0955 -0.1845 473  LEU A CB    
2734 C  CG    . LEU A 370 ? 1.5707 1.7961 1.0234 0.0927  -0.0883 -0.1733 473  LEU A CG    
2735 C  CD1   . LEU A 370 ? 1.5567 1.7794 0.9761 0.0941  -0.1026 -0.1796 473  LEU A CD1   
2736 C  CD2   . LEU A 370 ? 1.5516 1.7895 1.0254 0.0895  -0.0847 -0.1537 473  LEU A CD2   
2737 N  N     . GLU A 371 ? 1.6352 1.8246 1.0444 0.1065  -0.0772 -0.2168 474  GLU A N     
2738 C  CA    . GLU A 371 ? 1.5622 1.7484 0.9571 0.1173  -0.0589 -0.2213 474  GLU A CA    
2739 C  C     . GLU A 371 ? 1.4885 1.6911 0.8762 0.1224  -0.0441 -0.2054 474  GLU A C     
2740 O  O     . GLU A 371 ? 1.4411 1.6486 0.8075 0.1224  -0.0489 -0.1988 474  GLU A O     
2741 C  CB    . GLU A 371 ? 1.5839 1.7520 0.9401 0.1234  -0.0626 -0.2398 474  GLU A CB    
2742 C  CG    . GLU A 371 ? 1.6896 1.8504 1.0345 0.1352  -0.0448 -0.2480 474  GLU A CG    
2743 C  CD    . GLU A 371 ? 1.9924 2.1317 1.2970 0.1413  -0.0491 -0.2675 474  GLU A CD    
2744 O  OE1   . GLU A 371 ? 2.0108 2.1435 1.2937 0.1359  -0.0656 -0.2738 474  GLU A OE1   
2745 O  OE2   . GLU A 371 ? 2.0174 2.1465 1.3117 0.1517  -0.0361 -0.2768 474  GLU A OE2   
2746 N  N     . LEU A 372 ? 1.4936 1.7051 0.8990 0.1265  -0.0262 -0.1990 475  LEU A N     
2747 C  CA    . LEU A 372 ? 1.4345 1.6622 0.8378 0.1295  -0.0106 -0.1834 475  LEU A CA    
2748 C  C     . LEU A 372 ? 1.4084 1.6394 0.8030 0.1401  0.0091  -0.1874 475  LEU A C     
2749 O  O     . LEU A 372 ? 1.4726 1.6949 0.8712 0.1451  0.0114  -0.2002 475  LEU A O     
2750 C  CB    . LEU A 372 ? 1.5801 1.8212 1.0211 0.1211  -0.0077 -0.1672 475  LEU A CB    
2751 C  CG    . LEU A 372 ? 1.4830 1.7250 0.9379 0.1114  -0.0233 -0.1588 475  LEU A CG    
2752 C  CD1   . LEU A 372 ? 1.4734 1.7063 0.9500 0.1053  -0.0379 -0.1685 475  LEU A CD1   
2753 C  CD2   . LEU A 372 ? 1.4944 1.7497 0.9726 0.1064  -0.0139 -0.1404 475  LEU A CD2   
2754 N  N     . GLU A 373 ? 1.4047 1.6489 0.7879 0.1438  0.0238  -0.1757 476  GLU A N     
2755 C  CA    . GLU A 373 ? 1.5149 1.7686 0.8948 0.1533  0.0447  -0.1757 476  GLU A CA    
2756 C  C     . GLU A 373 ? 1.4314 1.7057 0.8289 0.1489  0.0590  -0.1565 476  GLU A C     
2757 O  O     . GLU A 373 ? 1.4350 1.7121 0.8219 0.1442  0.0569  -0.1445 476  GLU A O     
2758 C  CB    . GLU A 373 ? 1.5292 1.7748 0.8639 0.1647  0.0503  -0.1850 476  GLU A CB    
2759 C  CG    . GLU A 373 ? 1.5728 1.7966 0.8886 0.1704  0.0404  -0.2062 476  GLU A CG    
2760 C  CD    . GLU A 373 ? 1.8121 2.0287 1.0849 0.1835  0.0501  -0.2158 476  GLU A CD    
2761 O  OE1   . GLU A 373 ? 1.9279 2.1591 1.1971 0.1912  0.0703  -0.2086 476  GLU A OE1   
2762 O  OE2   . GLU A 373 ? 1.9159 2.1126 1.1582 0.1858  0.0378  -0.2307 476  GLU A OE2   
2763 N  N     . PHE A 374 ? 1.4123 1.7008 0.8364 0.1503  0.0730  -0.1534 477  PHE A N     
2764 C  CA    . PHE A 374 ? 1.4384 1.7475 0.8812 0.1451  0.0878  -0.1363 477  PHE A CA    
2765 C  C     . PHE A 374 ? 1.4690 1.7911 0.8957 0.1552  0.1087  -0.1354 477  PHE A C     
2766 O  O     . PHE A 374 ? 1.4830 1.8026 0.9009 0.1665  0.1142  -0.1481 477  PHE A O     
2767 C  CB    . PHE A 374 ? 1.4920 1.8113 0.9792 0.1379  0.0879  -0.1323 477  PHE A CB    
2768 C  CG    . PHE A 374 ? 1.3928 1.7008 0.8974 0.1280  0.0691  -0.1319 477  PHE A CG    
2769 C  CD1   . PHE A 374 ? 1.4210 1.7141 0.9301 0.1297  0.0555  -0.1458 477  PHE A CD1   
2770 C  CD2   . PHE A 374 ? 1.3276 1.6391 0.8433 0.1173  0.0657  -0.1174 477  PHE A CD2   
2771 C  CE1   . PHE A 374 ? 1.4098 1.6944 0.9357 0.1206  0.0390  -0.1449 477  PHE A CE1   
2772 C  CE2   . PHE A 374 ? 1.2906 1.5928 0.8223 0.1094  0.0492  -0.1167 477  PHE A CE2   
2773 C  CZ    . PHE A 374 ? 1.3194 1.6094 0.8568 0.1109  0.0360  -0.1303 477  PHE A CZ    
2774 N  N     . ASP A 375 ? 1.5519 1.8872 0.9742 0.1512  0.1210  -0.1201 478  ASP A N     
2775 C  CA    . ASP A 375 ? 1.6403 1.9875 1.0414 0.1602  0.1409  -0.1176 478  ASP A CA    
2776 C  C     . ASP A 375 ? 1.6467 2.0137 1.0735 0.1657  0.1564  -0.1201 478  ASP A C     
2777 O  O     . ASP A 375 ? 1.7205 2.1046 1.1834 0.1570  0.1614  -0.1108 478  ASP A O     
2778 C  CB    . ASP A 375 ? 1.6234 1.9795 1.0171 0.1527  0.1505  -0.0990 478  ASP A CB    
2779 C  CG    . ASP A 375 ? 1.7684 2.1304 1.1280 0.1624  0.1676  -0.0968 478  ASP A CG    
2780 O  OD1   . ASP A 375 ? 1.9874 2.3466 1.3286 0.1756  0.1721  -0.1103 478  ASP A OD1   
2781 O  OD2   . ASP A 375 ? 2.0168 2.3848 1.3666 0.1571  0.1772  -0.0814 478  ASP A OD2   
2782 N  N     . TRP A 376 ? 1.7218 2.0865 1.1293 0.1804  0.1637  -0.1328 479  TRP A N     
2783 C  CA    . TRP A 376 ? 1.6978 2.0832 1.1253 0.1887  0.1804  -0.1346 479  TRP A CA    
2784 C  C     . TRP A 376 ? 1.6773 2.0863 1.0980 0.1905  0.2029  -0.1223 479  TRP A C     
2785 O  O     . TRP A 376 ? 1.7595 2.1624 1.1459 0.1923  0.2072  -0.1182 479  TRP A O     
2786 C  CB    . TRP A 376 ? 1.6916 2.0626 1.1005 0.2051  0.1795  -0.1537 479  TRP A CB    
2787 C  CG    . TRP A 376 ? 1.7580 2.1503 1.1853 0.2166  0.1971  -0.1559 479  TRP A CG    
2788 C  CD1   . TRP A 376 ? 1.7427 2.1507 1.1543 0.2289  0.2177  -0.1550 479  TRP A CD1   
2789 C  CD2   . TRP A 376 ? 1.8081 2.2097 1.2732 0.2177  0.1957  -0.1588 479  TRP A CD2   
2790 N  NE1   . TRP A 376 ? 1.7606 2.1884 1.1991 0.2380  0.2291  -0.1572 479  TRP A NE1   
2791 C  CE2   . TRP A 376 ? 1.7837 2.2077 1.2547 0.2314  0.2156  -0.1594 479  TRP A CE2   
2792 C  CE3   . TRP A 376 ? 1.6987 2.0925 1.1926 0.2090  0.1798  -0.1605 479  TRP A CE3   
2793 C  CZ2   . TRP A 376 ? 1.7632 2.2024 1.2681 0.2371  0.2192  -0.1616 479  TRP A CZ2   
2794 C  CZ3   . TRP A 376 ? 1.7384 2.1457 1.2642 0.2142  0.1837  -0.1627 479  TRP A CZ3   
2795 C  CH2   . TRP A 376 ? 1.7580 2.1880 1.2892 0.2283  0.2029  -0.1632 479  TRP A CH2   
2796 N  N     . PHE A 377 ? 1.6041 2.0413 1.0578 0.1899  0.2173  -0.1159 480  PHE A N     
2797 C  CA    . PHE A 377 ? 1.6720 2.1355 1.1256 0.1893  0.2395  -0.1030 480  PHE A CA    
2798 C  C     . PHE A 377 ? 1.8198 2.3019 1.2731 0.2062  0.2574  -0.1098 480  PHE A C     
2799 O  O     . PHE A 377 ? 1.9909 2.4679 1.4084 0.2190  0.2673  -0.1146 480  PHE A O     
2800 C  CB    . PHE A 377 ? 1.5503 2.0354 1.0433 0.1718  0.2429  -0.0870 480  PHE A CB    
2801 C  CG    . PHE A 377 ? 1.5957 2.0625 1.0890 0.1562  0.2270  -0.0793 480  PHE A CG    
2802 C  CD1   . PHE A 377 ? 1.5889 2.0438 1.0512 0.1521  0.2281  -0.0705 480  PHE A CD1   
2803 C  CD2   . PHE A 377 ? 1.6056 2.0668 1.1290 0.1468  0.2115  -0.0806 480  PHE A CD2   
2804 C  CE1   . PHE A 377 ? 1.5817 2.0198 1.0438 0.1395  0.2139  -0.0630 480  PHE A CE1   
2805 C  CE2   . PHE A 377 ? 1.5867 2.0313 1.1101 0.1338  0.1977  -0.0735 480  PHE A CE2   
2806 C  CZ    . PHE A 377 ? 1.6025 2.0357 1.0956 0.1304  0.1989  -0.0646 480  PHE A CZ    
2807 N  N     . SER A 378 ? 1.7462 2.2504 1.2386 0.2072  0.2618  -0.1100 481  SER A N     
2808 C  CA    . SER A 378 ? 1.8644 2.3890 1.3605 0.2244  0.2790  -0.1158 481  SER A CA    
2809 C  C     . SER A 378 ? 1.8380 2.3650 1.3643 0.2307  0.2714  -0.1252 481  SER A C     
2810 O  O     . SER A 378 ? 1.9007 2.4115 1.4109 0.2474  0.2695  -0.1401 481  SER A O     
2811 C  CB    . SER A 378 ? 1.8431 2.4073 1.3581 0.2199  0.3014  -0.1003 481  SER A CB    
2812 O  OG    . SER A 378 ? 1.9732 2.5337 1.4592 0.2140  0.3092  -0.0905 481  SER A OG    
2813 N  N     . SER A 379 ? 1.7054 2.2510 1.2739 0.2175  0.2673  -0.1165 482  SER A N     
2814 C  CA    . SER A 379 ? 1.6695 2.2177 1.2680 0.2219  0.2590  -0.1236 482  SER A CA    
2815 C  C     . SER A 379 ? 1.5739 2.1097 1.1933 0.2034  0.2397  -0.1194 482  SER A C     
2816 O  O     . SER A 379 ? 1.5361 2.0540 1.1403 0.1909  0.2305  -0.1147 482  SER A O     
2817 C  CB    . SER A 379 ? 1.7771 2.3680 1.4096 0.2278  0.2760  -0.1176 482  SER A CB    
2818 O  OG    . SER A 379 ? 1.5254 2.1192 1.1862 0.2331  0.2677  -0.1237 482  SER A OG    
2819 N  N     . VAL A 380 ? 1.6378 2.1834 1.2918 0.2026  0.2335  -0.1208 483  VAL A N     
2820 C  CA    . VAL A 380 ? 1.4017 1.9374 1.0773 0.1860  0.2164  -0.1168 483  VAL A CA    
2821 C  C     . VAL A 380 ? 1.3182 1.8729 1.0093 0.1667  0.2212  -0.1005 483  VAL A C     
2822 O  O     . VAL A 380 ? 1.3933 1.9811 1.1001 0.1649  0.2376  -0.0915 483  VAL A O     
2823 C  CB    . VAL A 380 ? 1.3153 1.8605 1.0241 0.1906  0.2110  -0.1211 483  VAL A CB    
2824 C  CG1   . VAL A 380 ? 1.4287 1.9609 1.1569 0.1746  0.1931  -0.1180 483  VAL A CG1   
2825 C  CG2   . VAL A 380 ? 1.2778 1.8031 0.9694 0.2109  0.2088  -0.1368 483  VAL A CG2   
2826 N  N     . VAL A 381 ? 1.1738 1.7072 0.8602 0.1521  0.2074  -0.0964 484  VAL A N     
2827 C  CA    . VAL A 381 ? 1.2914 1.8355 0.9900 0.1331  0.2101  -0.0813 484  VAL A CA    
2828 C  C     . VAL A 381 ? 1.2882 1.8322 1.0194 0.1207  0.1970  -0.0788 484  VAL A C     
2829 O  O     . VAL A 381 ? 1.1823 1.7000 0.9095 0.1195  0.1800  -0.0849 484  VAL A O     
2830 C  CB    . VAL A 381 ? 1.2869 1.8067 0.9519 0.1271  0.2061  -0.0770 484  VAL A CB    
2831 C  CG1   . VAL A 381 ? 1.2442 1.7735 0.9203 0.1083  0.2111  -0.0607 484  VAL A CG1   
2832 C  CG2   . VAL A 381 ? 1.2783 1.7957 0.9074 0.1409  0.2178  -0.0810 484  VAL A CG2   
2833 N  N     . LYS A 382 ? 1.2637 1.8377 1.0270 0.1112  0.2049  -0.0699 485  LYS A N     
2834 C  CA    . LYS A 382 ? 1.2135 1.7913 1.0086 0.0995  0.1942  -0.0673 485  LYS A CA    
2835 C  C     . LYS A 382 ? 1.1969 1.7760 0.9990 0.0785  0.1950  -0.0539 485  LYS A C     
2836 O  O     . LYS A 382 ? 1.1506 1.7404 0.9433 0.0726  0.2084  -0.0448 485  LYS A O     
2837 C  CB    . LYS A 382 ? 1.2437 1.8556 1.0720 0.1046  0.2008  -0.0684 485  LYS A CB    
2838 C  CG    . LYS A 382 ? 1.2528 1.8558 1.0962 0.1124  0.1873  -0.0779 485  LYS A CG    
2839 C  CD    . LYS A 382 ? 1.2878 1.8699 1.1071 0.1324  0.1846  -0.0912 485  LYS A CD    
2840 C  CE    . LYS A 382 ? 1.3956 1.9735 1.2323 0.1415  0.1746  -0.0996 485  LYS A CE    
2841 N  NZ    . LYS A 382 ? 1.4974 2.0514 1.3094 0.1602  0.1722  -0.1130 485  LYS A NZ    
2842 N  N     . PHE A 383 ? 1.2552 1.8219 1.0726 0.0674  0.1812  -0.0525 486  PHE A N     
2843 C  CA    . PHE A 383 ? 1.2159 1.7839 1.0432 0.0474  0.1821  -0.0403 486  PHE A CA    
2844 C  C     . PHE A 383 ? 1.2153 1.8213 1.0738 0.0389  0.1938  -0.0340 486  PHE A C     
2845 O  O     . PHE A 383 ? 1.2049 1.8313 1.0872 0.0454  0.1926  -0.0395 486  PHE A O     
2846 C  CB    . PHE A 383 ? 1.1470 1.6914 0.9820 0.0391  0.1645  -0.0413 486  PHE A CB    
2847 C  CG    . PHE A 383 ? 1.1701 1.7015 1.0011 0.0215  0.1637  -0.0300 486  PHE A CG    
2848 C  CD1   . PHE A 383 ? 1.1288 1.6331 0.9296 0.0215  0.1607  -0.0267 486  PHE A CD1   
2849 C  CD2   . PHE A 383 ? 1.1491 1.6944 1.0054 0.0053  0.1659  -0.0226 486  PHE A CD2   
2850 C  CE1   . PHE A 383 ? 1.0790 1.5693 0.8747 0.0069  0.1605  -0.0158 486  PHE A CE1   
2851 C  CE2   . PHE A 383 ? 1.1468 1.6764 0.9973 -0.0106 0.1657  -0.0125 486  PHE A CE2   
2852 C  CZ    . PHE A 383 ? 1.1647 1.6662 0.9847 -0.0092 0.1634  -0.0087 486  PHE A CZ    
2853 N  N     . PRO A 384 ? 1.2242 1.8411 1.0833 0.0245  0.2054  -0.0222 487  PRO A N     
2854 C  CA    . PRO A 384 ? 1.2113 1.8675 1.1006 0.0151  0.2172  -0.0161 487  PRO A CA    
2855 C  C     . PRO A 384 ? 1.3166 1.9816 1.2381 0.0055  0.2063  -0.0173 487  PRO A C     
2856 O  O     . PRO A 384 ? 1.2163 1.8557 1.1364 -0.0038 0.1934  -0.0167 487  PRO A O     
2857 C  CB    . PRO A 384 ? 1.1929 1.8480 1.0718 -0.0015 0.2290  -0.0029 487  PRO A CB    
2858 C  CG    . PRO A 384 ? 1.2088 1.8212 1.0595 -0.0044 0.2184  -0.0013 487  PRO A CG    
2859 C  CD    . PRO A 384 ? 1.2127 1.8063 1.0449 0.0156  0.2081  -0.0135 487  PRO A CD    
2860 N  N     . ASP A 385 ? 1.3353 2.0377 1.2856 0.0087  0.2115  -0.0191 488  ASP A N     
2861 C  CA    . ASP A 385 ? 1.3582 2.0734 1.3395 0.0007  0.2016  -0.0204 488  ASP A CA    
2862 C  C     . ASP A 385 ? 1.4485 2.1638 1.4405 -0.0248 0.2019  -0.0105 488  ASP A C     
2863 O  O     . ASP A 385 ? 1.4408 2.1521 1.4200 -0.0362 0.2123  -0.0017 488  ASP A O     
2864 C  CB    . ASP A 385 ? 1.3336 2.0928 1.3429 0.0103  0.2083  -0.0232 488  ASP A CB    
2865 C  CG    . ASP A 385 ? 1.4440 2.2404 1.4634 0.0036  0.2273  -0.0148 488  ASP A CG    
2866 O  OD1   . ASP A 385 ? 1.4725 2.2857 1.5104 -0.0174 0.2306  -0.0066 488  ASP A OD1   
2867 O  OD2   . ASP A 385 ? 1.6438 2.4523 1.6521 0.0192  0.2394  -0.0166 488  ASP A OD2   
2868 N  N     . MET A 386 ? 1.5827 2.3013 1.5974 -0.0338 0.1905  -0.0121 489  MET A N     
2869 C  CA    . MET A 386 ? 1.5916 2.3037 1.6141 -0.0579 0.1885  -0.0044 489  MET A CA    
2870 C  C     . MET A 386 ? 1.5403 2.2865 1.5784 -0.0736 0.2042  0.0046  489  MET A C     
2871 O  O     . MET A 386 ? 1.6001 2.3333 1.6310 -0.0926 0.2086  0.0131  489  MET A O     
2872 C  CB    . MET A 386 ? 1.6226 2.3347 1.6665 -0.0630 0.1735  -0.0089 489  MET A CB    
2873 C  CG    . MET A 386 ? 1.7390 2.4364 1.7867 -0.0868 0.1693  -0.0028 489  MET A CG    
2874 S  SD    . MET A 386 ? 1.8066 2.4502 1.8176 -0.0915 0.1664  0.0017  489  MET A SD    
2875 C  CE    . MET A 386 ? 1.6181 2.2503 1.6393 -0.1186 0.1622  0.0077  489  MET A CE    
2876 N  N     . SER A 387 ? 1.5151 2.3046 1.5742 -0.0658 0.2131  0.0034  490  SER A N     
2877 C  CA    . SER A 387 ? 1.5497 2.3759 1.6263 -0.0810 0.2286  0.0122  490  SER A CA    
2878 C  C     . SER A 387 ? 1.6136 2.4279 1.6639 -0.0839 0.2439  0.0201  490  SER A C     
2879 O  O     . SER A 387 ? 1.6832 2.5073 1.7386 -0.1043 0.2543  0.0298  490  SER A O     
2880 C  CB    . SER A 387 ? 1.5676 2.4447 1.6724 -0.0690 0.2351  0.0091  490  SER A CB    
2881 O  OG    . SER A 387 ? 1.5487 2.4260 1.6366 -0.0443 0.2420  0.0045  490  SER A OG    
2882 N  N     . VAL A 388 ? 1.6275 2.4201 1.6488 -0.0644 0.2453  0.0162  491  VAL A N     
2883 C  CA    . VAL A 388 ? 1.5904 2.3683 1.5826 -0.0659 0.2587  0.0237  491  VAL A CA    
2884 C  C     . VAL A 388 ? 1.5959 2.3326 1.5682 -0.0824 0.2532  0.0303  491  VAL A C     
2885 O  O     . VAL A 388 ? 1.6447 2.3758 1.6034 -0.0947 0.2655  0.0407  491  VAL A O     
2886 C  CB    . VAL A 388 ? 1.5251 2.2901 1.4901 -0.0402 0.2602  0.0166  491  VAL A CB    
2887 C  CG1   . VAL A 388 ? 1.4582 2.2101 1.3918 -0.0409 0.2744  0.0245  491  VAL A CG1   
2888 C  CG2   . VAL A 388 ? 1.4919 2.2954 1.4760 -0.0225 0.2660  0.0099  491  VAL A CG2   
2889 N  N     . ILE A 389 ? 1.5663 2.2734 1.5359 -0.0825 0.2354  0.0248  492  ILE A N     
2890 C  CA    . ILE A 389 ? 1.5414 2.2094 1.4934 -0.0969 0.2297  0.0310  492  ILE A CA    
2891 C  C     . ILE A 389 ? 1.6741 2.3541 1.6441 -0.1232 0.2365  0.0401  492  ILE A C     
2892 O  O     . ILE A 389 ? 1.6283 2.2843 1.5806 -0.1370 0.2421  0.0495  492  ILE A O     
2893 C  CB    . ILE A 389 ? 1.4747 2.1133 1.4242 -0.0911 0.2096  0.0229  492  ILE A CB    
2894 C  CG1   . ILE A 389 ? 1.4145 2.0474 1.3524 -0.0662 0.2027  0.0124  492  ILE A CG1   
2895 C  CG2   . ILE A 389 ? 1.4754 2.0709 1.4011 -0.1007 0.2046  0.0290  492  ILE A CG2   
2896 C  CD1   . ILE A 389 ? 1.3478 1.9554 1.2494 -0.0553 0.2062  0.0139  492  ILE A CD1   
2897 N  N     . GLU A 390 ? 1.9086 2.6253 1.9134 -0.1307 0.2359  0.0376  493  GLU A N     
2898 C  CA    . GLU A 390 ? 1.9381 2.6690 1.9622 -0.1573 0.2415  0.0451  493  GLU A CA    
2899 C  C     . GLU A 390 ? 1.9486 2.6959 1.9674 -0.1672 0.2622  0.0561  493  GLU A C     
2900 O  O     . GLU A 390 ? 1.9830 2.7195 1.9994 -0.1898 0.2687  0.0652  493  GLU A O     
2901 C  CB    . GLU A 390 ? 2.0273 2.7994 2.0905 -0.1614 0.2360  0.0395  493  GLU A CB    
2902 C  CG    . GLU A 390 ? 1.9855 2.7470 2.0555 -0.1488 0.2168  0.0286  493  GLU A CG    
2903 C  CD    . GLU A 390 ? 2.1461 2.8743 2.2128 -0.1642 0.2039  0.0285  493  GLU A CD    
2904 O  OE1   . GLU A 390 ? 2.1837 2.8929 2.2405 -0.1840 0.2094  0.0365  493  GLU A OE1   
2905 O  OE2   . GLU A 390 ? 2.2135 2.9335 2.2868 -0.1562 0.1887  0.0204  493  GLU A OE2   
2906 N  N     . GLU A 391 ? 2.1484 2.9204 2.1643 -0.1506 0.2734  0.0554  494  GLU A N     
2907 C  CA    . GLU A 391 ? 2.1725 2.9631 2.1837 -0.1584 0.2945  0.0660  494  GLU A CA    
2908 C  C     . GLU A 391 ? 2.1931 2.9395 2.1663 -0.1639 0.2999  0.0750  494  GLU A C     
2909 O  O     . GLU A 391 ? 2.2046 2.9503 2.1755 -0.1841 0.3126  0.0864  494  GLU A O     
2910 C  CB    . GLU A 391 ? 2.2757 3.0983 2.2881 -0.1359 0.3047  0.0622  494  GLU A CB    
2911 C  CG    . GLU A 391 ? 2.3025 3.1679 2.3503 -0.1264 0.2996  0.0535  494  GLU A CG    
2912 C  CD    . GLU A 391 ? 2.2959 3.1818 2.3382 -0.0994 0.3072  0.0479  494  GLU A CD    
2913 O  OE1   . GLU A 391 ? 2.2456 3.1150 2.2570 -0.0896 0.3173  0.0508  494  GLU A OE1   
2914 O  OE2   . GLU A 391 ? 2.2979 3.2153 2.3654 -0.0872 0.3030  0.0404  494  GLU A OE2   
2915 N  N     . HIS A 392 ? 1.8696 2.5789 1.8125 -0.1463 0.2903  0.0704  495  HIS A N     
2916 C  CA    . HIS A 392 ? 1.7772 2.4452 1.6826 -0.1487 0.2943  0.0790  495  HIS A CA    
2917 C  C     . HIS A 392 ? 1.7744 2.4107 1.6778 -0.1701 0.2880  0.0850  495  HIS A C     
2918 O  O     . HIS A 392 ? 1.7753 2.3889 1.6580 -0.1820 0.2978  0.0966  495  HIS A O     
2919 C  CB    . HIS A 392 ? 1.6247 2.2643 1.5006 -0.1244 0.2839  0.0717  495  HIS A CB    
2920 C  CG    . HIS A 392 ? 1.6529 2.2542 1.4890 -0.1233 0.2879  0.0805  495  HIS A CG    
2921 N  ND1   . HIS A 392 ? 1.7334 2.3325 1.5572 -0.1372 0.3050  0.0943  495  HIS A ND1   
2922 C  CD2   . HIS A 392 ? 1.6124 2.1769 1.4184 -0.1099 0.2768  0.0778  495  HIS A CD2   
2923 C  CE1   . HIS A 392 ? 1.7355 2.2971 1.5220 -0.1313 0.3043  0.1000  495  HIS A CE1   
2924 N  NE2   . HIS A 392 ? 1.6802 2.2215 1.4559 -0.1147 0.2869  0.0901  495  HIS A NE2   
2925 N  N     . ALA A 393 ? 1.7636 2.3962 1.6866 -0.1746 0.2721  0.0774  496  ALA A N     
2926 C  CA    . ALA A 393 ? 1.7002 2.3012 1.6206 -0.1939 0.2657  0.0819  496  ALA A CA    
2927 C  C     . ALA A 393 ? 1.7603 2.3780 1.6969 -0.2211 0.2791  0.0913  496  ALA A C     
2928 O  O     . ALA A 393 ? 1.7491 2.3349 1.6700 -0.2377 0.2828  0.1002  496  ALA A O     
2929 C  CB    . ALA A 393 ? 1.6187 2.2149 1.5568 -0.1916 0.2463  0.0710  496  ALA A CB    
2930 N  N     . ASN A 394 ? 1.7802 2.4477 1.7483 -0.2263 0.2866  0.0896  497  ASN A N     
2931 C  CA    . ASN A 394 ? 1.7300 2.4183 1.7160 -0.2533 0.2998  0.0984  497  ASN A CA    
2932 C  C     . ASN A 394 ? 1.7803 2.4593 1.7424 -0.2590 0.3197  0.1118  497  ASN A C     
2933 O  O     . ASN A 394 ? 1.7862 2.4555 1.7475 -0.2835 0.3291  0.1217  497  ASN A O     
2934 C  CB    . ASN A 394 ? 1.6559 2.4045 1.6828 -0.2554 0.3028  0.0936  497  ASN A CB    
2935 C  CG    . ASN A 394 ? 1.6846 2.4436 1.7366 -0.2535 0.2839  0.0819  497  ASN A CG    
2936 O  OD1   . ASN A 394 ? 1.7291 2.4550 1.7755 -0.2627 0.2712  0.0795  497  ASN A OD1   
2937 N  ND2   . ASN A 394 ? 1.7154 2.5200 1.7942 -0.2406 0.2823  0.0748  497  ASN A ND2   
2938 N  N     . TRP A 395 ? 1.7949 2.4753 1.7360 -0.2369 0.3264  0.1124  498  TRP A N     
2939 C  CA    . TRP A 395 ? 1.7711 2.4457 1.6884 -0.2403 0.3462  0.1253  498  TRP A CA    
2940 C  C     . TRP A 395 ? 1.8084 2.4258 1.6874 -0.2444 0.3450  0.1338  498  TRP A C     
2941 O  O     . TRP A 395 ? 1.8492 2.4542 1.7162 -0.2619 0.3597  0.1469  498  TRP A O     
2942 C  CB    . TRP A 395 ? 1.7780 2.4729 1.6837 -0.2145 0.3535  0.1223  498  TRP A CB    
2943 C  CG    . TRP A 395 ? 1.8674 2.5487 1.7407 -0.2135 0.3718  0.1348  498  TRP A CG    
2944 C  CD1   . TRP A 395 ? 1.8679 2.5766 1.7476 -0.2261 0.3936  0.1457  498  TRP A CD1   
2945 C  CD2   . TRP A 395 ? 1.8442 2.4821 1.6733 -0.1990 0.3698  0.1383  498  TRP A CD2   
2946 N  NE1   . TRP A 395 ? 1.8547 2.5380 1.6954 -0.2200 0.4058  0.1559  498  TRP A NE1   
2947 C  CE2   . TRP A 395 ? 1.8729 2.5129 1.6818 -0.2032 0.3910  0.1515  498  TRP A CE2   
2948 C  CE3   . TRP A 395 ? 1.8577 2.4568 1.6628 -0.1831 0.3521  0.1318  498  TRP A CE3   
2949 C  CZ2   . TRP A 395 ? 2.0147 2.6186 1.7791 -0.1912 0.3945  0.1583  498  TRP A CZ2   
2950 C  CZ3   . TRP A 395 ? 1.8462 2.4115 1.6090 -0.1717 0.3551  0.1384  498  TRP A CZ3   
2951 C  CH2   . TRP A 395 ? 1.9600 2.5276 1.7022 -0.1755 0.3758  0.1515  498  TRP A CH2   
2952 N  N     . SER A 396 ? 1.8059 2.3882 1.6655 -0.2285 0.3281  0.1271  499  SER A N     
2953 C  CA    . SER A 396 ? 1.8138 2.3430 1.6367 -0.2292 0.3262  0.1353  499  SER A CA    
2954 C  C     . SER A 396 ? 1.8932 2.3966 1.7203 -0.2552 0.3255  0.1417  499  SER A C     
2955 O  O     . SER A 396 ? 1.9306 2.3897 1.7273 -0.2582 0.3270  0.1507  499  SER A O     
2956 C  CB    . SER A 396 ? 1.7586 2.2612 1.5639 -0.2061 0.3074  0.1261  499  SER A CB    
2957 O  OG    . SER A 396 ? 1.7368 2.2383 1.5649 -0.2087 0.2902  0.1156  499  SER A OG    
2958 N  N     . VAL A 397 ? 1.9571 2.4859 1.8196 -0.2733 0.3228  0.1370  500  VAL A N     
2959 C  CA    . VAL A 397 ? 1.9520 2.4593 1.8184 -0.3011 0.3251  0.1434  500  VAL A CA    
2960 C  C     . VAL A 397 ? 2.0398 2.5430 1.8925 -0.3180 0.3471  0.1590  500  VAL A C     
2961 O  O     . VAL A 397 ? 2.0343 2.4978 1.8686 -0.3344 0.3516  0.1684  500  VAL A O     
2962 C  CB    . VAL A 397 ? 2.0978 2.6395 2.0061 -0.3171 0.3178  0.1345  500  VAL A CB    
2963 C  CG1   . VAL A 397 ? 2.1894 2.7148 2.1033 -0.3495 0.3232  0.1413  500  VAL A CG1   
2964 C  CG2   . VAL A 397 ? 1.9758 2.5110 1.8926 -0.3022 0.2957  0.1205  500  VAL A CG2   
2965 N  N     . SER A 398 ? 2.0186 2.5611 1.8788 -0.3135 0.3619  0.1624  501  SER A N     
2966 C  CA    . SER A 398 ? 1.9637 2.5074 1.8120 -0.3283 0.3845  0.1776  501  SER A CA    
2967 C  C     . SER A 398 ? 2.0519 2.5720 1.8588 -0.3068 0.3919  0.1850  501  SER A C     
2968 O  O     . SER A 398 ? 2.1625 2.7114 1.9666 -0.2958 0.4046  0.1877  501  SER A O     
2969 C  CB    . SER A 398 ? 1.8960 2.5011 1.7804 -0.3387 0.3976  0.1776  501  SER A CB    
2970 O  OG    . SER A 398 ? 1.9115 2.5518 1.8023 -0.3127 0.3968  0.1698  501  SER A OG    
2971 N  N     . ARG A 399 ? 2.0315 2.4984 1.8055 -0.3001 0.3833  0.1882  502  ARG A N     
2972 C  CA    . ARG A 399 ? 2.0531 2.4927 1.7849 -0.2803 0.3879  0.1956  502  ARG A CA    
2973 C  C     . ARG A 399 ? 2.1078 2.4877 1.8062 -0.2852 0.3855  0.2056  502  ARG A C     
2974 O  O     . ARG A 399 ? 2.2019 2.5628 1.8956 -0.3083 0.3974  0.2171  502  ARG A O     
2975 C  CB    . ARG A 399 ? 1.9054 2.3536 1.6321 -0.2498 0.3729  0.1827  502  ARG A CB    
2976 N  N     . LEU A 420 ? 2.3916 2.1223 1.9735 -0.4233 0.2719  0.1709  523  LEU A N     
2977 C  CA    . LEU A 420 ? 2.3787 2.1607 1.9986 -0.4270 0.2583  0.1547  523  LEU A CA    
2978 C  C     . LEU A 420 ? 2.4659 2.2243 2.0846 -0.4226 0.2447  0.1429  523  LEU A C     
2979 O  O     . LEU A 420 ? 2.4251 2.2180 2.0674 -0.4119 0.2305  0.1309  523  LEU A O     
2980 C  CB    . LEU A 420 ? 2.2575 2.0722 1.9027 -0.4600 0.2648  0.1513  523  LEU A CB    
2981 C  CG    . LEU A 420 ? 2.1788 2.0504 1.8647 -0.4661 0.2518  0.1356  523  LEU A CG    
2982 C  CD1   . LEU A 420 ? 2.1066 2.0280 1.8111 -0.4399 0.2448  0.1330  523  LEU A CD1   
2983 C  CD2   . LEU A 420 ? 2.0134 1.9135 1.7220 -0.5004 0.2593  0.1339  523  LEU A CD2   
2984 N  N     . ARG A 421 ? 2.5497 2.2474 2.1393 -0.4304 0.2496  0.1468  524  ARG A N     
2985 C  CA    . ARG A 421 ? 2.5471 2.2179 2.1324 -0.4284 0.2386  0.1358  524  ARG A CA    
2986 C  C     . ARG A 421 ? 2.6030 2.2098 2.1495 -0.4105 0.2417  0.1440  524  ARG A C     
2987 O  O     . ARG A 421 ? 2.5465 2.1365 2.0885 -0.3957 0.2314  0.1366  524  ARG A O     
2988 C  CB    . ARG A 421 ? 2.5810 2.2443 2.1747 -0.4632 0.2397  0.1271  524  ARG A CB    
2989 C  CG    . ARG A 421 ? 2.5524 2.2792 2.1877 -0.4760 0.2298  0.1139  524  ARG A CG    
2990 C  CD    . ARG A 421 ? 2.5984 2.3172 2.2404 -0.5120 0.2310  0.1061  524  ARG A CD    
2991 N  NE    . ARG A 421 ? 2.6609 2.3150 2.2726 -0.5167 0.2306  0.1034  524  ARG A NE    
2992 C  CZ    . ARG A 421 ? 2.6826 2.3262 2.2939 -0.5081 0.2174  0.0914  524  ARG A CZ    
2993 N  NH1   . ARG A 421 ? 2.6029 2.2953 2.2423 -0.4946 0.2031  0.0811  524  ARG A NH1   
2994 N  NH2   . ARG A 421 ? 2.6946 2.2759 2.2753 -0.5127 0.2192  0.0898  524  ARG A NH2   
2995 N  N     . GLU A 422 ? 2.7002 2.2714 2.2184 -0.4110 0.2564  0.1597  525  GLU A N     
2996 C  CA    . GLU A 422 ? 2.7427 2.2506 2.2226 -0.3944 0.2605  0.1686  525  GLU A CA    
2997 C  C     . GLU A 422 ? 2.7283 2.2464 2.2059 -0.3569 0.2505  0.1701  525  GLU A C     
2998 O  O     . GLU A 422 ? 2.7664 2.2498 2.2278 -0.3407 0.2452  0.1684  525  GLU A O     
2999 C  CB    . GLU A 422 ? 2.7884 2.2575 2.2384 -0.4031 0.2789  0.1861  525  GLU A CB    
3000 C  CG    . GLU A 422 ? 2.8233 2.3219 2.2734 -0.3891 0.2850  0.1986  525  GLU A CG    
3001 C  CD    . GLU A 422 ? 2.7412 2.3008 2.2247 -0.4073 0.2866  0.1944  525  GLU A CD    
3002 O  OE1   . GLU A 422 ? 2.6989 2.2749 2.2041 -0.4342 0.2850  0.1838  525  GLU A OE1   
3003 O  OE2   . GLU A 422 ? 2.6966 2.2883 2.1844 -0.3943 0.2895  0.2017  525  GLU A OE2   
3004 N  N     . ASN A 423 ? 2.6849 2.2505 2.1786 -0.3430 0.2478  0.1730  526  ASN A N     
3005 C  CA    . ASN A 423 ? 2.6944 2.2772 2.1904 -0.3096 0.2368  0.1728  526  ASN A CA    
3006 C  C     . ASN A 423 ? 2.6463 2.2956 2.1754 -0.3030 0.2281  0.1657  526  ASN A C     
3007 O  O     . ASN A 423 ? 2.5646 2.2340 2.1040 -0.2804 0.2155  0.1599  526  ASN A O     
3008 C  CB    . ASN A 423 ? 2.7376 2.2879 2.2006 -0.2888 0.2446  0.1900  526  ASN A CB    
3009 C  CG    . ASN A 423 ? 2.7534 2.3248 2.2140 -0.2934 0.2552  0.2009  526  ASN A CG    
3010 O  OD1   . ASN A 423 ? 2.8492 2.3973 2.2956 -0.3140 0.2697  0.2094  526  ASN A OD1   
3011 N  ND2   . ASN A 423 ? 2.6792 2.2937 2.1525 -0.2743 0.2485  0.2008  526  ASN A ND2   
3012 N  N     . ASP A 424 ? 2.5397 2.2235 2.0857 -0.3217 0.2346  0.1658  527  ASP A N     
3013 C  CA    . ASP A 424 ? 2.4272 2.1732 2.0040 -0.3149 0.2271  0.1585  527  ASP A CA    
3014 C  C     . ASP A 424 ? 2.4339 2.2074 2.0389 -0.3137 0.2117  0.1418  527  ASP A C     
3015 O  O     . ASP A 424 ? 2.3917 2.2035 2.0151 -0.2963 0.2014  0.1357  527  ASP A O     
3016 C  CB    . ASP A 424 ? 2.3698 2.1461 1.9603 -0.3375 0.2382  0.1614  527  ASP A CB    
3017 C  CG    . ASP A 424 ? 2.4732 2.2235 2.0354 -0.3393 0.2545  0.1786  527  ASP A CG    
3018 O  OD1   . ASP A 424 ? 2.5287 2.2580 2.0668 -0.3157 0.2547  0.1879  527  ASP A OD1   
3019 O  OD2   . ASP A 424 ? 2.4479 2.1994 2.0119 -0.3645 0.2672  0.1833  527  ASP A OD2   
3020 N  N     . LYS A 425 ? 2.3746 2.1277 1.9818 -0.3320 0.2099  0.1343  528  LYS A N     
3021 C  CA    . LYS A 425 ? 2.3032 2.0790 1.9341 -0.3303 0.1953  0.1189  528  LYS A CA    
3022 C  C     . LYS A 425 ? 2.2550 2.0095 1.8745 -0.3035 0.1855  0.1173  528  LYS A C     
3023 O  O     . LYS A 425 ? 2.1636 1.9509 1.8027 -0.2878 0.1735  0.1092  528  LYS A O     
3024 C  CB    . LYS A 425 ? 2.3308 2.0911 1.9658 -0.3587 0.1962  0.1112  528  LYS A CB    
3025 C  CG    . LYS A 425 ? 2.2163 1.9975 1.8731 -0.3579 0.1813  0.0955  528  LYS A CG    
3026 C  CD    . LYS A 425 ? 2.1890 1.9525 1.8465 -0.3866 0.1818  0.0878  528  LYS A CD    
3027 C  CE    . LYS A 425 ? 2.3048 1.9996 1.9257 -0.3909 0.1895  0.0937  528  LYS A CE    
3028 N  NZ    . LYS A 425 ? 2.3937 2.0683 2.0129 -0.4199 0.1897  0.0852  528  LYS A NZ    
3029 N  N     . GLU A 426 ? 2.3047 2.0043 1.8926 -0.2977 0.1911  0.1253  529  GLU A N     
3030 C  CA    . GLU A 426 ? 2.2631 1.9417 1.8403 -0.2726 0.1827  0.1243  529  GLU A CA    
3031 C  C     . GLU A 426 ? 2.2380 1.9427 1.8188 -0.2453 0.1774  0.1291  529  GLU A C     
3032 O  O     . GLU A 426 ? 2.1640 1.8826 1.7552 -0.2266 0.1658  0.1229  529  GLU A O     
3033 C  CB    . GLU A 426 ? 2.3385 1.9523 1.8796 -0.2712 0.1913  0.1333  529  GLU A CB    
3034 C  CG    . GLU A 426 ? 2.3148 1.8955 1.8493 -0.2936 0.1933  0.1256  529  GLU A CG    
3035 C  CD    . GLU A 426 ? 2.4407 2.0225 1.9781 -0.3261 0.2033  0.1264  529  GLU A CD    
3036 O  OE1   . GLU A 426 ? 2.4831 2.0855 2.0237 -0.3301 0.2108  0.1349  529  GLU A OE1   
3037 O  OE2   . GLU A 426 ? 2.4289 1.9915 1.9652 -0.3481 0.2036  0.1183  529  GLU A OE2   
3038 N  N     . GLN A 427 ? 2.3313 2.0428 1.9030 -0.2430 0.1857  0.1402  530  GLN A N     
3039 C  CA    . GLN A 427 ? 2.2881 2.0248 1.8618 -0.2183 0.1803  0.1442  530  GLN A CA    
3040 C  C     . GLN A 427 ? 2.1777 1.9700 1.7853 -0.2151 0.1690  0.1318  530  GLN A C     
3041 O  O     . GLN A 427 ? 2.1091 1.9185 1.7238 -0.1938 0.1586  0.1287  530  GLN A O     
3042 C  CB    . GLN A 427 ? 2.3244 2.0574 1.8801 -0.2181 0.1921  0.1581  530  GLN A CB    
3043 C  CG    . GLN A 427 ? 2.4818 2.1583 2.0006 -0.2150 0.2027  0.1725  530  GLN A CG    
3044 C  CD    . GLN A 427 ? 2.6380 2.2879 2.1423 -0.1901 0.1951  0.1747  530  GLN A CD    
3045 O  OE1   . GLN A 427 ? 2.6842 2.3600 2.1984 -0.1687 0.1842  0.1721  530  GLN A OE1   
3046 N  NE2   . GLN A 427 ? 2.7339 2.3316 2.2147 -0.1930 0.2012  0.1796  530  GLN A NE2   
3047 N  N     . LEU A 428 ? 2.0693 1.8905 1.6984 -0.2362 0.1711  0.1247  531  LEU A N     
3048 C  CA    . LEU A 428 ? 1.9475 1.8190 1.6085 -0.2333 0.1606  0.1126  531  LEU A CA    
3049 C  C     . LEU A 428 ? 1.9118 1.7815 1.5842 -0.2264 0.1479  0.1017  531  LEU A C     
3050 O  O     . LEU A 428 ? 1.8409 1.7421 1.5319 -0.2127 0.1373  0.0942  531  LEU A O     
3051 C  CB    . LEU A 428 ? 1.8919 1.7944 1.5735 -0.2573 0.1659  0.1081  531  LEU A CB    
3052 C  CG    . LEU A 428 ? 1.8318 1.7505 1.5095 -0.2629 0.1778  0.1173  531  LEU A CG    
3053 C  CD1   . LEU A 428 ? 1.6962 1.6520 1.3996 -0.2856 0.1817  0.1115  531  LEU A CD1   
3054 C  CD2   . LEU A 428 ? 1.7837 1.7261 1.4611 -0.2389 0.1737  0.1195  531  LEU A CD2   
3055 N  N     . LYS A 429 ? 1.9448 1.7766 1.6050 -0.2358 0.1494  0.1005  532  LYS A N     
3056 C  CA    . LYS A 429 ? 1.9179 1.7436 1.5849 -0.2276 0.1384  0.0912  532  LYS A CA    
3057 C  C     . LYS A 429 ? 1.8824 1.6942 1.5373 -0.2000 0.1332  0.0959  532  LYS A C     
3058 O  O     . LYS A 429 ? 1.8232 1.6528 1.4928 -0.1866 0.1222  0.0884  532  LYS A O     
3059 C  CB    . LYS A 429 ? 1.9609 1.7472 1.6150 -0.2449 0.1421  0.0886  532  LYS A CB    
3060 C  CG    . LYS A 429 ? 1.9775 1.7780 1.6445 -0.2742 0.1462  0.0832  532  LYS A CG    
3061 C  CD    . LYS A 429 ? 1.9137 1.7629 1.6139 -0.2779 0.1353  0.0703  532  LYS A CD    
3062 C  CE    . LYS A 429 ? 1.9662 1.8007 1.6683 -0.2840 0.1275  0.0596  532  LYS A CE    
3063 N  NZ    . LYS A 429 ? 1.9586 1.7635 1.6487 -0.3106 0.1345  0.0587  532  LYS A NZ    
3064 N  N     . ALA A 430 ? 1.9084 1.6895 1.5369 -0.1912 0.1410  0.1088  533  ALA A N     
3065 C  CA    . ALA A 430 ? 1.8773 1.6475 1.4948 -0.1647 0.1359  0.1142  533  ALA A CA    
3066 C  C     . ALA A 430 ? 1.8498 1.6622 1.4823 -0.1494 0.1286  0.1134  533  ALA A C     
3067 O  O     . ALA A 430 ? 1.8510 1.6712 1.4883 -0.1297 0.1193  0.1116  533  ALA A O     
3068 C  CB    . ALA A 430 ? 1.9465 1.6715 1.5304 -0.1592 0.1463  0.1289  533  ALA A CB    
3069 N  N     . ILE A 431 ? 1.7972 1.6368 1.4371 -0.1581 0.1330  0.1144  534  ILE A N     
3070 C  CA    . ILE A 431 ? 1.7462 1.6253 1.3994 -0.1447 0.1263  0.1122  534  ILE A CA    
3071 C  C     . ILE A 431 ? 1.7146 1.6258 1.3963 -0.1415 0.1141  0.0984  534  ILE A C     
3072 O  O     . ILE A 431 ? 1.7164 1.6465 1.4060 -0.1241 0.1048  0.0956  534  ILE A O     
3073 C  CB    . ILE A 431 ? 1.7160 1.6162 1.3701 -0.1556 0.1350  0.1158  534  ILE A CB    
3074 C  CG1   . ILE A 431 ? 1.7882 1.6603 1.4119 -0.1515 0.1455  0.1310  534  ILE A CG1   
3075 C  CG2   . ILE A 431 ? 1.5454 1.4911 1.2190 -0.1460 0.1276  0.1090  534  ILE A CG2   
3076 C  CD1   . ILE A 431 ? 1.9006 1.7703 1.5112 -0.1262 0.1392  0.1370  534  ILE A CD1   
3077 N  N     . SER A 432 ? 1.6837 1.6011 1.3807 -0.1586 0.1137  0.0898  535  SER A N     
3078 C  CA    . SER A 432 ? 1.6280 1.5766 1.3515 -0.1564 0.1028  0.0772  535  SER A CA    
3079 C  C     . SER A 432 ? 1.6758 1.6097 1.3989 -0.1418 0.0939  0.0740  535  SER A C     
3080 O  O     . SER A 432 ? 1.6267 1.5857 1.3670 -0.1308 0.0842  0.0670  535  SER A O     
3081 C  CB    . SER A 432 ? 1.6126 1.5726 1.3516 -0.1786 0.1046  0.0695  535  SER A CB    
3082 O  OG    . SER A 432 ? 1.6321 1.6219 1.3957 -0.1757 0.0942  0.0581  535  SER A OG    
3083 N  N     . THR A 433 ? 1.7290 1.6220 1.4323 -0.1413 0.0977  0.0792  536  THR A N     
3084 C  CA    . THR A 433 ? 1.7029 1.5815 1.4055 -0.1277 0.0906  0.0765  536  THR A CA    
3085 C  C     . THR A 433 ? 1.7491 1.6319 1.4477 -0.1042 0.0854  0.0820  536  THR A C     
3086 O  O     . THR A 433 ? 1.7378 1.6189 1.4417 -0.0915 0.0784  0.0790  536  THR A O     
3087 C  CB    . THR A 433 ? 1.8073 1.6392 1.4883 -0.1336 0.0971  0.0801  536  THR A CB    
3088 O  OG1   . THR A 433 ? 1.8392 1.6427 1.4951 -0.1326 0.1070  0.0927  536  THR A OG1   
3089 C  CG2   . THR A 433 ? 1.8171 1.6462 1.5045 -0.1572 0.0995  0.0721  536  THR A CG2   
3090 N  N     . ARG A 434 ? 1.6759 1.5653 1.3653 -0.0983 0.0886  0.0899  537  ARG A N     
3091 C  CA    . ARG A 434 ? 1.6469 1.5417 1.3318 -0.0767 0.0828  0.0951  537  ARG A CA    
3092 C  C     . ARG A 434 ? 1.5498 1.4835 1.2595 -0.0689 0.0714  0.0856  537  ARG A C     
3093 O  O     . ARG A 434 ? 1.5082 1.4685 1.2359 -0.0790 0.0696  0.0770  537  ARG A O     
3094 C  CB    . ARG A 434 ? 1.6343 1.5258 1.3009 -0.0731 0.0890  0.1059  537  ARG A CB    
3095 C  CG    . ARG A 434 ? 1.6682 1.5168 1.3064 -0.0763 0.1002  0.1178  537  ARG A CG    
3096 C  CD    . ARG A 434 ? 1.6832 1.5241 1.3008 -0.0601 0.1017  0.1303  537  ARG A CD    
3097 N  NE    . ARG A 434 ? 1.7443 1.6139 1.3645 -0.0615 0.1022  0.1308  537  ARG A NE    
3098 C  CZ    . ARG A 434 ? 1.7181 1.5788 1.3217 -0.0702 0.1129  0.1389  537  ARG A CZ    
3099 N  NH1   . ARG A 434 ? 1.7184 1.5410 1.3014 -0.0790 0.1242  0.1476  537  ARG A NH1   
3100 N  NH2   . ARG A 434 ? 1.7088 1.5981 1.3157 -0.0700 0.1129  0.1384  537  ARG A NH2   
3101 N  N     . ASP A 435 ? 1.4878 1.4244 1.1984 -0.0507 0.0638  0.0873  538  ASP A N     
3102 C  CA    . ASP A 435 ? 1.4598 1.4292 1.1925 -0.0430 0.0528  0.0786  538  ASP A CA    
3103 C  C     . ASP A 435 ? 1.4218 1.4194 1.1585 -0.0426 0.0512  0.0772  538  ASP A C     
3104 O  O     . ASP A 435 ? 1.5086 1.4997 1.2280 -0.0423 0.0571  0.0852  538  ASP A O     
3105 C  CB    . ASP A 435 ? 1.4455 1.4110 1.1779 -0.0245 0.0457  0.0818  538  ASP A CB    
3106 C  CG    . ASP A 435 ? 1.5726 1.5183 1.2818 -0.0131 0.0492  0.0947  538  ASP A CG    
3107 O  OD1   . ASP A 435 ? 1.6286 1.5450 1.3181 -0.0191 0.0590  0.1022  538  ASP A OD1   
3108 O  OD2   . ASP A 435 ? 1.5762 1.5352 1.2864 0.0018  0.0419  0.0976  538  ASP A OD2   
3109 N  N     . PRO A 436 ? 1.3908 1.4186 1.1486 -0.0421 0.0437  0.0671  539  PRO A N     
3110 C  CA    . PRO A 436 ? 1.3881 1.4416 1.1484 -0.0409 0.0423  0.0647  539  PRO A CA    
3111 C  C     . PRO A 436 ? 1.4280 1.4839 1.1761 -0.0257 0.0377  0.0705  539  PRO A C     
3112 O  O     . PRO A 436 ? 1.4377 1.5087 1.1807 -0.0246 0.0383  0.0704  539  PRO A O     
3113 C  CB    . PRO A 436 ? 1.3554 1.4357 1.1406 -0.0422 0.0348  0.0523  539  PRO A CB    
3114 C  CG    . PRO A 436 ? 1.3675 1.4376 1.1614 -0.0381 0.0295  0.0499  539  PRO A CG    
3115 C  CD    . PRO A 436 ? 1.3826 1.4210 1.1614 -0.0434 0.0371  0.0573  539  PRO A CD    
3116 N  N     . LEU A 437 ? 1.4354 1.4781 1.1786 -0.0138 0.0329  0.0754  540  LEU A N     
3117 C  CA    . LEU A 437 ? 1.4437 1.4888 1.1744 0.0006  0.0280  0.0821  540  LEU A CA    
3118 C  C     . LEU A 437 ? 1.4909 1.5107 1.1947 0.0030  0.0365  0.0955  540  LEU A C     
3119 O  O     . LEU A 437 ? 1.5246 1.5472 1.2147 0.0142  0.0335  0.1019  540  LEU A O     
3120 C  CB    . LEU A 437 ? 1.3715 1.4193 1.1121 0.0134  0.0181  0.0814  540  LEU A CB    
3121 C  CG    . LEU A 437 ? 1.2639 1.3388 1.0283 0.0148  0.0078  0.0697  540  LEU A CG    
3122 C  CD1   . LEU A 437 ? 1.2781 1.3571 1.0490 0.0284  -0.0015 0.0717  540  LEU A CD1   
3123 C  CD2   . LEU A 437 ? 1.3174 1.4153 1.0827 0.0132  0.0049  0.0639  540  LEU A CD2   
3124 N  N     . SER A 438 ? 1.5569 1.5512 1.2519 -0.0071 0.0468  0.0999  541  SER A N     
3125 C  CA    . SER A 438 ? 1.7012 1.6675 1.3690 -0.0056 0.0561  0.1131  541  SER A CA    
3126 C  C     . SER A 438 ? 1.8377 1.8137 1.4938 -0.0108 0.0619  0.1162  541  SER A C     
3127 O  O     . SER A 438 ? 1.7789 1.7739 1.4469 -0.0227 0.0642  0.1084  541  SER A O     
3128 C  CB    . SER A 438 ? 1.6674 1.6024 1.3288 -0.0173 0.0659  0.1157  541  SER A CB    
3129 O  OG    . SER A 438 ? 1.7786 1.6832 1.4124 -0.0163 0.0757  0.1289  541  SER A OG    
3130 N  N     . GLU A 439 ? 2.2195 2.1830 1.8517 -0.0009 0.0645  0.1279  542  GLU A N     
3131 C  CA    . GLU A 439 ? 2.1572 2.1282 1.7747 -0.0041 0.0706  0.1322  542  GLU A CA    
3132 C  C     . GLU A 439 ? 2.1758 2.1286 1.7849 -0.0219 0.0853  0.1363  542  GLU A C     
3133 O  O     . GLU A 439 ? 2.2081 2.1319 1.8115 -0.0283 0.0917  0.1405  542  GLU A O     
3134 C  CB    . GLU A 439 ? 2.2720 2.2335 1.8643 0.0123  0.0690  0.1445  542  GLU A CB    
3135 C  CG    . GLU A 439 ? 2.2867 2.2084 1.8548 0.0152  0.0782  0.1591  542  GLU A CG    
3136 C  CD    . GLU A 439 ? 2.4822 2.3863 2.0569 0.0223  0.0741  0.1595  542  GLU A CD    
3137 O  OE1   . GLU A 439 ? 2.4242 2.3492 2.0205 0.0284  0.0627  0.1504  542  GLU A OE1   
3138 O  OE2   . GLU A 439 ? 2.6654 2.5337 2.2228 0.0218  0.0830  0.1690  542  GLU A OE2   
3139 N  N     . ILE A 440 ? 1.8298 1.8002 1.4380 -0.0303 0.0910  0.1346  543  ILE A N     
3140 C  CA    . ILE A 440 ? 1.7513 1.7100 1.3525 -0.0482 0.1055  0.1389  543  ILE A CA    
3141 C  C     . ILE A 440 ? 1.7721 1.7270 1.3475 -0.0439 0.1132  0.1500  543  ILE A C     
3142 O  O     . ILE A 440 ? 1.7469 1.7288 1.3236 -0.0394 0.1106  0.1463  543  ILE A O     
3143 C  CB    . ILE A 440 ? 1.6455 1.6322 1.2724 -0.0635 0.1067  0.1266  543  ILE A CB    
3144 C  CG1   . ILE A 440 ? 1.5988 1.5927 1.2507 -0.0647 0.0971  0.1151  543  ILE A CG1   
3145 C  CG2   . ILE A 440 ? 1.6625 1.6375 1.2847 -0.0836 0.1215  0.1313  543  ILE A CG2   
3146 N  N     . THR A 441 ? 1.7175 1.6376 1.2677 -0.0449 0.1230  0.1638  544  THR A N     
3147 C  CA    . THR A 441 ? 1.7416 1.6540 1.2638 -0.0396 0.1309  0.1763  544  THR A CA    
3148 C  C     . THR A 441 ? 1.7435 1.6749 1.2689 -0.0547 0.1416  0.1745  544  THR A C     
3149 O  O     . THR A 441 ? 1.7063 1.6480 1.2521 -0.0722 0.1460  0.1668  544  THR A O     
3150 C  CB    . THR A 441 ? 1.7288 1.5962 1.2233 -0.0388 0.1406  0.1919  544  THR A CB    
3151 O  OG1   . THR A 441 ? 1.7212 1.5700 1.2190 -0.0607 0.1529  0.1923  544  THR A OG1   
3152 C  CG2   . THR A 441 ? 1.7376 1.5867 1.2305 -0.0233 0.1310  0.1937  544  THR A CG2   
3153 N  N     . GLU A 442 ? 1.7128 1.6500 1.2172 -0.0473 0.1458  0.1821  545  GLU A N     
3154 C  CA    . GLU A 442 ? 1.7350 1.6924 1.2407 -0.0591 0.1566  0.1811  545  GLU A CA    
3155 C  C     . GLU A 442 ? 1.7028 1.6401 1.2056 -0.0806 0.1731  0.1881  545  GLU A C     
3156 O  O     . GLU A 442 ? 1.6448 1.6037 1.1637 -0.0961 0.1806  0.1827  545  GLU A O     
3157 C  CB    . GLU A 442 ? 1.8246 1.7868 1.3033 -0.0458 0.1587  0.1895  545  GLU A CB    
3158 C  CG    . GLU A 442 ? 1.8929 1.8873 1.3769 -0.0515 0.1650  0.1840  545  GLU A CG    
3159 C  CD    . GLU A 442 ? 1.8932 1.9236 1.4015 -0.0448 0.1515  0.1671  545  GLU A CD    
3160 O  OE1   . GLU A 442 ? 1.9339 1.9647 1.4511 -0.0338 0.1365  0.1609  545  GLU A OE1   
3161 O  OE2   . GLU A 442 ? 1.9291 1.9869 1.4474 -0.0503 0.1564  0.1602  545  GLU A OE2   
3162 N  N     . GLN A 443 ? 1.7015 1.5977 1.1840 -0.0817 0.1791  0.2000  546  GLN A N     
3163 C  CA    . GLN A 443 ? 1.7197 1.5928 1.1991 -0.1038 0.1942  0.2060  546  GLN A CA    
3164 C  C     . GLN A 443 ? 1.7836 1.6690 1.2953 -0.1208 0.1911  0.1925  546  GLN A C     
3165 O  O     . GLN A 443 ? 1.7552 1.6500 1.2785 -0.1416 0.2012  0.1907  546  GLN A O     
3166 C  CB    . GLN A 443 ? 1.7266 1.5493 1.1769 -0.0996 0.1998  0.2204  546  GLN A CB    
3167 C  CG    . GLN A 443 ? 1.8121 1.6038 1.2587 -0.1230 0.2138  0.2254  546  GLN A CG    
3168 C  CD    . GLN A 443 ? 2.0486 1.8258 1.5121 -0.1298 0.2071  0.2161  546  GLN A CD    
3169 O  OE1   . GLN A 443 ? 1.9317 1.7135 1.4039 -0.1141 0.1932  0.2094  546  GLN A OE1   
3170 N  NE2   . GLN A 443 ? 2.0231 1.7833 1.4911 -0.1537 0.2170  0.2155  546  GLN A NE2   
3171 N  N     . GLU A 444 ? 1.7618 1.6487 1.2887 -0.1121 0.1771  0.1831  547  GLU A N     
3172 C  CA    . GLU A 444 ? 1.7312 1.6308 1.2878 -0.1263 0.1729  0.1699  547  GLU A CA    
3173 C  C     . GLU A 444 ? 1.6709 1.6180 1.2543 -0.1317 0.1702  0.1582  547  GLU A C     
3174 O  O     . GLU A 444 ? 1.6493 1.6102 1.2543 -0.1496 0.1730  0.1508  547  GLU A O     
3175 C  CB    . GLU A 444 ? 1.8257 1.7164 1.3904 -0.1136 0.1590  0.1634  547  GLU A CB    
3176 C  CG    . GLU A 444 ? 1.8336 1.6767 1.3742 -0.1082 0.1619  0.1739  547  GLU A CG    
3177 C  CD    . GLU A 444 ? 1.7768 1.6157 1.3233 -0.0906 0.1482  0.1692  547  GLU A CD    
3178 O  OE1   . GLU A 444 ? 1.7326 1.6050 1.3001 -0.0821 0.1362  0.1587  547  GLU A OE1   
3179 O  OE2   . GLU A 444 ? 1.8686 1.6700 1.3985 -0.0851 0.1499  0.1762  547  GLU A OE2   
3180 N  N     . LYS A 445 ? 1.7215 1.6939 1.3035 -0.1161 0.1646  0.1562  548  LYS A N     
3181 C  CA    . LYS A 445 ? 1.6594 1.6749 1.2643 -0.1192 0.1629  0.1453  548  LYS A CA    
3182 C  C     . LYS A 445 ? 1.7059 1.7319 1.3120 -0.1377 0.1788  0.1497  548  LYS A C     
3183 O  O     . LYS A 445 ? 1.6822 1.7360 1.3141 -0.1501 0.1802  0.1408  548  LYS A O     
3184 C  CB    . LYS A 445 ? 1.6215 1.6564 1.2190 -0.0989 0.1549  0.1431  548  LYS A CB    
3185 C  CG    . LYS A 445 ? 1.6182 1.6476 1.2173 -0.0813 0.1387  0.1385  548  LYS A CG    
3186 C  CD    . LYS A 445 ? 1.7025 1.7464 1.2891 -0.0625 0.1313  0.1380  548  LYS A CD    
3187 C  CE    . LYS A 445 ? 1.6457 1.7278 1.2531 -0.0609 0.1258  0.1242  548  LYS A CE    
3188 N  NZ    . LYS A 445 ? 1.5080 1.6010 1.1420 -0.0590 0.1129  0.1116  548  LYS A NZ    
3189 N  N     . ASP A 446 ? 1.6760 1.6807 1.2545 -0.1395 0.1913  0.1639  549  ASP A N     
3190 C  CA    . ASP A 446 ? 1.7020 1.7138 1.2810 -0.1589 0.2079  0.1696  549  ASP A CA    
3191 C  C     . ASP A 446 ? 1.7228 1.7180 1.3134 -0.1820 0.2135  0.1693  549  ASP A C     
3192 O  O     . ASP A 446 ? 1.6713 1.6875 1.2792 -0.2009 0.2223  0.1670  549  ASP A O     
3193 C  CB    . ASP A 446 ? 1.7800 1.7703 1.3242 -0.1547 0.2203  0.1859  549  ASP A CB    
3194 C  CG    . ASP A 446 ? 1.7448 1.7566 1.2772 -0.1350 0.2168  0.1858  549  ASP A CG    
3195 O  OD1   . ASP A 446 ? 1.7219 1.7705 1.2754 -0.1300 0.2096  0.1732  549  ASP A OD1   
3196 O  OD2   . ASP A 446 ? 1.6403 1.6310 1.1408 -0.1244 0.2213  0.1982  549  ASP A OD2   
3197 N  N     . PHE A 447 ? 1.7342 1.6926 1.3155 -0.1808 0.2085  0.1713  550  PHE A N     
3198 C  CA    . PHE A 447 ? 1.7603 1.6990 1.3497 -0.2028 0.2131  0.1702  550  PHE A CA    
3199 C  C     . PHE A 447 ? 1.7310 1.7028 1.3566 -0.2121 0.2044  0.1543  550  PHE A C     
3200 O  O     . PHE A 447 ? 1.7631 1.7421 1.4036 -0.2348 0.2108  0.1517  550  PHE A O     
3201 C  CB    . PHE A 447 ? 1.8054 1.6956 1.3741 -0.1963 0.2096  0.1755  550  PHE A CB    
3202 C  CG    . PHE A 447 ? 1.8893 1.7555 1.4639 -0.2174 0.2126  0.1726  550  PHE A CG    
3203 C  CD1   . PHE A 447 ? 1.9307 1.7771 1.4953 -0.2401 0.2279  0.1807  550  PHE A CD1   
3204 C  CD2   . PHE A 447 ? 1.9289 1.7915 1.5181 -0.2152 0.2004  0.1615  550  PHE A CD2   
3205 C  CE1   . PHE A 447 ? 2.0369 1.8600 1.6057 -0.2607 0.2301  0.1772  550  PHE A CE1   
3206 C  CE2   . PHE A 447 ? 1.9895 1.8290 1.5819 -0.2346 0.2028  0.1581  550  PHE A CE2   
3207 C  CZ    . PHE A 447 ? 2.0682 1.8876 1.6503 -0.2577 0.2173  0.1655  550  PHE A CZ    
3208 N  N     . LEU A 448 ? 1.6863 1.6787 1.3263 -0.1952 0.1896  0.1438  551  LEU A N     
3209 C  CA    . LEU A 448 ? 1.6447 1.6709 1.3183 -0.2015 0.1812  0.1293  551  LEU A CA    
3210 C  C     . LEU A 448 ? 1.6022 1.6705 1.2939 -0.2110 0.1885  0.1266  551  LEU A C     
3211 O  O     . LEU A 448 ? 1.5898 1.6780 1.3047 -0.2287 0.1903  0.1204  551  LEU A O     
3212 C  CB    . LEU A 448 ? 1.5989 1.6374 1.2816 -0.1802 0.1650  0.1200  551  LEU A CB    
3213 C  CG    . LEU A 448 ? 1.4476 1.4622 1.1319 -0.1755 0.1542  0.1153  551  LEU A CG    
3214 C  CD1   . LEU A 448 ? 1.5949 1.5609 1.2498 -0.1740 0.1593  0.1269  551  LEU A CD1   
3215 C  CD2   . LEU A 448 ? 1.3885 1.4201 1.0817 -0.1542 0.1399  0.1075  551  LEU A CD2   
3216 N  N     . TRP A 449 ? 1.6048 1.6880 1.2859 -0.1989 0.1929  0.1311  552  TRP A N     
3217 C  CA    . TRP A 449 ? 1.5763 1.7008 1.2735 -0.2045 0.2003  0.1284  552  TRP A CA    
3218 C  C     . TRP A 449 ? 1.5917 1.7155 1.2907 -0.2294 0.2163  0.1360  552  TRP A C     
3219 O  O     . TRP A 449 ? 1.5513 1.7110 1.2754 -0.2418 0.2205  0.1308  552  TRP A O     
3220 C  CB    . TRP A 449 ? 1.6299 1.7647 1.3098 -0.1858 0.2023  0.1324  552  TRP A CB    
3221 C  CG    . TRP A 449 ? 1.6151 1.7911 1.3089 -0.1885 0.2107  0.1297  552  TRP A CG    
3222 C  CD1   . TRP A 449 ? 1.5249 1.7068 1.2046 -0.1927 0.2262  0.1396  552  TRP A CD1   
3223 C  CD2   . TRP A 449 ? 1.5644 1.7817 1.2886 -0.1864 0.2047  0.1167  552  TRP A CD2   
3224 N  NE1   . TRP A 449 ? 1.5602 1.7855 1.2601 -0.1930 0.2305  0.1332  552  TRP A NE1   
3225 C  CE2   . TRP A 449 ? 1.5307 1.7780 1.2580 -0.1889 0.2173  0.1192  552  TRP A CE2   
3226 C  CE3   . TRP A 449 ? 1.5133 1.7446 1.2614 -0.1820 0.1904  0.1036  552  TRP A CE3   
3227 C  CZ2   . TRP A 449 ? 1.5202 1.8107 1.2740 -0.1862 0.2160  0.1090  552  TRP A CZ2   
3228 C  CZ3   . TRP A 449 ? 1.5091 1.7821 1.2827 -0.1798 0.1888  0.0939  552  TRP A CZ3   
3229 C  CH2   . TRP A 449 ? 1.5498 1.8520 1.3263 -0.1814 0.2015  0.0965  552  TRP A CH2   
3230 N  N     . SER A 450 ? 1.6375 1.7210 1.3103 -0.2370 0.2255  0.1485  553  SER A N     
3231 C  CA    . SER A 450 ? 1.6587 1.7377 1.3315 -0.2623 0.2414  0.1564  553  SER A CA    
3232 C  C     . SER A 450 ? 1.6316 1.7145 1.3291 -0.2840 0.2379  0.1481  553  SER A C     
3233 O  O     . SER A 450 ? 1.5688 1.6742 1.2837 -0.3053 0.2470  0.1482  553  SER A O     
3234 C  CB    . SER A 450 ? 1.7086 1.7386 1.3448 -0.2642 0.2519  0.1721  553  SER A CB    
3235 O  OG    . SER A 450 ? 1.8247 1.8138 1.4473 -0.2578 0.2427  0.1718  553  SER A OG    
3236 N  N     . HIS A 451 ? 1.6584 1.7210 1.3577 -0.2789 0.2246  0.1408  554  HIS A N     
3237 C  CA    . HIS A 451 ? 1.6827 1.7479 1.4034 -0.2973 0.2192  0.1317  554  HIS A CA    
3238 C  C     . HIS A 451 ? 1.5841 1.6906 1.3360 -0.2891 0.2052  0.1169  554  HIS A C     
3239 O  O     . HIS A 451 ? 1.6548 1.7562 1.4187 -0.2941 0.1952  0.1080  554  HIS A O     
3240 C  CB    . HIS A 451 ? 1.7432 1.7561 1.4438 -0.2986 0.2149  0.1334  554  HIS A CB    
3241 C  CG    . HIS A 451 ? 1.8593 1.8303 1.5340 -0.3146 0.2294  0.1463  554  HIS A CG    
3242 N  ND1   . HIS A 451 ? 1.8477 1.8252 1.5145 -0.3245 0.2451  0.1572  554  HIS A ND1   
3243 C  CD2   . HIS A 451 ? 2.0017 1.9220 1.6557 -0.3224 0.2312  0.1503  554  HIS A CD2   
3244 C  CE1   . HIS A 451 ? 1.9843 1.9163 1.6265 -0.3382 0.2559  0.1676  554  HIS A CE1   
3245 N  NE2   . HIS A 451 ? 2.0433 1.9391 1.6769 -0.3370 0.2477  0.1635  554  HIS A NE2   
3246 N  N     . ARG A 452 ? 1.5742 1.7200 1.3379 -0.2763 0.2049  0.1141  555  ARG A N     
3247 C  CA    . ARG A 452 ? 1.5134 1.6967 1.3048 -0.2666 0.1924  0.1008  555  ARG A CA    
3248 C  C     . ARG A 452 ? 1.5129 1.7248 1.3345 -0.2873 0.1916  0.0933  555  ARG A C     
3249 O  O     . ARG A 452 ? 1.4892 1.7223 1.3321 -0.2819 0.1794  0.0821  555  ARG A O     
3250 C  CB    . ARG A 452 ? 1.5085 1.7255 1.3036 -0.2495 0.1943  0.1000  555  ARG A CB    
3251 C  CG    . ARG A 452 ? 1.5333 1.7931 1.3493 -0.2620 0.2049  0.1001  555  ARG A CG    
3252 C  CD    . ARG A 452 ? 1.5531 1.8293 1.3577 -0.2487 0.2141  0.1055  555  ARG A CD    
3253 N  NE    . ARG A 452 ? 1.5833 1.8271 1.3570 -0.2527 0.2265  0.1196  555  ARG A NE    
3254 C  CZ    . ARG A 452 ? 1.5310 1.7861 1.2926 -0.2495 0.2395  0.1276  555  ARG A CZ    
3255 N  NH1   . ARG A 452 ? 1.4797 1.7777 1.2574 -0.2425 0.2427  0.1228  555  ARG A NH1   
3256 N  NH2   . ARG A 452 ? 1.5943 1.8161 1.3259 -0.2529 0.2502  0.1411  555  ARG A NH2   
3257 N  N     . HIS A 453 ? 1.5297 1.7435 1.3538 -0.3111 0.2041  0.0995  556  HIS A N     
3258 C  CA    . HIS A 453 ? 1.5126 1.7541 1.3655 -0.3327 0.2027  0.0927  556  HIS A CA    
3259 C  C     . HIS A 453 ? 1.6119 1.8200 1.4608 -0.3454 0.1948  0.0882  556  HIS A C     
3260 O  O     . HIS A 453 ? 1.6795 1.9093 1.5521 -0.3541 0.1858  0.0782  556  HIS A O     
3261 C  CB    . HIS A 453 ? 1.5532 1.8127 1.4122 -0.3547 0.2193  0.1008  556  HIS A CB    
3262 C  CG    . HIS A 453 ? 1.5883 1.8884 1.4561 -0.3438 0.2275  0.1036  556  HIS A CG    
3263 N  ND1   . HIS A 453 ? 1.5485 1.8694 1.4207 -0.3177 0.2196  0.0976  556  HIS A ND1   
3264 C  CD2   . HIS A 453 ? 1.6476 1.9704 1.5197 -0.3555 0.2436  0.1118  556  HIS A CD2   
3265 C  CE1   . HIS A 453 ? 1.5008 1.8544 1.3784 -0.3130 0.2302  0.1013  556  HIS A CE1   
3266 N  NE2   . HIS A 453 ? 1.6124 1.9689 1.4906 -0.3353 0.2451  0.1102  556  HIS A NE2   
3267 N  N     . TYR A 454 ? 1.6510 1.8063 1.4694 -0.3460 0.1981  0.0955  557  TYR A N     
3268 C  CA    . TYR A 454 ? 1.6556 1.7746 1.4662 -0.3539 0.1903  0.0908  557  TYR A CA    
3269 C  C     . TYR A 454 ? 1.6295 1.7434 1.4409 -0.3310 0.1746  0.0823  557  TYR A C     
3270 O  O     . TYR A 454 ? 1.7077 1.8043 1.5205 -0.3362 0.1659  0.0753  557  TYR A O     
3271 C  CB    . TYR A 454 ? 1.7085 1.7707 1.4847 -0.3612 0.2002  0.1021  557  TYR A CB    
3272 C  CG    . TYR A 454 ? 1.6700 1.6909 1.4355 -0.3718 0.1947  0.0977  557  TYR A CG    
3273 C  CD1   . TYR A 454 ? 1.6414 1.6613 1.4166 -0.4009 0.1971  0.0939  557  TYR A CD1   
3274 C  CD2   . TYR A 454 ? 1.5559 1.5391 1.3011 -0.3529 0.1871  0.0973  557  TYR A CD2   
3275 N  N     . CYS A 455 ? 1.5916 1.7205 1.4020 -0.3064 0.1709  0.0826  558  CYS A N     
3276 C  CA    . CYS A 455 ? 1.6529 1.7794 1.4655 -0.2850 0.1565  0.0749  558  CYS A CA    
3277 C  C     . CYS A 455 ? 1.6188 1.7798 1.4613 -0.2875 0.1454  0.0621  558  CYS A C     
3278 O  O     . CYS A 455 ? 1.5814 1.7365 1.4262 -0.2737 0.1334  0.0552  558  CYS A O     
3279 C  CB    . CYS A 455 ? 1.5501 1.6874 1.3557 -0.2603 0.1554  0.0778  558  CYS A CB    
3280 S  SG    . CYS A 455 ? 1.6190 1.7098 1.3854 -0.2489 0.1629  0.0917  558  CYS A SG    
3281 N  N     . VAL A 456 ? 1.6209 1.8186 1.4867 -0.3042 0.1490  0.0591  559  VAL A N     
3282 C  CA    . VAL A 456 ? 1.5876 1.8195 1.4817 -0.3061 0.1382  0.0476  559  VAL A CA    
3283 C  C     . VAL A 456 ? 1.6741 1.8820 1.5666 -0.3202 0.1311  0.0419  559  VAL A C     
3284 O  O     . VAL A 456 ? 1.6636 1.8908 1.5741 -0.3182 0.1199  0.0322  559  VAL A O     
3285 C  CB    . VAL A 456 ? 1.5826 1.8647 1.5032 -0.3185 0.1441  0.0466  559  VAL A CB    
3286 C  CG1   . VAL A 456 ? 1.5132 1.8159 1.4319 -0.3045 0.1527  0.0524  559  VAL A CG1   
3287 C  CG2   . VAL A 456 ? 1.6767 1.9525 1.5980 -0.3484 0.1532  0.0506  559  VAL A CG2   
3288 N  N     . THR A 457 ? 1.8308 1.9956 1.7008 -0.3341 0.1377  0.0478  560  THR A N     
3289 C  CA    . THR A 457 ? 1.8739 2.0094 1.7374 -0.3460 0.1314  0.0421  560  THR A CA    
3290 C  C     . THR A 457 ? 1.8005 1.9050 1.6486 -0.3250 0.1221  0.0394  560  THR A C     
3291 O  O     . THR A 457 ? 1.8347 1.9191 1.6791 -0.3305 0.1150  0.0329  560  THR A O     
3292 C  CB    . THR A 457 ? 1.9459 2.0431 1.7891 -0.3689 0.1425  0.0491  560  THR A CB    
3293 O  OG1   . THR A 457 ? 2.1379 2.2206 1.9827 -0.3871 0.1365  0.0411  560  THR A OG1   
3294 C  CG2   . THR A 457 ? 1.8805 1.9261 1.6897 -0.3557 0.1480  0.0584  560  THR A CG2   
3295 N  N     . ILE A 458 ? 1.7090 1.8101 1.5481 -0.3015 0.1220  0.0440  561  ILE A N     
3296 C  CA    . ILE A 458 ? 1.6241 1.7019 1.4518 -0.2803 0.1133  0.0419  561  ILE A CA    
3297 C  C     . ILE A 458 ? 1.5022 1.6127 1.3432 -0.2581 0.1074  0.0397  561  ILE A C     
3298 O  O     . ILE A 458 ? 1.4876 1.5887 1.3149 -0.2425 0.1102  0.0463  561  ILE A O     
3299 C  CB    . ILE A 458 ? 1.6752 1.7023 1.4705 -0.2749 0.1199  0.0517  561  ILE A CB    
3300 C  CG1   . ILE A 458 ? 1.7004 1.7254 1.4842 -0.2798 0.1332  0.0630  561  ILE A CG1   
3301 C  CG2   . ILE A 458 ? 1.7675 1.7543 1.5481 -0.2899 0.1207  0.0501  561  ILE A CG2   
3302 N  N     . PRO A 459 ? 1.4477 1.5958 1.3142 -0.2560 0.0990  0.0304  562  PRO A N     
3303 C  CA    . PRO A 459 ? 1.3716 1.5514 1.2508 -0.2367 0.0947  0.0280  562  PRO A CA    
3304 C  C     . PRO A 459 ? 1.3418 1.5026 1.2092 -0.2139 0.0880  0.0284  562  PRO A C     
3305 O  O     . PRO A 459 ? 1.3739 1.5548 1.2469 -0.1981 0.0855  0.0275  562  PRO A O     
3306 C  CB    . PRO A 459 ? 1.3127 1.5298 1.2198 -0.2403 0.0866  0.0179  562  PRO A CB    
3307 C  CG    . PRO A 459 ? 1.3881 1.6025 1.2992 -0.2653 0.0892  0.0165  562  PRO A CG    
3308 C  CD    . PRO A 459 ? 1.4745 1.6381 1.3585 -0.2714 0.0932  0.0218  562  PRO A CD    
3309 N  N     . GLU A 460 ? 1.3678 1.4912 1.2192 -0.2118 0.0851  0.0294  563  GLU A N     
3310 C  CA    . GLU A 460 ? 1.3638 1.4704 1.2048 -0.1907 0.0792  0.0307  563  GLU A CA    
3311 C  C     . GLU A 460 ? 1.3216 1.4158 1.1440 -0.1806 0.0856  0.0404  563  GLU A C     
3312 O  O     . GLU A 460 ? 1.2985 1.3875 1.1153 -0.1623 0.0803  0.0414  563  GLU A O     
3313 C  CB    . GLU A 460 ? 1.3762 1.4467 1.2048 -0.1908 0.0756  0.0298  563  GLU A CB    
3314 C  CG    . GLU A 460 ? 1.4778 1.5126 1.2866 -0.2069 0.0845  0.0356  563  GLU A CG    
3315 C  CD    . GLU A 460 ? 1.5540 1.5964 1.3733 -0.2298 0.0852  0.0296  563  GLU A CD    
3316 O  OE1   . GLU A 460 ? 1.5179 1.5954 1.3605 -0.2320 0.0785  0.0214  563  GLU A OE1   
3317 O  OE2   . GLU A 460 ? 1.5749 1.5880 1.3789 -0.2456 0.0922  0.0331  563  GLU A OE2   
3318 N  N     . ILE A 461 ? 1.3473 1.4374 1.1602 -0.1925 0.0967  0.0477  564  ILE A N     
3319 C  CA    . ILE A 461 ? 1.3731 1.4525 1.1669 -0.1831 0.1033  0.0575  564  ILE A CA    
3320 C  C     . ILE A 461 ? 1.3154 1.4310 1.1198 -0.1737 0.1030  0.0558  564  ILE A C     
3321 O  O     . ILE A 461 ? 1.2867 1.3975 1.0753 -0.1647 0.1076  0.0631  564  ILE A O     
3322 C  CB    . ILE A 461 ? 1.3792 1.4353 1.1556 -0.1998 0.1164  0.0671  564  ILE A CB    
3323 C  CG1   . ILE A 461 ? 1.3951 1.4230 1.1437 -0.1878 0.1218  0.0787  564  ILE A CG1   
3324 C  CG2   . ILE A 461 ? 1.3351 1.4236 1.1255 -0.2146 0.1244  0.0669  564  ILE A CG2   
3325 C  CD1   . ILE A 461 ? 1.4918 1.4939 1.2208 -0.2031 0.1356  0.0893  564  ILE A CD1   
3326 N  N     . LEU A 462 ? 1.2586 1.4095 1.0877 -0.1747 0.0978  0.0464  565  LEU A N     
3327 C  CA    . LEU A 462 ? 1.3093 1.4939 1.1480 -0.1660 0.0986  0.0441  565  LEU A CA    
3328 C  C     . LEU A 462 ? 1.2675 1.4476 1.0947 -0.1448 0.0933  0.0452  565  LEU A C     
3329 O  O     . LEU A 462 ? 1.1123 1.3034 0.9317 -0.1394 0.0987  0.0488  565  LEU A O     
3330 C  CB    . LEU A 462 ? 1.2296 1.4495 1.0964 -0.1678 0.0926  0.0335  565  LEU A CB    
3331 C  CG    . LEU A 462 ? 1.2463 1.5018 1.1242 -0.1590 0.0941  0.0302  565  LEU A CG    
3332 C  CD1   . LEU A 462 ? 1.1999 1.4665 1.0729 -0.1692 0.1078  0.0373  565  LEU A CD1   
3333 C  CD2   . LEU A 462 ? 1.1423 1.4293 1.0469 -0.1585 0.0874  0.0202  565  LEU A CD2   
3334 N  N     . PRO A 463 ? 1.2975 1.4634 1.1231 -0.1328 0.0830  0.0421  566  PRO A N     
3335 C  CA    . PRO A 463 ? 1.2784 1.4410 1.0928 -0.1143 0.0780  0.0437  566  PRO A CA    
3336 C  C     . PRO A 463 ? 1.2377 1.3789 1.0260 -0.1118 0.0854  0.0552  566  PRO A C     
3337 O  O     . PRO A 463 ? 1.1904 1.3398 0.9694 -0.1006 0.0851  0.0570  566  PRO A O     
3338 C  CB    . PRO A 463 ? 1.2267 1.3746 1.0445 -0.1057 0.0673  0.0400  566  PRO A CB    
3339 C  CG    . PRO A 463 ? 1.2315 1.3888 1.0686 -0.1161 0.0647  0.0326  566  PRO A CG    
3340 C  CD    . PRO A 463 ? 1.1805 1.3376 1.0165 -0.1348 0.0751  0.0362  566  PRO A CD    
3341 N  N     . LYS A 464 ? 1.2469 1.3595 1.0215 -0.1218 0.0921  0.0630  567  LYS A N     
3342 C  CA    . LYS A 464 ? 1.3213 1.4115 1.0695 -0.1196 0.1002  0.0750  567  LYS A CA    
3343 C  C     . LYS A 464 ? 1.3242 1.4316 1.0690 -0.1273 0.1113  0.0789  567  LYS A C     
3344 O  O     . LYS A 464 ? 1.2419 1.3440 0.9673 -0.1194 0.1157  0.0866  567  LYS A O     
3345 C  CB    . LYS A 464 ? 1.3173 1.3696 1.0511 -0.1287 0.1054  0.0822  567  LYS A CB    
3346 C  CG    . LYS A 464 ? 1.3612 1.3962 1.0988 -0.1224 0.0962  0.0782  567  LYS A CG    
3347 C  CD    . LYS A 464 ? 1.3509 1.3825 1.0811 -0.1010 0.0874  0.0799  567  LYS A CD    
3348 C  CE    . LYS A 464 ? 1.4685 1.4836 1.2028 -0.0947 0.0796  0.0767  567  LYS A CE    
3349 N  NZ    . LYS A 464 ? 1.6642 1.6783 1.3934 -0.0746 0.0711  0.0789  567  LYS A NZ    
3350 N  N     . LEU A 465 ? 1.3089 1.4382 1.0724 -0.1424 0.1160  0.0740  568  LEU A N     
3351 C  CA    . LEU A 465 ? 1.2506 1.3992 1.0132 -0.1504 0.1276  0.0779  568  LEU A CA    
3352 C  C     . LEU A 465 ? 1.2296 1.4074 0.9963 -0.1357 0.1246  0.0731  568  LEU A C     
3353 O  O     . LEU A 465 ? 1.3211 1.5039 1.0736 -0.1331 0.1331  0.0792  568  LEU A O     
3354 C  CB    . LEU A 465 ? 1.2636 1.4306 1.0476 -0.1706 0.1328  0.0738  568  LEU A CB    
3355 C  CG    . LEU A 465 ? 1.2883 1.4812 1.0768 -0.1804 0.1454  0.0772  568  LEU A CG    
3356 C  CD1   . LEU A 465 ? 1.4059 1.5741 1.1669 -0.1845 0.1580  0.0909  568  LEU A CD1   
3357 C  CD2   . LEU A 465 ? 1.3179 1.5309 1.1304 -0.2008 0.1486  0.0728  568  LEU A CD2   
3358 N  N     . LEU A 466 ? 1.1805 1.3762 0.9648 -0.1260 0.1130  0.0621  569  LEU A N     
3359 C  CA    . LEU A 466 ? 1.1896 1.4099 0.9767 -0.1120 0.1098  0.0564  569  LEU A CA    
3360 C  C     . LEU A 466 ? 1.2694 1.4740 1.0312 -0.0972 0.1075  0.0619  569  LEU A C     
3361 O  O     . LEU A 466 ? 1.3282 1.5476 1.0819 -0.0893 0.1105  0.0615  569  LEU A O     
3362 C  CB    . LEU A 466 ? 1.0889 1.3256 0.8979 -0.1047 0.0975  0.0441  569  LEU A CB    
3363 C  CG    . LEU A 466 ? 1.1942 1.4516 1.0296 -0.1166 0.0977  0.0375  569  LEU A CG    
3364 C  CD1   . LEU A 466 ? 1.2361 1.5040 1.0889 -0.1070 0.0850  0.0268  569  LEU A CD1   
3365 C  CD2   . LEU A 466 ? 0.9684 1.2561 0.8130 -0.1229 0.1081  0.0373  569  LEU A CD2   
3366 N  N     . LEU A 467 ? 1.2606 1.4362 1.0092 -0.0925 0.1022  0.0670  570  LEU A N     
3367 C  CA    . LEU A 467 ? 1.3076 1.4688 1.0318 -0.0785 0.0996  0.0734  570  LEU A CA    
3368 C  C     . LEU A 467 ? 1.3490 1.4968 1.0490 -0.0831 0.1127  0.0860  570  LEU A C     
3369 O  O     . LEU A 467 ? 1.4233 1.5668 1.1022 -0.0714 0.1122  0.0911  570  LEU A O     
3370 C  CB    . LEU A 467 ? 1.3338 1.4703 1.0532 -0.0710 0.0900  0.0754  570  LEU A CB    
3371 C  CG    . LEU A 467 ? 1.2556 1.4024 0.9961 -0.0647 0.0768  0.0642  570  LEU A CG    
3372 C  CD1   . LEU A 467 ? 1.2434 1.3665 0.9766 -0.0560 0.0689  0.0681  570  LEU A CD1   
3373 C  CD2   . LEU A 467 ? 1.2481 1.4204 0.9947 -0.0540 0.0700  0.0553  570  LEU A CD2   
3374 N  N     . SER A 468 ? 1.3285 1.4695 1.0304 -0.1002 0.1241  0.0914  571  SER A N     
3375 C  CA    . SER A 468 ? 1.4497 1.5773 1.1291 -0.1064 0.1381  0.1040  571  SER A CA    
3376 C  C     . SER A 468 ? 1.4061 1.5623 1.0865 -0.1080 0.1472  0.1032  571  SER A C     
3377 O  O     . SER A 468 ? 1.3584 1.5069 1.0159 -0.1069 0.1571  0.1133  571  SER A O     
3378 C  CB    . SER A 468 ? 1.4107 1.5177 1.0913 -0.1258 0.1472  0.1100  571  SER A CB    
3379 O  OG    . SER A 468 ? 1.4484 1.5244 1.1228 -0.1230 0.1405  0.1121  571  SER A OG    
3380 N  N     . VAL A 469 ? 1.3846 1.5734 1.0902 -0.1097 0.1446  0.0918  572  VAL A N     
3381 C  CA    . VAL A 469 ? 1.3366 1.5544 1.0448 -0.1102 0.1539  0.0904  572  VAL A CA    
3382 C  C     . VAL A 469 ? 1.3868 1.6080 1.0754 -0.0913 0.1499  0.0895  572  VAL A C     
3383 O  O     . VAL A 469 ? 1.3839 1.6061 1.0751 -0.0779 0.1361  0.0814  572  VAL A O     
3384 C  CB    . VAL A 469 ? 1.3279 1.5792 1.0686 -0.1149 0.1514  0.0784  572  VAL A CB    
3385 C  CG1   . VAL A 469 ? 1.3314 1.6135 1.0751 -0.1145 0.1623  0.0774  572  VAL A CG1   
3386 C  CG2   . VAL A 469 ? 1.3567 1.6048 1.1161 -0.1338 0.1535  0.0786  572  VAL A CG2   
3387 N  N     . LYS A 470 ? 1.4136 1.6365 1.0819 -0.0907 0.1619  0.0977  573  LYS A N     
3388 C  CA    . LYS A 470 ? 1.4399 1.6689 1.0881 -0.0737 0.1592  0.0961  573  LYS A CA    
3389 C  C     . LYS A 470 ? 1.3376 1.6006 1.0044 -0.0685 0.1576  0.0831  573  LYS A C     
3390 O  O     . LYS A 470 ? 1.3308 1.6156 1.0041 -0.0747 0.1702  0.0835  573  LYS A O     
3391 C  CB    . LYS A 470 ? 1.4819 1.7015 1.1011 -0.0747 0.1735  0.1094  573  LYS A CB    
3392 C  CG    . LYS A 470 ? 1.4987 1.6825 1.0978 -0.0798 0.1769  0.1237  573  LYS A CG    
3393 C  CD    . LYS A 470 ? 1.5094 1.6827 1.0758 -0.0771 0.1897  0.1370  573  LYS A CD    
3394 C  CE    . LYS A 470 ? 1.6227 1.8162 1.1952 -0.0905 0.2079  0.1404  573  LYS A CE    
3395 N  NZ    . LYS A 470 ? 1.5611 1.7465 1.1495 -0.1123 0.2171  0.1458  573  LYS A NZ    
3396 N  N     . TRP A 471 ? 1.3609 1.6284 1.0366 -0.0570 0.1425  0.0715  574  TRP A N     
3397 C  CA    . TRP A 471 ? 1.3519 1.6477 1.0441 -0.0506 0.1401  0.0586  574  TRP A CA    
3398 C  C     . TRP A 471 ? 1.2788 1.5854 0.9499 -0.0393 0.1458  0.0574  574  TRP A C     
3399 O  O     . TRP A 471 ? 1.2083 1.5385 0.8903 -0.0341 0.1474  0.0479  574  TRP A O     
3400 C  CB    . TRP A 471 ? 1.3628 1.6565 1.0683 -0.0420 0.1226  0.0473  574  TRP A CB    
3401 C  CG    . TRP A 471 ? 1.3441 1.6284 1.0700 -0.0520 0.1171  0.0475  574  TRP A CG    
3402 C  CD1   . TRP A 471 ? 1.4357 1.6937 1.1546 -0.0535 0.1108  0.0535  574  TRP A CD1   
3403 C  CD2   . TRP A 471 ? 1.3480 1.6494 1.1036 -0.0613 0.1177  0.0414  574  TRP A CD2   
3404 N  NE1   . TRP A 471 ? 1.3861 1.6423 1.1273 -0.0634 0.1078  0.0511  574  TRP A NE1   
3405 C  CE2   . TRP A 471 ? 1.3324 1.6153 1.0963 -0.0686 0.1114  0.0437  574  TRP A CE2   
3406 C  CE3   . TRP A 471 ? 1.3623 1.6934 1.1379 -0.0632 0.1229  0.0345  574  TRP A CE3   
3407 C  CZ2   . TRP A 471 ? 1.3760 1.6687 1.1661 -0.0785 0.1096  0.0388  574  TRP A CZ2   
3408 C  CZ3   . TRP A 471 ? 1.2531 1.5955 1.0561 -0.0726 0.1208  0.0302  574  TRP A CZ3   
3409 C  CH2   . TRP A 471 ? 1.2241 1.5472 1.0336 -0.0805 0.1140  0.0323  574  TRP A CH2   
3410 N  N     . ASN A 472 ? 1.4901 1.7792 1.1300 -0.0345 0.1489  0.0670  575  ASN A N     
3411 C  CA    . ASN A 472 ? 1.3064 1.6044 0.9228 -0.0240 0.1551  0.0665  575  ASN A CA    
3412 C  C     . ASN A 472 ? 1.2966 1.6170 0.9189 -0.0316 0.1737  0.0696  575  ASN A C     
3413 O  O     . ASN A 472 ? 1.4457 1.7841 1.0618 -0.0225 0.1784  0.0633  575  ASN A O     
3414 C  CB    . ASN A 472 ? 1.2360 1.5100 0.8171 -0.0182 0.1549  0.0779  575  ASN A CB    
3415 C  CG    . ASN A 472 ? 1.3491 1.6038 0.9249 -0.0312 0.1646  0.0935  575  ASN A CG    
3416 O  OD1   . ASN A 472 ? 1.5612 1.7951 1.1399 -0.0339 0.1566  0.0974  575  ASN A OD1   
3417 N  ND2   . ASN A 472 ? 1.4783 1.7390 1.0459 -0.0392 0.1826  0.1026  575  ASN A ND2   
3418 N  N     . SER A 473 ? 1.3200 1.6398 0.9543 -0.0482 0.1845  0.0789  576  SER A N     
3419 C  CA    . SER A 473 ? 1.3799 1.7234 1.0231 -0.0575 0.2026  0.0827  576  SER A CA    
3420 C  C     . SER A 473 ? 1.3339 1.7066 1.0141 -0.0619 0.2013  0.0719  576  SER A C     
3421 O  O     . SER A 473 ? 1.3404 1.7112 1.0392 -0.0605 0.1874  0.0631  576  SER A O     
3422 C  CB    . SER A 473 ? 1.4034 1.7326 1.0416 -0.0749 0.2153  0.0982  576  SER A CB    
3423 O  OG    . SER A 473 ? 1.4598 1.7792 1.1199 -0.0879 0.2089  0.0981  576  SER A OG    
3424 N  N     . ARG A 474 ? 1.3690 1.7700 1.0597 -0.0667 0.2165  0.0732  577  ARG A N     
3425 C  CA    . ARG A 474 ? 1.3263 1.7588 1.0525 -0.0711 0.2173  0.0647  577  ARG A CA    
3426 C  C     . ARG A 474 ? 1.4001 1.8451 1.1484 -0.0928 0.2282  0.0727  577  ARG A C     
3427 O  O     . ARG A 474 ? 1.4201 1.8862 1.2001 -0.0992 0.2248  0.0664  577  ARG A O     
3428 C  CB    . ARG A 474 ? 1.3953 1.8568 1.1213 -0.0580 0.2253  0.0578  577  ARG A CB    
3429 C  CG    . ARG A 474 ? 1.5082 1.9897 1.2307 -0.0654 0.2468  0.0677  577  ARG A CG    
3430 C  CD    . ARG A 474 ? 1.5191 2.0274 1.2385 -0.0501 0.2551  0.0607  577  ARG A CD    
3431 N  NE    . ARG A 474 ? 1.6183 2.1539 1.3446 -0.0590 0.2761  0.0694  577  ARG A NE    
3432 C  CZ    . ARG A 474 ? 1.6446 2.2040 1.3647 -0.0475 0.2887  0.0672  577  ARG A CZ    
3433 N  NH1   . ARG A 474 ? 1.6538 2.2107 1.3581 -0.0266 0.2824  0.0560  577  ARG A NH1   
3434 N  NH2   . ARG A 474 ? 1.6630 2.2487 1.3924 -0.0575 0.3083  0.0763  577  ARG A NH2   
3435 N  N     . ASP A 475 ? 1.4546 1.8870 1.1865 -0.1046 0.2411  0.0865  578  ASP A N     
3436 C  CA    . ASP A 475 ? 1.4973 1.9391 1.2492 -0.1275 0.2514  0.0942  578  ASP A CA    
3437 C  C     . ASP A 475 ? 1.4572 1.8782 1.2224 -0.1390 0.2390  0.0928  578  ASP A C     
3438 O  O     . ASP A 475 ? 1.4506 1.8881 1.2438 -0.1548 0.2403  0.0915  578  ASP A O     
3439 C  CB    . ASP A 475 ? 1.5945 2.0235 1.3226 -0.1372 0.2686  0.1098  578  ASP A CB    
3440 C  CG    . ASP A 475 ? 1.6671 2.1163 1.3799 -0.1258 0.2822  0.1118  578  ASP A CG    
3441 O  OD1   . ASP A 475 ? 1.6377 2.1092 1.3574 -0.1098 0.2780  0.1005  578  ASP A OD1   
3442 O  OD2   . ASP A 475 ? 1.8717 2.3131 1.5642 -0.1326 0.2977  0.1248  578  ASP A OD2   
3443 N  N     . GLU A 476 ? 1.4888 1.8744 1.2338 -0.1309 0.2269  0.0931  579  GLU A N     
3444 C  CA    . GLU A 476 ? 1.4601 1.8236 1.2149 -0.1397 0.2153  0.0917  579  GLU A CA    
3445 C  C     . GLU A 476 ? 1.4018 1.7813 1.1825 -0.1327 0.2004  0.0774  579  GLU A C     
3446 O  O     . GLU A 476 ? 1.3775 1.7600 1.1807 -0.1450 0.1957  0.0743  579  GLU A O     
3447 C  CB    . GLU A 476 ? 1.4472 1.7688 1.1716 -0.1326 0.2086  0.0980  579  GLU A CB    
3448 C  CG    . GLU A 476 ? 1.4543 1.7540 1.1521 -0.1409 0.2229  0.1137  579  GLU A CG    
3449 C  CD    . GLU A 476 ? 1.6057 1.8657 1.2732 -0.1311 0.2158  0.1203  579  GLU A CD    
3450 O  OE1   . GLU A 476 ? 1.5365 1.7916 1.2005 -0.1148 0.2008  0.1125  579  GLU A OE1   
3451 O  OE2   . GLU A 476 ? 1.7400 1.9736 1.3872 -0.1397 0.2252  0.1336  579  GLU A OE2   
3452 N  N     . VAL A 477 ? 1.3571 1.7458 1.1338 -0.1132 0.1929  0.0684  580  VAL A N     
3453 C  CA    . VAL A 477 ? 1.3725 1.7749 1.1722 -0.1056 0.1795  0.0552  580  VAL A CA    
3454 C  C     . VAL A 477 ? 1.3647 1.8052 1.1959 -0.1137 0.1856  0.0509  580  VAL A C     
3455 O  O     . VAL A 477 ? 1.3744 1.8246 1.2296 -0.1158 0.1762  0.0433  580  VAL A O     
3456 C  CB    . VAL A 477 ? 1.2994 1.7010 1.0855 -0.0837 0.1712  0.0468  580  VAL A CB    
3457 C  CG1   . VAL A 477 ? 1.2855 1.6993 1.0943 -0.0760 0.1582  0.0337  580  VAL A CG1   
3458 C  CG2   . VAL A 477 ? 1.3040 1.6708 1.0610 -0.0765 0.1638  0.0514  580  VAL A CG2   
3459 N  N     . ALA A 478 ? 1.3551 1.8191 1.1872 -0.1181 0.2015  0.0561  581  ALA A N     
3460 C  CA    . ALA A 478 ? 1.3518 1.8551 1.2155 -0.1268 0.2082  0.0534  581  ALA A CA    
3461 C  C     . ALA A 478 ? 1.3855 1.8867 1.2675 -0.1497 0.2079  0.0576  581  ALA A C     
3462 O  O     . ALA A 478 ? 1.4144 1.9401 1.3258 -0.1553 0.2034  0.0515  581  ALA A O     
3463 C  CB    . ALA A 478 ? 1.3855 1.9146 1.2452 -0.1266 0.2265  0.0592  581  ALA A CB    
3464 N  N     . GLN A 479 ? 1.3650 1.8361 1.2289 -0.1628 0.2126  0.0679  582  GLN A N     
3465 C  CA    . GLN A 479 ? 1.3874 1.8501 1.2648 -0.1849 0.2116  0.0712  582  GLN A CA    
3466 C  C     . GLN A 479 ? 1.3416 1.7855 1.2258 -0.1818 0.1938  0.0631  582  GLN A C     
3467 O  O     . GLN A 479 ? 1.3153 1.7688 1.2220 -0.1951 0.1891  0.0595  582  GLN A O     
3468 C  CB    . GLN A 479 ? 1.4589 1.8894 1.3117 -0.1984 0.2219  0.0845  582  GLN A CB    
3469 C  CG    . GLN A 479 ? 1.4669 1.9146 1.3129 -0.2047 0.2412  0.0941  582  GLN A CG    
3470 C  CD    . GLN A 479 ? 1.5421 1.9537 1.3611 -0.2171 0.2512  0.1080  582  GLN A CD    
3471 O  OE1   . GLN A 479 ? 1.5293 1.9034 1.3363 -0.2219 0.2439  0.1102  582  GLN A OE1   
3472 N  NE2   . GLN A 479 ? 1.6805 2.1022 1.4890 -0.2216 0.2686  0.1177  582  GLN A NE2   
3473 N  N     . MET A 480 ? 1.3764 1.7946 1.2413 -0.1646 0.1836  0.0602  583  MET A N     
3474 C  CA    . MET A 480 ? 1.3306 1.7306 1.2008 -0.1606 0.1674  0.0532  583  MET A CA    
3475 C  C     . MET A 480 ? 1.3273 1.7583 1.2267 -0.1555 0.1590  0.0417  583  MET A C     
3476 O  O     . MET A 480 ? 1.3172 1.7428 1.2301 -0.1608 0.1490  0.0369  583  MET A O     
3477 C  CB    . MET A 480 ? 1.3309 1.7023 1.1762 -0.1425 0.1589  0.0526  583  MET A CB    
3478 C  CG    . MET A 480 ? 1.3753 1.7221 1.2218 -0.1395 0.1440  0.0481  583  MET A CG    
3479 S  SD    . MET A 480 ? 1.6700 1.9782 1.5043 -0.1567 0.1460  0.0575  583  MET A SD    
3480 C  CE    . MET A 480 ? 1.3744 1.7013 1.2402 -0.1749 0.1434  0.0513  583  MET A CE    
3481 N  N     . TYR A 481 ? 1.3139 1.7766 1.2220 -0.1445 0.1633  0.0373  584  TYR A N     
3482 C  CA    . TYR A 481 ? 1.3409 1.8342 1.2766 -0.1389 0.1566  0.0274  584  TYR A CA    
3483 C  C     . TYR A 481 ? 1.3789 1.8963 1.3412 -0.1584 0.1598  0.0284  584  TYR A C     
3484 O  O     . TYR A 481 ? 1.3136 1.8449 1.2972 -0.1582 0.1502  0.0211  584  TYR A O     
3485 C  CB    . TYR A 481 ? 1.3268 1.8477 1.2643 -0.1225 0.1623  0.0232  584  TYR A CB    
3486 C  CG    . TYR A 481 ? 1.3312 1.8343 1.2500 -0.1014 0.1540  0.0171  584  TYR A CG    
3487 C  CD1   . TYR A 481 ? 1.3119 1.7796 1.2155 -0.0980 0.1424  0.0164  584  TYR A CD1   
3488 C  CD2   . TYR A 481 ? 1.4399 1.9620 1.3565 -0.0849 0.1579  0.0117  584  TYR A CD2   
3489 C  CE1   . TYR A 481 ? 1.3644 1.8177 1.2524 -0.0802 0.1344  0.0107  584  TYR A CE1   
3490 C  CE2   . TYR A 481 ? 1.3908 1.8956 1.2897 -0.0671 0.1498  0.0053  584  TYR A CE2   
3491 C  CZ    . TYR A 481 ? 1.4057 1.8771 1.2911 -0.0655 0.1378  0.0049  584  TYR A CZ    
3492 O  OH    . TYR A 481 ? 1.1994 1.6554 1.0686 -0.0492 0.1293  -0.0016 584  TYR A OH    
3493 N  N     . CYS A 482 ? 1.3429 1.8659 1.3041 -0.1757 0.1730  0.0373  585  CYS A N     
3494 C  CA    . CYS A 482 ? 1.4454 1.9923 1.4321 -0.1965 0.1759  0.0383  585  CYS A CA    
3495 C  C     . CYS A 482 ? 1.3404 1.8589 1.3268 -0.2101 0.1658  0.0374  585  CYS A C     
3496 O  O     . CYS A 482 ? 1.2391 1.7761 1.2489 -0.2202 0.1597  0.0325  585  CYS A O     
3497 C  CB    . CYS A 482 ? 1.3371 1.8968 1.3221 -0.2123 0.1935  0.0485  585  CYS A CB    
3498 S  SG    . CYS A 482 ? 1.7040 2.3048 1.6940 -0.1980 0.2074  0.0494  585  CYS A SG    
3499 N  N     . LEU A 483 ? 1.3133 1.7872 1.2727 -0.2100 0.1640  0.0420  586  LEU A N     
3500 C  CA    . LEU A 483 ? 1.2766 1.7202 1.2328 -0.2207 0.1549  0.0409  586  LEU A CA    
3501 C  C     . LEU A 483 ? 1.2766 1.7203 1.2429 -0.2073 0.1388  0.0305  586  LEU A C     
3502 O  O     . LEU A 483 ? 1.2665 1.7137 1.2480 -0.2171 0.1312  0.0258  586  LEU A O     
3503 C  CB    . LEU A 483 ? 1.2930 1.6892 1.2170 -0.2211 0.1577  0.0491  586  LEU A CB    
3504 C  CG    . LEU A 483 ? 1.2861 1.6721 1.1958 -0.2367 0.1735  0.0608  586  LEU A CG    
3505 C  CD1   . LEU A 483 ? 1.3167 1.6531 1.1937 -0.2337 0.1740  0.0685  586  LEU A CD1   
3506 C  CD2   . LEU A 483 ? 1.3238 1.7222 1.2516 -0.2632 0.1783  0.0620  586  LEU A CD2   
3507 N  N     . VAL A 484 ? 1.2746 1.7142 1.2319 -0.1852 0.1336  0.0269  587  VAL A N     
3508 C  CA    . VAL A 484 ? 1.2051 1.6440 1.1711 -0.1718 0.1192  0.0176  587  VAL A CA    
3509 C  C     . VAL A 484 ? 1.2195 1.6992 1.2153 -0.1722 0.1162  0.0106  587  VAL A C     
3510 O  O     . VAL A 484 ? 1.2575 1.7381 1.2650 -0.1693 0.1048  0.0039  587  VAL A O     
3511 C  CB    . VAL A 484 ? 1.1639 1.5911 1.1137 -0.1495 0.1153  0.0153  587  VAL A CB    
3512 C  CG1   . VAL A 484 ? 1.0980 1.5280 1.0586 -0.1357 0.1018  0.0057  587  VAL A CG1   
3513 C  CG2   . VAL A 484 ? 1.1792 1.5660 1.1007 -0.1486 0.1158  0.0222  587  VAL A CG2   
3514 N  N     . LYS A 485 ? 1.2471 1.7619 1.2558 -0.1756 0.1266  0.0125  588  LYS A N     
3515 C  CA    . LYS A 485 ? 1.2453 1.8022 1.2836 -0.1757 0.1243  0.0068  588  LYS A CA    
3516 C  C     . LYS A 485 ? 1.2125 1.7741 1.2668 -0.1956 0.1191  0.0058  588  LYS A C     
3517 O  O     . LYS A 485 ? 1.2162 1.8004 1.2912 -0.1930 0.1106  -0.0006 588  LYS A O     
3518 C  CB    . LYS A 485 ? 1.2802 1.8746 1.3289 -0.1760 0.1380  0.0102  588  LYS A CB    
3519 C  CG    . LYS A 485 ? 1.2962 1.9370 1.3750 -0.1707 0.1361  0.0045  588  LYS A CG    
3520 C  CD    . LYS A 485 ? 1.3479 1.9882 1.4261 -0.1458 0.1270  -0.0036 588  LYS A CD    
3521 C  CE    . LYS A 485 ? 1.3836 2.0525 1.4887 -0.1431 0.1178  -0.0100 588  LYS A CE    
3522 N  NZ    . LYS A 485 ? 1.3263 1.9759 1.4337 -0.1562 0.1064  -0.0116 588  LYS A NZ    
3523 N  N     . ASP A 486 ? 1.1810 1.7203 1.2246 -0.2155 0.1240  0.0121  589  ASP A N     
3524 C  CA    . ASP A 486 ? 1.2180 1.7575 1.2733 -0.2365 0.1195  0.0108  589  ASP A CA    
3525 C  C     . ASP A 486 ? 1.2741 1.7628 1.3059 -0.2438 0.1152  0.0128  589  ASP A C     
3526 O  O     . ASP A 486 ? 1.3357 1.8126 1.3665 -0.2654 0.1171  0.0152  589  ASP A O     
3527 C  CB    . ASP A 486 ? 1.2420 1.8097 1.3118 -0.2583 0.1311  0.0161  589  ASP A CB    
3528 C  CG    . ASP A 486 ? 1.3283 1.9513 1.4260 -0.2521 0.1344  0.0136  589  ASP A CG    
3529 O  OD1   . ASP A 486 ? 1.4458 2.0807 1.5397 -0.2346 0.1408  0.0147  589  ASP A OD1   
3530 O  OD2   . ASP A 486 ? 1.3139 1.9688 1.4369 -0.2643 0.1306  0.0104  589  ASP A OD2   
3531 N  N     . TRP A 487 ? 1.2393 1.6978 1.2522 -0.2261 0.1095  0.0118  590  TRP A N     
3532 C  CA    . TRP A 487 ? 1.2284 1.6399 1.2195 -0.2298 0.1053  0.0138  590  TRP A CA    
3533 C  C     . TRP A 487 ? 1.2659 1.6724 1.2663 -0.2320 0.0924  0.0062  590  TRP A C     
3534 O  O     . TRP A 487 ? 1.3272 1.7543 1.3422 -0.2190 0.0838  -0.0007 590  TRP A O     
3535 C  CB    . TRP A 487 ? 1.2102 1.5948 1.1791 -0.2098 0.1039  0.0160  590  TRP A CB    
3536 C  CG    . TRP A 487 ? 1.2071 1.5442 1.1509 -0.2129 0.1034  0.0210  590  TRP A CG    
3537 C  CD1   . TRP A 487 ? 1.2366 1.5466 1.1731 -0.2068 0.0933  0.0176  590  TRP A CD1   
3538 C  CD2   . TRP A 487 ? 1.2449 1.5559 1.1670 -0.2217 0.1142  0.0310  590  TRP A CD2   
3539 N  NE1   . TRP A 487 ? 1.2517 1.5211 1.1638 -0.2105 0.0970  0.0246  590  TRP A NE1   
3540 C  CE2   . TRP A 487 ? 1.2519 1.5201 1.1543 -0.2196 0.1096  0.0330  590  TRP A CE2   
3541 C  CE3   . TRP A 487 ? 1.3064 1.6257 1.2233 -0.2307 0.1278  0.0388  590  TRP A CE3   
3542 C  CZ2   . TRP A 487 ? 1.3350 1.5677 1.2124 -0.2254 0.1178  0.0426  590  TRP A CZ2   
3543 C  CZ3   . TRP A 487 ? 1.3643 1.6478 1.2558 -0.2374 0.1360  0.0486  590  TRP A CZ3   
3544 C  CH2   . TRP A 487 ? 1.3811 1.6213 1.2530 -0.2344 0.1308  0.0505  590  TRP A CH2   
3545 N  N     . PRO A 488 ? 1.2644 1.6428 1.2554 -0.2481 0.0912  0.0072  591  PRO A N     
3546 C  CA    . PRO A 488 ? 1.2709 1.6434 1.2686 -0.2509 0.0793  -0.0001 591  PRO A CA    
3547 C  C     . PRO A 488 ? 1.2892 1.6428 1.2782 -0.2292 0.0699  -0.0037 591  PRO A C     
3548 O  O     . PRO A 488 ? 1.2883 1.6132 1.2573 -0.2186 0.0722  0.0008  591  PRO A O     
3549 C  CB    . PRO A 488 ? 1.2723 1.6096 1.2541 -0.2715 0.0824  0.0030  591  PRO A CB    
3550 C  CG    . PRO A 488 ? 1.3111 1.6500 1.2874 -0.2845 0.0964  0.0114  591  PRO A CG    
3551 C  CD    . PRO A 488 ? 1.2680 1.6179 1.2408 -0.2650 0.1013  0.0153  591  PRO A CD    
3552 N  N     . PRO A 489 ? 1.2894 1.6591 1.2932 -0.2221 0.0593  -0.0113 592  PRO A N     
3553 C  CA    . PRO A 489 ? 1.2919 1.6450 1.2889 -0.2023 0.0508  -0.0145 592  PRO A CA    
3554 C  C     . PRO A 489 ? 1.3475 1.6548 1.3223 -0.2038 0.0490  -0.0123 592  PRO A C     
3555 O  O     . PRO A 489 ? 1.2654 1.5544 1.2329 -0.2206 0.0507  -0.0114 592  PRO A O     
3556 C  CB    . PRO A 489 ? 1.3015 1.6807 1.3188 -0.1992 0.0408  -0.0223 592  PRO A CB    
3557 C  CG    . PRO A 489 ? 1.3558 1.7760 1.3938 -0.2106 0.0450  -0.0228 592  PRO A CG    
3558 C  CD    . PRO A 489 ? 1.3650 1.7728 1.3936 -0.2307 0.0549  -0.0168 592  PRO A CD    
3559 N  N     . ILE A 490 ? 1.2623 1.5511 1.2263 -0.1858 0.0456  -0.0116 593  ILE A N     
3560 C  CA    . ILE A 490 ? 1.2325 1.4799 1.1760 -0.1831 0.0441  -0.0089 593  ILE A CA    
3561 C  C     . ILE A 490 ? 1.1659 1.4089 1.1136 -0.1705 0.0336  -0.0147 593  ILE A C     
3562 O  O     . ILE A 490 ? 1.1403 1.4101 1.1051 -0.1635 0.0278  -0.0202 593  ILE A O     
3563 C  CB    . ILE A 490 ? 1.1875 1.4155 1.1130 -0.1732 0.0498  -0.0015 593  ILE A CB    
3564 C  CG1   . ILE A 490 ? 1.1262 1.3755 1.0593 -0.1553 0.0470  -0.0034 593  ILE A CG1   
3565 C  CG2   . ILE A 490 ? 1.2324 1.4565 1.1489 -0.1871 0.0612  0.0056  593  ILE A CG2   
3566 C  CD1   . ILE A 490 ? 1.0890 1.3210 1.0042 -0.1443 0.0505  0.0029  593  ILE A CD1   
3567 N  N     . LYS A 491 ? 1.1570 1.3650 1.0882 -0.1673 0.0319  -0.0128 594  LYS A N     
3568 C  CA    . LYS A 491 ? 1.1972 1.3982 1.1307 -0.1557 0.0232  -0.0173 594  LYS A CA    
3569 C  C     . LYS A 491 ? 1.1807 1.3953 1.1209 -0.1369 0.0195  -0.0180 594  LYS A C     
3570 O  O     . LYS A 491 ? 1.1396 1.3547 1.0742 -0.1309 0.0237  -0.0137 594  LYS A O     
3571 C  CB    . LYS A 491 ? 1.1794 1.3400 1.0928 -0.1548 0.0238  -0.0141 594  LYS A CB    
3572 C  CG    . LYS A 491 ? 1.1579 1.2991 1.0616 -0.1733 0.0271  -0.0144 594  LYS A CG    
3573 N  N     . PRO A 492 ? 1.1816 1.4066 1.1330 -0.1278 0.0117  -0.0235 595  PRO A N     
3574 C  CA    . PRO A 492 ? 1.1724 1.4094 1.1304 -0.1113 0.0082  -0.0248 595  PRO A CA    
3575 C  C     . PRO A 492 ? 1.1887 1.4027 1.1329 -0.1007 0.0084  -0.0203 595  PRO A C     
3576 O  O     . PRO A 492 ? 1.1782 1.4006 1.1230 -0.0910 0.0084  -0.0196 595  PRO A O     
3577 C  CB    . PRO A 492 ? 1.0922 1.3391 1.0624 -0.1059 0.0002  -0.0309 595  PRO A CB    
3578 C  CG    . PRO A 492 ? 1.1363 1.3654 1.1000 -0.1160 -0.0010 -0.0315 595  PRO A CG    
3579 C  CD    . PRO A 492 ? 1.1299 1.3557 1.0873 -0.1323 0.0058  -0.0287 595  PRO A CD    
3580 N  N     . GLU A 493 ? 1.2536 1.4392 1.1852 -0.1017 0.0084  -0.0173 596  GLU A N     
3581 C  CA    . GLU A 493 ? 1.1871 1.3526 1.1061 -0.0913 0.0089  -0.0120 596  GLU A CA    
3582 C  C     . GLU A 493 ? 1.3256 1.4880 1.2334 -0.0932 0.0155  -0.0059 596  GLU A C     
3583 O  O     . GLU A 493 ? 1.5092 1.6676 1.4108 -0.0825 0.0147  -0.0025 596  GLU A O     
3584 C  CB    . GLU A 493 ? 1.3237 1.4594 1.2307 -0.0918 0.0090  -0.0095 596  GLU A CB    
3585 C  CG    . GLU A 493 ? 1.3516 1.4867 1.2664 -0.0854 0.0025  -0.0141 596  GLU A CG    
3586 C  CD    . GLU A 493 ? 1.5374 1.6818 1.4600 -0.0956 0.0004  -0.0201 596  GLU A CD    
3587 O  OE1   . GLU A 493 ? 1.4174 1.5693 1.3406 -0.1087 0.0038  -0.0208 596  GLU A OE1   
3588 O  OE2   . GLU A 493 ? 1.4838 1.6288 1.4121 -0.0907 -0.0048 -0.0238 596  GLU A OE2   
3589 N  N     . GLN A 494 ? 1.2368 1.4014 1.1417 -0.1070 0.0220  -0.0042 597  GLN A N     
3590 C  CA    . GLN A 494 ? 1.2302 1.3923 1.1239 -0.1094 0.0294  0.0022  597  GLN A CA    
3591 C  C     . GLN A 494 ? 1.1839 1.3756 1.0875 -0.1048 0.0298  -0.0003 597  GLN A C     
3592 O  O     . GLN A 494 ? 1.2476 1.4383 1.1415 -0.0984 0.0326  0.0040  597  GLN A O     
3593 C  CB    . GLN A 494 ? 1.1965 1.3481 1.0829 -0.1272 0.0372  0.0053  597  GLN A CB    
3594 C  CG    . GLN A 494 ? 1.1742 1.2919 1.0469 -0.1322 0.0379  0.0076  597  GLN A CG    
3595 C  CD    . GLN A 494 ? 1.2341 1.3413 1.1004 -0.1519 0.0449  0.0092  597  GLN A CD    
3596 O  OE1   . GLN A 494 ? 1.2541 1.3854 1.1324 -0.1635 0.0474  0.0067  597  GLN A OE1   
3597 N  NE2   . GLN A 494 ? 1.2596 1.3306 1.1071 -0.1559 0.0485  0.0134  597  GLN A NE2   
3598 N  N     . ALA A 495 ? 1.1568 1.3748 1.0787 -0.1071 0.0270  -0.0071 598  ALA A N     
3599 C  CA    . ALA A 495 ? 1.0996 1.3454 1.0309 -0.1014 0.0279  -0.0100 598  ALA A CA    
3600 C  C     . ALA A 495 ? 1.1506 1.3968 1.0808 -0.0848 0.0219  -0.0122 598  ALA A C     
3601 O  O     . ALA A 495 ? 1.1339 1.3945 1.0638 -0.0787 0.0238  -0.0131 598  ALA A O     
3602 C  CB    . ALA A 495 ? 1.0752 1.3485 1.0266 -0.1062 0.0259  -0.0164 598  ALA A CB    
3603 N  N     . MET A 496 ? 1.1702 1.4012 1.0998 -0.0778 0.0151  -0.0132 599  MET A N     
3604 C  CA    . MET A 496 ? 1.2024 1.4329 1.1311 -0.0638 0.0093  -0.0150 599  MET A CA    
3605 C  C     . MET A 496 ? 1.2177 1.4380 1.1297 -0.0594 0.0121  -0.0091 599  MET A C     
3606 O  O     . MET A 496 ? 1.1803 1.4070 1.0907 -0.0496 0.0085  -0.0111 599  MET A O     
3607 C  CB    . MET A 496 ? 1.1828 1.3992 1.1144 -0.0585 0.0025  -0.0161 599  MET A CB    
3608 C  CG    . MET A 496 ? 1.1652 1.3919 1.1122 -0.0600 -0.0016 -0.0222 599  MET A CG    
3609 S  SD    . MET A 496 ? 1.1749 1.3863 1.1244 -0.0516 -0.0089 -0.0231 599  MET A SD    
3610 C  CE    . MET A 496 ? 1.0971 1.2794 1.0296 -0.0552 -0.0051 -0.0153 599  MET A CE    
3611 N  N     . GLU A 497 ? 1.2952 1.4987 1.1934 -0.0665 0.0183  -0.0017 600  GLU A N     
3612 C  CA    . GLU A 497 ? 1.3412 1.5353 1.2218 -0.0621 0.0216  0.0050  600  GLU A CA    
3613 C  C     . GLU A 497 ? 1.3409 1.5550 1.2204 -0.0617 0.0260  0.0037  600  GLU A C     
3614 O  O     . GLU A 497 ? 1.3001 1.5137 1.1682 -0.0534 0.0253  0.0058  600  GLU A O     
3615 C  CB    . GLU A 497 ? 1.4103 1.5806 1.2758 -0.0704 0.0285  0.0136  600  GLU A CB    
3616 C  CG    . GLU A 497 ? 1.6386 1.7964 1.4836 -0.0654 0.0324  0.0222  600  GLU A CG    
3617 C  CD    . GLU A 497 ? 1.6570 1.7881 1.4859 -0.0735 0.0401  0.0310  600  GLU A CD    
3618 O  OE1   . GLU A 497 ? 1.6897 1.8093 1.5226 -0.0822 0.0412  0.0299  600  GLU A OE1   
3619 O  OE2   . GLU A 497 ? 1.4581 1.5783 1.2689 -0.0710 0.0451  0.0392  600  GLU A OE2   
3620 N  N     . LEU A 498 ? 1.2226 1.4552 1.1136 -0.0700 0.0305  0.0002  601  LEU A N     
3621 C  CA    . LEU A 498 ? 1.1105 1.3643 1.0019 -0.0693 0.0359  -0.0013 601  LEU A CA    
3622 C  C     . LEU A 498 ? 1.0753 1.3458 0.9753 -0.0573 0.0297  -0.0096 601  LEU A C     
3623 O  O     . LEU A 498 ? 1.0318 1.3220 0.9350 -0.0557 0.0340  -0.0126 601  LEU A O     
3624 C  CB    . LEU A 498 ? 1.0733 1.3437 0.9761 -0.0825 0.0432  -0.0018 601  LEU A CB    
3625 C  CG    . LEU A 498 ? 1.0854 1.3389 0.9810 -0.0972 0.0495  0.0052  601  LEU A CG    
3626 C  CD1   . LEU A 498 ? 0.9007 1.1753 0.8109 -0.1111 0.0553  0.0036  601  LEU A CD1   
3627 C  CD2   . LEU A 498 ? 1.2582 1.4946 1.1315 -0.0972 0.0565  0.0144  601  LEU A CD2   
3628 N  N     . LEU A 499 ? 1.1064 1.3688 1.0099 -0.0490 0.0203  -0.0132 602  LEU A N     
3629 C  CA    . LEU A 499 ? 1.0591 1.3334 0.9700 -0.0387 0.0142  -0.0213 602  LEU A CA    
3630 C  C     . LEU A 499 ? 1.0703 1.3334 0.9705 -0.0288 0.0073  -0.0214 602  LEU A C     
3631 O  O     . LEU A 499 ? 1.1018 1.3716 1.0065 -0.0209 0.0017  -0.0285 602  LEU A O     
3632 C  CB    . LEU A 499 ? 1.1125 1.3922 1.0418 -0.0386 0.0087  -0.0270 602  LEU A CB    
3633 C  CG    . LEU A 499 ? 1.0892 1.3881 1.0323 -0.0457 0.0135  -0.0294 602  LEU A CG    
3634 C  CD1   . LEU A 499 ? 0.8619 1.1638 0.8207 -0.0448 0.0073  -0.0342 602  LEU A CD1   
3635 C  CD2   . LEU A 499 ? 0.9645 1.2845 0.9092 -0.0410 0.0181  -0.0332 602  LEU A CD2   
3636 N  N     . ASP A 500 ? 1.0504 1.2967 0.9364 -0.0290 0.0075  -0.0139 603  ASP A N     
3637 C  CA    . ASP A 500 ? 1.1862 1.4251 1.0621 -0.0197 0.0006  -0.0134 603  ASP A CA    
3638 C  C     . ASP A 500 ? 1.2225 1.4692 1.0838 -0.0156 0.0035  -0.0139 603  ASP A C     
3639 O  O     . ASP A 500 ? 1.1955 1.4551 1.0572 -0.0184 0.0106  -0.0160 603  ASP A O     
3640 C  CB    . ASP A 500 ? 1.1753 1.3944 1.0423 -0.0198 -0.0006 -0.0047 603  ASP A CB    
3641 C  CG    . ASP A 500 ? 1.2809 1.4901 1.1337 -0.0267 0.0090  0.0043  603  ASP A CG    
3642 O  OD1   . ASP A 500 ? 1.3273 1.5466 1.1772 -0.0318 0.0165  0.0042  603  ASP A OD1   
3643 O  OD2   . ASP A 500 ? 1.3068 1.4974 1.1511 -0.0268 0.0094  0.0119  603  ASP A OD2   
3644 N  N     . CYS A 501 ? 1.2248 1.4648 1.0727 -0.0084 -0.0019 -0.0119 604  CYS A N     
3645 C  CA    . CYS A 501 ? 1.2387 1.4854 1.0709 -0.0033 -0.0007 -0.0135 604  CYS A CA    
3646 C  C     . CYS A 501 ? 1.1957 1.4393 1.0109 -0.0072 0.0098  -0.0047 604  CYS A C     
3647 O  O     . CYS A 501 ? 1.1656 1.4166 0.9676 -0.0038 0.0132  -0.0060 604  CYS A O     
3648 C  CB    . CYS A 501 ? 1.2569 1.4986 1.0802 0.0051  -0.0113 -0.0144 604  CYS A CB    
3649 S  SG    . CYS A 501 ? 1.5268 1.7514 1.3463 0.0064  -0.0156 -0.0038 604  CYS A SG    
3650 N  N     . ASN A 502 ? 1.2103 1.4420 1.0244 -0.0144 0.0154  0.0040  605  ASN A N     
3651 C  CA    . ASN A 502 ? 1.1380 1.3632 0.9347 -0.0189 0.0257  0.0135  605  ASN A CA    
3652 C  C     . ASN A 502 ? 1.1247 1.3632 0.9279 -0.0281 0.0368  0.0126  605  ASN A C     
3653 O  O     . ASN A 502 ? 1.1867 1.4218 0.9764 -0.0332 0.0468  0.0203  605  ASN A O     
3654 C  CB    . ASN A 502 ? 1.1680 1.3711 0.9585 -0.0227 0.0274  0.0236  605  ASN A CB    
3655 C  CG    . ASN A 502 ? 1.4318 1.6233 1.2131 -0.0124 0.0181  0.0271  605  ASN A CG    
3656 O  OD1   . ASN A 502 ? 1.5741 1.7747 1.3592 -0.0044 0.0085  0.0205  605  ASN A OD1   
3657 N  ND2   . ASN A 502 ? 1.5530 1.7244 1.3222 -0.0126 0.0210  0.0377  605  ASN A ND2   
3658 N  N     . TYR A 503 ? 1.0929 1.3470 0.9165 -0.0303 0.0356  0.0039  606  TYR A N     
3659 C  CA    . TYR A 503 ? 1.0750 1.3463 0.9083 -0.0385 0.0453  0.0026  606  TYR A CA    
3660 C  C     . TYR A 503 ? 1.0663 1.3584 0.9108 -0.0314 0.0427  -0.0082 606  TYR A C     
3661 O  O     . TYR A 503 ? 1.1092 1.4085 0.9725 -0.0313 0.0377  -0.0148 606  TYR A O     
3662 C  CB    . TYR A 503 ? 1.0047 1.2734 0.8534 -0.0505 0.0474  0.0044  606  TYR A CB    
3663 C  CG    . TYR A 503 ? 0.9768 1.2208 0.8136 -0.0572 0.0500  0.0142  606  TYR A CG    
3664 C  CD1   . TYR A 503 ? 1.1028 1.3274 0.9366 -0.0523 0.0418  0.0158  606  TYR A CD1   
3665 C  CD2   . TYR A 503 ? 0.9531 1.1928 0.7818 -0.0685 0.0613  0.0222  606  TYR A CD2   
3666 C  CE1   . TYR A 503 ? 1.1483 1.3487 0.9700 -0.0569 0.0447  0.0248  606  TYR A CE1   
3667 C  CE2   . TYR A 503 ? 1.0572 1.2710 0.8732 -0.0743 0.0642  0.0312  606  TYR A CE2   
3668 C  CZ    . TYR A 503 ? 1.1302 1.3239 0.9422 -0.0678 0.0559  0.0323  606  TYR A CZ    
3669 O  OH    . TYR A 503 ? 1.1906 1.3569 0.9888 -0.0720 0.0594  0.0413  606  TYR A OH    
3670 N  N     . PRO A 504 ? 1.1460 1.4468 0.9778 -0.0248 0.0464  -0.0100 607  PRO A N     
3671 C  CA    . PRO A 504 ? 1.0514 1.3696 0.8907 -0.0168 0.0451  -0.0205 607  PRO A CA    
3672 C  C     . PRO A 504 ? 1.0598 1.4010 0.9092 -0.0206 0.0562  -0.0215 607  PRO A C     
3673 O  O     . PRO A 504 ? 1.0632 1.4190 0.9201 -0.0131 0.0559  -0.0299 607  PRO A O     
3674 C  CB    . PRO A 504 ? 1.0454 1.3580 0.8616 -0.0069 0.0428  -0.0219 607  PRO A CB    
3675 C  CG    . PRO A 504 ? 1.1203 1.4244 0.9182 -0.0121 0.0508  -0.0104 607  PRO A CG    
3676 C  CD    . PRO A 504 ? 1.0932 1.3857 0.9001 -0.0228 0.0514  -0.0027 607  PRO A CD    
3677 N  N     . ASP A 505 ? 1.0857 1.4306 0.9356 -0.0319 0.0663  -0.0131 608  ASP A N     
3678 C  CA    . ASP A 505 ? 1.0229 1.3928 0.8826 -0.0359 0.0777  -0.0132 608  ASP A CA    
3679 C  C     . ASP A 505 ? 1.0981 1.4859 0.9847 -0.0370 0.0746  -0.0200 608  ASP A C     
3680 O  O     . ASP A 505 ? 1.0144 1.3960 0.9136 -0.0449 0.0696  -0.0189 608  ASP A O     
3681 C  CB    . ASP A 505 ? 1.0196 1.3883 0.8752 -0.0501 0.0887  -0.0023 608  ASP A CB    
3682 C  CG    . ASP A 505 ? 1.2823 1.6781 1.1443 -0.0539 0.1021  -0.0010 608  ASP A CG    
3683 O  OD1   . ASP A 505 ? 1.2230 1.6424 1.1077 -0.0550 0.1030  -0.0062 608  ASP A OD1   
3684 O  OD2   . ASP A 505 ? 1.3582 1.7527 1.2025 -0.0552 0.1120  0.0058  608  ASP A OD2   
3685 N  N     . PRO A 506 ? 1.0884 1.4980 0.9832 -0.0286 0.0777  -0.0269 609  PRO A N     
3686 C  CA    . PRO A 506 ? 0.9958 1.4220 0.9152 -0.0274 0.0739  -0.0330 609  PRO A CA    
3687 C  C     . PRO A 506 ? 1.0130 1.4531 0.9513 -0.0422 0.0779  -0.0282 609  PRO A C     
3688 O  O     . PRO A 506 ? 1.0542 1.4951 1.0086 -0.0449 0.0705  -0.0310 609  PRO A O     
3689 C  CB    . PRO A 506 ? 1.0001 1.4476 0.9209 -0.0152 0.0798  -0.0393 609  PRO A CB    
3690 C  CG    . PRO A 506 ? 1.1642 1.5977 1.0583 -0.0072 0.0814  -0.0397 609  PRO A CG    
3691 C  CD    . PRO A 506 ? 1.0875 1.5057 0.9677 -0.0182 0.0843  -0.0296 609  PRO A CD    
3692 N  N     . MET A 507 ? 1.0453 1.4963 0.9816 -0.0525 0.0895  -0.0209 610  MET A N     
3693 C  CA    . MET A 507 ? 1.0222 1.4852 0.9755 -0.0690 0.0930  -0.0164 610  MET A CA    
3694 C  C     . MET A 507 ? 1.0593 1.4946 1.0086 -0.0789 0.0857  -0.0130 610  MET A C     
3695 O  O     . MET A 507 ? 1.0608 1.5016 1.0260 -0.0898 0.0830  -0.0130 610  MET A O     
3696 C  CB    . MET A 507 ? 1.0379 1.5155 0.9879 -0.0791 0.1076  -0.0088 610  MET A CB    
3697 C  CG    . MET A 507 ? 1.1927 1.7005 1.1474 -0.0696 0.1169  -0.0114 610  MET A CG    
3698 S  SD    . MET A 507 ? 1.1661 1.7163 1.1555 -0.0702 0.1180  -0.0163 610  MET A SD    
3699 C  CE    . MET A 507 ? 1.0809 1.6261 1.0724 -0.0487 0.1058  -0.0277 610  MET A CE    
3700 N  N     . VAL A 508 ? 1.0430 1.4491 0.9708 -0.0750 0.0822  -0.0101 611  VAL A N     
3701 C  CA    . VAL A 508 ? 1.0469 1.4257 0.9701 -0.0815 0.0752  -0.0071 611  VAL A CA    
3702 C  C     . VAL A 508 ? 0.9959 1.3715 0.9313 -0.0745 0.0629  -0.0146 611  VAL A C     
3703 O  O     . VAL A 508 ? 0.9752 1.3434 0.9194 -0.0826 0.0584  -0.0145 611  VAL A O     
3704 C  CB    . VAL A 508 ? 1.0689 1.4200 0.9661 -0.0777 0.0753  -0.0011 611  VAL A CB    
3705 C  CG1   . VAL A 508 ? 0.9705 1.2937 0.8633 -0.0805 0.0674  0.0013  611  VAL A CG1   
3706 C  CG2   . VAL A 508 ? 1.0408 1.3917 0.9250 -0.0868 0.0883  0.0081  611  VAL A CG2   
3707 N  N     . ARG A 509 ? 0.9850 1.3648 0.9201 -0.0596 0.0577  -0.0215 612  ARG A N     
3708 C  CA    . ARG A 509 ? 0.9518 1.3294 0.8988 -0.0527 0.0470  -0.0284 612  ARG A CA    
3709 C  C     . ARG A 509 ? 1.0214 1.4211 0.9911 -0.0582 0.0470  -0.0313 612  ARG A C     
3710 O  O     . ARG A 509 ? 0.9159 1.3089 0.8947 -0.0608 0.0398  -0.0330 612  ARG A O     
3711 C  CB    . ARG A 509 ? 0.9483 1.3276 0.8908 -0.0369 0.0428  -0.0355 612  ARG A CB    
3712 C  CG    . ARG A 509 ? 1.0232 1.3908 0.9434 -0.0310 0.0449  -0.0335 612  ARG A CG    
3713 C  CD    . ARG A 509 ? 0.9535 1.2942 0.8612 -0.0305 0.0373  -0.0304 612  ARG A CD    
3714 N  NE    . ARG A 509 ? 0.8688 1.2019 0.7812 -0.0216 0.0265  -0.0372 612  ARG A NE    
3715 C  CZ    . ARG A 509 ? 0.9787 1.2922 0.8834 -0.0191 0.0187  -0.0360 612  ARG A CZ    
3716 N  NH1   . ARG A 509 ? 0.9912 1.2900 0.8823 -0.0231 0.0199  -0.0281 612  ARG A NH1   
3717 N  NH2   . ARG A 509 ? 1.0598 1.3688 0.9709 -0.0121 0.0097  -0.0423 612  ARG A NH2   
3718 N  N     . GLY A 510 ? 0.9290 1.3563 0.9080 -0.0596 0.0552  -0.0316 613  GLY A N     
3719 C  CA    . GLY A 510 ? 0.9421 1.3947 0.9437 -0.0643 0.0550  -0.0339 613  GLY A CA    
3720 C  C     . GLY A 510 ? 0.9582 1.4060 0.9659 -0.0815 0.0541  -0.0298 613  GLY A C     
3721 O  O     . GLY A 510 ? 0.9091 1.3677 0.9328 -0.0846 0.0486  -0.0328 613  GLY A O     
3722 N  N     . PHE A 511 ? 0.9824 1.4127 0.9761 -0.0927 0.0593  -0.0229 614  PHE A N     
3723 C  CA    . PHE A 511 ? 0.9318 1.3515 0.9278 -0.1094 0.0585  -0.0195 614  PHE A CA    
3724 C  C     . PHE A 511 ? 0.9683 1.3620 0.9602 -0.1063 0.0478  -0.0218 614  PHE A C     
3725 O  O     . PHE A 511 ? 1.0431 1.4373 1.0447 -0.1146 0.0432  -0.0236 614  PHE A O     
3726 C  CB    . PHE A 511 ? 0.9612 1.3652 0.9409 -0.1212 0.0677  -0.0110 614  PHE A CB    
3727 C  CG    . PHE A 511 ? 0.9689 1.3539 0.9459 -0.1379 0.0671  -0.0076 614  PHE A CG    
3728 C  CD1   . PHE A 511 ? 1.0512 1.4552 1.0435 -0.1543 0.0700  -0.0076 614  PHE A CD1   
3729 C  CD2   . PHE A 511 ? 0.9108 1.2591 0.8698 -0.1371 0.0635  -0.0045 614  PHE A CD2   
3730 C  CE1   . PHE A 511 ? 1.0788 1.4628 1.0667 -0.1704 0.0692  -0.0053 614  PHE A CE1   
3731 C  CE2   . PHE A 511 ? 0.9848 1.3127 0.9392 -0.1517 0.0635  -0.0018 614  PHE A CE2   
3732 C  CZ    . PHE A 511 ? 1.0635 1.4079 1.0315 -0.1688 0.0663  -0.0025 614  PHE A CZ    
3733 N  N     . ALA A 512 ? 0.9437 1.3156 0.9213 -0.0945 0.0438  -0.0219 615  ALA A N     
3734 C  CA    . ALA A 512 ? 0.9778 1.3264 0.9521 -0.0908 0.0346  -0.0236 615  ALA A CA    
3735 C  C     . ALA A 512 ? 0.9107 1.2729 0.9016 -0.0837 0.0267  -0.0307 615  ALA A C     
3736 O  O     . ALA A 512 ? 1.0194 1.3731 1.0149 -0.0879 0.0211  -0.0319 615  ALA A O     
3737 C  CB    . ALA A 512 ? 1.0396 1.3665 0.9970 -0.0796 0.0320  -0.0219 615  ALA A CB    
3738 N  N     . VAL A 513 ? 0.9112 1.2934 0.9099 -0.0725 0.0266  -0.0353 616  VAL A N     
3739 C  CA    . VAL A 513 ? 0.8263 1.2206 0.8397 -0.0644 0.0197  -0.0414 616  VAL A CA    
3740 C  C     . VAL A 513 ? 0.9583 1.3741 0.9883 -0.0744 0.0198  -0.0420 616  VAL A C     
3741 O  O     . VAL A 513 ? 1.0240 1.4406 1.0626 -0.0727 0.0127  -0.0451 616  VAL A O     
3742 C  CB    . VAL A 513 ? 0.8165 1.2247 0.8320 -0.0497 0.0207  -0.0460 616  VAL A CB    
3743 C  CG1   . VAL A 513 ? 0.8487 1.2712 0.8796 -0.0413 0.0152  -0.0515 616  VAL A CG1   
3744 C  CG2   . VAL A 513 ? 0.8480 1.2333 0.8474 -0.0405 0.0179  -0.0466 616  VAL A CG2   
3745 N  N     . ARG A 514 ? 0.9132 1.3471 0.9476 -0.0853 0.0277  -0.0389 617  ARG A N     
3746 C  CA    . ARG A 514 ? 0.9713 1.4267 1.0218 -0.0972 0.0271  -0.0394 617  ARG A CA    
3747 C  C     . ARG A 514 ? 1.0665 1.4991 1.1111 -0.1101 0.0228  -0.0378 617  ARG A C     
3748 O  O     . ARG A 514 ? 1.0230 1.4646 1.0784 -0.1151 0.0170  -0.0406 617  ARG A O     
3749 C  CB    . ARG A 514 ? 0.8645 1.3456 0.9219 -0.1071 0.0372  -0.0361 617  ARG A CB    
3750 C  CG    . ARG A 514 ? 0.9074 1.4245 0.9808 -0.0963 0.0401  -0.0391 617  ARG A CG    
3751 C  CD    . ARG A 514 ? 0.9366 1.4814 1.0180 -0.1063 0.0511  -0.0352 617  ARG A CD    
3752 N  NE    . ARG A 514 ? 1.0344 1.5725 1.1011 -0.1005 0.0601  -0.0323 617  ARG A NE    
3753 C  CZ    . ARG A 514 ? 1.0555 1.5751 1.1065 -0.1110 0.0667  -0.0263 617  ARG A CZ    
3754 N  NH1   . ARG A 514 ? 1.0883 1.5923 1.1358 -0.1283 0.0661  -0.0227 617  ARG A NH1   
3755 N  NH2   . ARG A 514 ? 0.9974 1.5127 1.0343 -0.1036 0.0743  -0.0239 617  ARG A NH2   
3756 N  N     . CYS A 515 ? 1.0246 1.4268 1.0507 -0.1148 0.0255  -0.0334 618  CYS A N     
3757 C  CA    . CYS A 515 ? 1.0117 1.3877 1.0293 -0.1247 0.0218  -0.0322 618  CYS A CA    
3758 C  C     . CYS A 515 ? 0.9915 1.3556 1.0101 -0.1144 0.0121  -0.0364 618  CYS A C     
3759 O  O     . CYS A 515 ? 1.0923 1.4446 1.1096 -0.1217 0.0077  -0.0375 618  CYS A O     
3760 C  CB    . CYS A 515 ? 1.0247 1.3698 1.0213 -0.1285 0.0271  -0.0260 618  CYS A CB    
3761 S  SG    . CYS A 515 ? 1.1059 1.4560 1.0978 -0.1463 0.0391  -0.0196 618  CYS A SG    
3762 N  N     . LEU A 516 ? 0.9524 1.3183 0.9722 -0.0979 0.0090  -0.0388 619  LEU A N     
3763 C  CA    . LEU A 516 ? 0.9893 1.3450 1.0108 -0.0882 0.0006  -0.0422 619  LEU A CA    
3764 C  C     . LEU A 516 ? 1.0236 1.4038 1.0621 -0.0864 -0.0043 -0.0467 619  LEU A C     
3765 O  O     . LEU A 516 ? 0.9742 1.3460 1.0138 -0.0853 -0.0108 -0.0487 619  LEU A O     
3766 C  CB    . LEU A 516 ? 0.9154 1.2626 0.9317 -0.0726 -0.0011 -0.0432 619  LEU A CB    
3767 C  CG    . LEU A 516 ? 0.8560 1.1795 0.8553 -0.0719 0.0018  -0.0387 619  LEU A CG    
3768 C  CD1   . LEU A 516 ? 0.9040 1.2192 0.8999 -0.0574 -0.0024 -0.0407 619  LEU A CD1   
3769 C  CD2   . LEU A 516 ? 0.9074 1.2056 0.8964 -0.0806 0.0014  -0.0349 619  LEU A CD2   
3770 N  N     . GLU A 517 ? 1.2138 1.6248 1.2652 -0.0853 -0.0011 -0.0481 620  GLU A N     
3771 C  CA    . GLU A 517 ? 1.1102 1.5475 1.1784 -0.0822 -0.0057 -0.0517 620  GLU A CA    
3772 C  C     . GLU A 517 ? 1.1385 1.5819 1.2118 -0.0976 -0.0088 -0.0519 620  GLU A C     
3773 O  O     . GLU A 517 ? 1.2848 1.7439 1.3690 -0.0950 -0.0151 -0.0548 620  GLU A O     
3774 C  CB    . GLU A 517 ? 1.0531 1.5233 1.1339 -0.0768 -0.0005 -0.0525 620  GLU A CB    
3775 C  CG    . GLU A 517 ? 1.1063 1.5720 1.1821 -0.0601 0.0015  -0.0540 620  GLU A CG    
3776 C  CD    . GLU A 517 ? 1.4256 1.9219 1.5113 -0.0546 0.0083  -0.0547 620  GLU A CD    
3777 O  OE1   . GLU A 517 ? 1.3061 1.8285 1.4036 -0.0647 0.0122  -0.0531 620  GLU A OE1   
3778 O  OE2   . GLU A 517 ? 1.5400 2.0343 1.6216 -0.0402 0.0099  -0.0570 620  GLU A OE2   
3779 N  N     . LYS A 518 ? 1.0501 1.4803 1.1147 -0.1135 -0.0047 -0.0489 621  LYS A N     
3780 C  CA    . LYS A 518 ? 1.0634 1.4964 1.1307 -0.1303 -0.0074 -0.0497 621  LYS A CA    
3781 C  C     . LYS A 518 ? 1.1186 1.5160 1.1701 -0.1337 -0.0119 -0.0500 621  LYS A C     
3782 O  O     . LYS A 518 ? 1.1534 1.5526 1.2075 -0.1390 -0.0184 -0.0532 621  LYS A O     
3783 C  CB    . LYS A 518 ? 1.0892 1.5297 1.1566 -0.1478 0.0007  -0.0464 621  LYS A CB    
3784 C  CG    . LYS A 518 ? 1.3208 1.7951 1.4019 -0.1450 0.0075  -0.0450 621  LYS A CG    
3785 C  CD    . LYS A 518 ? 1.5492 2.0232 1.6260 -0.1616 0.0173  -0.0403 621  LYS A CD    
3786 C  CE    . LYS A 518 ? 1.3626 1.8666 1.4497 -0.1568 0.0257  -0.0382 621  LYS A CE    
3787 N  NZ    . LYS A 518 ? 1.3656 1.9142 1.4774 -0.1564 0.0237  -0.0410 621  LYS A NZ    
3788 N  N     . TYR A 519 ? 1.0818 1.4476 1.1166 -0.1300 -0.0086 -0.0468 622  TYR A N     
3789 C  CA    . TYR A 519 ? 1.0457 1.3770 1.0643 -0.1346 -0.0106 -0.0461 622  TYR A CA    
3790 C  C     . TYR A 519 ? 0.9809 1.2919 0.9926 -0.1188 -0.0149 -0.0464 622  TYR A C     
3791 O  O     . TYR A 519 ? 1.0305 1.3189 1.0324 -0.1203 -0.0180 -0.0470 622  TYR A O     
3792 C  CB    . TYR A 519 ? 1.1205 1.4285 1.1238 -0.1449 -0.0028 -0.0411 622  TYR A CB    
3793 C  CG    . TYR A 519 ? 1.1420 1.4640 1.1497 -0.1639 0.0021  -0.0402 622  TYR A CG    
3794 C  CD1   . TYR A 519 ? 1.1409 1.4895 1.1634 -0.1736 -0.0021 -0.0446 622  TYR A CD1   
3795 C  CD2   . TYR A 519 ? 1.2034 1.5127 1.2004 -0.1724 0.0111  -0.0348 622  TYR A CD2   
3796 C  CE1   . TYR A 519 ? 1.1948 1.5585 1.2232 -0.1924 0.0023  -0.0438 622  TYR A CE1   
3797 C  CE2   . TYR A 519 ? 1.2710 1.5928 1.2725 -0.1911 0.0163  -0.0336 622  TYR A CE2   
3798 C  CZ    . TYR A 519 ? 1.2601 1.6098 1.2781 -0.2015 0.0119  -0.0383 622  TYR A CZ    
3799 O  OH    . TYR A 519 ? 1.2831 1.6474 1.3073 -0.2214 0.0169  -0.0371 622  TYR A OH    
3800 N  N     . LEU A 520 ? 1.0025 1.3204 1.0185 -0.1043 -0.0148 -0.0461 623  LEU A N     
3801 C  CA    . LEU A 520 ? 0.9830 1.2821 0.9932 -0.0908 -0.0183 -0.0459 623  LEU A CA    
3802 C  C     . LEU A 520 ? 0.9419 1.2490 0.9604 -0.0844 -0.0255 -0.0498 623  LEU A C     
3803 O  O     . LEU A 520 ? 0.9991 1.3300 1.0306 -0.0776 -0.0277 -0.0524 623  LEU A O     
3804 C  CB    . LEU A 520 ? 0.8622 1.1651 0.8732 -0.0791 -0.0162 -0.0449 623  LEU A CB    
3805 C  CG    . LEU A 520 ? 0.8564 1.1398 0.8616 -0.0670 -0.0196 -0.0443 623  LEU A CG    
3806 C  CD1   . LEU A 520 ? 0.8591 1.1141 0.8491 -0.0707 -0.0175 -0.0399 623  LEU A CD1   
3807 C  CD2   . LEU A 520 ? 0.8757 1.1667 0.8833 -0.0561 -0.0190 -0.0451 623  LEU A CD2   
3808 N  N     . THR A 521 ? 0.8655 1.1520 0.8756 -0.0856 -0.0286 -0.0499 624  THR A N     
3809 C  CA    . THR A 521 ? 0.9643 1.2546 0.9793 -0.0788 -0.0350 -0.0528 624  THR A CA    
3810 C  C     . THR A 521 ? 0.9556 1.2401 0.9724 -0.0631 -0.0365 -0.0521 624  THR A C     
3811 O  O     . THR A 521 ? 1.0618 1.3335 1.0733 -0.0586 -0.0336 -0.0496 624  THR A O     
3812 C  CB    . THR A 521 ? 0.9007 1.1696 0.9038 -0.0853 -0.0371 -0.0532 624  THR A CB    
3813 O  OG1   . THR A 521 ? 0.8713 1.1113 0.8617 -0.0810 -0.0342 -0.0498 624  THR A OG1   
3814 C  CG2   . THR A 521 ? 0.8647 1.1355 0.8642 -0.1027 -0.0354 -0.0542 624  THR A CG2   
3815 N  N     . ASP A 522 ? 0.8835 1.1775 0.9076 -0.0551 -0.0415 -0.0543 625  ASP A N     
3816 C  CA    . ASP A 522 ? 0.8290 1.1155 0.8546 -0.0414 -0.0430 -0.0538 625  ASP A CA    
3817 C  C     . ASP A 522 ? 0.8628 1.1218 0.8776 -0.0396 -0.0424 -0.0511 625  ASP A C     
3818 O  O     . ASP A 522 ? 0.8667 1.1174 0.8820 -0.0307 -0.0423 -0.0498 625  ASP A O     
3819 C  CB    . ASP A 522 ? 0.8952 1.1949 0.9290 -0.0335 -0.0478 -0.0559 625  ASP A CB    
3820 C  CG    . ASP A 522 ? 0.9810 1.3101 1.0271 -0.0322 -0.0482 -0.0582 625  ASP A CG    
3821 O  OD1   . ASP A 522 ? 1.1730 1.5134 1.2214 -0.0395 -0.0445 -0.0583 625  ASP A OD1   
3822 O  OD2   . ASP A 522 ? 1.0483 1.3892 1.1013 -0.0233 -0.0517 -0.0594 625  ASP A OD2   
3823 N  N     . ASP A 523 ? 1.0355 1.2802 1.0404 -0.0477 -0.0419 -0.0502 626  ASP A N     
3824 C  CA    . ASP A 523 ? 1.0073 1.2262 1.0014 -0.0454 -0.0401 -0.0471 626  ASP A CA    
3825 C  C     . ASP A 523 ? 1.0442 1.2539 1.0340 -0.0453 -0.0358 -0.0438 626  ASP A C     
3826 O  O     . ASP A 523 ? 1.1161 1.3158 1.1051 -0.0374 -0.0355 -0.0413 626  ASP A O     
3827 C  CB    . ASP A 523 ? 1.0597 1.2642 1.0422 -0.0539 -0.0400 -0.0476 626  ASP A CB    
3828 C  CG    . ASP A 523 ? 1.1548 1.3318 1.1243 -0.0521 -0.0364 -0.0440 626  ASP A CG    
3829 O  OD1   . ASP A 523 ? 1.1549 1.3249 1.1261 -0.0419 -0.0363 -0.0415 626  ASP A OD1   
3830 O  OD2   . ASP A 523 ? 1.0700 1.2325 1.0279 -0.0609 -0.0333 -0.0434 626  ASP A OD2   
3831 N  N     . LYS A 524 ? 1.0440 1.2579 1.0310 -0.0544 -0.0326 -0.0435 627  LYS A N     
3832 C  CA    . LYS A 524 ? 0.9271 1.1324 0.9082 -0.0540 -0.0286 -0.0398 627  LYS A CA    
3833 C  C     . LYS A 524 ? 0.8860 1.1060 0.8757 -0.0462 -0.0293 -0.0405 627  LYS A C     
3834 O  O     . LYS A 524 ? 0.9574 1.1693 0.9429 -0.0415 -0.0281 -0.0377 627  LYS A O     
3835 C  CB    . LYS A 524 ? 0.9929 1.1969 0.9671 -0.0665 -0.0241 -0.0386 627  LYS A CB    
3836 C  CG    . LYS A 524 ? 1.0454 1.2270 1.0064 -0.0746 -0.0223 -0.0375 627  LYS A CG    
3837 C  CD    . LYS A 524 ? 1.1446 1.3008 1.0943 -0.0676 -0.0201 -0.0328 627  LYS A CD    
3838 C  CE    . LYS A 524 ? 1.4647 1.5954 1.3984 -0.0752 -0.0168 -0.0315 627  LYS A CE    
3839 N  NZ    . LYS A 524 ? 1.5254 1.6532 1.4521 -0.0881 -0.0122 -0.0304 627  LYS A NZ    
3840 N  N     . LEU A 525 ? 0.8017 1.0430 0.8025 -0.0442 -0.0314 -0.0444 628  LEU A N     
3841 C  CA    . LEU A 525 ? 0.8232 1.0761 0.8302 -0.0362 -0.0319 -0.0460 628  LEU A CA    
3842 C  C     . LEU A 525 ? 0.8296 1.0713 0.8371 -0.0264 -0.0348 -0.0455 628  LEU A C     
3843 O  O     . LEU A 525 ? 0.8806 1.1204 0.8866 -0.0220 -0.0346 -0.0451 628  LEU A O     
3844 C  CB    . LEU A 525 ? 0.7891 1.0654 0.8076 -0.0342 -0.0333 -0.0501 628  LEU A CB    
3845 C  CG    . LEU A 525 ? 0.8781 1.1691 0.9013 -0.0281 -0.0317 -0.0524 628  LEU A CG    
3846 C  CD1   . LEU A 525 ? 0.9520 1.2683 0.9852 -0.0294 -0.0308 -0.0551 628  LEU A CD1   
3847 C  CD2   . LEU A 525 ? 0.8384 1.1235 0.8637 -0.0167 -0.0349 -0.0543 628  LEU A CD2   
3848 N  N     . SER A 526 ? 0.8593 1.0938 0.8687 -0.0234 -0.0376 -0.0456 629  SER A N     
3849 C  CA    . SER A 526 ? 0.8197 1.0437 0.8305 -0.0155 -0.0398 -0.0444 629  SER A CA    
3850 C  C     . SER A 526 ? 0.7259 0.9337 0.7289 -0.0161 -0.0381 -0.0399 629  SER A C     
3851 O  O     . SER A 526 ? 0.6592 0.8619 0.6645 -0.0103 -0.0397 -0.0387 629  SER A O     
3852 C  CB    . SER A 526 ? 0.7701 0.9907 0.7842 -0.0121 -0.0422 -0.0449 629  SER A CB    
3853 O  OG    . SER A 526 ? 1.0721 1.2845 1.0792 -0.0180 -0.0412 -0.0434 629  SER A OG    
3854 N  N     . GLN A 527 ? 0.7298 0.9293 0.7237 -0.0229 -0.0349 -0.0373 630  GLN A N     
3855 C  CA    . GLN A 527 ? 0.8280 1.0116 0.8134 -0.0220 -0.0328 -0.0323 630  GLN A CA    
3856 C  C     . GLN A 527 ? 0.8886 1.0762 0.8716 -0.0207 -0.0321 -0.0308 630  GLN A C     
3857 O  O     . GLN A 527 ? 0.7982 0.9794 0.7796 -0.0155 -0.0330 -0.0277 630  GLN A O     
3858 C  CB    . GLN A 527 ? 0.8702 1.0398 0.8443 -0.0292 -0.0291 -0.0300 630  GLN A CB    
3859 C  CG    . GLN A 527 ? 0.9029 1.0536 0.8667 -0.0267 -0.0262 -0.0243 630  GLN A CG    
3860 C  CD    . GLN A 527 ? 1.0946 1.2382 1.0619 -0.0181 -0.0277 -0.0222 630  GLN A CD    
3861 O  OE1   . GLN A 527 ? 1.1953 1.3295 1.1599 -0.0178 -0.0269 -0.0223 630  GLN A OE1   
3862 N  NE2   . GLN A 527 ? 1.0237 1.1723 0.9968 -0.0114 -0.0297 -0.0202 630  GLN A NE2   
3863 N  N     . TYR A 528 ? 0.9108 1.1102 0.8935 -0.0252 -0.0305 -0.0330 631  TYR A N     
3864 C  CA    . TYR A 528 ? 0.9693 1.1729 0.9476 -0.0241 -0.0293 -0.0318 631  TYR A CA    
3865 C  C     . TYR A 528 ? 0.8557 1.0745 0.8419 -0.0189 -0.0323 -0.0368 631  TYR A C     
3866 O  O     . TYR A 528 ? 0.9808 1.2061 0.9628 -0.0185 -0.0309 -0.0373 631  TYR A O     
3867 C  CB    . TYR A 528 ? 0.9185 1.1237 0.8892 -0.0328 -0.0241 -0.0301 631  TYR A CB    
3868 C  CG    . TYR A 528 ? 0.9173 1.1046 0.8780 -0.0391 -0.0206 -0.0257 631  TYR A CG    
3869 C  CD1   . TYR A 528 ? 0.9379 1.1068 0.8908 -0.0347 -0.0204 -0.0208 631  TYR A CD1   
3870 C  CD2   . TYR A 528 ? 0.9381 1.1267 0.8970 -0.0496 -0.0174 -0.0267 631  TYR A CD2   
3871 C  CE1   . TYR A 528 ? 0.9752 1.1248 0.9170 -0.0394 -0.0165 -0.0171 631  TYR A CE1   
3872 C  CE2   . TYR A 528 ? 0.9960 1.1651 0.9438 -0.0561 -0.0141 -0.0235 631  TYR A CE2   
3873 C  CZ    . TYR A 528 ? 1.0968 1.2450 1.0352 -0.0505 -0.0134 -0.0187 631  TYR A CZ    
3874 O  OH    . TYR A 528 ? 1.2067 1.3326 1.1321 -0.0560 -0.0095 -0.0158 631  TYR A OH    
3875 N  N     . LEU A 529 ? 0.8434 1.0660 0.8392 -0.0145 -0.0358 -0.0405 632  LEU A N     
3876 C  CA    . LEU A 529 ? 0.8582 1.0925 0.8601 -0.0094 -0.0379 -0.0457 632  LEU A CA    
3877 C  C     . LEU A 529 ? 0.9454 1.1773 0.9437 -0.0051 -0.0403 -0.0461 632  LEU A C     
3878 O  O     . LEU A 529 ? 0.9943 1.2348 0.9914 -0.0026 -0.0403 -0.0502 632  LEU A O     
3879 C  CB    . LEU A 529 ? 0.7749 1.0097 0.7860 -0.0050 -0.0410 -0.0485 632  LEU A CB    
3880 C  CG    . LEU A 529 ? 0.7215 0.9655 0.7381 0.0010  -0.0426 -0.0541 632  LEU A CG    
3881 C  CD1   . LEU A 529 ? 0.7278 0.9880 0.7462 -0.0003 -0.0396 -0.0567 632  LEU A CD1   
3882 C  CD2   . LEU A 529 ? 0.9167 1.1559 0.9404 0.0059  -0.0456 -0.0553 632  LEU A CD2   
3883 N  N     . ILE A 530 ? 0.9623 1.1834 0.9583 -0.0038 -0.0423 -0.0422 633  ILE A N     
3884 C  CA    . ILE A 530 ? 0.9187 1.1395 0.9121 -0.0002 -0.0459 -0.0427 633  ILE A CA    
3885 C  C     . ILE A 530 ? 1.0036 1.2279 0.9858 -0.0017 -0.0435 -0.0413 633  ILE A C     
3886 O  O     . ILE A 530 ? 1.1218 1.3508 1.1003 0.0011  -0.0459 -0.0446 633  ILE A O     
3887 C  CB    . ILE A 530 ? 0.9226 1.1343 0.9182 0.0018  -0.0486 -0.0380 633  ILE A CB    
3888 C  CG1   . ILE A 530 ? 1.0422 1.2566 1.0369 0.0050  -0.0537 -0.0389 633  ILE A CG1   
3889 C  CG2   . ILE A 530 ? 0.9489 1.1517 0.9369 -0.0005 -0.0447 -0.0311 633  ILE A CG2   
3890 C  CD1   . ILE A 530 ? 1.2054 1.4245 1.2064 0.0068  -0.0577 -0.0462 633  ILE A CD1   
3891 N  N     . GLN A 531 ? 0.9737 1.1946 0.9490 -0.0065 -0.0385 -0.0367 634  GLN A N     
3892 C  CA    . GLN A 531 ? 0.9514 1.1751 0.9152 -0.0084 -0.0350 -0.0346 634  GLN A CA    
3893 C  C     . GLN A 531 ? 1.0000 1.2374 0.9650 -0.0097 -0.0320 -0.0398 634  GLN A C     
3894 O  O     . GLN A 531 ? 1.0708 1.3139 1.0283 -0.0076 -0.0312 -0.0413 634  GLN A O     
3895 C  CB    . GLN A 531 ? 0.9244 1.1377 0.8797 -0.0139 -0.0298 -0.0277 634  GLN A CB    
3896 C  CG    . GLN A 531 ? 1.0092 1.2089 0.9580 -0.0106 -0.0313 -0.0212 634  GLN A CG    
3897 C  CD    . GLN A 531 ? 1.0150 1.2068 0.9720 -0.0088 -0.0335 -0.0203 634  GLN A CD    
3898 O  OE1   . GLN A 531 ? 1.0082 1.2012 0.9726 -0.0117 -0.0328 -0.0235 634  GLN A OE1   
3899 N  NE2   . GLN A 531 ? 0.9741 1.1587 0.9295 -0.0034 -0.0360 -0.0157 634  GLN A NE2   
3900 N  N     . LEU A 532 ? 0.9122 1.1563 0.8863 -0.0124 -0.0302 -0.0425 635  LEU A N     
3901 C  CA    . LEU A 532 ? 0.9893 1.2492 0.9664 -0.0127 -0.0268 -0.0468 635  LEU A CA    
3902 C  C     . LEU A 532 ? 1.0155 1.2811 0.9943 -0.0048 -0.0300 -0.0532 635  LEU A C     
3903 O  O     . LEU A 532 ? 1.0908 1.3678 1.0673 -0.0029 -0.0267 -0.0565 635  LEU A O     
3904 C  CB    . LEU A 532 ? 0.9642 1.2315 0.9518 -0.0163 -0.0256 -0.0481 635  LEU A CB    
3905 C  CG    . LEU A 532 ? 0.9636 1.2267 0.9485 -0.0261 -0.0218 -0.0432 635  LEU A CG    
3906 C  CD1   . LEU A 532 ? 1.0093 1.2795 1.0046 -0.0292 -0.0228 -0.0453 635  LEU A CD1   
3907 C  CD2   . LEU A 532 ? 1.0771 1.3478 1.0551 -0.0320 -0.0153 -0.0408 635  LEU A CD2   
3908 N  N     . VAL A 533 ? 1.0484 1.3055 1.0306 -0.0003 -0.0360 -0.0552 636  VAL A N     
3909 C  CA    . VAL A 533 ? 0.9837 1.2425 0.9658 0.0062  -0.0393 -0.0618 636  VAL A CA    
3910 C  C     . VAL A 533 ? 1.0450 1.3009 1.0149 0.0075  -0.0411 -0.0620 636  VAL A C     
3911 O  O     . VAL A 533 ? 1.1675 1.4271 1.1317 0.0116  -0.0415 -0.0677 636  VAL A O     
3912 C  CB    . VAL A 533 ? 0.9537 1.2045 0.9449 0.0091  -0.0446 -0.0639 636  VAL A CB    
3913 C  CG1   . VAL A 533 ? 0.9044 1.1524 0.8936 0.0142  -0.0486 -0.0707 636  VAL A CG1   
3914 C  CG2   . VAL A 533 ? 0.8925 1.1477 0.8938 0.0095  -0.0428 -0.0646 636  VAL A CG2   
3915 N  N     . GLN A 534 ? 1.0123 1.2613 0.9764 0.0047  -0.0422 -0.0556 637  GLN A N     
3916 C  CA    . GLN A 534 ? 1.0185 1.2658 0.9702 0.0066  -0.0447 -0.0550 637  GLN A CA    
3917 C  C     . GLN A 534 ? 1.0716 1.3262 1.0114 0.0059  -0.0385 -0.0545 637  GLN A C     
3918 O  O     . GLN A 534 ? 1.0493 1.3064 0.9788 0.0094  -0.0399 -0.0584 637  GLN A O     
3919 C  CB    . GLN A 534 ? 0.9628 1.2017 0.9120 0.0053  -0.0472 -0.0473 637  GLN A CB    
3920 C  CG    . GLN A 534 ? 1.0604 1.2944 1.0201 0.0071  -0.0539 -0.0480 637  GLN A CG    
3921 C  CD    . GLN A 534 ? 1.1223 1.3587 1.0825 0.0101  -0.0603 -0.0554 637  GLN A CD    
3922 O  OE1   . GLN A 534 ? 1.2346 1.4731 1.1845 0.0117  -0.0637 -0.0564 637  GLN A OE1   
3923 N  NE2   . GLN A 534 ? 1.0875 1.3227 1.0584 0.0107  -0.0622 -0.0607 637  GLN A NE2   
3924 N  N     . VAL A 535 ? 1.0362 1.2942 0.9767 0.0009  -0.0315 -0.0501 638  VAL A N     
3925 C  CA    . VAL A 535 ? 0.9884 1.2543 0.9187 -0.0007 -0.0243 -0.0489 638  VAL A CA    
3926 C  C     . VAL A 535 ? 1.0139 1.2926 0.9470 0.0033  -0.0217 -0.0564 638  VAL A C     
3927 O  O     . VAL A 535 ? 1.0611 1.3486 0.9860 0.0031  -0.0152 -0.0561 638  VAL A O     
3928 C  CB    . VAL A 535 ? 0.9880 1.2543 0.9194 -0.0089 -0.0172 -0.0421 638  VAL A CB    
3929 C  CG1   . VAL A 535 ? 1.0112 1.2624 0.9343 -0.0115 -0.0181 -0.0340 638  VAL A CG1   
3930 C  CG2   . VAL A 535 ? 1.0469 1.3181 0.9943 -0.0120 -0.0170 -0.0443 638  VAL A CG2   
3931 N  N     . LEU A 536 ? 0.9581 1.2377 0.9019 0.0074  -0.0258 -0.0628 639  LEU A N     
3932 C  CA    . LEU A 536 ? 0.9937 1.2821 0.9375 0.0137  -0.0239 -0.0705 639  LEU A CA    
3933 C  C     . LEU A 536 ? 1.0718 1.3561 1.0000 0.0187  -0.0264 -0.0750 639  LEU A C     
3934 O  O     . LEU A 536 ? 1.0378 1.3291 0.9600 0.0238  -0.0224 -0.0804 639  LEU A O     
3935 C  CB    . LEU A 536 ? 1.0041 1.2904 0.9608 0.0177  -0.0280 -0.0757 639  LEU A CB    
3936 C  CG    . LEU A 536 ? 1.0183 1.3114 0.9897 0.0145  -0.0257 -0.0729 639  LEU A CG    
3937 C  CD1   . LEU A 536 ? 0.9463 1.2358 0.9277 0.0201  -0.0298 -0.0778 639  LEU A CD1   
3938 C  CD2   . LEU A 536 ? 0.9794 1.2906 0.9530 0.0130  -0.0176 -0.0720 639  LEU A CD2   
3939 N  N     . LYS A 537 ? 1.0754 1.3491 0.9965 0.0177  -0.0328 -0.0729 640  LYS A N     
3940 C  CA    . LYS A 537 ? 1.0908 1.3615 0.9955 0.0215  -0.0361 -0.0768 640  LYS A CA    
3941 C  C     . LYS A 537 ? 1.0727 1.3491 0.9621 0.0207  -0.0293 -0.0721 640  LYS A C     
3942 O  O     . LYS A 537 ? 1.1260 1.4040 1.0004 0.0252  -0.0286 -0.0768 640  LYS A O     
3943 C  CB    . LYS A 537 ? 1.1018 1.3627 1.0054 0.0204  -0.0458 -0.0753 640  LYS A CB    
3944 C  CG    . LYS A 537 ? 1.0420 1.2970 0.9615 0.0199  -0.0518 -0.0781 640  LYS A CG    
3945 C  CD    . LYS A 537 ? 1.1556 1.4045 1.0758 0.0183  -0.0604 -0.0753 640  LYS A CD    
3946 C  CE    . LYS A 537 ? 1.0452 1.2886 0.9810 0.0173  -0.0657 -0.0778 640  LYS A CE    
3947 N  NZ    . LYS A 537 ? 1.1151 1.3559 1.0530 0.0158  -0.0740 -0.0752 640  LYS A NZ    
3948 N  N     . TYR A 538 ? 1.0431 1.3211 0.9344 0.0149  -0.0239 -0.0631 641  TYR A N     
3949 C  CA    . TYR A 538 ? 1.0786 1.3608 0.9556 0.0131  -0.0161 -0.0574 641  TYR A CA    
3950 C  C     . TYR A 538 ? 1.0499 1.3464 0.9272 0.0143  -0.0067 -0.0605 641  TYR A C     
3951 O  O     . TYR A 538 ? 1.0649 1.3663 0.9294 0.0134  0.0008  -0.0566 641  TYR A O     
3952 C  CB    . TYR A 538 ? 1.1117 1.3888 0.9906 0.0057  -0.0126 -0.0468 641  TYR A CB    
3953 C  CG    . TYR A 538 ? 1.1949 1.4587 1.0716 0.0057  -0.0201 -0.0418 641  TYR A CG    
3954 C  CD1   . TYR A 538 ? 1.2606 1.5202 1.1282 0.0113  -0.0285 -0.0444 641  TYR A CD1   
3955 C  CD2   . TYR A 538 ? 1.2364 1.4923 1.1199 0.0003  -0.0188 -0.0346 641  TYR A CD2   
3956 C  CE1   . TYR A 538 ? 1.4168 1.6675 1.2843 0.0119  -0.0353 -0.0393 641  TYR A CE1   
3957 C  CE2   . TYR A 538 ? 1.1959 1.4403 1.0775 0.0018  -0.0248 -0.0297 641  TYR A CE2   
3958 C  CZ    . TYR A 538 ? 1.3236 1.5670 1.1983 0.0078  -0.0330 -0.0317 641  TYR A CZ    
3959 O  OH    . TYR A 538 ? 1.3463 1.5815 1.2211 0.0099  -0.0389 -0.0262 641  TYR A OH    
3960 N  N     . GLU A 539 ? 1.0318 1.3357 0.9233 0.0169  -0.0062 -0.0669 642  GLU A N     
3961 C  CA    . GLU A 539 ? 1.1049 1.4252 0.9992 0.0191  0.0030  -0.0695 642  GLU A CA    
3962 C  C     . GLU A 539 ? 0.9849 1.3064 0.8620 0.0275  0.0049  -0.0759 642  GLU A C     
3963 O  O     . GLU A 539 ? 0.9109 1.2222 0.7817 0.0333  -0.0027 -0.0832 642  GLU A O     
3964 C  CB    . GLU A 539 ? 1.0367 1.3644 0.9505 0.0212  0.0023  -0.0740 642  GLU A CB    
3965 C  CG    . GLU A 539 ? 1.0275 1.3578 0.9573 0.0127  0.0024  -0.0679 642  GLU A CG    
3966 C  CD    . GLU A 539 ? 1.0481 1.3914 0.9790 0.0047  0.0119  -0.0611 642  GLU A CD    
3967 O  OE1   . GLU A 539 ? 1.0716 1.4294 0.9986 0.0073  0.0199  -0.0622 642  GLU A OE1   
3968 O  OE2   . GLU A 539 ? 1.1492 1.4876 1.0845 -0.0046 0.0119  -0.0546 642  GLU A OE2   
3969 N  N     . GLN A 540 ? 0.9964 1.3303 0.8655 0.0277  0.0152  -0.0734 643  GLN A N     
3970 C  CA    . GLN A 540 ? 1.0286 1.3635 0.8785 0.0360  0.0183  -0.0791 643  GLN A CA    
3971 C  C     . GLN A 540 ? 1.0119 1.3500 0.8661 0.0457  0.0181  -0.0899 643  GLN A C     
3972 O  O     . GLN A 540 ? 0.9269 1.2573 0.7644 0.0533  0.0159  -0.0977 643  GLN A O     
3973 C  CB    . GLN A 540 ? 0.9727 1.3213 0.8141 0.0338  0.0311  -0.0729 643  GLN A CB    
3974 C  CG    . GLN A 540 ? 1.1831 1.5225 0.9999 0.0332  0.0314  -0.0682 643  GLN A CG    
3975 C  CD    . GLN A 540 ? 1.1508 1.5034 0.9574 0.0320  0.0453  -0.0625 643  GLN A CD    
3976 O  OE1   . GLN A 540 ? 1.0643 1.4327 0.8859 0.0267  0.0545  -0.0582 643  GLN A OE1   
3977 N  NE2   . GLN A 540 ? 1.1278 1.4748 0.9088 0.0367  0.0469  -0.0623 643  GLN A NE2   
3978 N  N     . TYR A 541 ? 1.0812 1.4298 0.9563 0.0461  0.0203  -0.0907 644  TYR A N     
3979 C  CA    . TYR A 541 ? 1.0342 1.3865 0.9138 0.0566  0.0215  -0.0998 644  TYR A CA    
3980 C  C     . TYR A 541 ? 1.0002 1.3478 0.8992 0.0561  0.0145  -0.1014 644  TYR A C     
3981 O  O     . TYR A 541 ? 1.0592 1.4046 0.9696 0.0474  0.0103  -0.0952 644  TYR A O     
3982 C  CB    . TYR A 541 ? 1.0270 1.4029 0.9115 0.0609  0.0344  -0.0988 644  TYR A CB    
3983 C  CG    . TYR A 541 ? 1.0501 1.4335 0.9180 0.0591  0.0434  -0.0944 644  TYR A CG    
3984 C  CD1   . TYR A 541 ? 1.1328 1.5062 0.9759 0.0665  0.0439  -0.1002 644  TYR A CD1   
3985 C  CD2   . TYR A 541 ? 0.9629 1.3623 0.8386 0.0495  0.0514  -0.0845 644  TYR A CD2   
3986 C  CE1   . TYR A 541 ? 1.0678 1.4476 0.8940 0.0655  0.0525  -0.0956 644  TYR A CE1   
3987 C  CE2   . TYR A 541 ? 1.0701 1.4752 0.9298 0.0476  0.0604  -0.0796 644  TYR A CE2   
3988 C  CZ    . TYR A 541 ? 1.0897 1.4852 0.9244 0.0561  0.0611  -0.0849 644  TYR A CZ    
3989 O  OH    . TYR A 541 ? 0.9118 1.3126 0.7289 0.0549  0.0705  -0.0796 644  TYR A OH    
3990 N  N     . LEU A 542 ? 0.9435 1.2883 0.8445 0.0663  0.0139  -0.1097 645  LEU A N     
3991 C  CA    . LEU A 542 ? 0.9896 1.3290 0.9072 0.0674  0.0079  -0.1111 645  LEU A CA    
3992 C  C     . LEU A 542 ? 1.0648 1.4254 1.0033 0.0646  0.0128  -0.1051 645  LEU A C     
3993 O  O     . LEU A 542 ? 0.9940 1.3525 0.9460 0.0583  0.0076  -0.1010 645  LEU A O     
3994 C  CB    . LEU A 542 ? 0.9451 1.2734 0.8569 0.0796  0.0067  -0.1213 645  LEU A CB    
3995 C  CG    . LEU A 542 ? 0.9594 1.2641 0.8518 0.0813  -0.0003 -0.1291 645  LEU A CG    
3996 C  CD1   . LEU A 542 ? 0.9381 1.2298 0.8260 0.0928  -0.0007 -0.1390 645  LEU A CD1   
3997 C  CD2   . LEU A 542 ? 0.9470 1.2377 0.8427 0.0713  -0.0109 -0.1258 645  LEU A CD2   
3998 N  N     . ASP A 543 ? 1.0702 1.4526 1.0117 0.0694  0.0228  -0.1046 646  ASP A N     
3999 C  CA    . ASP A 543 ? 0.9415 1.3481 0.9038 0.0670  0.0273  -0.0996 646  ASP A CA    
4000 C  C     . ASP A 543 ? 0.9774 1.3956 0.9423 0.0533  0.0314  -0.0908 646  ASP A C     
4001 O  O     . ASP A 543 ? 0.9848 1.4147 0.9420 0.0523  0.0400  -0.0887 646  ASP A O     
4002 C  CB    . ASP A 543 ? 0.9273 1.3538 0.8935 0.0797  0.0361  -0.1033 646  ASP A CB    
4003 C  CG    . ASP A 543 ? 0.9524 1.4049 0.9424 0.0794  0.0386  -0.0992 646  ASP A CG    
4004 O  OD1   . ASP A 543 ? 0.9114 1.3706 0.9132 0.0667  0.0358  -0.0928 646  ASP A OD1   
4005 O  OD2   . ASP A 543 ? 1.0749 1.5414 1.0712 0.0923  0.0432  -0.1026 646  ASP A OD2   
4006 N  N     . ASN A 544 ? 0.9919 1.4055 0.9667 0.0426  0.0257  -0.0856 647  ASN A N     
4007 C  CA    . ASN A 544 ? 0.9400 1.3620 0.9184 0.0288  0.0293  -0.0774 647  ASN A CA    
4008 C  C     . ASN A 544 ? 0.9980 1.4291 0.9961 0.0220  0.0259  -0.0743 647  ASN A C     
4009 O  O     . ASN A 544 ? 1.0312 1.4619 1.0391 0.0288  0.0207  -0.0779 647  ASN A O     
4010 C  CB    . ASN A 544 ? 0.9094 1.3089 0.8719 0.0216  0.0254  -0.0739 647  ASN A CB    
4011 C  CG    . ASN A 544 ? 0.9660 1.3431 0.9284 0.0224  0.0144  -0.0760 647  ASN A CG    
4012 O  OD1   . ASN A 544 ? 1.0752 1.4480 1.0471 0.0151  0.0102  -0.0722 647  ASN A OD1   
4013 N  ND2   . ASN A 544 ? 1.0450 1.4077 0.9960 0.0308  0.0098  -0.0822 647  ASN A ND2   
4014 N  N     . LEU A 545 ? 0.9875 1.4256 0.9901 0.0084  0.0288  -0.0674 648  LEU A N     
4015 C  CA    . LEU A 545 ? 0.7944 1.2419 0.8141 0.0005  0.0256  -0.0649 648  LEU A CA    
4016 C  C     . LEU A 545 ? 0.8867 1.3098 0.9046 -0.0031 0.0161  -0.0643 648  LEU A C     
4017 O  O     . LEU A 545 ? 0.9192 1.3466 0.9496 -0.0052 0.0115  -0.0643 648  LEU A O     
4018 C  CB    . LEU A 545 ? 0.7780 1.2411 0.8027 -0.0140 0.0326  -0.0585 648  LEU A CB    
4019 C  CG    . LEU A 545 ? 0.7853 1.2783 0.8163 -0.0121 0.0431  -0.0580 648  LEU A CG    
4020 C  CD1   . LEU A 545 ? 0.8377 1.3459 0.8758 -0.0290 0.0494  -0.0513 648  LEU A CD1   
4021 C  CD2   . LEU A 545 ? 0.7095 1.2250 0.7566 -0.0002 0.0422  -0.0629 648  LEU A CD2   
4022 N  N     . LEU A 546 ? 0.8991 1.2980 0.9016 -0.0034 0.0131  -0.0635 649  LEU A N     
4023 C  CA    . LEU A 546 ? 0.9402 1.3175 0.9416 -0.0060 0.0048  -0.0625 649  LEU A CA    
4024 C  C     . LEU A 546 ? 0.9456 1.3164 0.9519 0.0048  -0.0018 -0.0682 649  LEU A C     
4025 O  O     . LEU A 546 ? 1.0422 1.4052 1.0553 0.0033  -0.0075 -0.0677 649  LEU A O     
4026 C  CB    . LEU A 546 ? 0.9317 1.2880 0.9165 -0.0088 0.0037  -0.0592 649  LEU A CB    
4027 C  CG    . LEU A 546 ? 1.0555 1.3904 1.0390 -0.0106 -0.0040 -0.0575 649  LEU A CG    
4028 C  CD1   . LEU A 546 ? 0.9582 1.2935 0.9507 -0.0200 -0.0045 -0.0538 649  LEU A CD1   
4029 C  CD2   . LEU A 546 ? 1.0409 1.3588 1.0085 -0.0119 -0.0049 -0.0537 649  LEU A CD2   
4030 N  N     . VAL A 547 ? 0.9057 1.2781 0.9074 0.0157  -0.0008 -0.0738 650  VAL A N     
4031 C  CA    . VAL A 547 ? 0.8800 1.2432 0.8847 0.0256  -0.0065 -0.0792 650  VAL A CA    
4032 C  C     . VAL A 547 ? 0.8725 1.2525 0.8928 0.0299  -0.0060 -0.0802 650  VAL A C     
4033 O  O     . VAL A 547 ? 0.8733 1.2447 0.8990 0.0344  -0.0115 -0.0818 650  VAL A O     
4034 C  CB    . VAL A 547 ? 0.7327 1.0890 0.7251 0.0355  -0.0056 -0.0855 650  VAL A CB    
4035 C  CG1   . VAL A 547 ? 0.8647 1.2417 0.8586 0.0427  0.0025  -0.0883 650  VAL A CG1   
4036 C  CG2   . VAL A 547 ? 0.7033 1.0423 0.6957 0.0428  -0.0124 -0.0907 650  VAL A CG2   
4037 N  N     . ARG A 548 ? 0.7888 1.1939 0.8169 0.0286  0.0005  -0.0787 651  ARG A N     
4038 C  CA    . ARG A 548 ? 0.8259 1.2507 0.8701 0.0325  0.0002  -0.0789 651  ARG A CA    
4039 C  C     . ARG A 548 ? 0.8902 1.3153 0.9431 0.0217  -0.0044 -0.0745 651  ARG A C     
4040 O  O     . ARG A 548 ? 0.8531 1.2859 0.9167 0.0255  -0.0082 -0.0749 651  ARG A O     
4041 C  CB    . ARG A 548 ? 0.8140 1.2690 0.8655 0.0344  0.0087  -0.0785 651  ARG A CB    
4042 C  CG    . ARG A 548 ? 0.8995 1.3559 0.9427 0.0479  0.0140  -0.0837 651  ARG A CG    
4043 C  CD    . ARG A 548 ? 0.9183 1.4069 0.9698 0.0499  0.0235  -0.0825 651  ARG A CD    
4044 N  NE    . ARG A 548 ? 0.9499 1.4388 0.9918 0.0641  0.0293  -0.0878 651  ARG A NE    
4045 C  CZ    . ARG A 548 ? 0.9515 1.4487 0.9987 0.0796  0.0307  -0.0919 651  ARG A CZ    
4046 N  NH1   . ARG A 548 ? 0.9763 1.4840 1.0389 0.0834  0.0264  -0.0908 651  ARG A NH1   
4047 N  NH2   . ARG A 548 ? 1.1018 1.5957 1.1370 0.0922  0.0365  -0.0971 651  ARG A NH2   
4048 N  N     . PHE A 549 ? 0.8829 1.2986 0.9298 0.0089  -0.0042 -0.0703 652  PHE A N     
4049 C  CA    . PHE A 549 ? 0.8131 1.2249 0.8650 -0.0016 -0.0084 -0.0668 652  PHE A CA    
4050 C  C     . PHE A 549 ? 0.9206 1.3087 0.9690 0.0023  -0.0158 -0.0676 652  PHE A C     
4051 O  O     . PHE A 549 ? 0.9196 1.3089 0.9754 0.0019  -0.0202 -0.0672 652  PHE A O     
4052 C  CB    . PHE A 549 ? 0.8587 1.2649 0.9033 -0.0156 -0.0048 -0.0620 652  PHE A CB    
4053 C  CG    . PHE A 549 ? 0.8757 1.2680 0.9196 -0.0257 -0.0091 -0.0590 652  PHE A CG    
4054 C  CD1   . PHE A 549 ? 0.8898 1.2967 0.9444 -0.0332 -0.0105 -0.0583 652  PHE A CD1   
4055 C  CD2   . PHE A 549 ? 0.8920 1.2573 0.9240 -0.0274 -0.0117 -0.0569 652  PHE A CD2   
4056 C  CE1   . PHE A 549 ? 0.8876 1.2798 0.9392 -0.0424 -0.0142 -0.0562 652  PHE A CE1   
4057 C  CE2   . PHE A 549 ? 0.9122 1.2637 0.9422 -0.0355 -0.0148 -0.0542 652  PHE A CE2   
4058 C  CZ    . PHE A 549 ? 0.9505 1.3140 0.9893 -0.0431 -0.0159 -0.0542 652  PHE A CZ    
4059 N  N     . LEU A 550 ? 0.9022 1.2695 0.9394 0.0059  -0.0172 -0.0687 653  LEU A N     
4060 C  CA    . LEU A 550 ? 0.8436 1.1896 0.8785 0.0090  -0.0235 -0.0691 653  LEU A CA    
4061 C  C     . LEU A 550 ? 0.8333 1.1811 0.8748 0.0204  -0.0264 -0.0729 653  LEU A C     
4062 O  O     . LEU A 550 ? 0.8714 1.2100 0.9162 0.0215  -0.0309 -0.0720 653  LEU A O     
4063 C  CB    . LEU A 550 ? 0.9183 1.2454 0.9411 0.0097  -0.0247 -0.0693 653  LEU A CB    
4064 C  CG    . LEU A 550 ? 0.9712 1.2927 0.9853 0.0001  -0.0221 -0.0645 653  LEU A CG    
4065 C  CD1   . LEU A 550 ? 0.8603 1.1654 0.8632 0.0027  -0.0246 -0.0648 653  LEU A CD1   
4066 C  CD2   . LEU A 550 ? 0.9537 1.2687 0.9703 -0.0086 -0.0236 -0.0599 653  LEU A CD2   
4067 N  N     . LEU A 551 ? 0.8650 1.2232 0.9071 0.0295  -0.0232 -0.0769 654  LEU A N     
4068 C  CA    . LEU A 551 ? 0.8347 1.1916 0.8810 0.0416  -0.0252 -0.0804 654  LEU A CA    
4069 C  C     . LEU A 551 ? 0.9555 1.3291 1.0141 0.0428  -0.0266 -0.0783 654  LEU A C     
4070 O  O     . LEU A 551 ? 0.9071 1.2723 0.9683 0.0487  -0.0307 -0.0783 654  LEU A O     
4071 C  CB    . LEU A 551 ? 0.7026 1.0658 0.7449 0.0519  -0.0207 -0.0854 654  LEU A CB    
4072 C  CG    . LEU A 551 ? 0.7342 1.0910 0.7776 0.0659  -0.0219 -0.0895 654  LEU A CG    
4073 C  CD1   . LEU A 551 ? 0.8430 1.1711 0.8797 0.0664  -0.0273 -0.0909 654  LEU A CD1   
4074 C  CD2   . LEU A 551 ? 0.7833 1.1473 0.8217 0.0763  -0.0162 -0.0946 654  LEU A CD2   
4075 N  N     . LYS A 552 ? 0.8726 1.2706 0.9388 0.0370  -0.0234 -0.0763 655  LYS A N     
4076 C  CA    . LYS A 552 ? 0.9102 1.3273 0.9886 0.0372  -0.0257 -0.0745 655  LYS A CA    
4077 C  C     . LYS A 552 ? 0.8479 1.2514 0.9254 0.0295  -0.0315 -0.0716 655  LYS A C     
4078 O  O     . LYS A 552 ? 0.8099 1.2167 0.8928 0.0344  -0.0357 -0.0709 655  LYS A O     
4079 C  CB    . LYS A 552 ? 0.8125 1.2598 0.9000 0.0302  -0.0211 -0.0730 655  LYS A CB    
4080 C  CG    . LYS A 552 ? 0.8305 1.2989 0.9307 0.0261  -0.0248 -0.0709 655  LYS A CG    
4081 C  CD    . LYS A 552 ? 0.7809 1.2834 0.8929 0.0200  -0.0201 -0.0699 655  LYS A CD    
4082 C  CE    . LYS A 552 ? 0.8924 1.4196 1.0144 0.0353  -0.0170 -0.0717 655  LYS A CE    
4083 N  NZ    . LYS A 552 ? 0.8522 1.4180 0.9896 0.0292  -0.0132 -0.0699 655  LYS A NZ    
4084 N  N     . LYS A 553 ? 0.8784 1.2661 0.9480 0.0184  -0.0316 -0.0695 656  LYS A N     
4085 C  CA    . LYS A 553 ? 0.8361 1.2087 0.9030 0.0120  -0.0362 -0.0669 656  LYS A CA    
4086 C  C     . LYS A 553 ? 0.8063 1.1575 0.8693 0.0208  -0.0399 -0.0675 656  LYS A C     
4087 O  O     . LYS A 553 ? 0.8794 1.2257 0.9438 0.0219  -0.0438 -0.0660 656  LYS A O     
4088 C  CB    . LYS A 553 ? 0.8357 1.1957 0.8943 -0.0004 -0.0344 -0.0643 656  LYS A CB    
4089 C  CG    . LYS A 553 ? 0.8941 1.2707 0.9563 -0.0127 -0.0319 -0.0627 656  LYS A CG    
4090 C  CD    . LYS A 553 ? 0.9757 1.3566 1.0422 -0.0178 -0.0366 -0.0620 656  LYS A CD    
4091 C  CE    . LYS A 553 ? 1.0891 1.4963 1.1644 -0.0276 -0.0351 -0.0619 656  LYS A CE    
4092 N  NZ    . LYS A 553 ? 1.2188 1.6548 1.3068 -0.0187 -0.0338 -0.0638 656  LYS A NZ    
4093 N  N     . ALA A 554 ? 0.8407 1.1790 0.8981 0.0266  -0.0387 -0.0696 657  ALA A N     
4094 C  CA    . ALA A 554 ? 0.8328 1.1510 0.8873 0.0337  -0.0417 -0.0702 657  ALA A CA    
4095 C  C     . ALA A 554 ? 0.8557 1.1799 0.9158 0.0449  -0.0432 -0.0713 657  ALA A C     
4096 O  O     . ALA A 554 ? 0.8562 1.1660 0.9153 0.0489  -0.0460 -0.0700 657  ALA A O     
4097 C  CB    . ALA A 554 ? 0.7511 1.0562 0.7987 0.0365  -0.0406 -0.0732 657  ALA A CB    
4098 N  N     . LEU A 555 ? 0.8384 1.1841 0.9044 0.0505  -0.0408 -0.0732 658  LEU A N     
4099 C  CA    . LEU A 555 ? 0.8344 1.1878 0.9056 0.0630  -0.0418 -0.0736 658  LEU A CA    
4100 C  C     . LEU A 555 ? 0.8505 1.2216 0.9294 0.0609  -0.0450 -0.0704 658  LEU A C     
4101 O  O     . LEU A 555 ? 0.9589 1.3397 1.0426 0.0717  -0.0463 -0.0700 658  LEU A O     
4102 C  CB    . LEU A 555 ? 0.9128 1.2812 0.9864 0.0725  -0.0372 -0.0773 658  LEU A CB    
4103 C  CG    . LEU A 555 ? 0.9447 1.2950 1.0089 0.0779  -0.0345 -0.0818 658  LEU A CG    
4104 C  CD1   . LEU A 555 ? 0.9144 1.2816 0.9801 0.0876  -0.0291 -0.0853 658  LEU A CD1   
4105 C  CD2   . LEU A 555 ? 0.9472 1.2715 1.0060 0.0853  -0.0373 -0.0825 658  LEU A CD2   
4106 N  N     . THR A 556 ? 0.8139 1.1891 0.8932 0.0475  -0.0464 -0.0683 659  THR A N     
4107 C  CA    . THR A 556 ? 0.8461 1.2345 0.9303 0.0436  -0.0505 -0.0660 659  THR A CA    
4108 C  C     . THR A 556 ? 0.8533 1.2204 0.9297 0.0357  -0.0536 -0.0636 659  THR A C     
4109 O  O     . THR A 556 ? 0.8333 1.2079 0.9105 0.0289  -0.0569 -0.0623 659  THR A O     
4110 C  CB    . THR A 556 ? 0.7455 1.1619 0.8378 0.0341  -0.0492 -0.0662 659  THR A CB    
4111 O  OG1   . THR A 556 ? 0.7072 1.1148 0.7939 0.0214  -0.0459 -0.0661 659  THR A OG1   
4112 C  CG2   . THR A 556 ? 0.8094 1.2508 0.9111 0.0436  -0.0456 -0.0680 659  THR A CG2   
4113 N  N     . ASN A 557 ? 0.8012 1.1425 0.8698 0.0366  -0.0526 -0.0632 660  ASN A N     
4114 C  CA    . ASN A 557 ? 0.8346 1.1557 0.8960 0.0303  -0.0544 -0.0606 660  ASN A CA    
4115 C  C     . ASN A 557 ? 0.8393 1.1372 0.8961 0.0360  -0.0535 -0.0603 660  ASN A C     
4116 O  O     . ASN A 557 ? 0.9029 1.1937 0.9575 0.0336  -0.0512 -0.0616 660  ASN A O     
4117 C  CB    . ASN A 557 ? 0.7991 1.1187 0.8567 0.0168  -0.0527 -0.0601 660  ASN A CB    
4118 C  CG    . ASN A 557 ? 0.8522 1.1523 0.9018 0.0111  -0.0540 -0.0573 660  ASN A CG    
4119 O  OD1   . ASN A 557 ? 0.8129 1.0952 0.8590 0.0162  -0.0544 -0.0557 660  ASN A OD1   
4120 N  ND2   . ASN A 557 ? 0.7537 1.0566 0.8001 0.0003  -0.0542 -0.0569 660  ASN A ND2   
4121 N  N     . GLN A 558 ? 0.7936 1.0803 0.8489 0.0430  -0.0554 -0.0583 661  GLN A N     
4122 C  CA    . GLN A 558 ? 0.8135 1.0792 0.8659 0.0476  -0.0544 -0.0580 661  GLN A CA    
4123 C  C     . GLN A 558 ? 0.7881 1.0384 0.8364 0.0393  -0.0536 -0.0561 661  GLN A C     
4124 O  O     . GLN A 558 ? 0.8353 1.0735 0.8828 0.0399  -0.0527 -0.0569 661  GLN A O     
4125 C  CB    . GLN A 558 ? 0.9426 1.1993 0.9939 0.0564  -0.0558 -0.0553 661  GLN A CB    
4126 C  CG    . GLN A 558 ? 0.9423 1.2035 0.9961 0.0684  -0.0554 -0.0572 661  GLN A CG    
4127 C  CD    . GLN A 558 ? 1.0310 1.2756 1.0815 0.0771  -0.0557 -0.0540 661  GLN A CD    
4128 O  OE1   . GLN A 558 ? 1.1725 1.4022 1.2193 0.0737  -0.0558 -0.0504 661  GLN A OE1   
4129 N  NE2   . GLN A 558 ? 0.9697 1.2160 1.0208 0.0890  -0.0551 -0.0550 661  GLN A NE2   
4130 N  N     . ARG A 559 ? 0.7900 1.0404 0.8351 0.0318  -0.0540 -0.0537 662  ARG A N     
4131 C  CA    . ARG A 559 ? 0.8780 1.1148 0.9190 0.0252  -0.0526 -0.0516 662  ARG A CA    
4132 C  C     . ARG A 559 ? 0.9138 1.1547 0.9547 0.0206  -0.0510 -0.0536 662  ARG A C     
4133 O  O     . ARG A 559 ? 0.9151 1.1453 0.9542 0.0190  -0.0503 -0.0526 662  ARG A O     
4134 C  CB    . ARG A 559 ? 0.8544 1.0881 0.8899 0.0191  -0.0528 -0.0491 662  ARG A CB    
4135 C  CG    . ARG A 559 ? 0.8487 1.0658 0.8793 0.0154  -0.0508 -0.0458 662  ARG A CG    
4136 C  CD    . ARG A 559 ? 1.0108 1.2235 1.0335 0.0089  -0.0502 -0.0443 662  ARG A CD    
4137 N  NE    . ARG A 559 ? 1.2105 1.4330 1.2317 0.0011  -0.0498 -0.0464 662  ARG A NE    
4138 C  CZ    . ARG A 559 ? 1.3256 1.5615 1.3472 -0.0027 -0.0517 -0.0487 662  ARG A CZ    
4139 N  NH1   . ARG A 559 ? 1.0320 1.2733 1.0546 0.0015  -0.0548 -0.0491 662  ARG A NH1   
4140 N  NH2   . ARG A 559 ? 1.0477 1.2924 1.0689 -0.0110 -0.0506 -0.0502 662  ARG A NH2   
4141 N  N     . ILE A 560 ? 1.0060 1.2634 1.0487 0.0185  -0.0504 -0.0561 663  ILE A N     
4142 C  CA    . ILE A 560 ? 0.8459 1.1080 0.8875 0.0155  -0.0482 -0.0580 663  ILE A CA    
4143 C  C     . ILE A 560 ? 0.8212 1.0808 0.8643 0.0230  -0.0484 -0.0613 663  ILE A C     
4144 O  O     . ILE A 560 ? 0.8798 1.1320 0.9196 0.0218  -0.0481 -0.0620 663  ILE A O     
4145 C  CB    . ILE A 560 ? 0.8510 1.1328 0.8948 0.0109  -0.0466 -0.0593 663  ILE A CB    
4146 C  CG1   . ILE A 560 ? 0.8584 1.1393 0.8988 0.0011  -0.0464 -0.0567 663  ILE A CG1   
4147 C  CG2   . ILE A 560 ? 0.8240 1.1111 0.8658 0.0094  -0.0435 -0.0611 663  ILE A CG2   
4148 C  CD1   . ILE A 560 ? 0.9994 1.2656 1.0318 -0.0055 -0.0444 -0.0541 663  ILE A CD1   
4149 N  N     . GLY A 561 ? 0.7551 1.0200 0.8022 0.0312  -0.0490 -0.0634 664  GLY A N     
4150 C  CA    . GLY A 561 ? 0.8322 1.0925 0.8790 0.0386  -0.0487 -0.0672 664  GLY A CA    
4151 C  C     . GLY A 561 ? 0.8958 1.1359 0.9404 0.0391  -0.0503 -0.0668 664  GLY A C     
4152 O  O     . GLY A 561 ? 0.9912 1.2249 1.0332 0.0411  -0.0505 -0.0705 664  GLY A O     
4153 N  N     . HIS A 562 ? 0.8890 1.1194 0.9344 0.0369  -0.0514 -0.0625 665  HIS A N     
4154 C  CA    . HIS A 562 ? 0.9124 1.1259 0.9578 0.0366  -0.0525 -0.0613 665  HIS A CA    
4155 C  C     . HIS A 562 ? 0.8516 1.0625 0.8950 0.0306  -0.0532 -0.0619 665  HIS A C     
4156 O  O     . HIS A 562 ? 0.7654 0.9699 0.8082 0.0313  -0.0545 -0.0651 665  HIS A O     
4157 C  CB    . HIS A 562 ? 0.7702 0.9759 0.8166 0.0356  -0.0525 -0.0559 665  HIS A CB    
4158 C  CG    . HIS A 562 ? 0.7556 0.9473 0.8036 0.0332  -0.0528 -0.0534 665  HIS A CG    
4159 N  ND1   . HIS A 562 ? 0.7641 0.9446 0.8143 0.0365  -0.0531 -0.0543 665  HIS A ND1   
4160 C  CD2   . HIS A 562 ? 0.7454 0.9335 0.7938 0.0279  -0.0525 -0.0499 665  HIS A CD2   
4161 C  CE1   . HIS A 562 ? 0.8043 0.9768 0.8575 0.0322  -0.0533 -0.0515 665  HIS A CE1   
4162 N  NE2   . HIS A 562 ? 0.7709 0.9487 0.8234 0.0278  -0.0529 -0.0486 665  HIS A NE2   
4163 N  N     . PHE A 563 ? 0.8623 1.0775 0.9038 0.0248  -0.0524 -0.0587 666  PHE A N     
4164 C  CA    . PHE A 563 ? 0.8738 1.0873 0.9125 0.0203  -0.0531 -0.0582 666  PHE A CA    
4165 C  C     . PHE A 563 ? 0.9633 1.1852 0.9977 0.0205  -0.0527 -0.0627 666  PHE A C     
4166 O  O     . PHE A 563 ? 1.0138 1.2333 1.0449 0.0187  -0.0543 -0.0637 666  PHE A O     
4167 C  CB    . PHE A 563 ? 0.8243 1.0371 0.8602 0.0151  -0.0516 -0.0530 666  PHE A CB    
4168 C  CG    . PHE A 563 ? 0.8752 1.0784 0.9136 0.0154  -0.0513 -0.0485 666  PHE A CG    
4169 C  CD1   . PHE A 563 ? 0.8719 1.0676 0.9129 0.0149  -0.0522 -0.0456 666  PHE A CD1   
4170 C  CD2   . PHE A 563 ? 0.8822 1.0852 0.9202 0.0163  -0.0502 -0.0471 666  PHE A CD2   
4171 C  CE1   . PHE A 563 ? 0.7658 0.9538 0.8093 0.0157  -0.0509 -0.0411 666  PHE A CE1   
4172 C  CE2   . PHE A 563 ? 0.8987 1.0924 0.9372 0.0171  -0.0493 -0.0429 666  PHE A CE2   
4173 C  CZ    . PHE A 563 ? 1.0517 1.2376 1.0930 0.0170  -0.0491 -0.0398 666  PHE A CZ    
4174 N  N     . PHE A 564 ? 0.9038 1.1367 0.9381 0.0229  -0.0507 -0.0652 667  PHE A N     
4175 C  CA    . PHE A 564 ? 0.8354 1.0765 0.8655 0.0248  -0.0494 -0.0698 667  PHE A CA    
4176 C  C     . PHE A 564 ? 0.8434 1.0754 0.8716 0.0294  -0.0516 -0.0750 667  PHE A C     
4177 O  O     . PHE A 564 ? 0.8904 1.1213 0.9125 0.0283  -0.0525 -0.0778 667  PHE A O     
4178 C  CB    . PHE A 564 ? 0.8149 1.0711 0.8478 0.0279  -0.0464 -0.0713 667  PHE A CB    
4179 C  CG    . PHE A 564 ? 0.8321 1.0991 0.8610 0.0302  -0.0436 -0.0754 667  PHE A CG    
4180 C  CD1   . PHE A 564 ? 0.8611 1.1349 0.8849 0.0242  -0.0411 -0.0738 667  PHE A CD1   
4181 C  CD2   . PHE A 564 ? 0.8087 1.0783 0.8378 0.0390  -0.0425 -0.0805 667  PHE A CD2   
4182 C  CE1   . PHE A 564 ? 0.8550 1.1391 0.8742 0.0265  -0.0376 -0.0771 667  PHE A CE1   
4183 C  CE2   . PHE A 564 ? 0.8327 1.1125 0.8573 0.0420  -0.0390 -0.0843 667  PHE A CE2   
4184 C  CZ    . PHE A 564 ? 0.8634 1.1511 0.8831 0.0356  -0.0364 -0.0825 667  PHE A CZ    
4185 N  N     . PHE A 565 ? 0.8574 1.0816 0.8896 0.0344  -0.0525 -0.0762 668  PHE A N     
4186 C  CA    . PHE A 565 ? 0.8507 1.0628 0.8803 0.0379  -0.0544 -0.0814 668  PHE A CA    
4187 C  C     . PHE A 565 ? 0.8961 1.0990 0.9249 0.0319  -0.0582 -0.0809 668  PHE A C     
4188 O  O     . PHE A 565 ? 1.0049 1.2035 1.0281 0.0315  -0.0604 -0.0861 668  PHE A O     
4189 C  CB    . PHE A 565 ? 0.8816 1.0845 0.9152 0.0438  -0.0541 -0.0811 668  PHE A CB    
4190 C  CG    . PHE A 565 ? 0.8826 1.0682 0.9137 0.0455  -0.0560 -0.0855 668  PHE A CG    
4191 C  CD1   . PHE A 565 ? 0.9017 1.0755 0.9365 0.0398  -0.0587 -0.0830 668  PHE A CD1   
4192 C  CD2   . PHE A 565 ? 0.9085 1.0891 0.9336 0.0526  -0.0547 -0.0920 668  PHE A CD2   
4193 C  CE1   . PHE A 565 ? 0.9339 1.0917 0.9670 0.0395  -0.0606 -0.0872 668  PHE A CE1   
4194 C  CE2   . PHE A 565 ? 0.9392 1.1009 0.9606 0.0532  -0.0564 -0.0966 668  PHE A CE2   
4195 C  CZ    . PHE A 565 ? 0.8963 1.0465 0.9219 0.0458  -0.0596 -0.0943 668  PHE A CZ    
4196 N  N     . TRP A 566 ? 0.8045 1.0051 0.8387 0.0274  -0.0591 -0.0748 669  TRP A N     
4197 C  CA    . TRP A 566 ? 0.9514 1.1451 0.9877 0.0226  -0.0628 -0.0737 669  TRP A CA    
4198 C  C     . TRP A 566 ? 0.8957 1.0963 0.9266 0.0189  -0.0647 -0.0737 669  TRP A C     
4199 O  O     . TRP A 566 ? 1.0282 1.2259 1.0580 0.0164  -0.0689 -0.0762 669  TRP A O     
4200 C  CB    . TRP A 566 ? 0.9458 1.1356 0.9896 0.0203  -0.0622 -0.0667 669  TRP A CB    
4201 C  CG    . TRP A 566 ? 0.8916 1.0706 0.9403 0.0227  -0.0618 -0.0666 669  TRP A CG    
4202 C  CD1   . TRP A 566 ? 0.9187 1.0954 0.9691 0.0266  -0.0589 -0.0636 669  TRP A CD1   
4203 C  CD2   . TRP A 566 ? 0.9152 1.0833 0.9665 0.0211  -0.0642 -0.0697 669  TRP A CD2   
4204 N  NE1   . TRP A 566 ? 1.0148 1.1790 1.0682 0.0283  -0.0588 -0.0638 669  TRP A NE1   
4205 C  CE2   . TRP A 566 ? 0.9108 1.0689 0.9651 0.0244  -0.0618 -0.0676 669  TRP A CE2   
4206 C  CE3   . TRP A 566 ? 0.9338 1.0995 0.9846 0.0166  -0.0685 -0.0739 669  TRP A CE3   
4207 C  CZ2   . TRP A 566 ? 0.9397 1.0839 0.9966 0.0229  -0.0627 -0.0694 669  TRP A CZ2   
4208 C  CZ3   . TRP A 566 ? 0.9692 1.1221 1.0233 0.0143  -0.0701 -0.0765 669  TRP A CZ3   
4209 C  CH2   . TRP A 566 ? 0.9696 1.1113 1.0268 0.0172  -0.0668 -0.0740 669  TRP A CH2   
4210 N  N     . HIS A 567 ? 0.8853 1.0951 0.9123 0.0183  -0.0618 -0.0709 670  HIS A N     
4211 C  CA    . HIS A 567 ? 0.9050 1.1202 0.9247 0.0158  -0.0628 -0.0705 670  HIS A CA    
4212 C  C     . HIS A 567 ? 0.9351 1.1516 0.9466 0.0181  -0.0642 -0.0779 670  HIS A C     
4213 O  O     . HIS A 567 ? 0.9138 1.1304 0.9195 0.0163  -0.0679 -0.0794 670  HIS A O     
4214 C  CB    . HIS A 567 ? 0.9192 1.1418 0.9353 0.0142  -0.0583 -0.0660 670  HIS A CB    
4215 C  CG    . HIS A 567 ? 0.9739 1.1930 0.9944 0.0116  -0.0571 -0.0590 670  HIS A CG    
4216 N  ND1   . HIS A 567 ? 0.9549 1.1671 0.9814 0.0112  -0.0596 -0.0559 670  HIS A ND1   
4217 C  CD2   . HIS A 567 ? 0.9415 1.1625 0.9603 0.0092  -0.0534 -0.0549 670  HIS A CD2   
4218 C  CE1   . HIS A 567 ? 0.9686 1.1780 0.9961 0.0098  -0.0571 -0.0501 670  HIS A CE1   
4219 N  NE2   . HIS A 567 ? 0.9408 1.1544 0.9631 0.0082  -0.0535 -0.0497 670  HIS A NE2   
4220 N  N     . LEU A 568 ? 0.9037 1.1211 0.9139 0.0228  -0.0613 -0.0828 671  LEU A N     
4221 C  CA    . LEU A 568 ? 0.9057 1.1224 0.9067 0.0262  -0.0617 -0.0905 671  LEU A CA    
4222 C  C     . LEU A 568 ? 0.9573 1.1610 0.9580 0.0257  -0.0669 -0.0959 671  LEU A C     
4223 O  O     . LEU A 568 ? 1.0022 1.2035 0.9940 0.0247  -0.0704 -0.1012 671  LEU A O     
4224 C  CB    . LEU A 568 ? 0.9013 1.1236 0.9018 0.0327  -0.0565 -0.0936 671  LEU A CB    
4225 C  CG    . LEU A 568 ? 0.9021 1.1397 0.9036 0.0320  -0.0513 -0.0891 671  LEU A CG    
4226 C  CD1   . LEU A 568 ? 0.8409 1.0867 0.8451 0.0389  -0.0467 -0.0919 671  LEU A CD1   
4227 C  CD2   . LEU A 568 ? 0.8149 1.0591 0.8062 0.0292  -0.0500 -0.0889 671  LEU A CD2   
4228 N  N     . LYS A 569 ? 0.9495 1.1440 0.9590 0.0259  -0.0676 -0.0948 672  LYS A N     
4229 C  CA    . LYS A 569 ? 0.9501 1.1309 0.9601 0.0239  -0.0720 -0.0996 672  LYS A CA    
4230 C  C     . LYS A 569 ? 0.9225 1.1048 0.9346 0.0165  -0.0781 -0.0979 672  LYS A C     
4231 O  O     . LYS A 569 ? 0.9294 1.1044 0.9380 0.0134  -0.0831 -0.1039 672  LYS A O     
4232 C  CB    . LYS A 569 ? 0.9652 1.1359 0.9842 0.0253  -0.0704 -0.0971 672  LYS A CB    
4233 C  CG    . LYS A 569 ? 0.9430 1.0971 0.9627 0.0225  -0.0739 -0.1019 672  LYS A CG    
4234 C  CD    . LYS A 569 ? 0.9846 1.1288 0.9921 0.0272  -0.0736 -0.1117 672  LYS A CD    
4235 C  CE    . LYS A 569 ? 1.0241 1.1492 1.0305 0.0226  -0.0774 -0.1172 672  LYS A CE    
4236 N  NZ    . LYS A 569 ? 0.9710 1.0840 0.9860 0.0231  -0.0750 -0.1128 672  LYS A NZ    
4237 N  N     . SER A 570 ? 0.9289 1.1205 0.9462 0.0139  -0.0778 -0.0900 673  SER A N     
4238 C  CA    . SER A 570 ? 0.9954 1.1908 1.0160 0.0084  -0.0834 -0.0872 673  SER A CA    
4239 C  C     . SER A 570 ? 0.9733 1.1732 0.9818 0.0076  -0.0877 -0.0923 673  SER A C     
4240 O  O     . SER A 570 ? 0.9863 1.1859 0.9954 0.0033  -0.0944 -0.0949 673  SER A O     
4241 C  CB    . SER A 570 ? 0.9155 1.1185 0.9420 0.0078  -0.0811 -0.0775 673  SER A CB    
4242 O  OG    . SER A 570 ? 0.8102 1.0198 0.8283 0.0103  -0.0770 -0.0755 673  SER A OG    
4243 N  N     . GLU A 571 ? 0.9871 1.1919 0.9845 0.0116  -0.0839 -0.0936 674  GLU A N     
4244 C  CA    . GLU A 571 ? 1.0490 1.2580 1.0325 0.0118  -0.0869 -0.0978 674  GLU A CA    
4245 C  C     . GLU A 571 ? 1.1031 1.3037 1.0761 0.0142  -0.0877 -0.1088 674  GLU A C     
4246 O  O     . GLU A 571 ? 1.0697 1.2730 1.0283 0.0157  -0.0890 -0.1133 674  GLU A O     
4247 C  CB    . GLU A 571 ? 1.0036 1.2220 0.9795 0.0144  -0.0813 -0.0929 674  GLU A CB    
4248 C  CG    . GLU A 571 ? 0.9650 1.1885 0.9478 0.0124  -0.0799 -0.0826 674  GLU A CG    
4249 C  CD    . GLU A 571 ? 1.1307 1.3609 1.1021 0.0125  -0.0799 -0.0783 674  GLU A CD    
4250 O  OE1   . GLU A 571 ? 1.2183 1.4502 1.1773 0.0135  -0.0827 -0.0833 674  GLU A OE1   
4251 O  OE2   . GLU A 571 ? 1.1939 1.4262 1.1673 0.0118  -0.0768 -0.0699 674  GLU A OE2   
4252 N  N     . MET A 572 ? 1.0416 1.2308 1.0199 0.0153  -0.0867 -0.1130 675  MET A N     
4253 C  CA    . MET A 572 ? 1.0621 1.2401 1.0293 0.0188  -0.0865 -0.1235 675  MET A CA    
4254 C  C     . MET A 572 ? 1.1824 1.3538 1.1413 0.0135  -0.0949 -0.1310 675  MET A C     
4255 O  O     . MET A 572 ? 1.1770 1.3403 1.1208 0.0164  -0.0953 -0.1404 675  MET A O     
4256 C  CB    . MET A 572 ? 1.0186 1.1839 0.9932 0.0218  -0.0831 -0.1249 675  MET A CB    
4257 C  CG    . MET A 572 ? 1.0544 1.2079 1.0169 0.0290  -0.0798 -0.1342 675  MET A CG    
4258 S  SD    . MET A 572 ? 1.0562 1.2237 1.0093 0.0386  -0.0716 -0.1344 675  MET A SD    
4259 C  CE    . MET A 572 ? 1.0396 1.2236 1.0086 0.0378  -0.0674 -0.1221 675  MET A CE    
4260 N  N     . HIS A 573 ? 1.2021 1.3774 1.1703 0.0059  -0.1018 -0.1273 676  HIS A N     
4261 C  CA    . HIS A 573 ? 1.1801 1.3529 1.1414 -0.0003 -0.1110 -0.1342 676  HIS A CA    
4262 C  C     . HIS A 573 ? 1.1583 1.3408 1.1030 0.0020  -0.1133 -0.1360 676  HIS A C     
4263 O  O     . HIS A 573 ? 1.2121 1.3891 1.1425 0.0003  -0.1188 -0.1454 676  HIS A O     
4264 C  CB    . HIS A 573 ? 1.1999 1.3793 1.1778 -0.0086 -0.1175 -0.1284 676  HIS A CB    
4265 C  CG    . HIS A 573 ? 1.1933 1.3901 1.1776 -0.0076 -0.1173 -0.1175 676  HIS A CG    
4266 N  ND1   . HIS A 573 ? 1.0377 1.2385 1.0326 -0.0044 -0.1104 -0.1080 676  HIS A ND1   
4267 C  CD2   . HIS A 573 ? 1.2863 1.4963 1.2663 -0.0089 -0.1232 -0.1146 676  HIS A CD2   
4268 C  CE1   . HIS A 573 ? 1.0482 1.2620 1.0449 -0.0039 -0.1114 -0.0999 676  HIS A CE1   
4269 N  NE2   . HIS A 573 ? 1.2739 1.4939 1.2620 -0.0061 -0.1190 -0.1032 676  HIS A NE2   
4270 N  N     . ASN A 574 ? 1.1478 1.3435 1.0929 0.0057  -0.1089 -0.1272 677  ASN A N     
4271 C  CA    . ASN A 574 ? 1.1652 1.3699 1.0940 0.0083  -0.1096 -0.1270 677  ASN A CA    
4272 C  C     . ASN A 574 ? 1.1742 1.3721 1.0853 0.0145  -0.1044 -0.1356 677  ASN A C     
4273 O  O     . ASN A 574 ? 1.1756 1.3742 1.0879 0.0200  -0.0951 -0.1336 677  ASN A O     
4274 C  CB    . ASN A 574 ? 1.1561 1.3727 1.0898 0.0105  -0.1045 -0.1149 677  ASN A CB    
4275 C  CG    . ASN A 574 ? 1.1465 1.3716 1.0634 0.0129  -0.1050 -0.1128 677  ASN A CG    
4276 O  OD1   . ASN A 574 ? 1.2998 1.5239 1.2019 0.0127  -0.1107 -0.1198 677  ASN A OD1   
4277 N  ND2   . ASN A 574 ? 1.0274 1.2598 0.9453 0.0149  -0.0989 -0.1029 677  ASN A ND2   
4278 N  N     . LYS A 575 ? 1.1986 1.3907 1.0931 0.0136  -0.1102 -0.1453 678  LYS A N     
4279 C  CA    . LYS A 575 ? 1.2253 1.4094 1.1011 0.0203  -0.1050 -0.1545 678  LYS A CA    
4280 C  C     . LYS A 575 ? 1.2106 1.4068 1.0751 0.0265  -0.0975 -0.1495 678  LYS A C     
4281 O  O     . LYS A 575 ? 1.2591 1.4522 1.1115 0.0335  -0.0902 -0.1548 678  LYS A O     
4282 C  CB    . LYS A 575 ? 1.2326 1.4060 1.0913 0.0172  -0.1137 -0.1668 678  LYS A CB    
4283 C  CG    . LYS A 575 ? 1.2076 1.3652 1.0750 0.0108  -0.1196 -0.1737 678  LYS A CG    
4284 C  CD    . LYS A 575 ? 1.3546 1.4994 1.2288 0.0162  -0.1106 -0.1752 678  LYS A CD    
4285 C  CE    . LYS A 575 ? 1.3855 1.5148 1.2717 0.0091  -0.1152 -0.1785 678  LYS A CE    
4286 N  NZ    . LYS A 575 ? 1.2984 1.4168 1.1927 0.0154  -0.1062 -0.1773 678  LYS A NZ    
4287 N  N     . THR A 576 ? 1.1960 1.4054 1.0640 0.0243  -0.0985 -0.1393 679  THR A N     
4288 C  CA    . THR A 576 ? 1.1969 1.4165 1.0553 0.0290  -0.0903 -0.1331 679  THR A CA    
4289 C  C     . THR A 576 ? 1.2685 1.4910 1.1376 0.0328  -0.0791 -0.1295 679  THR A C     
4290 O  O     . THR A 576 ? 1.3153 1.5432 1.1747 0.0379  -0.0706 -0.1297 679  THR A O     
4291 C  CB    . THR A 576 ? 1.1952 1.4250 1.0561 0.0258  -0.0934 -0.1219 679  THR A CB    
4292 O  OG1   . THR A 576 ? 1.2697 1.5001 1.1187 0.0236  -0.1040 -0.1253 679  THR A OG1   
4293 C  CG2   . THR A 576 ? 1.1981 1.4363 1.0505 0.0293  -0.0838 -0.1143 679  THR A CG2   
4294 N  N     . VAL A 577 ? 1.2054 1.4255 1.0943 0.0303  -0.0790 -0.1261 680  VAL A N     
4295 C  CA    . VAL A 577 ? 1.1167 1.3411 1.0172 0.0333  -0.0700 -0.1222 680  VAL A CA    
4296 C  C     . VAL A 577 ? 1.0204 1.2344 0.9292 0.0361  -0.0695 -0.1285 680  VAL A C     
4297 O  O     . VAL A 577 ? 0.9635 1.1814 0.8825 0.0393  -0.0630 -0.1256 680  VAL A O     
4298 C  CB    . VAL A 577 ? 1.0643 1.2958 0.9794 0.0288  -0.0688 -0.1106 680  VAL A CB    
4299 C  CG1   . VAL A 577 ? 1.1173 1.3577 1.0228 0.0275  -0.0666 -0.1034 680  VAL A CG1   
4300 C  CG2   . VAL A 577 ? 1.0856 1.3111 1.0127 0.0237  -0.0770 -0.1087 680  VAL A CG2   
4301 N  N     . SER A 578 ? 1.0502 1.2505 0.9540 0.0349  -0.0762 -0.1370 681  SER A N     
4302 C  CA    . SER A 578 ? 1.0553 1.2421 0.9663 0.0370  -0.0757 -0.1422 681  SER A CA    
4303 C  C     . SER A 578 ? 1.0184 1.2042 0.9237 0.0469  -0.0669 -0.1468 681  SER A C     
4304 O  O     . SER A 578 ? 0.9953 1.1734 0.9091 0.0507  -0.0644 -0.1478 681  SER A O     
4305 C  CB    . SER A 578 ? 1.1456 1.3164 1.0499 0.0326  -0.0844 -0.1513 681  SER A CB    
4306 O  OG    . SER A 578 ? 1.2337 1.3996 1.1165 0.0359  -0.0851 -0.1607 681  SER A OG    
4307 N  N     . GLN A 579 ? 1.1954 1.3893 1.0865 0.0520  -0.0619 -0.1490 682  GLN A N     
4308 C  CA    . GLN A 579 ? 1.0588 1.2550 0.9459 0.0624  -0.0527 -0.1527 682  GLN A CA    
4309 C  C     . GLN A 579 ? 1.0125 1.2289 0.9125 0.0642  -0.0448 -0.1433 682  GLN A C     
4310 O  O     . GLN A 579 ? 0.9842 1.2040 0.8922 0.0712  -0.0391 -0.1433 682  GLN A O     
4311 C  CB    . GLN A 579 ? 0.9987 1.1932 0.8629 0.0678  -0.0501 -0.1608 682  GLN A CB    
4312 C  CG    . GLN A 579 ? 1.0381 1.2333 0.8969 0.0802  -0.0404 -0.1658 682  GLN A CG    
4313 C  CD    . GLN A 579 ? 1.0781 1.2708 0.9126 0.0862  -0.0370 -0.1740 682  GLN A CD    
4314 O  OE1   . GLN A 579 ? 1.1528 1.3590 0.9792 0.0845  -0.0345 -0.1702 682  GLN A OE1   
4315 N  NE2   . GLN A 579 ? 0.9687 1.1424 0.7898 0.0937  -0.0364 -0.1851 682  GLN A NE2   
4316 N  N     . ARG A 580 ? 0.9761 1.2056 0.8778 0.0580  -0.0446 -0.1353 683  ARG A N     
4317 C  CA    . ARG A 580 ? 0.9123 1.1595 0.8264 0.0572  -0.0379 -0.1265 683  ARG A CA    
4318 C  C     . ARG A 580 ? 0.9922 1.2380 0.9255 0.0550  -0.0398 -0.1219 683  ARG A C     
4319 O  O     . ARG A 580 ? 0.9781 1.2347 0.9218 0.0584  -0.0343 -0.1190 683  ARG A O     
4320 C  CB    . ARG A 580 ? 0.9039 1.1604 0.8140 0.0502  -0.0377 -0.1189 683  ARG A CB    
4321 C  CG    . ARG A 580 ? 0.9512 1.2206 0.8758 0.0454  -0.0334 -0.1091 683  ARG A CG    
4322 C  CD    . ARG A 580 ? 0.9433 1.2286 0.8623 0.0453  -0.0246 -0.1052 683  ARG A CD    
4323 N  NE    . ARG A 580 ? 1.0876 1.3708 0.9908 0.0420  -0.0257 -0.1028 683  ARG A NE    
4324 C  CZ    . ARG A 580 ? 1.1546 1.4487 1.0492 0.0410  -0.0182 -0.0986 683  ARG A CZ    
4325 N  NH1   . ARG A 580 ? 1.0642 1.3739 0.9660 0.0421  -0.0090 -0.0965 683  ARG A NH1   
4326 N  NH2   . ARG A 580 ? 1.0721 1.3621 0.9507 0.0389  -0.0200 -0.0960 683  ARG A NH2   
4327 N  N     . PHE A 581 ? 0.9250 1.1586 0.8629 0.0493  -0.0476 -0.1210 684  PHE A N     
4328 C  CA    . PHE A 581 ? 0.9474 1.1783 0.9017 0.0473  -0.0491 -0.1164 684  PHE A CA    
4329 C  C     . PHE A 581 ? 0.9825 1.2018 0.9393 0.0542  -0.0489 -0.1223 684  PHE A C     
4330 O  O     . PHE A 581 ? 1.0951 1.3174 1.0635 0.0570  -0.0465 -0.1189 684  PHE A O     
4331 C  CB    . PHE A 581 ? 0.9357 1.1597 0.8949 0.0390  -0.0563 -0.1121 684  PHE A CB    
4332 C  CG    . PHE A 581 ? 0.9290 1.1632 0.8888 0.0333  -0.0557 -0.1039 684  PHE A CG    
4333 C  CD1   . PHE A 581 ? 0.8489 1.0965 0.8061 0.0339  -0.0489 -0.1004 684  PHE A CD1   
4334 C  CD2   . PHE A 581 ? 0.8574 1.0875 0.8206 0.0273  -0.0615 -0.0993 684  PHE A CD2   
4335 C  CE1   . PHE A 581 ? 0.7397 0.9933 0.6958 0.0283  -0.0477 -0.0927 684  PHE A CE1   
4336 C  CE2   . PHE A 581 ? 0.8658 1.1027 0.8279 0.0232  -0.0604 -0.0915 684  PHE A CE2   
4337 C  CZ    . PHE A 581 ? 0.7665 1.0135 0.7243 0.0235  -0.0535 -0.0882 684  PHE A CZ    
4338 N  N     . GLY A 582 ? 0.9649 1.1697 0.9098 0.0571  -0.0514 -0.1312 685  GLY A N     
4339 C  CA    . GLY A 582 ? 1.0039 1.1937 0.9487 0.0641  -0.0506 -0.1369 685  GLY A CA    
4340 C  C     . GLY A 582 ? 1.0093 1.2090 0.9557 0.0752  -0.0424 -0.1372 685  GLY A C     
4341 O  O     . GLY A 582 ? 1.0063 1.2014 0.9606 0.0809  -0.0408 -0.1362 685  GLY A O     
4342 N  N     . LEU A 583 ? 1.0327 1.2475 0.9719 0.0789  -0.0369 -0.1382 686  LEU A N     
4343 C  CA    . LEU A 583 ? 1.0406 1.2704 0.9840 0.0891  -0.0287 -0.1374 686  LEU A CA    
4344 C  C     . LEU A 583 ? 0.9350 1.1828 0.8967 0.0859  -0.0273 -0.1279 686  LEU A C     
4345 O  O     . LEU A 583 ? 1.0519 1.3093 1.0220 0.0941  -0.0232 -0.1266 686  LEU A O     
4346 C  CB    . LEU A 583 ? 1.0009 1.2443 0.9328 0.0927  -0.0224 -0.1400 686  LEU A CB    
4347 C  CG    . LEU A 583 ? 1.0057 1.2332 0.9168 0.0991  -0.0217 -0.1506 686  LEU A CG    
4348 C  CD1   . LEU A 583 ? 1.0441 1.2877 0.9442 0.1017  -0.0149 -0.1513 686  LEU A CD1   
4349 C  CD2   . LEU A 583 ? 1.0479 1.2626 0.9568 0.1119  -0.0185 -0.1568 686  LEU A CD2   
4350 N  N     . LEU A 584 ? 0.8283 1.0809 0.7956 0.0746  -0.0309 -0.1215 687  LEU A N     
4351 C  CA    . LEU A 584 ? 0.9301 1.1969 0.9127 0.0705  -0.0302 -0.1133 687  LEU A CA    
4352 C  C     . LEU A 584 ? 0.9838 1.2391 0.9756 0.0723  -0.0339 -0.1117 687  LEU A C     
4353 O  O     . LEU A 584 ? 1.0414 1.3078 1.0439 0.0754  -0.0320 -0.1078 687  LEU A O     
4354 C  CB    . LEU A 584 ? 0.8781 1.1493 0.8613 0.0588  -0.0323 -0.1071 687  LEU A CB    
4355 C  CG    . LEU A 584 ? 0.8623 1.1473 0.8583 0.0531  -0.0310 -0.0993 687  LEU A CG    
4356 C  CD1   . LEU A 584 ? 0.7928 1.0992 0.7951 0.0584  -0.0245 -0.0989 687  LEU A CD1   
4357 C  CD2   . LEU A 584 ? 0.7429 1.0300 0.7359 0.0428  -0.0316 -0.0938 687  LEU A CD2   
4358 N  N     . LEU A 585 ? 0.9506 1.1844 0.9382 0.0700  -0.0393 -0.1146 688  LEU A N     
4359 C  CA    . LEU A 585 ? 0.9512 1.1722 0.9462 0.0715  -0.0420 -0.1128 688  LEU A CA    
4360 C  C     . LEU A 585 ? 0.9814 1.1980 0.9754 0.0843  -0.0385 -0.1164 688  LEU A C     
4361 O  O     . LEU A 585 ? 1.0514 1.2670 1.0536 0.0881  -0.0385 -0.1125 688  LEU A O     
4362 C  CB    . LEU A 585 ? 0.9759 1.1760 0.9672 0.0651  -0.0480 -0.1149 688  LEU A CB    
4363 C  CG    . LEU A 585 ? 1.0137 1.2167 1.0097 0.0539  -0.0521 -0.1092 688  LEU A CG    
4364 C  CD1   . LEU A 585 ? 0.9964 1.1818 0.9903 0.0483  -0.0580 -0.1118 688  LEU A CD1   
4365 C  CD2   . LEU A 585 ? 0.9800 1.1902 0.9880 0.0519  -0.0514 -0.1011 688  LEU A CD2   
4366 N  N     . GLU A 586 ? 1.0031 1.2162 0.9859 0.0919  -0.0352 -0.1238 689  GLU A N     
4367 C  CA    . GLU A 586 ? 1.0533 1.2609 1.0338 0.1058  -0.0311 -0.1273 689  GLU A CA    
4368 C  C     . GLU A 586 ? 1.0015 1.2340 0.9941 0.1126  -0.0269 -0.1216 689  GLU A C     
4369 O  O     . GLU A 586 ? 1.0352 1.2647 1.0330 0.1211  -0.0263 -0.1195 689  GLU A O     
4370 C  CB    . GLU A 586 ? 1.0093 1.2099 0.9740 0.1131  -0.0275 -0.1364 689  GLU A CB    
4371 C  CG    . GLU A 586 ? 1.0389 1.2310 0.9991 0.1293  -0.0224 -0.1406 689  GLU A CG    
4372 C  CD    . GLU A 586 ? 1.2037 1.3965 1.1492 0.1384  -0.0167 -0.1486 689  GLU A CD    
4373 O  OE1   . GLU A 586 ? 1.1604 1.3662 1.1013 0.1325  -0.0157 -0.1496 689  GLU A OE1   
4374 O  OE2   . GLU A 586 ? 1.2545 1.4340 1.1920 0.1520  -0.0125 -0.1537 689  GLU A OE2   
4375 N  N     . SER A 587 ? 0.9515 1.2090 0.9484 0.1086  -0.0240 -0.1189 690  SER A N     
4376 C  CA    . SER A 587 ? 0.9625 1.2468 0.9724 0.1127  -0.0207 -0.1135 690  SER A CA    
4377 C  C     . SER A 587 ? 1.0362 1.3220 1.0576 0.1066  -0.0255 -0.1065 690  SER A C     
4378 O  O     . SER A 587 ? 1.1320 1.4296 1.1625 0.1136  -0.0248 -0.1032 690  SER A O     
4379 C  CB    . SER A 587 ? 0.9011 1.2104 0.9130 0.1071  -0.0165 -0.1119 690  SER A CB    
4380 O  OG    . SER A 587 ? 0.9526 1.2593 0.9638 0.0925  -0.0201 -0.1085 690  SER A OG    
4381 N  N     . TYR A 588 ? 0.9785 1.2529 0.9992 0.0943  -0.0302 -0.1041 691  TYR A N     
4382 C  CA    . TYR A 588 ? 0.9550 1.2282 0.9844 0.0889  -0.0342 -0.0978 691  TYR A CA    
4383 C  C     . TYR A 588 ? 0.9888 1.2438 1.0180 0.0971  -0.0359 -0.0978 691  TYR A C     
4384 O  O     . TYR A 588 ? 1.0182 1.2805 1.0546 0.1015  -0.0365 -0.0934 691  TYR A O     
4385 C  CB    . TYR A 588 ? 0.9065 1.1703 0.9341 0.0755  -0.0379 -0.0953 691  TYR A CB    
4386 C  CG    . TYR A 588 ? 0.9545 1.2115 0.9884 0.0710  -0.0416 -0.0896 691  TYR A CG    
4387 C  CD1   . TYR A 588 ? 0.9221 1.1947 0.9634 0.0665  -0.0418 -0.0843 691  TYR A CD1   
4388 C  CD2   . TYR A 588 ? 1.0188 1.2534 1.0506 0.0707  -0.0446 -0.0897 691  TYR A CD2   
4389 C  CE1   . TYR A 588 ? 0.9323 1.1977 0.9772 0.0630  -0.0448 -0.0795 691  TYR A CE1   
4390 C  CE2   . TYR A 588 ? 1.0911 1.3197 1.1278 0.0672  -0.0470 -0.0841 691  TYR A CE2   
4391 C  CZ    . TYR A 588 ? 0.9754 1.2190 1.0179 0.0639  -0.0470 -0.0792 691  TYR A CZ    
4392 O  OH    . TYR A 588 ? 0.9998 1.2364 1.0450 0.0610  -0.0490 -0.0741 691  TYR A OH    
4393 N  N     . CYS A 589 ? 0.9674 1.1979 0.9874 0.0989  -0.0369 -0.1027 692  CYS A N     
4394 C  CA    . CYS A 589 ? 0.9958 1.2051 1.0142 0.1054  -0.0380 -0.1023 692  CYS A CA    
4395 C  C     . CYS A 589 ? 1.0336 1.2488 1.0526 0.1212  -0.0342 -0.1028 692  CYS A C     
4396 O  O     . CYS A 589 ? 1.0650 1.2712 1.0859 0.1275  -0.0349 -0.0991 692  CYS A O     
4397 C  CB    . CYS A 589 ? 0.9268 1.1089 0.9349 0.1028  -0.0396 -0.1084 692  CYS A CB    
4398 S  SG    . CYS A 589 ? 1.0044 1.1781 1.0143 0.0859  -0.0451 -0.1063 692  CYS A SG    
4399 N  N     . ARG A 590 ? 1.0236 1.2541 1.0406 0.1285  -0.0299 -0.1067 693  ARG A N     
4400 C  CA    . ARG A 590 ? 1.1239 1.3624 1.1420 0.1451  -0.0258 -0.1069 693  ARG A CA    
4401 C  C     . ARG A 590 ? 1.0515 1.3181 1.0836 0.1474  -0.0265 -0.0998 693  ARG A C     
4402 O  O     . ARG A 590 ? 1.0606 1.3341 1.0954 0.1617  -0.0245 -0.0981 693  ARG A O     
4403 C  CB    . ARG A 590 ? 1.0503 1.2976 1.0619 0.1527  -0.0201 -0.1134 693  ARG A CB    
4404 C  CG    . ARG A 590 ? 1.1790 1.4245 1.1871 0.1724  -0.0150 -0.1156 693  ARG A CG    
4405 C  CD    . ARG A 590 ? 1.2531 1.5004 1.2509 0.1797  -0.0088 -0.1232 693  ARG A CD    
4406 N  NE    . ARG A 590 ? 1.1504 1.3681 1.1324 0.1728  -0.0104 -0.1306 693  ARG A NE    
4407 C  CZ    . ARG A 590 ? 1.1936 1.3781 1.1619 0.1796  -0.0101 -0.1364 693  ARG A CZ    
4408 N  NH1   . ARG A 590 ? 1.2463 1.4202 1.2135 0.1946  -0.0075 -0.1351 693  ARG A NH1   
4409 N  NH2   . ARG A 590 ? 1.2008 1.3618 1.1557 0.1709  -0.0126 -0.1434 693  ARG A NH2   
4410 N  N     . ALA A 591 ? 1.0225 1.3047 1.0626 0.1339  -0.0295 -0.0955 694  ALA A N     
4411 C  CA    . ALA A 591 ? 1.0270 1.3369 1.0795 0.1340  -0.0308 -0.0898 694  ALA A CA    
4412 C  C     . ALA A 591 ? 1.0157 1.3215 1.0720 0.1229  -0.0362 -0.0842 694  ALA A C     
4413 O  O     . ALA A 591 ? 0.9525 1.2793 1.0176 0.1218  -0.0382 -0.0799 694  ALA A O     
4414 C  CB    . ALA A 591 ? 1.0300 1.3705 1.0892 0.1289  -0.0277 -0.0904 694  ALA A CB    
4415 N  N     . CYS A 592 ? 0.9966 1.2770 1.0465 0.1147  -0.0385 -0.0844 695  CYS A N     
4416 C  CA    . CYS A 592 ? 0.9748 1.2508 1.0274 0.1054  -0.0426 -0.0790 695  CYS A CA    
4417 C  C     . CYS A 592 ? 1.0360 1.3062 1.0896 0.1142  -0.0444 -0.0746 695  CYS A C     
4418 O  O     . CYS A 592 ? 0.9583 1.2307 1.0144 0.1086  -0.0475 -0.0698 695  CYS A O     
4419 C  CB    . CYS A 592 ? 0.9458 1.1987 0.9927 0.0952  -0.0440 -0.0799 695  CYS A CB    
4420 S  SG    . CYS A 592 ? 1.0443 1.2645 1.0826 0.1016  -0.0435 -0.0832 695  CYS A SG    
4421 N  N     . GLY A 593 ? 1.0110 1.2725 1.0610 0.1284  -0.0424 -0.0760 696  GLY A N     
4422 C  CA    . GLY A 593 ? 1.0018 1.2583 1.0516 0.1387  -0.0437 -0.0711 696  GLY A CA    
4423 C  C     . GLY A 593 ? 1.0862 1.3097 1.1283 0.1379  -0.0441 -0.0691 696  GLY A C     
4424 O  O     . GLY A 593 ? 1.2827 1.4838 1.3183 0.1366  -0.0422 -0.0732 696  GLY A O     
4425 N  N     . MET A 594 ? 1.0427 1.2634 1.0851 0.1381  -0.0466 -0.0627 697  MET A N     
4426 C  CA    . MET A 594 ? 1.0984 1.2892 1.1341 0.1377  -0.0461 -0.0594 697  MET A CA    
4427 C  C     . MET A 594 ? 0.9976 1.1752 1.0331 0.1222  -0.0466 -0.0605 697  MET A C     
4428 O  O     . MET A 594 ? 0.9938 1.1459 1.0248 0.1203  -0.0453 -0.0596 697  MET A O     
4429 C  CB    . MET A 594 ? 1.1854 1.3787 1.2204 0.1427  -0.0482 -0.0518 697  MET A CB    
4430 C  CG    . MET A 594 ? 1.1538 1.3166 1.1809 0.1457  -0.0464 -0.0472 697  MET A CG    
4431 S  SD    . MET A 594 ? 1.5904 1.7272 1.6092 0.1593  -0.0419 -0.0500 697  MET A SD    
4432 C  CE    . MET A 594 ? 1.2986 1.4607 1.3194 0.1781  -0.0425 -0.0490 697  MET A CE    
4433 N  N     . TYR A 595 ? 0.9599 1.1544 1.0004 0.1113  -0.0482 -0.0620 698  TYR A N     
4434 C  CA    . TYR A 595 ? 0.9714 1.1556 1.0122 0.0980  -0.0488 -0.0621 698  TYR A CA    
4435 C  C     . TYR A 595 ? 0.9949 1.1617 1.0322 0.0954  -0.0476 -0.0675 698  TYR A C     
4436 O  O     . TYR A 595 ? 0.9660 1.1204 1.0037 0.0862  -0.0483 -0.0668 698  TYR A O     
4437 C  CB    . TYR A 595 ? 0.9365 1.1412 0.9817 0.0882  -0.0504 -0.0625 698  TYR A CB    
4438 C  CG    . TYR A 595 ? 0.9340 1.1300 0.9795 0.0763  -0.0511 -0.0604 698  TYR A CG    
4439 C  CD1   . TYR A 595 ? 0.9605 1.1458 1.0052 0.0745  -0.0513 -0.0548 698  TYR A CD1   
4440 C  CD2   . TYR A 595 ? 0.9745 1.1738 1.0206 0.0679  -0.0513 -0.0636 698  TYR A CD2   
4441 C  CE1   . TYR A 595 ? 0.9690 1.1477 1.0146 0.0650  -0.0513 -0.0525 698  TYR A CE1   
4442 C  CE2   . TYR A 595 ? 0.9507 1.1434 0.9975 0.0586  -0.0520 -0.0611 698  TYR A CE2   
4443 C  CZ    . TYR A 595 ? 0.9348 1.1176 0.9818 0.0574  -0.0518 -0.0556 698  TYR A CZ    
4444 O  OH    . TYR A 595 ? 0.9013 1.0788 0.9497 0.0494  -0.0518 -0.0528 698  TYR A OH    
4445 N  N     . LEU A 596 ? 0.9862 1.1524 1.0200 0.1036  -0.0459 -0.0729 699  LEU A N     
4446 C  CA    . LEU A 596 ? 0.9811 1.1285 1.0093 0.1015  -0.0452 -0.0791 699  LEU A CA    
4447 C  C     . LEU A 596 ? 0.9907 1.1102 1.0155 0.1005  -0.0447 -0.0770 699  LEU A C     
4448 O  O     . LEU A 596 ? 0.9913 1.0968 1.0151 0.0914  -0.0459 -0.0797 699  LEU A O     
4449 C  CB    . LEU A 596 ? 1.0384 1.1881 1.0613 0.1127  -0.0425 -0.0853 699  LEU A CB    
4450 C  CG    . LEU A 596 ? 1.0258 1.1530 1.0396 0.1122  -0.0417 -0.0928 699  LEU A CG    
4451 C  CD1   . LEU A 596 ? 1.0144 1.1453 1.0286 0.0988  -0.0444 -0.0966 699  LEU A CD1   
4452 C  CD2   . LEU A 596 ? 1.0208 1.1490 1.0278 0.1259  -0.0379 -0.0985 699  LEU A CD2   
4453 N  N     . LYS A 597 ? 1.0172 1.1290 1.0404 0.1097  -0.0431 -0.0718 700  LYS A N     
4454 C  CA    . LYS A 597 ? 1.0196 1.1043 1.0393 0.1085  -0.0418 -0.0685 700  LYS A CA    
4455 C  C     . LYS A 597 ? 0.9727 1.0568 0.9985 0.0952  -0.0433 -0.0639 700  LYS A C     
4456 O  O     . LYS A 597 ? 0.9581 1.0230 0.9837 0.0879  -0.0428 -0.0639 700  LYS A O     
4457 C  CB    . LYS A 597 ? 1.0858 1.1644 1.1015 0.1219  -0.0396 -0.0625 700  LYS A CB    
4458 C  CG    . LYS A 597 ? 1.1924 1.2410 1.2030 0.1217  -0.0370 -0.0580 700  LYS A CG    
4459 C  CD    . LYS A 597 ? 1.3878 1.4308 1.3926 0.1367  -0.0348 -0.0515 700  LYS A CD    
4460 C  CE    . LYS A 597 ? 1.4948 1.5063 1.4934 0.1363  -0.0313 -0.0462 700  LYS A CE    
4461 N  NZ    . LYS A 597 ? 1.4118 1.4165 1.4028 0.1521  -0.0291 -0.0390 700  LYS A NZ    
4462 N  N     . HIS A 598 ? 0.8938 0.9987 0.9249 0.0918  -0.0449 -0.0600 701  HIS A N     
4463 C  CA    . HIS A 598 ? 0.9293 1.0348 0.9657 0.0804  -0.0457 -0.0559 701  HIS A CA    
4464 C  C     . HIS A 598 ? 1.0209 1.1279 1.0605 0.0698  -0.0477 -0.0609 701  HIS A C     
4465 O  O     . HIS A 598 ? 1.0123 1.1104 1.0556 0.0612  -0.0479 -0.0589 701  HIS A O     
4466 C  CB    . HIS A 598 ? 0.9567 1.0818 0.9956 0.0800  -0.0468 -0.0514 701  HIS A CB    
4467 C  CG    . HIS A 598 ? 1.0319 1.1562 1.0672 0.0892  -0.0459 -0.0457 701  HIS A CG    
4468 N  ND1   . HIS A 598 ? 0.9610 1.0689 0.9936 0.0900  -0.0436 -0.0392 701  HIS A ND1   
4469 C  CD2   . HIS A 598 ? 0.9934 1.1326 1.0272 0.0982  -0.0471 -0.0451 701  HIS A CD2   
4470 C  CE1   . HIS A 598 ? 0.9205 1.0320 0.9486 0.0996  -0.0437 -0.0349 701  HIS A CE1   
4471 N  NE2   . HIS A 598 ? 0.9400 1.0713 0.9693 0.1047  -0.0462 -0.0385 701  HIS A NE2   
4472 N  N     . LEU A 599 ? 1.0544 1.1738 1.0927 0.0704  -0.0491 -0.0670 702  LEU A N     
4473 C  CA    . LEU A 599 ? 0.9778 1.0993 1.0173 0.0613  -0.0515 -0.0718 702  LEU A CA    
4474 C  C     . LEU A 599 ? 0.9886 1.0890 1.0253 0.0583  -0.0520 -0.0762 702  LEU A C     
4475 O  O     . LEU A 599 ? 1.0061 1.1037 1.0466 0.0483  -0.0544 -0.0767 702  LEU A O     
4476 C  CB    . LEU A 599 ? 0.9510 1.0890 0.9877 0.0639  -0.0520 -0.0771 702  LEU A CB    
4477 C  CG    . LEU A 599 ? 0.9509 1.1108 0.9911 0.0622  -0.0520 -0.0736 702  LEU A CG    
4478 C  CD1   . LEU A 599 ? 0.9190 1.0947 0.9566 0.0663  -0.0511 -0.0783 702  LEU A CD1   
4479 C  CD2   . LEU A 599 ? 0.9342 1.0975 0.9779 0.0516  -0.0538 -0.0708 702  LEU A CD2   
4480 N  N     . ASN A 600 ? 0.9240 1.0093 0.9539 0.0667  -0.0500 -0.0794 703  ASN A N     
4481 C  CA    . ASN A 600 ? 1.0358 1.0974 1.0614 0.0631  -0.0503 -0.0841 703  ASN A CA    
4482 C  C     . ASN A 600 ? 1.0817 1.1311 1.1136 0.0546  -0.0500 -0.0782 703  ASN A C     
4483 O  O     . ASN A 600 ? 1.1928 1.2320 1.2266 0.0447  -0.0522 -0.0813 703  ASN A O     
4484 C  CB    . ASN A 600 ? 1.0897 1.1343 1.1054 0.0752  -0.0471 -0.0875 703  ASN A CB    
4485 C  CG    . ASN A 600 ? 1.1685 1.2198 1.1767 0.0817  -0.0471 -0.0960 703  ASN A CG    
4486 O  OD1   . ASN A 600 ? 1.1807 1.2395 1.1882 0.0745  -0.0501 -0.1015 703  ASN A OD1   
4487 N  ND2   . ASN A 600 ? 1.2512 1.3004 1.2534 0.0960  -0.0436 -0.0967 703  ASN A ND2   
4488 N  N     . ARG A 601 ? 1.0735 1.1247 1.1088 0.0582  -0.0473 -0.0695 704  ARG A N     
4489 C  CA    . ARG A 601 ? 1.0701 1.1115 1.1115 0.0507  -0.0458 -0.0629 704  ARG A CA    
4490 C  C     . ARG A 601 ? 1.0305 1.0876 1.0818 0.0396  -0.0485 -0.0610 704  ARG A C     
4491 O  O     . ARG A 601 ? 1.0527 1.1033 1.1108 0.0308  -0.0481 -0.0580 704  ARG A O     
4492 C  CB    . ARG A 601 ? 1.0747 1.1137 1.1145 0.0587  -0.0419 -0.0542 704  ARG A CB    
4493 C  CG    . ARG A 601 ? 1.1738 1.1976 1.2172 0.0531  -0.0385 -0.0470 704  ARG A CG    
4494 C  CD    . ARG A 601 ? 1.2406 1.2560 1.2778 0.0635  -0.0343 -0.0394 704  ARG A CD    
4495 N  NE    . ARG A 601 ? 1.4449 1.4474 1.4852 0.0581  -0.0301 -0.0315 704  ARG A NE    
4496 C  CZ    . ARG A 601 ? 1.4931 1.4712 1.5314 0.0550  -0.0268 -0.0305 704  ARG A CZ    
4497 N  NH1   . ARG A 601 ? 1.3155 1.2769 1.3474 0.0568  -0.0276 -0.0374 704  ARG A NH1   
4498 N  NH2   . ARG A 601 ? 1.5340 1.5033 1.5761 0.0496  -0.0222 -0.0223 704  ARG A NH2   
4499 N  N     . GLN A 602 ? 1.0692 1.1469 1.1214 0.0401  -0.0508 -0.0624 705  GLN A N     
4500 C  CA    . GLN A 602 ? 1.0402 1.1317 1.1000 0.0310  -0.0533 -0.0610 705  GLN A CA    
4501 C  C     . GLN A 602 ? 1.0824 1.1728 1.1425 0.0238  -0.0578 -0.0684 705  GLN A C     
4502 O  O     . GLN A 602 ? 1.1738 1.2681 1.2419 0.0149  -0.0601 -0.0669 705  GLN A O     
4503 C  CB    . GLN A 602 ? 0.9997 1.1107 1.0587 0.0339  -0.0538 -0.0594 705  GLN A CB    
4504 C  CG    . GLN A 602 ? 1.0891 1.2030 1.1470 0.0398  -0.0505 -0.0528 705  GLN A CG    
4505 C  CD    . GLN A 602 ? 1.1235 1.2553 1.1795 0.0413  -0.0513 -0.0527 705  GLN A CD    
4506 O  OE1   . GLN A 602 ? 0.9865 1.1282 1.0439 0.0362  -0.0533 -0.0546 705  GLN A OE1   
4507 N  NE2   . GLN A 602 ? 1.1624 1.2983 1.2150 0.0480  -0.0499 -0.0502 705  GLN A NE2   
4508 N  N     . VAL A 603 ? 1.0645 1.1508 1.1159 0.0280  -0.0591 -0.0764 706  VAL A N     
4509 C  CA    . VAL A 603 ? 1.0621 1.1460 1.1108 0.0216  -0.0637 -0.0844 706  VAL A CA    
4510 C  C     . VAL A 603 ? 1.0844 1.1504 1.1367 0.0134  -0.0648 -0.0855 706  VAL A C     
4511 O  O     . VAL A 603 ? 1.0949 1.1653 1.1532 0.0033  -0.0692 -0.0872 706  VAL A O     
4512 C  CB    . VAL A 603 ? 1.1149 1.1958 1.1515 0.0292  -0.0636 -0.0928 706  VAL A CB    
4513 C  CG1   . VAL A 603 ? 1.0669 1.1396 1.0977 0.0229  -0.0682 -0.1020 706  VAL A CG1   
4514 C  CG2   . VAL A 603 ? 1.0593 1.1616 1.0944 0.0341  -0.0630 -0.0918 706  VAL A CG2   
4515 N  N     . GLU A 604 ? 1.0797 1.1257 1.1285 0.0175  -0.0607 -0.0843 707  GLU A N     
4516 C  CA    . GLU A 604 ? 1.1028 1.1294 1.1546 0.0087  -0.0609 -0.0850 707  GLU A CA    
4517 C  C     . GLU A 604 ? 1.1009 1.1366 1.1676 -0.0005 -0.0605 -0.0766 707  GLU A C     
4518 O  O     . GLU A 604 ? 1.1101 1.1408 1.1838 -0.0120 -0.0630 -0.0779 707  GLU A O     
4519 C  CB    . GLU A 604 ? 1.0522 1.0537 1.0958 0.0163  -0.0555 -0.0841 707  GLU A CB    
4520 C  CG    . GLU A 604 ? 1.2043 1.1806 1.2477 0.0069  -0.0552 -0.0864 707  GLU A CG    
4521 C  CD    . GLU A 604 ? 1.4192 1.3670 1.4505 0.0160  -0.0497 -0.0866 707  GLU A CD    
4522 O  OE1   . GLU A 604 ? 1.5313 1.4815 1.5552 0.0305  -0.0468 -0.0852 707  GLU A OE1   
4523 O  OE2   . GLU A 604 ? 1.5390 1.4622 1.5684 0.0086  -0.0484 -0.0880 707  GLU A OE2   
4524 N  N     . ALA A 605 ? 1.0998 1.1493 1.1714 0.0043  -0.0574 -0.0681 708  ALA A N     
4525 C  CA    . ALA A 605 ? 1.0838 1.1432 1.1687 -0.0027 -0.0562 -0.0599 708  ALA A CA    
4526 C  C     . ALA A 605 ? 1.0515 1.1292 1.1446 -0.0112 -0.0621 -0.0622 708  ALA A C     
4527 O  O     . ALA A 605 ? 1.0270 1.1070 1.1314 -0.0212 -0.0637 -0.0604 708  ALA A O     
4528 C  CB    . ALA A 605 ? 1.0553 1.1240 1.1402 0.0053  -0.0517 -0.0515 708  ALA A CB    
4529 N  N     . MET A 606 ? 1.0564 1.1482 1.1444 -0.0072 -0.0654 -0.0657 709  MET A N     
4530 C  CA    . MET A 606 ? 1.0585 1.1670 1.1519 -0.0137 -0.0712 -0.0677 709  MET A CA    
4531 C  C     . MET A 606 ? 1.0771 1.1783 1.1697 -0.0223 -0.0772 -0.0762 709  MET A C     
4532 O  O     . MET A 606 ? 1.0277 1.1405 1.1298 -0.0310 -0.0822 -0.0762 709  MET A O     
4533 C  CB    . MET A 606 ? 0.9704 1.0922 1.0558 -0.0073 -0.0726 -0.0695 709  MET A CB    
4534 C  CG    . MET A 606 ? 0.9997 1.1294 1.0852 -0.0004 -0.0677 -0.0620 709  MET A CG    
4535 S  SD    . MET A 606 ? 1.1243 1.2648 1.2233 -0.0042 -0.0655 -0.0516 709  MET A SD    
4536 C  CE    . MET A 606 ? 0.9408 1.0660 1.0423 -0.0020 -0.0587 -0.0457 709  MET A CE    
4537 N  N     . GLU A 607 ? 1.1134 1.1956 1.1946 -0.0199 -0.0769 -0.0838 710  GLU A N     
4538 C  CA    . GLU A 607 ? 1.1165 1.1882 1.1941 -0.0284 -0.0825 -0.0932 710  GLU A CA    
4539 C  C     . GLU A 607 ? 1.1866 1.2520 1.2770 -0.0406 -0.0832 -0.0905 710  GLU A C     
4540 O  O     . GLU A 607 ? 1.2049 1.2751 1.3002 -0.0516 -0.0900 -0.0953 710  GLU A O     
4541 C  CB    . GLU A 607 ? 1.1832 1.2325 1.2443 -0.0216 -0.0805 -0.1014 710  GLU A CB    
4542 C  CG    . GLU A 607 ? 1.4073 1.4558 1.4558 -0.0224 -0.0863 -0.1128 710  GLU A CG    
4543 C  CD    . GLU A 607 ? 1.6398 1.6824 1.6909 -0.0364 -0.0934 -0.1194 710  GLU A CD    
4544 O  OE1   . GLU A 607 ? 1.5771 1.6069 1.6362 -0.0448 -0.0923 -0.1173 710  GLU A OE1   
4545 O  OE2   . GLU A 607 ? 1.6368 1.6879 1.6815 -0.0396 -0.1001 -0.1267 710  GLU A OE2   
4546 N  N     . LYS A 608 ? 1.1463 1.2020 1.2424 -0.0392 -0.0762 -0.0826 711  LYS A N     
4547 C  CA    . LYS A 608 ? 1.1232 1.1736 1.2325 -0.0513 -0.0755 -0.0788 711  LYS A CA    
4548 C  C     . LYS A 608 ? 1.0599 1.1375 1.1872 -0.0579 -0.0781 -0.0721 711  LYS A C     
4549 O  O     . LYS A 608 ? 1.0427 1.1246 1.1825 -0.0708 -0.0815 -0.0725 711  LYS A O     
4550 C  CB    . LYS A 608 ? 1.1197 1.1520 1.2284 -0.0470 -0.0664 -0.0712 711  LYS A CB    
4551 C  CG    . LYS A 608 ? 1.1749 1.1777 1.2669 -0.0410 -0.0636 -0.0770 711  LYS A CG    
4552 C  CD    . LYS A 608 ? 1.2214 1.2061 1.3095 -0.0525 -0.0683 -0.0870 711  LYS A CD    
4553 C  CE    . LYS A 608 ? 1.2609 1.2141 1.3301 -0.0448 -0.0651 -0.0934 711  LYS A CE    
4554 N  NZ    . LYS A 608 ? 1.3754 1.3080 1.4429 -0.0400 -0.0563 -0.0850 711  LYS A NZ    
4555 N  N     . LEU A 609 ? 1.0565 1.1526 1.1855 -0.0494 -0.0764 -0.0661 712  LEU A N     
4556 C  CA    . LEU A 609 ? 1.0438 1.1651 1.1882 -0.0535 -0.0785 -0.0597 712  LEU A CA    
4557 C  C     . LEU A 609 ? 1.0557 1.1916 1.2019 -0.0600 -0.0885 -0.0667 712  LEU A C     
4558 O  O     . LEU A 609 ? 1.0358 1.1894 1.1976 -0.0681 -0.0922 -0.0635 712  LEU A O     
4559 C  CB    . LEU A 609 ? 1.0425 1.1758 1.1849 -0.0423 -0.0740 -0.0523 712  LEU A CB    
4560 C  CG    . LEU A 609 ? 1.0247 1.1481 1.1665 -0.0359 -0.0646 -0.0442 712  LEU A CG    
4561 C  CD1   . LEU A 609 ? 1.0050 1.1407 1.1438 -0.0264 -0.0615 -0.0383 712  LEU A CD1   
4562 C  CD2   . LEU A 609 ? 0.9503 1.0732 1.1073 -0.0439 -0.0606 -0.0372 712  LEU A CD2   
4563 N  N     . ILE A 610 ? 1.1264 1.2566 1.2567 -0.0561 -0.0928 -0.0758 713  ILE A N     
4564 C  CA    . ILE A 610 ? 1.0523 1.1949 1.1810 -0.0618 -0.1025 -0.0829 713  ILE A CA    
4565 C  C     . ILE A 610 ? 1.0620 1.1965 1.1961 -0.0759 -0.1082 -0.0896 713  ILE A C     
4566 O  O     . ILE A 610 ? 1.0463 1.1988 1.1920 -0.0851 -0.1156 -0.0899 713  ILE A O     
4567 C  CB    . ILE A 610 ? 1.0303 1.1675 1.1390 -0.0535 -0.1044 -0.0908 713  ILE A CB    
4568 C  CG1   . ILE A 610 ? 0.9804 1.1294 1.0858 -0.0420 -0.0998 -0.0841 713  ILE A CG1   
4569 C  CG2   . ILE A 610 ? 1.1149 1.2608 1.2187 -0.0596 -0.1145 -0.0993 713  ILE A CG2   
4570 C  CD1   . ILE A 610 ? 0.8396 0.9841 0.9268 -0.0337 -0.0997 -0.0904 713  ILE A CD1   
4571 N  N     . ASN A 611 ? 1.0725 1.1798 1.1983 -0.0779 -0.1050 -0.0948 714  ASN A N     
4572 C  CA    . ASN A 611 ? 1.1126 1.2076 1.2417 -0.0926 -0.1098 -0.1017 714  ASN A CA    
4573 C  C     . ASN A 611 ? 1.1302 1.2398 1.2832 -0.1042 -0.1097 -0.0936 714  ASN A C     
4574 O  O     . ASN A 611 ? 1.1788 1.2972 1.3412 -0.1180 -0.1176 -0.0979 714  ASN A O     
4575 C  CB    . ASN A 611 ? 1.1765 1.2364 1.2919 -0.0910 -0.1041 -0.1066 714  ASN A CB    
4576 C  CG    . ASN A 611 ? 1.3350 1.3815 1.4277 -0.0789 -0.1037 -0.1148 714  ASN A CG    
4577 O  OD1   . ASN A 611 ? 1.3273 1.3832 1.4113 -0.0780 -0.1106 -0.1222 714  ASN A OD1   
4578 N  ND2   . ASN A 611 ? 1.4220 1.4473 1.5049 -0.0689 -0.0955 -0.1131 714  ASN A ND2   
4579 N  N     . LEU A 612 ? 1.1253 1.2389 1.2884 -0.0989 -0.1006 -0.0817 715  LEU A N     
4580 C  CA    . LEU A 612 ? 1.0974 1.2260 1.2835 -0.1086 -0.0987 -0.0729 715  LEU A CA    
4581 C  C     . LEU A 612 ? 1.0743 1.2379 1.2751 -0.1111 -0.1060 -0.0700 715  LEU A C     
4582 O  O     . LEU A 612 ? 1.0655 1.2440 1.2836 -0.1244 -0.1113 -0.0698 715  LEU A O     
4583 C  CB    . LEU A 612 ? 1.0686 1.1929 1.2588 -0.1001 -0.0868 -0.0610 715  LEU A CB    
4584 C  CG    . LEU A 612 ? 1.0472 1.1857 1.2602 -0.1078 -0.0819 -0.0503 715  LEU A CG    
4585 C  CD1   . LEU A 612 ? 1.1434 1.2720 1.3660 -0.1257 -0.0842 -0.0540 715  LEU A CD1   
4586 C  CD2   . LEU A 612 ? 1.0614 1.1902 1.2721 -0.0978 -0.0698 -0.0399 715  LEU A CD2   
4587 N  N     . THR A 613 ? 1.0533 1.2305 1.2473 -0.0985 -0.1064 -0.0676 716  THR A N     
4588 C  CA    . THR A 613 ? 1.0503 1.2590 1.2558 -0.0986 -0.1130 -0.0642 716  THR A CA    
4589 C  C     . THR A 613 ? 1.1263 1.3423 1.3288 -0.1078 -0.1258 -0.0747 716  THR A C     
4590 O  O     . THR A 613 ? 1.1628 1.4058 1.3797 -0.1129 -0.1330 -0.0723 716  THR A O     
4591 C  CB    . THR A 613 ? 1.0195 1.2362 1.2154 -0.0831 -0.1098 -0.0594 716  THR A CB    
4592 O  OG1   . THR A 613 ? 1.0767 1.2748 1.2499 -0.0762 -0.1101 -0.0675 716  THR A OG1   
4593 C  CG2   . THR A 613 ? 0.9610 1.1768 1.1630 -0.0753 -0.0985 -0.0480 716  THR A CG2   
4594 N  N     . ASP A 614 ? 1.1300 1.3230 1.3133 -0.1094 -0.1290 -0.0864 717  ASP A N     
4595 C  CA    . ASP A 614 ? 1.1132 1.3101 1.2910 -0.1188 -0.1413 -0.0976 717  ASP A CA    
4596 C  C     . ASP A 614 ? 1.1453 1.3446 1.3399 -0.1373 -0.1462 -0.1000 717  ASP A C     
4597 O  O     . ASP A 614 ? 1.1645 1.3866 1.3694 -0.1466 -0.1568 -0.1025 717  ASP A O     
4598 C  CB    . ASP A 614 ? 1.1304 1.3000 1.2815 -0.1145 -0.1420 -0.1096 717  ASP A CB    
4599 C  CG    . ASP A 614 ? 1.2305 1.4033 1.3659 -0.0984 -0.1392 -0.1083 717  ASP A CG    
4600 O  OD1   . ASP A 614 ? 1.2324 1.4254 1.3763 -0.0908 -0.1366 -0.0983 717  ASP A OD1   
4601 O  OD2   . ASP A 614 ? 1.2116 1.3661 1.3259 -0.0933 -0.1392 -0.1173 717  ASP A OD2   
4602 N  N     . ILE A 615 ? 1.1472 1.3233 1.3446 -0.1433 -0.1387 -0.0992 718  ILE A N     
4603 C  CA    . ILE A 615 ? 1.1685 1.3454 1.3829 -0.1623 -0.1419 -0.1005 718  ILE A CA    
4604 C  C     . ILE A 615 ? 1.1940 1.4064 1.4376 -0.1664 -0.1417 -0.0885 718  ILE A C     
4605 O  O     . ILE A 615 ? 1.2567 1.4860 1.5182 -0.1823 -0.1490 -0.0899 718  ILE A O     
4606 C  CB    . ILE A 615 ? 1.1685 1.3099 1.3776 -0.1663 -0.1323 -0.1009 718  ILE A CB    
4607 C  CG1   . ILE A 615 ? 1.2373 1.3443 1.4171 -0.1595 -0.1319 -0.1123 718  ILE A CG1   
4608 C  CG2   . ILE A 615 ? 1.1882 1.3275 1.4135 -0.1879 -0.1355 -0.1031 718  ILE A CG2   
4609 C  CD1   . ILE A 615 ? 1.3244 1.3940 1.4964 -0.1621 -0.1229 -0.1130 718  ILE A CD1   
4610 N  N     . LEU A 616 ? 1.1466 1.3715 1.3953 -0.1521 -0.1333 -0.0766 719  LEU A N     
4611 C  CA    . LEU A 616 ? 1.1316 1.3895 1.4068 -0.1535 -0.1316 -0.0646 719  LEU A CA    
4612 C  C     . LEU A 616 ? 1.2179 1.5100 1.5021 -0.1552 -0.1440 -0.0659 719  LEU A C     
4613 O  O     . LEU A 616 ? 1.2449 1.5658 1.5541 -0.1637 -0.1472 -0.0602 719  LEU A O     
4614 C  CB    . LEU A 616 ? 1.1302 1.3891 1.4043 -0.1367 -0.1195 -0.0528 719  LEU A CB    
4615 C  CG    . LEU A 616 ? 1.0455 1.3302 1.3451 -0.1365 -0.1130 -0.0391 719  LEU A CG    
4616 C  CD1   . LEU A 616 ? 1.0394 1.3169 1.3550 -0.1514 -0.1077 -0.0363 719  LEU A CD1   
4617 C  CD2   . LEU A 616 ? 0.7712 1.0526 1.0635 -0.1187 -0.1019 -0.0297 719  LEU A CD2   
4618 N  N     . LYS A 617 ? 1.2440 1.5346 1.5083 -0.1469 -0.1509 -0.0730 720  LYS A N     
4619 C  CA    . LYS A 617 ? 1.2324 1.5539 1.5016 -0.1463 -0.1627 -0.0737 720  LYS A CA    
4620 C  C     . LYS A 617 ? 1.3310 1.6564 1.6004 -0.1629 -0.1768 -0.0858 720  LYS A C     
4621 O  O     . LYS A 617 ? 1.4709 1.8274 1.7512 -0.1663 -0.1877 -0.0853 720  LYS A O     
4622 C  CB    . LYS A 617 ? 1.1630 1.4816 1.4099 -0.1294 -0.1629 -0.0745 720  LYS A CB    
4623 C  CG    . LYS A 617 ? 1.3902 1.7416 1.6421 -0.1243 -0.1723 -0.0711 720  LYS A CG    
4624 C  CD    . LYS A 617 ? 1.6412 1.9857 1.8687 -0.1090 -0.1718 -0.0723 720  LYS A CD    
4625 C  CE    . LYS A 617 ? 1.4630 1.8379 1.6933 -0.1039 -0.1814 -0.0687 720  LYS A CE    
4626 N  NZ    . LYS A 617 ? 1.3476 1.7148 1.5537 -0.0896 -0.1802 -0.0690 720  LYS A NZ    
4627 N  N     . GLN A 618 ? 1.3388 1.6330 1.5955 -0.1730 -0.1771 -0.0968 721  GLN A N     
4628 C  CA    . GLN A 618 ? 1.4022 1.6955 1.6558 -0.1897 -0.1905 -0.1098 721  GLN A CA    
4629 C  C     . GLN A 618 ? 1.4245 1.7207 1.7010 -0.2104 -0.1915 -0.1097 721  GLN A C     
4630 O  O     . GLN A 618 ? 1.4514 1.7636 1.7365 -0.2261 -0.2044 -0.1168 721  GLN A O     
4631 C  CB    . GLN A 618 ? 1.4438 1.6988 1.6655 -0.1881 -0.1912 -0.1238 721  GLN A CB    
4632 C  CG    . GLN A 618 ? 1.5900 1.8404 1.8024 -0.2037 -0.2055 -0.1391 721  GLN A CG    
4633 C  CD    . GLN A 618 ? 1.6062 1.8932 1.8232 -0.2041 -0.2197 -0.1400 721  GLN A CD    
4634 O  OE1   . GLN A 618 ? 1.6198 1.9195 1.8275 -0.1880 -0.2197 -0.1356 721  GLN A OE1   
4635 N  NE2   . GLN A 618 ? 1.5529 1.8571 1.7842 -0.2229 -0.2319 -0.1455 721  GLN A NE2   
4636 N  N     . GLU A 619 ? 1.4861 1.7680 1.7726 -0.2114 -0.1784 -0.1017 722  GLU A N     
4637 C  CA    . GLU A 619 ? 1.5721 1.8527 1.8791 -0.2316 -0.1773 -0.1010 722  GLU A CA    
4638 C  C     . GLU A 619 ? 1.5462 1.8640 1.8871 -0.2338 -0.1730 -0.0861 722  GLU A C     
4639 O  O     . GLU A 619 ? 1.5120 1.8502 1.8761 -0.2523 -0.1791 -0.0862 722  GLU A O     
4640 C  CB    . GLU A 619 ? 1.6007 1.8369 1.8946 -0.2326 -0.1650 -0.1022 722  GLU A CB    
4641 C  CG    . GLU A 619 ? 1.6748 1.8999 1.9833 -0.2554 -0.1641 -0.1041 722  GLU A CG    
4642 C  CD    . GLU A 619 ? 1.8687 2.0807 2.1666 -0.2732 -0.1776 -0.1209 722  GLU A CD    
4643 O  OE1   . GLU A 619 ? 1.8359 2.0371 2.1090 -0.2657 -0.1851 -0.1319 722  GLU A OE1   
4644 O  OE2   . GLU A 619 ? 1.8826 2.0949 2.1965 -0.2952 -0.1805 -0.1232 722  GLU A OE2   
4645 N  N     . LYS A 620 ? 1.3631 1.6908 1.7076 -0.2158 -0.1626 -0.0734 723  LYS A N     
4646 C  CA    . LYS A 620 ? 1.3125 1.6719 1.6870 -0.2152 -0.1558 -0.0585 723  LYS A CA    
4647 C  C     . LYS A 620 ? 1.2881 1.6781 1.6658 -0.1970 -0.1571 -0.0503 723  LYS A C     
4648 O  O     . LYS A 620 ? 1.2807 1.6789 1.6662 -0.1842 -0.1458 -0.0379 723  LYS A O     
4649 C  CB    . LYS A 620 ? 1.2735 1.6100 1.6491 -0.2116 -0.1386 -0.0495 723  LYS A CB    
4650 C  CG    . LYS A 620 ? 1.2592 1.5527 1.6200 -0.2228 -0.1349 -0.0578 723  LYS A CG    
4651 C  CD    . LYS A 620 ? 1.1733 1.4672 1.5570 -0.2398 -0.1277 -0.0513 723  LYS A CD    
4652 C  CE    . LYS A 620 ? 1.2257 1.5502 1.6344 -0.2611 -0.1397 -0.0549 723  LYS A CE    
4653 N  NZ    . LYS A 620 ? 1.1364 1.4578 1.5662 -0.2804 -0.1326 -0.0498 723  LYS A NZ    
4654 N  N     . LYS A 621 ? 1.3002 1.7063 1.6706 -0.1952 -0.1709 -0.0572 724  LYS A N     
4655 C  CA    . LYS A 621 ? 1.2781 1.7103 1.6489 -0.1775 -0.1724 -0.0495 724  LYS A CA    
4656 C  C     . LYS A 621 ? 1.2552 1.7328 1.6594 -0.1799 -0.1743 -0.0384 724  LYS A C     
4657 O  O     . LYS A 621 ? 1.2456 1.7360 1.6602 -0.1668 -0.1639 -0.0254 724  LYS A O     
4658 C  CB    . LYS A 621 ? 1.3212 1.7538 1.6706 -0.1739 -0.1859 -0.0600 724  LYS A CB    
4659 C  CG    . LYS A 621 ? 1.3559 1.8121 1.7027 -0.1554 -0.1876 -0.0521 724  LYS A CG    
4660 C  CD    . LYS A 621 ? 1.4449 1.9029 1.7708 -0.1531 -0.2012 -0.0620 724  LYS A CD    
4661 C  CE    . LYS A 621 ? 1.5229 2.0034 1.8459 -0.1349 -0.2024 -0.0530 724  LYS A CE    
4662 N  NZ    . LYS A 621 ? 1.5744 2.0587 1.8772 -0.1327 -0.2158 -0.0616 724  LYS A NZ    
4663 N  N     . ASP A 622 ? 1.2603 1.7631 1.6814 -0.1963 -0.1877 -0.0434 725  ASP A N     
4664 C  CA    . ASP A 622 ? 1.2517 1.8022 1.7067 -0.1990 -0.1909 -0.0330 725  ASP A CA    
4665 C  C     . ASP A 622 ? 1.3257 1.8823 1.8075 -0.2080 -0.1786 -0.0235 725  ASP A C     
4666 O  O     . ASP A 622 ? 1.2885 1.8856 1.8004 -0.2086 -0.1783 -0.0132 725  ASP A O     
4667 C  CB    . ASP A 622 ? 1.3552 1.9325 1.8203 -0.2151 -0.2102 -0.0420 725  ASP A CB    
4668 C  CG    . ASP A 622 ? 1.5546 2.1053 2.0127 -0.2382 -0.2159 -0.0563 725  ASP A CG    
4669 O  OD1   . ASP A 622 ? 1.5575 2.0681 2.0020 -0.2402 -0.2047 -0.0589 725  ASP A OD1   
4670 O  OD2   . ASP A 622 ? 1.5580 2.1272 2.0232 -0.2540 -0.2319 -0.0651 725  ASP A OD2   
4671 N  N     . GLU A 623 ? 1.3287 1.8470 1.8001 -0.2142 -0.1680 -0.0262 726  GLU A N     
4672 C  CA    . GLU A 623 ? 1.2070 1.7274 1.7006 -0.2217 -0.1548 -0.0164 726  GLU A CA    
4673 C  C     . GLU A 623 ? 1.0644 1.5964 1.5640 -0.2009 -0.1406 -0.0012 726  GLU A C     
4674 O  O     . GLU A 623 ? 0.9903 1.5134 1.4696 -0.1810 -0.1383 0.0003  726  GLU A O     
4675 C  CB    . GLU A 623 ? 1.2121 1.6846 1.6884 -0.2309 -0.1467 -0.0227 726  GLU A CB    
4676 C  CG    . GLU A 623 ? 1.2772 1.7312 1.7446 -0.2516 -0.1590 -0.0384 726  GLU A CG    
4677 C  CD    . GLU A 623 ? 1.3908 1.8646 1.8884 -0.2768 -0.1625 -0.0381 726  GLU A CD    
4678 O  OE1   . GLU A 623 ? 1.2903 1.8006 1.8188 -0.2779 -0.1575 -0.0255 726  GLU A OE1   
4679 O  OE2   . GLU A 623 ? 1.5626 2.0149 2.0527 -0.2959 -0.1700 -0.0505 726  GLU A OE2   
4680 N  N     . THR A 624 ? 1.0582 1.6097 1.5854 -0.2062 -0.1306 0.0101  727  THR A N     
4681 C  CA    . THR A 624 ? 0.9892 1.5505 1.5221 -0.1872 -0.1159 0.0245  727  THR A CA    
4682 C  C     . THR A 624 ? 0.9541 1.4701 1.4576 -0.1751 -0.1032 0.0245  727  THR A C     
4683 O  O     . THR A 624 ? 0.9581 1.4373 1.4435 -0.1836 -0.1029 0.0158  727  THR A O     
4684 C  CB    . THR A 624 ? 0.9258 1.5158 1.4937 -0.1964 -0.1068 0.0363  727  THR A CB    
4685 O  OG1   . THR A 624 ? 1.0821 1.6868 1.6556 -0.1760 -0.0940 0.0501  727  THR A OG1   
4686 C  CG2   . THR A 624 ? 0.8980 1.4565 1.4644 -0.2117 -0.0969 0.0353  727  THR A CG2   
4687 N  N     . GLN A 625 ? 0.9293 1.4483 1.4277 -0.1544 -0.0927 0.0344  728  GLN A N     
4688 C  CA    . GLN A 625 ? 0.9491 1.4287 1.4193 -0.1416 -0.0817 0.0346  728  GLN A CA    
4689 C  C     . GLN A 625 ? 0.9608 1.4166 1.4326 -0.1510 -0.0695 0.0376  728  GLN A C     
4690 O  O     . GLN A 625 ? 0.9600 1.3776 1.4070 -0.1472 -0.0645 0.0334  728  GLN A O     
4691 C  CB    . GLN A 625 ? 0.9262 1.4154 1.3919 -0.1191 -0.0732 0.0446  728  GLN A CB    
4692 C  CG    . GLN A 625 ? 0.9522 1.4048 1.3847 -0.1043 -0.0673 0.0418  728  GLN A CG    
4693 C  CD    . GLN A 625 ? 1.0354 1.4680 1.4629 -0.0989 -0.0507 0.0495  728  GLN A CD    
4694 O  OE1   . GLN A 625 ? 1.1539 1.5922 1.5993 -0.1087 -0.0434 0.0554  728  GLN A OE1   
4695 N  NE2   . GLN A 625 ? 0.9956 1.4049 1.3980 -0.0834 -0.0448 0.0498  728  GLN A NE2   
4696 N  N     . LYS A 626 ? 0.9609 1.4392 1.4618 -0.1631 -0.0644 0.0453  729  LYS A N     
4697 C  CA    . LYS A 626 ? 0.9544 1.4098 1.4572 -0.1740 -0.0530 0.0485  729  LYS A CA    
4698 C  C     . LYS A 626 ? 1.0093 1.4328 1.4984 -0.1905 -0.0606 0.0356  729  LYS A C     
4699 O  O     . LYS A 626 ? 1.0733 1.4580 1.5422 -0.1896 -0.0530 0.0338  729  LYS A O     
4700 C  CB    . LYS A 626 ? 0.9989 1.4885 1.5379 -0.1855 -0.0466 0.0592  729  LYS A CB    
4701 C  CG    . LYS A 626 ? 1.1004 1.6142 1.6511 -0.1683 -0.0340 0.0736  729  LYS A CG    
4702 C  CD    . LYS A 626 ? 1.1416 1.6869 1.7280 -0.1809 -0.0259 0.0844  729  LYS A CD    
4703 C  CE    . LYS A 626 ? 1.1828 1.6990 1.7676 -0.1970 -0.0165 0.0852  729  LYS A CE    
4704 N  NZ    . LYS A 626 ? 1.1819 1.7289 1.8019 -0.2103 -0.0074 0.0964  729  LYS A NZ    
4705 N  N     . VAL A 627 ? 1.0319 1.4710 1.5309 -0.2052 -0.0758 0.0263  730  VAL A N     
4706 C  CA    . VAL A 627 ? 0.9998 1.4078 1.4846 -0.2213 -0.0837 0.0130  730  VAL A CA    
4707 C  C     . VAL A 627 ? 1.0139 1.3846 1.4620 -0.2075 -0.0854 0.0041  730  VAL A C     
4708 O  O     . VAL A 627 ? 1.0486 1.3802 1.4779 -0.2127 -0.0827 -0.0023 730  VAL A O     
4709 C  CB    . VAL A 627 ? 1.0112 1.4461 1.5125 -0.2387 -0.1009 0.0042  730  VAL A CB    
4710 C  CG1   . VAL A 627 ? 1.1129 1.5126 1.5923 -0.2514 -0.1105 -0.0119 730  VAL A CG1   
4711 C  CG2   . VAL A 627 ? 0.9376 1.4042 1.4758 -0.2571 -0.0985 0.0119  730  VAL A CG2   
4712 N  N     . GLN A 628 ? 1.0135 1.3955 1.4507 -0.1895 -0.0893 0.0042  731  GLN A N     
4713 C  CA    . GLN A 628 ? 1.0204 1.3706 1.4246 -0.1760 -0.0900 -0.0032 731  GLN A CA    
4714 C  C     . GLN A 628 ? 1.0517 1.3712 1.4411 -0.1661 -0.0749 0.0028  731  GLN A C     
4715 O  O     . GLN A 628 ? 1.1211 1.4058 1.4857 -0.1627 -0.0742 -0.0044 731  GLN A O     
4716 C  CB    . GLN A 628 ? 1.0024 1.3724 1.3999 -0.1591 -0.0956 -0.0025 731  GLN A CB    
4717 C  CG    . GLN A 628 ? 1.0484 1.4489 1.4572 -0.1662 -0.1112 -0.0081 731  GLN A CG    
4718 C  CD    . GLN A 628 ? 1.0810 1.4974 1.4806 -0.1484 -0.1156 -0.0063 731  GLN A CD    
4719 O  OE1   . GLN A 628 ? 1.0395 1.4424 1.4234 -0.1317 -0.1071 -0.0018 731  GLN A OE1   
4720 N  NE2   . GLN A 628 ? 1.1260 1.5708 1.5345 -0.1521 -0.1290 -0.0097 731  GLN A NE2   
4721 N  N     . MET A 629 ? 1.0257 1.3582 1.4293 -0.1608 -0.0628 0.0160  732  MET A N     
4722 C  CA    . MET A 629 ? 1.0159 1.3210 1.4047 -0.1508 -0.0487 0.0223  732  MET A CA    
4723 C  C     . MET A 629 ? 1.0722 1.3463 1.4566 -0.1644 -0.0440 0.0199  732  MET A C     
4724 O  O     . MET A 629 ? 1.1063 1.3464 1.4674 -0.1571 -0.0386 0.0181  732  MET A O     
4725 C  CB    . MET A 629 ? 1.0577 1.3847 1.4620 -0.1420 -0.0366 0.0368  732  MET A CB    
4726 C  CG    . MET A 629 ? 1.0104 1.3557 1.4099 -0.1236 -0.0377 0.0400  732  MET A CG    
4727 S  SD    . MET A 629 ? 1.0022 1.3140 1.3643 -0.1065 -0.0378 0.0335  732  MET A SD    
4728 C  CE    . MET A 629 ? 0.9847 1.2675 1.3357 -0.1021 -0.0215 0.0412  732  MET A CE    
4729 N  N     . LYS A 630 ? 1.0540 1.3394 1.4605 -0.1842 -0.0460 0.0202  733  LYS A N     
4730 C  CA    . LYS A 630 ? 1.1263 1.3797 1.5280 -0.1987 -0.0419 0.0175  733  LYS A CA    
4731 C  C     . LYS A 630 ? 1.1743 1.3943 1.5497 -0.1997 -0.0507 0.0030  733  LYS A C     
4732 O  O     . LYS A 630 ? 1.2603 1.4423 1.6169 -0.1988 -0.0444 0.0014  733  LYS A O     
4733 C  CB    . LYS A 630 ? 1.0713 1.3454 1.5025 -0.2219 -0.0442 0.0192  733  LYS A CB    
4734 C  CG    . LYS A 630 ? 1.1769 1.4914 1.6377 -0.2209 -0.0367 0.0331  733  LYS A CG    
4735 C  CD    . LYS A 630 ? 1.5398 1.8408 1.9946 -0.2089 -0.0187 0.0460  733  LYS A CD    
4736 C  CE    . LYS A 630 ? 1.4701 1.8111 1.9470 -0.1996 -0.0115 0.0589  733  LYS A CE    
4737 N  NZ    . LYS A 630 ? 1.1712 1.5303 1.6407 -0.1814 -0.0187 0.0566  733  LYS A NZ    
4738 N  N     . PHE A 631 ? 1.1522 1.3859 1.5251 -0.2005 -0.0649 -0.0074 734  PHE A N     
4739 C  CA    . PHE A 631 ? 1.1989 1.4030 1.5452 -0.1986 -0.0728 -0.0212 734  PHE A CA    
4740 C  C     . PHE A 631 ? 1.1433 1.3271 1.4641 -0.1769 -0.0669 -0.0202 734  PHE A C     
4741 O  O     . PHE A 631 ? 1.1751 1.3246 1.4731 -0.1739 -0.0664 -0.0274 734  PHE A O     
4742 C  CB    . PHE A 631 ? 1.1676 1.3942 1.5169 -0.2033 -0.0889 -0.0314 734  PHE A CB    
4743 C  CG    . PHE A 631 ? 1.2089 1.4066 1.5321 -0.2038 -0.0973 -0.0464 734  PHE A CG    
4744 C  CD1   . PHE A 631 ? 1.3196 1.4956 1.6397 -0.2220 -0.1022 -0.0563 734  PHE A CD1   
4745 C  CD2   . PHE A 631 ? 1.1928 1.3846 1.4941 -0.1863 -0.0999 -0.0508 734  PHE A CD2   
4746 C  CE1   . PHE A 631 ? 1.3196 1.4679 1.6143 -0.2214 -0.1092 -0.0704 734  PHE A CE1   
4747 C  CE2   . PHE A 631 ? 1.2493 1.4158 1.5268 -0.1859 -0.1066 -0.0643 734  PHE A CE2   
4748 C  CZ    . PHE A 631 ? 1.3742 1.5187 1.6480 -0.2028 -0.1112 -0.0742 734  PHE A CZ    
4749 N  N     . LEU A 632 ? 1.1260 1.3305 1.4502 -0.1618 -0.0623 -0.0113 735  LEU A N     
4750 C  CA    . LEU A 632 ? 1.1313 1.3194 1.4325 -0.1423 -0.0575 -0.0105 735  LEU A CA    
4751 C  C     . LEU A 632 ? 1.1483 1.3068 1.4389 -0.1383 -0.0448 -0.0044 735  LEU A C     
4752 O  O     . LEU A 632 ? 1.1661 1.2966 1.4338 -0.1298 -0.0436 -0.0092 735  LEU A O     
4753 C  CB    . LEU A 632 ? 1.0884 1.3048 1.3956 -0.1286 -0.0557 -0.0028 735  LEU A CB    
4754 C  CG    . LEU A 632 ? 1.0842 1.2876 1.3688 -0.1097 -0.0519 -0.0024 735  LEU A CG    
4755 C  CD1   . LEU A 632 ? 1.0758 1.2712 1.3426 -0.1062 -0.0622 -0.0144 735  LEU A CD1   
4756 C  CD2   . LEU A 632 ? 1.0644 1.2915 1.3560 -0.0978 -0.0471 0.0072  735  LEU A CD2   
4757 N  N     . VAL A 633 ? 1.1462 1.3115 1.4533 -0.1437 -0.0351 0.0067  736  VAL A N     
4758 C  CA    . VAL A 633 ? 1.1681 1.3067 1.4643 -0.1385 -0.0224 0.0141  736  VAL A CA    
4759 C  C     . VAL A 633 ? 1.2195 1.3220 1.5033 -0.1481 -0.0227 0.0074  736  VAL A C     
4760 O  O     . VAL A 633 ? 1.2709 1.3440 1.5361 -0.1396 -0.0153 0.0098  736  VAL A O     
4761 C  CB    . VAL A 633 ? 1.0769 1.2323 1.3935 -0.1422 -0.0111 0.0280  736  VAL A CB    
4762 C  CG1   . VAL A 633 ? 0.9748 1.1616 1.2995 -0.1296 -0.0095 0.0347  736  VAL A CG1   
4763 C  CG2   . VAL A 633 ? 1.1026 1.2709 1.4440 -0.1640 -0.0135 0.0281  736  VAL A CG2   
4764 N  N     . GLU A 634 ? 1.2330 1.3359 1.5257 -0.1654 -0.0313 -0.0011 737  GLU A N     
4765 C  CA    . GLU A 634 ? 1.2965 1.3619 1.5758 -0.1749 -0.0315 -0.0083 737  GLU A CA    
4766 C  C     . GLU A 634 ? 1.3302 1.3726 1.5822 -0.1629 -0.0374 -0.0195 737  GLU A C     
4767 O  O     . GLU A 634 ? 1.4038 1.4113 1.6363 -0.1571 -0.0319 -0.0204 737  GLU A O     
4768 C  CB    . GLU A 634 ? 1.3104 1.3831 1.6070 -0.1984 -0.0392 -0.0147 737  GLU A CB    
4769 C  CG    . GLU A 634 ? 1.3311 1.4161 1.6528 -0.2135 -0.0311 -0.0038 737  GLU A CG    
4770 C  CD    . GLU A 634 ? 1.3918 1.4816 1.7298 -0.2386 -0.0394 -0.0112 737  GLU A CD    
4771 O  OE1   . GLU A 634 ? 1.4106 1.5047 1.7439 -0.2431 -0.0530 -0.0242 737  GLU A OE1   
4772 O  OE2   . GLU A 634 ? 1.3801 1.4692 1.7349 -0.2543 -0.0322 -0.0041 737  GLU A OE2   
4773 N  N     . GLN A 635 ? 1.2768 1.3388 1.5272 -0.1585 -0.0481 -0.0275 738  GLN A N     
4774 C  CA    . GLN A 635 ? 1.3413 1.3849 1.5671 -0.1475 -0.0535 -0.0381 738  GLN A CA    
4775 C  C     . GLN A 635 ? 1.2952 1.3320 1.5054 -0.1266 -0.0465 -0.0326 738  GLN A C     
4776 O  O     . GLN A 635 ? 1.3462 1.3649 1.5357 -0.1165 -0.0486 -0.0399 738  GLN A O     
4777 C  CB    . GLN A 635 ? 1.2924 1.3600 1.5207 -0.1490 -0.0665 -0.0475 738  GLN A CB    
4778 C  CG    . GLN A 635 ? 1.3279 1.4058 1.5712 -0.1698 -0.0755 -0.0540 738  GLN A CG    
4779 C  CD    . GLN A 635 ? 1.5357 1.5775 1.7699 -0.1828 -0.0749 -0.0613 738  GLN A CD    
4780 O  OE1   . GLN A 635 ? 1.6416 1.6529 1.8520 -0.1761 -0.0753 -0.0697 738  GLN A OE1   
4781 N  NE2   . GLN A 635 ? 1.5257 1.5701 1.7786 -0.2016 -0.0734 -0.0579 738  GLN A NE2   
4782 N  N     . MET A 636 ? 1.2862 1.3377 1.5055 -0.1200 -0.0383 -0.0202 739  MET A N     
4783 C  CA    . MET A 636 ? 1.2742 1.3197 1.4785 -0.1014 -0.0321 -0.0150 739  MET A CA    
4784 C  C     . MET A 636 ? 1.3479 1.3657 1.5429 -0.0977 -0.0211 -0.0075 739  MET A C     
4785 O  O     . MET A 636 ? 1.3405 1.3434 1.5172 -0.0832 -0.0180 -0.0069 739  MET A O     
4786 C  CB    . MET A 636 ? 1.2328 1.3093 1.4484 -0.0942 -0.0299 -0.0066 739  MET A CB    
4787 C  CG    . MET A 636 ? 1.1958 1.2978 1.4154 -0.0927 -0.0399 -0.0128 739  MET A CG    
4788 S  SD    . MET A 636 ? 1.2391 1.3715 1.4679 -0.0819 -0.0361 -0.0028 739  MET A SD    
4789 C  CE    . MET A 636 ? 1.1088 1.2222 1.3140 -0.0640 -0.0293 -0.0001 739  MET A CE    
4790 N  N     . ARG A 637 ? 1.4826 1.4936 1.6897 -0.1105 -0.0151 -0.0013 740  ARG A N     
4791 C  CA    . ARG A 637 ? 1.4101 1.3935 1.6076 -0.1073 -0.0039 0.0069  740  ARG A CA    
4792 C  C     . ARG A 637 ? 1.4952 1.4405 1.6737 -0.1078 -0.0048 -0.0005 740  ARG A C     
4793 O  O     . ARG A 637 ? 1.5363 1.4553 1.7025 -0.1020 0.0040  0.0060  740  ARG A O     
4794 C  CB    . ARG A 637 ? 1.3787 1.3683 1.5960 -0.1215 0.0039  0.0170  740  ARG A CB    
4795 C  CG    . ARG A 637 ? 1.4053 1.3905 1.6357 -0.1431 -0.0009 0.0107  740  ARG A CG    
4796 C  CD    . ARG A 637 ? 1.5034 1.4992 1.7560 -0.1574 0.0076  0.0217  740  ARG A CD    
4797 N  NE    . ARG A 637 ? 1.6793 1.6735 1.9462 -0.1800 0.0022  0.0154  740  ARG A NE    
4798 C  CZ    . ARG A 637 ? 1.7191 1.7246 2.0086 -0.1969 0.0076  0.0229  740  ARG A CZ    
4799 N  NH1   . ARG A 637 ? 1.7258 1.7446 2.0259 -0.1931 0.0195  0.0373  740  ARG A NH1   
4800 N  NH2   . ARG A 637 ? 1.6652 1.6688 1.9666 -0.2184 0.0011  0.0155  740  ARG A NH2   
4801 N  N     . ARG A 638 ? 1.4357 1.3766 1.6104 -0.1136 -0.0147 -0.0136 741  ARG A N     
4802 C  CA    . ARG A 638 ? 1.4869 1.3905 1.6416 -0.1123 -0.0153 -0.0215 741  ARG A CA    
4803 C  C     . ARG A 638 ? 1.4707 1.3621 1.6040 -0.0904 -0.0125 -0.0206 741  ARG A C     
4804 O  O     . ARG A 638 ? 1.4852 1.4000 1.6184 -0.0785 -0.0146 -0.0191 741  ARG A O     
4805 C  CB    . ARG A 638 ? 1.5849 1.4889 1.7385 -0.1218 -0.0269 -0.0365 741  ARG A CB    
4806 C  CG    . ARG A 638 ? 1.6201 1.5542 1.7749 -0.1139 -0.0359 -0.0426 741  ARG A CG    
4807 C  CD    . ARG A 638 ? 1.6510 1.5819 1.8009 -0.1223 -0.0469 -0.0575 741  ARG A CD    
4808 N  NE    . ARG A 638 ? 1.6454 1.5752 1.8094 -0.1443 -0.0504 -0.0606 741  ARG A NE    
4809 C  CZ    . ARG A 638 ? 1.7352 1.6600 1.8960 -0.1557 -0.0601 -0.0736 741  ARG A CZ    
4810 N  NH1   . ARG A 638 ? 1.7966 1.7166 1.9399 -0.1467 -0.0667 -0.0847 741  ARG A NH1   
4811 N  NH2   . ARG A 638 ? 1.7818 1.7070 1.9570 -0.1771 -0.0632 -0.0757 741  ARG A NH2   
4812 N  N     . PRO A 639 ? 1.5468 1.4016 1.6616 -0.0846 -0.0078 -0.0213 742  PRO A N     
4813 C  CA    . PRO A 639 ? 1.5556 1.4015 1.6518 -0.0632 -0.0046 -0.0187 742  PRO A CA    
4814 C  C     . PRO A 639 ? 1.5673 1.4255 1.6549 -0.0524 -0.0131 -0.0292 742  PRO A C     
4815 O  O     . PRO A 639 ? 1.5304 1.4024 1.6125 -0.0373 -0.0126 -0.0259 742  PRO A O     
4816 C  CB    . PRO A 639 ? 1.6087 1.4114 1.6882 -0.0612 0.0020  -0.0174 742  PRO A CB    
4817 C  CG    . PRO A 639 ? 1.7090 1.4961 1.7933 -0.0804 -0.0017 -0.0261 742  PRO A CG    
4818 C  CD    . PRO A 639 ? 1.6290 1.4487 1.7386 -0.0970 -0.0049 -0.0241 742  PRO A CD    
4819 N  N     . ASP A 640 ? 1.6019 1.4553 1.6875 -0.0603 -0.0206 -0.0418 743  ASP A N     
4820 C  CA    . ASP A 640 ? 1.5286 1.3922 1.6047 -0.0499 -0.0276 -0.0516 743  ASP A CA    
4821 C  C     . ASP A 640 ? 1.4722 1.3754 1.5605 -0.0479 -0.0324 -0.0500 743  ASP A C     
4822 O  O     . ASP A 640 ? 1.4586 1.3735 1.5391 -0.0352 -0.0351 -0.0532 743  ASP A O     
4823 C  CB    . ASP A 640 ? 1.7021 1.5512 1.7722 -0.0596 -0.0344 -0.0656 743  ASP A CB    
4824 C  CG    . ASP A 640 ? 1.8239 1.6831 1.9114 -0.0812 -0.0391 -0.0679 743  ASP A CG    
4825 O  OD1   . ASP A 640 ? 1.7762 1.6358 1.8768 -0.0908 -0.0338 -0.0584 743  ASP A OD1   
4826 O  OD2   . ASP A 640 ? 1.7804 1.6486 1.8685 -0.0886 -0.0481 -0.0788 743  ASP A OD2   
4827 N  N     . PHE A 641 ? 1.4233 1.3473 1.5307 -0.0600 -0.0330 -0.0448 744  PHE A N     
4828 C  CA    . PHE A 641 ? 1.3432 1.3024 1.4614 -0.0570 -0.0364 -0.0421 744  PHE A CA    
4829 C  C     . PHE A 641 ? 1.2999 1.2664 1.4167 -0.0447 -0.0292 -0.0309 744  PHE A C     
4830 O  O     . PHE A 641 ? 1.2329 1.2188 1.3479 -0.0354 -0.0314 -0.0305 744  PHE A O     
4831 C  CB    . PHE A 641 ? 1.2963 1.2763 1.4355 -0.0732 -0.0398 -0.0407 744  PHE A CB    
4832 C  CG    . PHE A 641 ? 1.2105 1.2249 1.3598 -0.0700 -0.0437 -0.0385 744  PHE A CG    
4833 C  CD1   . PHE A 641 ? 1.2032 1.2333 1.3610 -0.0652 -0.0376 -0.0272 744  PHE A CD1   
4834 C  CD2   . PHE A 641 ? 1.1584 1.1878 1.3069 -0.0714 -0.0531 -0.0476 744  PHE A CD2   
4835 C  CE1   . PHE A 641 ? 1.1415 1.2001 1.3070 -0.0616 -0.0406 -0.0252 744  PHE A CE1   
4836 C  CE2   . PHE A 641 ? 1.1083 1.1670 1.2647 -0.0679 -0.0562 -0.0449 744  PHE A CE2   
4837 C  CZ    . PHE A 641 ? 1.1322 1.2048 1.2972 -0.0630 -0.0499 -0.0337 744  PHE A CZ    
4838 N  N     . MET A 642 ? 1.3567 1.3069 1.4731 -0.0450 -0.0207 -0.0217 745  MET A N     
4839 C  CA    . MET A 642 ? 1.2703 1.2259 1.3833 -0.0334 -0.0139 -0.0112 745  MET A CA    
4840 C  C     . MET A 642 ? 1.2880 1.2358 1.3827 -0.0164 -0.0144 -0.0135 745  MET A C     
4841 O  O     . MET A 642 ? 1.2379 1.2005 1.3297 -0.0064 -0.0135 -0.0092 745  MET A O     
4842 C  CB    . MET A 642 ? 1.3930 1.3311 1.5081 -0.0375 -0.0043 -0.0007 745  MET A CB    
4843 C  CG    . MET A 642 ? 1.3980 1.3489 1.5339 -0.0537 -0.0023 0.0038  745  MET A CG    
4844 S  SD    . MET A 642 ? 1.5297 1.5169 1.6798 -0.0507 -0.0004 0.0120  745  MET A SD    
4845 C  CE    . MET A 642 ? 1.3171 1.2909 1.4536 -0.0372 0.0108  0.0244  745  MET A CE    
4846 N  N     . ASP A 643 ? 1.3537 1.2787 1.4358 -0.0130 -0.0159 -0.0205 746  ASP A N     
4847 C  CA    . ASP A 643 ? 1.3697 1.2891 1.4358 0.0038  -0.0161 -0.0222 746  ASP A CA    
4848 C  C     . ASP A 643 ? 1.2627 1.2052 1.3286 0.0084  -0.0234 -0.0301 746  ASP A C     
4849 O  O     . ASP A 643 ? 1.2782 1.2281 1.3358 0.0215  -0.0236 -0.0296 746  ASP A O     
4850 C  CB    . ASP A 643 ? 1.4570 1.3435 1.5091 0.0076  -0.0143 -0.0265 746  ASP A CB    
4851 C  CG    . ASP A 643 ? 1.6164 1.4764 1.6656 0.0047  -0.0060 -0.0175 746  ASP A CG    
4852 O  OD1   . ASP A 643 ? 1.5955 1.4640 1.6554 -0.0024 -0.0017 -0.0086 746  ASP A OD1   
4853 O  OD2   . ASP A 643 ? 1.6001 1.4301 1.6356 0.0100  -0.0031 -0.0191 746  ASP A OD2   
4854 N  N     . ALA A 644 ? 1.2291 1.1841 1.3041 -0.0025 -0.0294 -0.0373 747  ALA A N     
4855 C  CA    . ALA A 644 ? 1.2332 1.2088 1.3071 0.0011  -0.0358 -0.0444 747  ALA A CA    
4856 C  C     . ALA A 644 ? 1.1802 1.1839 1.2640 0.0007  -0.0367 -0.0392 747  ALA A C     
4857 O  O     . ALA A 644 ? 1.1561 1.1758 1.2365 0.0068  -0.0401 -0.0424 747  ALA A O     
4858 C  CB    . ALA A 644 ? 1.2398 1.2139 1.3156 -0.0091 -0.0423 -0.0551 747  ALA A CB    
4859 N  N     . LEU A 645 ? 1.1361 1.1453 1.2313 -0.0061 -0.0332 -0.0310 748  LEU A N     
4860 C  CA    . LEU A 645 ? 1.1187 1.1522 1.2226 -0.0063 -0.0333 -0.0259 748  LEU A CA    
4861 C  C     . LEU A 645 ? 1.1139 1.1474 1.2133 0.0026  -0.0268 -0.0165 748  LEU A C     
4862 O  O     . LEU A 645 ? 1.0966 1.1464 1.2020 0.0026  -0.0254 -0.0114 748  LEU A O     
4863 C  CB    . LEU A 645 ? 1.1230 1.1671 1.2439 -0.0193 -0.0341 -0.0235 748  LEU A CB    
4864 C  CG    . LEU A 645 ? 1.0868 1.1473 1.2143 -0.0264 -0.0424 -0.0311 748  LEU A CG    
4865 C  CD1   . LEU A 645 ? 1.0490 1.1284 1.1729 -0.0186 -0.0450 -0.0316 748  LEU A CD1   
4866 C  CD2   . LEU A 645 ? 1.1055 1.1513 1.2252 -0.0297 -0.0476 -0.0419 748  LEU A CD2   
4867 N  N     . GLN A 646 ? 1.1793 1.1945 1.2673 0.0106  -0.0230 -0.0141 749  GLN A N     
4868 C  CA    . GLN A 646 ? 1.1422 1.1563 1.2236 0.0195  -0.0174 -0.0055 749  GLN A CA    
4869 C  C     . GLN A 646 ? 1.1406 1.1491 1.2073 0.0324  -0.0188 -0.0080 749  GLN A C     
4870 O  O     . GLN A 646 ? 1.1792 1.1711 1.2392 0.0357  -0.0193 -0.0119 749  GLN A O     
4871 C  CB    . GLN A 646 ? 1.1167 1.1137 1.1996 0.0163  -0.0097 0.0033  749  GLN A CB    
4872 C  CG    . GLN A 646 ? 1.1516 1.1585 1.2507 0.0046  -0.0069 0.0080  749  GLN A CG    
4873 C  CD    . GLN A 646 ? 1.1962 1.1859 1.2974 0.0002  0.0014  0.0166  749  GLN A CD    
4874 O  OE1   . GLN A 646 ? 1.2063 1.2048 1.3173 -0.0044 0.0068  0.0243  749  GLN A OE1   
4875 N  NE2   . GLN A 646 ? 1.1559 1.1204 1.2475 0.0020  0.0031  0.0157  749  GLN A NE2   
4876 N  N     . GLY A 647 ? 1.0878 1.1103 1.1498 0.0397  -0.0195 -0.0058 750  GLY A N     
4877 C  CA    . GLY A 647 ? 1.1005 1.1222 1.1505 0.0519  -0.0210 -0.0072 750  GLY A CA    
4878 C  C     . GLY A 647 ? 1.1401 1.1764 1.1895 0.0540  -0.0272 -0.0160 750  GLY A C     
4879 O  O     . GLY A 647 ? 1.2108 1.2435 1.2528 0.0625  -0.0288 -0.0196 750  GLY A O     
4880 N  N     . PHE A 648 ? 1.0881 1.1411 1.1449 0.0471  -0.0302 -0.0190 751  PHE A N     
4881 C  CA    . PHE A 648 ? 1.0513 1.1189 1.1075 0.0480  -0.0354 -0.0265 751  PHE A CA    
4882 C  C     . PHE A 648 ? 1.0188 1.1046 1.0770 0.0460  -0.0365 -0.0248 751  PHE A C     
4883 O  O     . PHE A 648 ? 1.0154 1.1019 1.0759 0.0435  -0.0334 -0.0186 751  PHE A O     
4884 C  CB    . PHE A 648 ? 1.0631 1.1290 1.1244 0.0406  -0.0386 -0.0338 751  PHE A CB    
4885 C  CG    . PHE A 648 ? 1.0452 1.1181 1.1172 0.0299  -0.0394 -0.0324 751  PHE A CG    
4886 C  CD1   . PHE A 648 ? 1.0363 1.0992 1.1151 0.0236  -0.0361 -0.0276 751  PHE A CD1   
4887 C  CD2   . PHE A 648 ? 1.0163 1.1064 1.0916 0.0264  -0.0430 -0.0354 751  PHE A CD2   
4888 C  CE1   . PHE A 648 ? 1.0429 1.1157 1.1333 0.0144  -0.0370 -0.0259 751  PHE A CE1   
4889 C  CE2   . PHE A 648 ? 1.0218 1.1196 1.1069 0.0181  -0.0440 -0.0335 751  PHE A CE2   
4890 C  CZ    . PHE A 648 ? 1.0326 1.1232 1.1261 0.0123  -0.0411 -0.0289 751  PHE A CZ    
4891 N  N     . LEU A 649 ? 0.9898 1.0893 1.0462 0.0473  -0.0402 -0.0302 752  LEU A N     
4892 C  CA    . LEU A 649 ? 1.0071 1.1215 1.0631 0.0456  -0.0412 -0.0292 752  LEU A CA    
4893 C  C     . LEU A 649 ? 1.0124 1.1335 1.0754 0.0373  -0.0426 -0.0305 752  LEU A C     
4894 O  O     . LEU A 649 ? 1.0396 1.1601 1.1063 0.0335  -0.0451 -0.0352 752  LEU A O     
4895 C  CB    . LEU A 649 ? 0.9914 1.1180 1.0423 0.0503  -0.0441 -0.0336 752  LEU A CB    
4896 C  CG    . LEU A 649 ? 1.0242 1.1498 1.0687 0.0598  -0.0438 -0.0323 752  LEU A CG    
4897 C  CD1   . LEU A 649 ? 0.9909 1.1062 1.0341 0.0657  -0.0437 -0.0353 752  LEU A CD1   
4898 C  CD2   . LEU A 649 ? 0.9749 1.1184 1.0167 0.0616  -0.0465 -0.0347 752  LEU A CD2   
4899 N  N     . SER A 650 ? 1.0498 1.1768 1.1133 0.0351  -0.0410 -0.0263 753  SER A N     
4900 C  CA    . SER A 650 ? 1.0000 1.1341 1.0695 0.0289  -0.0420 -0.0262 753  SER A CA    
4901 C  C     . SER A 650 ? 1.0533 1.1977 1.1204 0.0276  -0.0460 -0.0322 753  SER A C     
4902 O  O     . SER A 650 ? 1.1064 1.2567 1.1670 0.0300  -0.0464 -0.0334 753  SER A O     
4903 C  CB    . SER A 650 ? 0.9943 1.1303 1.0628 0.0289  -0.0385 -0.0201 753  SER A CB    
4904 O  OG    . SER A 650 ? 1.0100 1.1534 1.0837 0.0246  -0.0393 -0.0195 753  SER A OG    
4905 N  N     . PRO A 651 ? 0.9724 1.1197 1.0440 0.0233  -0.0491 -0.0360 754  PRO A N     
4906 C  CA    . PRO A 651 ? 0.8990 1.0561 0.9668 0.0223  -0.0522 -0.0409 754  PRO A CA    
4907 C  C     . PRO A 651 ? 0.8555 1.0201 0.9208 0.0208  -0.0513 -0.0376 754  PRO A C     
4908 O  O     . PRO A 651 ? 0.8591 1.0305 0.9188 0.0207  -0.0522 -0.0403 754  PRO A O     
4909 C  CB    . PRO A 651 ? 0.8999 1.0568 0.9723 0.0179  -0.0558 -0.0449 754  PRO A CB    
4910 C  CG    . PRO A 651 ? 0.9229 1.0679 1.0002 0.0172  -0.0549 -0.0443 754  PRO A CG    
4911 C  CD    . PRO A 651 ? 0.9559 1.0972 1.0352 0.0191  -0.0502 -0.0367 754  PRO A CD    
4912 N  N     . LEU A 652 ? 0.8643 1.0271 0.9332 0.0197  -0.0489 -0.0317 755  LEU A N     
4913 C  CA    . LEU A 652 ? 0.8615 1.0278 0.9260 0.0193  -0.0472 -0.0284 755  LEU A CA    
4914 C  C     . LEU A 652 ? 0.9113 1.0757 0.9669 0.0215  -0.0450 -0.0281 755  LEU A C     
4915 O  O     . LEU A 652 ? 0.9375 1.1044 0.9866 0.0201  -0.0445 -0.0281 755  LEU A O     
4916 C  CB    . LEU A 652 ? 0.8515 1.0161 0.9220 0.0191  -0.0444 -0.0219 755  LEU A CB    
4917 C  CG    . LEU A 652 ? 0.9141 1.0848 0.9946 0.0160  -0.0471 -0.0213 755  LEU A CG    
4918 C  CD1   . LEU A 652 ? 0.9068 1.0780 0.9951 0.0169  -0.0434 -0.0141 755  LEU A CD1   
4919 C  CD2   . LEU A 652 ? 0.8293 1.0074 0.9060 0.0147  -0.0505 -0.0235 755  LEU A CD2   
4920 N  N     . ASN A 653 ? 0.9260 1.0855 0.9805 0.0247  -0.0439 -0.0278 756  ASN A N     
4921 C  CA    . ASN A 653 ? 0.8685 1.0280 0.9148 0.0268  -0.0431 -0.0279 756  ASN A CA    
4922 C  C     . ASN A 653 ? 0.9085 1.0653 0.9551 0.0314  -0.0437 -0.0290 756  ASN A C     
4923 O  O     . ASN A 653 ? 0.8931 1.0414 0.9411 0.0340  -0.0413 -0.0251 756  ASN A O     
4924 C  CB    . ASN A 653 ? 0.9176 1.0706 0.9586 0.0273  -0.0394 -0.0228 756  ASN A CB    
4925 C  CG    . ASN A 653 ? 0.9668 1.1204 0.9975 0.0276  -0.0396 -0.0240 756  ASN A CG    
4926 O  OD1   . ASN A 653 ? 0.9243 1.0841 0.9538 0.0287  -0.0424 -0.0275 756  ASN A OD1   
4927 N  ND2   . ASN A 653 ? 0.8778 1.0250 0.9007 0.0268  -0.0367 -0.0213 756  ASN A ND2   
4928 N  N     . PRO A 654 ? 0.8767 1.0408 0.9219 0.0333  -0.0463 -0.0336 757  PRO A N     
4929 C  CA    . PRO A 654 ? 0.9296 1.0908 0.9746 0.0395  -0.0467 -0.0343 757  PRO A CA    
4930 C  C     . PRO A 654 ? 0.9318 1.0897 0.9707 0.0435  -0.0456 -0.0303 757  PRO A C     
4931 O  O     . PRO A 654 ? 0.9614 1.1141 0.9993 0.0496  -0.0453 -0.0290 757  PRO A O     
4932 C  CB    . PRO A 654 ? 0.8369 1.0098 0.8818 0.0410  -0.0494 -0.0399 757  PRO A CB    
4933 C  CG    . PRO A 654 ? 0.8079 0.9905 0.8506 0.0351  -0.0499 -0.0410 757  PRO A CG    
4934 C  CD    . PRO A 654 ? 0.7838 0.9592 0.8274 0.0303  -0.0483 -0.0379 757  PRO A CD    
4935 N  N     . ALA A 655 ? 0.9150 1.0746 0.9483 0.0407  -0.0449 -0.0285 758  ALA A N     
4936 C  CA    . ALA A 655 ? 0.9155 1.0706 0.9410 0.0444  -0.0439 -0.0249 758  ALA A CA    
4937 C  C     . ALA A 655 ? 0.9948 1.1361 1.0205 0.0468  -0.0396 -0.0191 758  ALA A C     
4938 O  O     . ALA A 655 ? 1.0909 1.2264 1.1107 0.0520  -0.0384 -0.0157 758  ALA A O     
4939 C  CB    . ALA A 655 ? 0.8612 1.0194 0.8788 0.0400  -0.0443 -0.0255 758  ALA A CB    
4940 N  N     . HIS A 656 ? 0.9156 1.0528 0.9482 0.0430  -0.0371 -0.0176 759  HIS A N     
4941 C  CA    . HIS A 656 ? 0.8425 0.9692 0.8779 0.0440  -0.0324 -0.0117 759  HIS A CA    
4942 C  C     . HIS A 656 ? 0.9004 1.0215 0.9423 0.0458  -0.0325 -0.0118 759  HIS A C     
4943 O  O     . HIS A 656 ? 1.0351 1.1587 1.0847 0.0424  -0.0347 -0.0154 759  HIS A O     
4944 C  CB    . HIS A 656 ? 0.9289 1.0566 0.9705 0.0393  -0.0301 -0.0098 759  HIS A CB    
4945 C  CG    . HIS A 656 ? 0.9818 1.1109 1.0154 0.0382  -0.0290 -0.0094 759  HIS A CG    
4946 N  ND1   . HIS A 656 ? 1.0364 1.1680 1.0735 0.0349  -0.0279 -0.0087 759  HIS A ND1   
4947 C  CD2   . HIS A 656 ? 1.0099 1.1370 1.0312 0.0398  -0.0289 -0.0098 759  HIS A CD2   
4948 C  CE1   . HIS A 656 ? 1.0993 1.2283 1.1259 0.0349  -0.0265 -0.0086 759  HIS A CE1   
4949 N  NE2   . HIS A 656 ? 1.0814 1.2075 1.0982 0.0371  -0.0273 -0.0097 759  HIS A NE2   
4950 N  N     . GLN A 657 ? 0.9213 1.0333 0.9584 0.0511  -0.0302 -0.0077 760  GLN A N     
4951 C  CA    . GLN A 657 ? 0.9932 1.0954 1.0345 0.0528  -0.0292 -0.0069 760  GLN A CA    
4952 C  C     . GLN A 657 ? 0.9758 1.0705 1.0255 0.0479  -0.0244 -0.0021 760  GLN A C     
4953 O  O     . GLN A 657 ? 0.9733 1.0682 1.0228 0.0468  -0.0203 0.0029  760  GLN A O     
4954 C  CB    . GLN A 657 ? 0.9858 1.0803 1.0176 0.0613  -0.0282 -0.0037 760  GLN A CB    
4955 C  CG    . GLN A 657 ? 1.0211 1.1261 1.0466 0.0667  -0.0333 -0.0080 760  GLN A CG    
4956 C  CD    . GLN A 657 ? 1.2268 1.3252 1.2437 0.0765  -0.0330 -0.0045 760  GLN A CD    
4957 O  OE1   . GLN A 657 ? 1.2787 1.3618 1.2934 0.0793  -0.0286 0.0012  760  GLN A OE1   
4958 N  NE2   . GLN A 657 ? 1.2479 1.3583 1.2600 0.0819  -0.0376 -0.0073 760  GLN A NE2   
4959 N  N     . LEU A 658 ? 0.9539 1.0423 1.0110 0.0447  -0.0249 -0.0039 761  LEU A N     
4960 C  CA    . LEU A 658 ? 1.0101 1.0933 1.0776 0.0382  -0.0212 -0.0001 761  LEU A CA    
4961 C  C     . LEU A 658 ? 1.0574 1.1232 1.1228 0.0402  -0.0176 0.0035  761  LEU A C     
4962 O  O     . LEU A 658 ? 1.1496 1.2073 1.2156 0.0395  -0.0200 -0.0011 761  LEU A O     
4963 C  CB    . LEU A 658 ? 1.0361 1.1267 1.1142 0.0305  -0.0255 -0.0058 761  LEU A CB    
4964 C  CG    . LEU A 658 ? 0.9999 1.1061 1.0791 0.0288  -0.0290 -0.0090 761  LEU A CG    
4965 C  CD1   . LEU A 658 ? 1.0241 1.1368 1.1124 0.0219  -0.0336 -0.0142 761  LEU A CD1   
4966 C  CD2   . LEU A 658 ? 0.9832 1.0944 1.0635 0.0290  -0.0246 -0.0025 761  LEU A CD2   
4967 N  N     . GLY A 659 ? 1.0721 1.1305 1.1336 0.0430  -0.0113 0.0117  762  GLY A N     
4968 C  CA    . GLY A 659 ? 1.1075 1.1475 1.1655 0.0450  -0.0067 0.0166  762  GLY A CA    
4969 C  C     . GLY A 659 ? 1.1383 1.1719 1.2094 0.0349  -0.0034 0.0186  762  GLY A C     
4970 O  O     . GLY A 659 ? 1.1663 1.2048 1.2470 0.0275  -0.0079 0.0123  762  GLY A O     
4971 N  N     . ASN A 660 ? 1.2052 1.2285 1.2765 0.0341  0.0043  0.0274  763  ASN A N     
4972 C  CA    . ASN A 660 ? 1.1831 1.2018 1.2684 0.0231  0.0081  0.0302  763  ASN A CA    
4973 C  C     . ASN A 660 ? 1.1604 1.1996 1.2606 0.0161  0.0081  0.0310  763  ASN A C     
4974 O  O     . ASN A 660 ? 1.1647 1.2150 1.2619 0.0209  0.0100  0.0340  763  ASN A O     
4975 C  CB    . ASN A 660 ? 1.2259 1.2276 1.3067 0.0243  0.0174  0.0403  763  ASN A CB    
4976 C  CG    . ASN A 660 ? 1.2185 1.1972 1.2856 0.0307  0.0177  0.0402  763  ASN A CG    
4977 O  OD1   . ASN A 660 ? 1.2692 1.2467 1.3290 0.0365  0.0111  0.0328  763  ASN A OD1   
4978 N  ND2   . ASN A 660 ? 1.2851 1.2454 1.3484 0.0304  0.0259  0.0489  763  ASN A ND2   
4979 N  N     . LEU A 661 ? 1.1600 1.2037 1.2756 0.0048  0.0059  0.0282  764  LEU A N     
4980 C  CA    . LEU A 661 ? 1.1910 1.2562 1.3224 -0.0015 0.0049  0.0288  764  LEU A CA    
4981 C  C     . LEU A 661 ? 1.1113 1.1784 1.2557 -0.0080 0.0134  0.0382  764  LEU A C     
4982 O  O     . LEU A 661 ? 1.1044 1.1567 1.2515 -0.0140 0.0173  0.0411  764  LEU A O     
4983 C  CB    . LEU A 661 ? 1.2201 1.2936 1.3610 -0.0097 -0.0041 0.0196  764  LEU A CB    
4984 C  CG    . LEU A 661 ? 1.1781 1.2409 1.3273 -0.0211 -0.0058 0.0165  764  LEU A CG    
4985 C  CD1   . LEU A 661 ? 1.2426 1.3230 1.4132 -0.0328 -0.0060 0.0189  764  LEU A CD1   
4986 C  CD2   . LEU A 661 ? 1.1892 1.2454 1.3310 -0.0215 -0.0145 0.0051  764  LEU A CD2   
4987 N  N     . ARG A 662 ? 1.1165 1.2014 1.2688 -0.0066 0.0170  0.0433  765  ARG A N     
4988 C  CA    . ARG A 662 ? 1.1761 1.2677 1.3425 -0.0118 0.0260  0.0530  765  ARG A CA    
4989 C  C     . ARG A 662 ? 1.1365 1.2451 1.3258 -0.0245 0.0215  0.0505  765  ARG A C     
4990 O  O     . ARG A 662 ? 1.0858 1.2157 1.2846 -0.0242 0.0179  0.0492  765  ARG A O     
4991 C  CB    . ARG A 662 ? 1.2918 1.3940 1.4543 -0.0025 0.0325  0.0596  765  ARG A CB    
4992 C  CG    . ARG A 662 ? 1.3020 1.3888 1.4408 0.0095  0.0359  0.0613  765  ARG A CG    
4993 C  CD    . ARG A 662 ? 1.4276 1.5228 1.5613 0.0178  0.0427  0.0672  765  ARG A CD    
4994 N  NE    . ARG A 662 ? 1.5781 1.6592 1.6881 0.0285  0.0449  0.0682  765  ARG A NE    
4995 C  CZ    . ARG A 662 ? 1.6044 1.6720 1.7040 0.0326  0.0532  0.0757  765  ARG A CZ    
4996 N  NH1   . ARG A 662 ? 1.5727 1.6376 1.6834 0.0266  0.0613  0.0835  765  ARG A NH1   
4997 N  NH2   . ARG A 662 ? 1.5209 1.5777 1.5981 0.0425  0.0534  0.0756  765  ARG A NH2   
4998 N  N     . LEU A 663 ? 1.1411 1.2397 1.3385 -0.0358 0.0215  0.0499  766  LEU A N     
4999 C  CA    . LEU A 663 ? 1.1617 1.2754 1.3798 -0.0495 0.0155  0.0460  766  LEU A CA    
5000 C  C     . LEU A 663 ? 1.1927 1.3334 1.4320 -0.0529 0.0201  0.0539  766  LEU A C     
5001 O  O     . LEU A 663 ? 1.1324 1.2947 1.3881 -0.0597 0.0132  0.0505  766  LEU A O     
5002 C  CB    . LEU A 663 ? 1.1438 1.2383 1.3652 -0.0619 0.0160  0.0445  766  LEU A CB    
5003 C  CG    . LEU A 663 ? 1.1430 1.2127 1.3477 -0.0614 0.0095  0.0346  766  LEU A CG    
5004 C  CD1   . LEU A 663 ? 1.1802 1.2259 1.3627 -0.0488 0.0154  0.0380  766  LEU A CD1   
5005 C  CD2   . LEU A 663 ? 1.2421 1.2998 1.4558 -0.0775 0.0074  0.0309  766  LEU A CD2   
5006 N  N     . GLU A 664 ? 1.1697 1.3106 1.4088 -0.0474 0.0319  0.0646  767  GLU A N     
5007 C  CA    . GLU A 664 ? 1.1395 1.3069 1.3988 -0.0489 0.0378  0.0728  767  GLU A CA    
5008 C  C     . GLU A 664 ? 1.0875 1.2750 1.3468 -0.0393 0.0334  0.0709  767  GLU A C     
5009 O  O     . GLU A 664 ? 1.0565 1.2701 1.3355 -0.0412 0.0346  0.0752  767  GLU A O     
5010 C  CB    . GLU A 664 ? 1.2668 1.4275 1.5226 -0.0438 0.0526  0.0848  767  GLU A CB    
5011 C  CG    . GLU A 664 ? 1.2815 1.4294 1.5122 -0.0272 0.0571  0.0865  767  GLU A CG    
5012 C  CD    . GLU A 664 ? 1.3547 1.4728 1.5621 -0.0234 0.0551  0.0825  767  GLU A CD    
5013 O  OE1   . GLU A 664 ? 1.3646 1.4694 1.5741 -0.0328 0.0513  0.0786  767  GLU A OE1   
5014 O  OE2   . GLU A 664 ? 1.3892 1.4971 1.5755 -0.0107 0.0573  0.0831  767  GLU A OE2   
5015 N  N     . GLU A 665 ? 1.1059 1.2822 1.3441 -0.0289 0.0287  0.0648  768  GLU A N     
5016 C  CA    . GLU A 665 ? 1.1086 1.2997 1.3440 -0.0203 0.0244  0.0624  768  GLU A CA    
5017 C  C     . GLU A 665 ? 1.0635 1.2634 1.3033 -0.0255 0.0112  0.0527  768  GLU A C     
5018 O  O     . GLU A 665 ? 0.9844 1.1995 1.2257 -0.0202 0.0073  0.0515  768  GLU A O     
5019 C  CB    . GLU A 665 ? 1.1909 1.3660 1.4008 -0.0070 0.0269  0.0615  768  GLU A CB    
5020 C  CG    . GLU A 665 ? 1.2395 1.4102 1.4428 0.0012  0.0396  0.0711  768  GLU A CG    
5021 C  CD    . GLU A 665 ? 1.2563 1.4479 1.4701 0.0068  0.0447  0.0771  768  GLU A CD    
5022 O  OE1   . GLU A 665 ? 1.3444 1.5488 1.5615 0.0088  0.0378  0.0729  768  GLU A OE1   
5023 O  OE2   . GLU A 665 ? 1.2372 1.4319 1.4551 0.0099  0.0561  0.0864  768  GLU A OE2   
5024 N  N     . CYS A 666 ? 1.0520 1.2413 1.2923 -0.0353 0.0048  0.0458  769  CYS A N     
5025 C  CA    . CYS A 666 ? 0.9709 1.1675 1.2139 -0.0407 -0.0075 0.0362  769  CYS A CA    
5026 C  C     . CYS A 666 ? 0.9479 1.1705 1.2160 -0.0508 -0.0112 0.0380  769  CYS A C     
5027 O  O     . CYS A 666 ? 0.9613 1.1873 1.2452 -0.0611 -0.0074 0.0422  769  CYS A O     
5028 C  CB    . CYS A 666 ? 0.9969 1.1709 1.2295 -0.0468 -0.0124 0.0278  769  CYS A CB    
5029 S  SG    . CYS A 666 ? 1.0023 1.1485 1.2073 -0.0348 -0.0088 0.0260  769  CYS A SG    
5030 N  N     . ARG A 667 ? 0.9134 1.1551 1.1855 -0.0479 -0.0187 0.0351  770  ARG A N     
5031 C  CA    . ARG A 667 ? 0.9080 1.1786 1.2042 -0.0554 -0.0230 0.0375  770  ARG A CA    
5032 C  C     . ARG A 667 ? 0.9396 1.2213 1.2334 -0.0556 -0.0357 0.0294  770  ARG A C     
5033 O  O     . ARG A 667 ? 0.8309 1.1015 1.1052 -0.0473 -0.0389 0.0243  770  ARG A O     
5034 C  CB    . ARG A 667 ? 0.7763 1.0672 1.0847 -0.0472 -0.0142 0.0489  770  ARG A CB    
5035 C  CG    . ARG A 667 ? 0.8640 1.1527 1.1558 -0.0311 -0.0120 0.0503  770  ARG A CG    
5036 C  CD    . ARG A 667 ? 0.8899 1.1954 1.1918 -0.0221 -0.0021 0.0614  770  ARG A CD    
5037 N  NE    . ARG A 667 ? 0.9395 1.2353 1.2214 -0.0071 0.0018  0.0624  770  ARG A NE    
5038 C  CZ    . ARG A 667 ? 0.9886 1.2952 1.2677 0.0007  -0.0028 0.0618  770  ARG A CZ    
5039 N  NH1   . ARG A 667 ? 0.8936 1.2229 1.1882 -0.0037 -0.0117 0.0605  770  ARG A NH1   
5040 N  NH2   . ARG A 667 ? 0.9998 1.2934 1.2590 0.0131  0.0016  0.0626  770  ARG A NH2   
5041 N  N     . ILE A 668 ? 0.9385 1.2433 1.2524 -0.0657 -0.0430 0.0286  771  ILE A N     
5042 C  CA    . ILE A 668 ? 0.9200 1.2406 1.2340 -0.0657 -0.0551 0.0226  771  ILE A CA    
5043 C  C     . ILE A 668 ? 0.9150 1.2604 1.2375 -0.0544 -0.0529 0.0311  771  ILE A C     
5044 O  O     . ILE A 668 ? 0.8838 1.2510 1.2278 -0.0558 -0.0482 0.0397  771  ILE A O     
5045 C  CB    . ILE A 668 ? 0.8852 1.2186 1.2154 -0.0824 -0.0653 0.0168  771  ILE A CB    
5046 C  CG1   . ILE A 668 ? 0.8670 1.1714 1.1864 -0.0928 -0.0666 0.0082  771  ILE A CG1   
5047 C  CG2   . ILE A 668 ? 0.9050 1.2563 1.2342 -0.0813 -0.0781 0.0112  771  ILE A CG2   
5048 C  CD1   . ILE A 668 ? 0.9162 1.2288 1.2514 -0.1114 -0.0748 0.0027  771  ILE A CD1   
5049 N  N     . MET A 669 ? 0.9294 1.2710 1.2348 -0.0429 -0.0556 0.0291  772  MET A N     
5050 C  CA    . MET A 669 ? 0.9763 1.3353 1.2851 -0.0301 -0.0522 0.0373  772  MET A CA    
5051 C  C     . MET A 669 ? 1.1464 1.5388 1.4760 -0.0336 -0.0609 0.0394  772  MET A C     
5052 O  O     . MET A 669 ? 1.1801 1.5797 1.5138 -0.0440 -0.0724 0.0319  772  MET A O     
5053 C  CB    . MET A 669 ? 0.9725 1.3160 1.2563 -0.0184 -0.0529 0.0342  772  MET A CB    
5054 C  CG    . MET A 669 ? 0.9218 1.2352 1.1850 -0.0147 -0.0457 0.0318  772  MET A CG    
5055 S  SD    . MET A 669 ? 0.9191 1.2176 1.1557 -0.0023 -0.0458 0.0291  772  MET A SD    
5056 C  CE    . MET A 669 ? 0.8842 1.1983 1.1268 0.0107  -0.0388 0.0404  772  MET A CE    
5057 N  N     . SER A 670 ? 1.3113 1.7247 1.6536 -0.0240 -0.0553 0.0496  773  SER A N     
5058 C  CA    . SER A 670 ? 1.3443 1.7929 1.7070 -0.0241 -0.0629 0.0535  773  SER A CA    
5059 C  C     . SER A 670 ? 1.2953 1.7470 1.6434 -0.0136 -0.0705 0.0517  773  SER A C     
5060 O  O     . SER A 670 ? 1.3039 1.7797 1.6621 -0.0043 -0.0715 0.0590  773  SER A O     
5061 C  CB    . SER A 670 ? 1.3689 1.8399 1.7525 -0.0172 -0.0525 0.0661  773  SER A CB    
5062 O  OG    . SER A 670 ? 1.4992 1.9568 1.8667 0.0001  -0.0420 0.0720  773  SER A OG    
5063 N  N     . SER A 671 ? 1.2949 1.7226 1.6190 -0.0144 -0.0754 0.0425  774  SER A N     
5064 C  CA    . SER A 671 ? 1.3418 1.7686 1.6492 -0.0056 -0.0819 0.0404  774  SER A CA    
5065 C  C     . SER A 671 ? 1.4290 1.8639 1.7364 -0.0165 -0.0966 0.0311  774  SER A C     
5066 O  O     . SER A 671 ? 1.4817 1.9296 1.8066 -0.0301 -0.1025 0.0278  774  SER A O     
5067 C  CB    . SER A 671 ? 1.3556 1.7500 1.6353 0.0023  -0.0751 0.0378  774  SER A CB    
5068 O  OG    . SER A 671 ? 1.2906 1.6772 1.5690 0.0119  -0.0621 0.0458  774  SER A OG    
5069 N  N     . ALA A 672 ? 1.4327 1.8588 1.7195 -0.0110 -0.1024 0.0266  775  ALA A N     
5070 C  CA    . ALA A 672 ? 1.4996 1.9329 1.7827 -0.0194 -0.1162 0.0178  775  ALA A CA    
5071 C  C     . ALA A 672 ? 1.5177 1.9259 1.7881 -0.0303 -0.1179 0.0061  775  ALA A C     
5072 O  O     . ALA A 672 ? 1.4669 1.8491 1.7216 -0.0268 -0.1098 0.0043  775  ALA A O     
5073 C  CB    . ALA A 672 ? 1.5132 1.9475 1.7783 -0.0083 -0.1208 0.0187  775  ALA A CB    
5074 N  N     . LYS A 673 ? 1.4535 1.8699 1.7307 -0.0435 -0.1286 -0.0019 776  LYS A N     
5075 C  CA    . LYS A 673 ? 1.4170 1.8104 1.6814 -0.0538 -0.1318 -0.0140 776  LYS A CA    
5076 C  C     . LYS A 673 ? 1.2929 1.6652 1.5599 -0.0585 -0.1217 -0.0142 776  LYS A C     
5077 O  O     . LYS A 673 ? 1.2284 1.5755 1.4800 -0.0620 -0.1208 -0.0225 776  LYS A O     
5078 C  CB    . LYS A 673 ? 1.3390 1.7142 1.5754 -0.0466 -0.1335 -0.0202 776  LYS A CB    
5079 C  CG    . LYS A 673 ? 1.3504 1.7427 1.5803 -0.0441 -0.1448 -0.0220 776  LYS A CG    
5080 C  CD    . LYS A 673 ? 1.2761 1.6491 1.4782 -0.0390 -0.1459 -0.0289 776  LYS A CD    
5081 C  CE    . LYS A 673 ? 1.2431 1.6323 1.4370 -0.0367 -0.1572 -0.0307 776  LYS A CE    
5082 N  NZ    . LYS A 673 ? 1.3336 1.7377 1.5376 -0.0497 -0.1698 -0.0382 776  LYS A NZ    
5083 N  N     . ARG A 674 ? 1.2515 1.6339 1.5374 -0.0579 -0.1137 -0.0047 777  ARG A N     
5084 C  CA    . ARG A 674 ? 1.1410 1.5069 1.4321 -0.0632 -0.1042 -0.0033 777  ARG A CA    
5085 C  C     . ARG A 674 ? 1.0572 1.3914 1.3251 -0.0562 -0.0967 -0.0063 777  ARG A C     
5086 O  O     . ARG A 674 ? 1.0439 1.3572 1.3015 -0.0628 -0.0982 -0.0148 777  ARG A O     
5087 C  CB    . ARG A 674 ? 1.1296 1.4939 1.4310 -0.0809 -0.1104 -0.0107 777  ARG A CB    
5088 C  CG    . ARG A 674 ? 1.2078 1.6055 1.5345 -0.0904 -0.1186 -0.0083 777  ARG A CG    
5089 C  CD    . ARG A 674 ? 1.2933 1.7116 1.6432 -0.0871 -0.1095 0.0048  777  ARG A CD    
5090 N  NE    . ARG A 674 ? 1.4216 1.8774 1.7972 -0.0939 -0.1176 0.0082  777  ARG A NE    
5091 C  CZ    . ARG A 674 ? 1.4517 1.9343 1.8330 -0.0837 -0.1221 0.0139  777  ARG A CZ    
5092 N  NH1   . ARG A 674 ? 1.3494 1.8237 1.7121 -0.0669 -0.1188 0.0168  777  ARG A NH1   
5093 N  NH2   . ARG A 674 ? 1.3271 1.8458 1.7335 -0.0907 -0.1301 0.0169  777  ARG A NH2   
5094 N  N     . PRO A 675 ? 1.0350 1.3647 1.2939 -0.0429 -0.0887 0.0003  778  PRO A N     
5095 C  CA    . PRO A 675 ? 1.0094 1.3117 1.2482 -0.0371 -0.0818 -0.0022 778  PRO A CA    
5096 C  C     . PRO A 675 ? 0.9673 1.2557 1.2112 -0.0408 -0.0729 0.0006  778  PRO A C     
5097 O  O     . PRO A 675 ? 0.9201 1.2202 1.1816 -0.0430 -0.0678 0.0082  778  PRO A O     
5098 C  CB    . PRO A 675 ? 1.0137 1.3181 1.2435 -0.0233 -0.0764 0.0045  778  PRO A CB    
5099 C  CG    . PRO A 675 ? 1.0835 1.4143 1.3249 -0.0209 -0.0822 0.0090  778  PRO A CG    
5100 C  CD    . PRO A 675 ? 1.1062 1.4551 1.3710 -0.0322 -0.0864 0.0096  778  PRO A CD    
5101 N  N     . LEU A 676 ? 0.9493 1.2131 1.1773 -0.0408 -0.0708 -0.0052 779  LEU A N     
5102 C  CA    . LEU A 676 ? 0.8993 1.1464 1.1280 -0.0429 -0.0625 -0.0027 779  LEU A CA    
5103 C  C     . LEU A 676 ? 0.8980 1.1375 1.1173 -0.0311 -0.0527 0.0043  779  LEU A C     
5104 O  O     . LEU A 676 ? 0.9002 1.1294 1.1020 -0.0235 -0.0526 0.0012  779  LEU A O     
5105 C  CB    . LEU A 676 ? 0.9037 1.1278 1.1194 -0.0475 -0.0650 -0.0119 779  LEU A CB    
5106 C  CG    . LEU A 676 ? 0.9279 1.1497 1.1532 -0.0615 -0.0705 -0.0176 779  LEU A CG    
5107 C  CD1   . LEU A 676 ? 0.9855 1.1796 1.1948 -0.0628 -0.0705 -0.0257 779  LEU A CD1   
5108 C  CD2   . LEU A 676 ? 0.9500 1.1796 1.1956 -0.0690 -0.0649 -0.0096 779  LEU A CD2   
5109 N  N     . TRP A 677 ? 0.8978 1.1427 1.1286 -0.0301 -0.0444 0.0133  780  TRP A N     
5110 C  CA    . TRP A 677 ? 0.8962 1.1312 1.1172 -0.0199 -0.0344 0.0196  780  TRP A CA    
5111 C  C     . TRP A 677 ? 0.9024 1.1154 1.1157 -0.0220 -0.0293 0.0188  780  TRP A C     
5112 O  O     . TRP A 677 ? 0.9126 1.1249 1.1379 -0.0289 -0.0252 0.0226  780  TRP A O     
5113 C  CB    . TRP A 677 ? 0.9214 1.1732 1.1569 -0.0162 -0.0272 0.0300  780  TRP A CB    
5114 C  CG    . TRP A 677 ? 0.9481 1.1892 1.1721 -0.0056 -0.0167 0.0362  780  TRP A CG    
5115 C  CD1   . TRP A 677 ? 0.9614 1.1867 1.1796 -0.0049 -0.0086 0.0394  780  TRP A CD1   
5116 C  CD2   . TRP A 677 ? 0.9792 1.2233 1.1945 0.0058  -0.0131 0.0400  780  TRP A CD2   
5117 N  NE1   . TRP A 677 ? 0.9777 1.1968 1.1837 0.0060  -0.0008 0.0442  780  TRP A NE1   
5118 C  CE2   . TRP A 677 ? 0.9683 1.1978 1.1722 0.0124  -0.0032 0.0444  780  TRP A CE2   
5119 C  CE3   . TRP A 677 ? 0.9276 1.1836 1.1421 0.0112  -0.0172 0.0401  780  TRP A CE3   
5120 C  CZ2   . TRP A 677 ? 0.9793 1.2051 1.1710 0.0234  0.0025  0.0480  780  TRP A CZ2   
5121 C  CZ3   . TRP A 677 ? 0.9590 1.2102 1.1616 0.0225  -0.0109 0.0443  780  TRP A CZ3   
5122 C  CH2   . TRP A 677 ? 1.0301 1.2660 1.2213 0.0282  -0.0013 0.0478  780  TRP A CH2   
5123 N  N     . LEU A 678 ? 0.8974 1.0931 1.0912 -0.0162 -0.0294 0.0143  781  LEU A N     
5124 C  CA    . LEU A 678 ? 0.9440 1.1186 1.1284 -0.0163 -0.0256 0.0132  781  LEU A CA    
5125 C  C     . LEU A 678 ? 0.9874 1.1530 1.1593 -0.0064 -0.0174 0.0188  781  LEU A C     
5126 O  O     . LEU A 678 ? 0.9867 1.1564 1.1500 0.0010  -0.0172 0.0192  781  LEU A O     
5127 C  CB    . LEU A 678 ? 0.9752 1.1378 1.1472 -0.0172 -0.0326 0.0032  781  LEU A CB    
5128 C  CG    . LEU A 678 ? 0.9408 1.1077 1.1213 -0.0274 -0.0408 -0.0038 781  LEU A CG    
5129 C  CD1   . LEU A 678 ? 0.9568 1.1076 1.1231 -0.0269 -0.0453 -0.0131 781  LEU A CD1   
5130 C  CD2   . LEU A 678 ? 0.9505 1.1180 1.1473 -0.0376 -0.0382 0.0000  781  LEU A CD2   
5131 N  N     . ASN A 679 ? 1.0105 1.1628 1.1802 -0.0064 -0.0108 0.0231  782  ASN A N     
5132 C  CA    . ASN A 679 ? 1.0299 1.1734 1.1874 0.0026  -0.0028 0.0290  782  ASN A CA    
5133 C  C     . ASN A 679 ? 1.0663 1.1892 1.2112 0.0043  -0.0013 0.0277  782  ASN A C     
5134 O  O     . ASN A 679 ? 1.0946 1.2089 1.2454 -0.0010 0.0021  0.0306  782  ASN A O     
5135 C  CB    . ASN A 679 ? 1.1050 1.2566 1.2739 0.0026  0.0064  0.0390  782  ASN A CB    
5136 C  CG    . ASN A 679 ? 1.1594 1.3031 1.3137 0.0128  0.0146  0.0447  782  ASN A CG    
5137 O  OD1   . ASN A 679 ? 1.1617 1.2892 1.3005 0.0170  0.0162  0.0441  782  ASN A OD1   
5138 N  ND2   . ASN A 679 ? 1.1894 1.3448 1.3478 0.0174  0.0197  0.0501  782  ASN A ND2   
5139 N  N     . TRP A 680 ? 1.0878 1.2033 1.2158 0.0116  -0.0038 0.0236  783  TRP A N     
5140 C  CA    . TRP A 680 ? 1.1147 1.2128 1.2292 0.0162  -0.0022 0.0234  783  TRP A CA    
5141 C  C     . TRP A 680 ? 1.1429 1.2361 1.2451 0.0246  0.0046  0.0299  783  TRP A C     
5142 O  O     . TRP A 680 ? 1.1144 1.2164 1.2152 0.0277  0.0068  0.0321  783  TRP A O     
5143 C  CB    . TRP A 680 ? 1.0818 1.1771 1.1863 0.0191  -0.0098 0.0146  783  TRP A CB    
5144 C  CG    . TRP A 680 ? 1.0975 1.1929 1.2094 0.0122  -0.0161 0.0075  783  TRP A CG    
5145 C  CD1   . TRP A 680 ? 1.0981 1.1790 1.2092 0.0096  -0.0166 0.0051  783  TRP A CD1   
5146 C  CD2   . TRP A 680 ? 1.0929 1.2018 1.2119 0.0074  -0.0226 0.0017  783  TRP A CD2   
5147 N  NE1   . TRP A 680 ? 1.1110 1.1952 1.2279 0.0031  -0.0232 -0.0026 783  TRP A NE1   
5148 C  CE2   . TRP A 680 ? 1.0772 1.1796 1.1991 0.0017  -0.0272 -0.0047 783  TRP A CE2   
5149 C  CE3   . TRP A 680 ? 1.0487 1.1733 1.1704 0.0079  -0.0248 0.0014  783  TRP A CE3   
5150 C  CZ2   . TRP A 680 ? 1.0615 1.1738 1.1886 -0.0036 -0.0342 -0.0115 783  TRP A CZ2   
5151 C  CZ3   . TRP A 680 ? 0.9946 1.1291 1.1219 0.0031  -0.0316 -0.0045 783  TRP A CZ3   
5152 C  CH2   . TRP A 680 ? 1.0361 1.1652 1.1660 -0.0027 -0.0365 -0.0110 783  TRP A CH2   
5153 N  N     . GLU A 681 ? 1.2726 1.3507 1.3645 0.0287  0.0078  0.0327  784  GLU A N     
5154 C  CA    . GLU A 681 ? 1.3281 1.4002 1.4047 0.0374  0.0129  0.0377  784  GLU A CA    
5155 C  C     . GLU A 681 ? 1.2651 1.3354 1.3266 0.0438  0.0065  0.0316  784  GLU A C     
5156 O  O     . GLU A 681 ? 1.2696 1.3371 1.3308 0.0433  0.0007  0.0259  784  GLU A O     
5157 C  CB    . GLU A 681 ? 1.3493 1.4066 1.4221 0.0390  0.0206  0.0459  784  GLU A CB    
5158 C  CG    . GLU A 681 ? 1.4598 1.5017 1.5220 0.0430  0.0181  0.0442  784  GLU A CG    
5159 C  CD    . GLU A 681 ? 1.6403 1.6659 1.6965 0.0454  0.0266  0.0535  784  GLU A CD    
5160 O  OE1   . GLU A 681 ? 1.5032 1.5305 1.5654 0.0427  0.0348  0.0610  784  GLU A OE1   
5161 O  OE2   . GLU A 681 ? 1.6914 1.7025 1.7366 0.0507  0.0256  0.0537  784  GLU A OE2   
5162 N  N     . ASN A 682 ? 1.1227 1.1951 1.1719 0.0496  0.0076  0.0326  785  ASN A N     
5163 C  CA    . ASN A 682 ? 1.0450 1.1182 1.0805 0.0547  0.0017  0.0273  785  ASN A CA    
5164 C  C     . ASN A 682 ? 1.0810 1.1424 1.1044 0.0617  0.0029  0.0307  785  ASN A C     
5165 O  O     . ASN A 682 ? 1.1783 1.2324 1.1920 0.0661  0.0089  0.0374  785  ASN A O     
5166 C  CB    . ASN A 682 ? 1.0089 1.0875 1.0351 0.0569  0.0021  0.0266  785  ASN A CB    
5167 C  CG    . ASN A 682 ? 0.9634 1.0459 0.9780 0.0596  -0.0049 0.0202  785  ASN A CG    
5168 O  OD1   . ASN A 682 ? 0.9530 1.0341 0.9638 0.0627  -0.0090 0.0180  785  ASN A OD1   
5169 N  ND2   . ASN A 682 ? 1.0007 1.0883 1.0097 0.0585  -0.0061 0.0173  785  ASN A ND2   
5170 N  N     . PRO A 683 ? 1.0548 1.1136 1.0771 0.0637  -0.0023 0.0266  786  PRO A N     
5171 C  CA    . PRO A 683 ? 1.0412 1.0883 1.0518 0.0717  -0.0012 0.0305  786  PRO A CA    
5172 C  C     . PRO A 683 ? 1.0333 1.0846 1.0278 0.0795  -0.0044 0.0300  786  PRO A C     
5173 O  O     . PRO A 683 ? 1.0650 1.1093 1.0492 0.0874  -0.0052 0.0327  786  PRO A O     
5174 C  CB    . PRO A 683 ? 1.0492 1.0935 1.0654 0.0716  -0.0058 0.0254  786  PRO A CB    
5175 C  CG    . PRO A 683 ? 1.0410 1.1005 1.0651 0.0664  -0.0120 0.0169  786  PRO A CG    
5176 C  CD    . PRO A 683 ? 1.0397 1.1060 1.0709 0.0597  -0.0089 0.0185  786  PRO A CD    
5177 N  N     . ASP A 684 ? 1.0530 1.1147 1.0441 0.0774  -0.0066 0.0266  787  ASP A N     
5178 C  CA    . ASP A 684 ? 1.1452 1.2108 1.1204 0.0830  -0.0102 0.0255  787  ASP A CA    
5179 C  C     . ASP A 684 ? 1.2204 1.2749 1.1818 0.0885  -0.0037 0.0335  787  ASP A C     
5180 O  O     . ASP A 684 ? 1.0981 1.1462 1.0625 0.0861  0.0041  0.0388  787  ASP A O     
5181 C  CB    . ASP A 684 ? 1.1371 1.2141 1.1120 0.0778  -0.0138 0.0193  787  ASP A CB    
5182 C  CG    . ASP A 684 ? 1.2818 1.3657 1.2426 0.0812  -0.0199 0.0157  787  ASP A CG    
5183 O  OD1   . ASP A 684 ? 1.4104 1.4881 1.3564 0.0872  -0.0186 0.0199  787  ASP A OD1   
5184 O  OD2   . ASP A 684 ? 1.2299 1.3259 1.1942 0.0773  -0.0262 0.0088  787  ASP A OD2   
5185 N  N     . ILE A 685 ? 1.2199 1.2733 1.1658 0.0963  -0.0070 0.0347  788  ILE A N     
5186 C  CA    . ILE A 685 ? 1.2781 1.3204 1.2078 0.1026  -0.0012 0.0424  788  ILE A CA    
5187 C  C     . ILE A 685 ? 1.2303 1.2728 1.1522 0.0997  0.0025  0.0420  788  ILE A C     
5188 O  O     . ILE A 685 ? 1.3086 1.3411 1.2243 0.1018  0.0113  0.0489  788  ILE A O     
5189 C  CB    . ILE A 685 ? 1.3414 1.3848 1.2552 0.1121  -0.0071 0.0432  788  ILE A CB    
5190 C  CG1   . ILE A 685 ? 1.4298 1.4903 1.3413 0.1103  -0.0173 0.0342  788  ILE A CG1   
5191 C  CG2   . ILE A 685 ? 1.2491 1.2861 1.1676 0.1177  -0.0074 0.0467  788  ILE A CG2   
5192 N  N     . MET A 686 ? 1.1487 1.2017 1.0702 0.0952  -0.0035 0.0340  789  MET A N     
5193 C  CA    . MET A 686 ? 1.2191 1.2702 1.1324 0.0924  -0.0002 0.0325  789  MET A CA    
5194 C  C     . MET A 686 ? 1.2183 1.2734 1.1484 0.0850  0.0026  0.0303  789  MET A C     
5195 O  O     . MET A 686 ? 1.2511 1.3089 1.1780 0.0812  0.0013  0.0255  789  MET A O     
5196 C  CB    . MET A 686 ? 1.2523 1.3096 1.1510 0.0919  -0.0083 0.0254  789  MET A CB    
5197 C  CG    . MET A 686 ? 1.3508 1.4060 1.2311 0.0996  -0.0119 0.0275  789  MET A CG    
5198 S  SD    . MET A 686 ? 1.5100 1.5739 1.3734 0.0969  -0.0220 0.0186  789  MET A SD    
5199 C  CE    . MET A 686 ? 1.3443 1.4063 1.1877 0.1079  -0.0255 0.0234  789  MET A CE    
5200 N  N     . SER A 687 ? 1.2311 1.2859 1.1786 0.0828  0.0063  0.0339  790  SER A N     
5201 C  CA    . SER A 687 ? 1.1364 1.1974 1.1009 0.0760  0.0075  0.0319  790  SER A CA    
5202 C  C     . SER A 687 ? 1.1576 1.2155 1.1189 0.0761  0.0151  0.0350  790  SER A C     
5203 O  O     . SER A 687 ? 1.1555 1.2192 1.1245 0.0719  0.0146  0.0319  790  SER A O     
5204 C  CB    . SER A 687 ? 1.0639 1.1247 1.0463 0.0732  0.0098  0.0353  790  SER A CB    
5205 O  OG    . SER A 687 ? 1.1559 1.2067 1.1360 0.0765  0.0182  0.0441  790  SER A OG    
5206 N  N     . GLU A 688 ? 1.2161 1.2645 1.1650 0.0817  0.0226  0.0415  791  GLU A N     
5207 C  CA    . GLU A 688 ? 1.2609 1.3059 1.2061 0.0835  0.0313  0.0450  791  GLU A CA    
5208 C  C     . GLU A 688 ? 1.2423 1.2864 1.1747 0.0829  0.0279  0.0382  791  GLU A C     
5209 O  O     . GLU A 688 ? 1.1197 1.1633 1.0541 0.0830  0.0332  0.0390  791  GLU A O     
5210 C  CB    . GLU A 688 ? 1.3431 1.3773 1.2742 0.0905  0.0402  0.0529  791  GLU A CB    
5211 C  CG    . GLU A 688 ? 1.4190 1.4458 1.3263 0.0957  0.0357  0.0509  791  GLU A CG    
5212 C  CD    . GLU A 688 ? 1.7671 1.7824 1.6577 0.1033  0.0450  0.0590  791  GLU A CD    
5213 O  OE1   . GLU A 688 ? 1.9045 1.9182 1.8040 0.1041  0.0556  0.0667  791  GLU A OE1   
5214 O  OE2   . GLU A 688 ? 1.7393 1.7483 1.6079 0.1084  0.0417  0.0578  791  GLU A OE2   
5215 N  N     . LEU A 689 ? 1.2202 1.2641 1.1395 0.0823  0.0194  0.0317  792  LEU A N     
5216 C  CA    . LEU A 689 ? 1.2229 1.2640 1.1285 0.0803  0.0160  0.0248  792  LEU A CA    
5217 C  C     . LEU A 689 ? 1.2675 1.3167 1.1869 0.0735  0.0120  0.0197  792  LEU A C     
5218 O  O     . LEU A 689 ? 1.3781 1.4226 1.2877 0.0713  0.0114  0.0153  792  LEU A O     
5219 C  CB    . LEU A 689 ? 1.3340 1.3750 1.2230 0.0805  0.0076  0.0195  792  LEU A CB    
5220 C  CG    . LEU A 689 ? 1.3414 1.3741 1.2125 0.0880  0.0102  0.0241  792  LEU A CG    
5221 C  CD1   . LEU A 689 ? 1.2223 1.2588 1.0789 0.0877  0.0000  0.0183  792  LEU A CD1   
5222 C  CD2   . LEU A 689 ? 1.2236 1.2426 1.0784 0.0926  0.0200  0.0274  792  LEU A CD2   
5223 N  N     . LEU A 690 ? 1.1879 1.2475 1.1281 0.0700  0.0093  0.0202  793  LEU A N     
5224 C  CA    . LEU A 690 ? 1.1382 1.2059 1.0914 0.0642  0.0058  0.0162  793  LEU A CA    
5225 C  C     . LEU A 690 ? 1.1184 1.1903 1.0896 0.0641  0.0116  0.0217  793  LEU A C     
5226 O  O     . LEU A 690 ? 1.1390 1.2091 1.1103 0.0652  0.0164  0.0235  793  LEU A O     
5227 C  CB    . LEU A 690 ? 1.1675 1.2454 1.1285 0.0598  -0.0033 0.0108  793  LEU A CB    
5228 C  CG    . LEU A 690 ? 1.0565 1.1424 1.0255 0.0536  -0.0081 0.0054  793  LEU A CG    
5229 C  CD1   . LEU A 690 ? 0.9337 1.0141 0.8872 0.0511  -0.0093 0.0009  793  LEU A CD1   
5230 C  CD2   . LEU A 690 ? 1.0294 1.1259 1.0072 0.0509  -0.0155 0.0012  793  LEU A CD2   
5231 N  N     . PHE A 691 ? 1.0452 1.1227 1.0315 0.0629  0.0111  0.0245  794  PHE A N     
5232 C  CA    . PHE A 691 ? 1.0220 1.1046 1.0260 0.0619  0.0164  0.0302  794  PHE A CA    
5233 C  C     . PHE A 691 ? 0.9622 1.0442 0.9747 0.0612  0.0169  0.0335  794  PHE A C     
5234 O  O     . PHE A 691 ? 0.9753 1.0568 0.9859 0.0603  0.0108  0.0297  794  PHE A O     
5235 C  CB    . PHE A 691 ? 1.1633 1.2565 1.1817 0.0568  0.0123  0.0270  794  PHE A CB    
5236 C  CG    . PHE A 691 ? 1.1060 1.2050 1.1295 0.0520  0.0033  0.0204  794  PHE A CG    
5237 C  CD1   . PHE A 691 ? 1.0266 1.1260 1.0401 0.0505  -0.0025 0.0139  794  PHE A CD1   
5238 C  CD2   . PHE A 691 ? 1.0634 1.1671 1.1014 0.0486  0.0010  0.0205  794  PHE A CD2   
5239 C  CE1   . PHE A 691 ? 1.0563 1.1625 1.0747 0.0467  -0.0098 0.0082  794  PHE A CE1   
5240 C  CE2   . PHE A 691 ? 1.0973 1.2053 1.1384 0.0453  -0.0065 0.0142  794  PHE A CE2   
5241 C  CZ    . PHE A 691 ? 1.1064 1.2166 1.1380 0.0448  -0.0117 0.0083  794  PHE A CZ    
5242 N  N     . GLN A 692 ? 0.9966 1.0785 1.0186 0.0617  0.0247  0.0410  795  GLN A N     
5243 C  CA    . GLN A 692 ? 1.1771 1.2550 1.2055 0.0606  0.0269  0.0453  795  GLN A CA    
5244 C  C     . GLN A 692 ? 1.1760 1.2619 1.2257 0.0530  0.0237  0.0441  795  GLN A C     
5245 O  O     . GLN A 692 ? 1.1830 1.2636 1.2357 0.0508  0.0216  0.0437  795  GLN A O     
5246 C  CB    . GLN A 692 ? 1.2350 1.3072 1.2606 0.0646  0.0381  0.0547  795  GLN A CB    
5247 C  CG    . GLN A 692 ? 1.3535 1.4169 1.3799 0.0645  0.0414  0.0600  795  GLN A CG    
5248 C  CD    . GLN A 692 ? 1.6748 1.7304 1.6920 0.0700  0.0527  0.0693  795  GLN A CD    
5249 O  OE1   . GLN A 692 ? 1.6999 1.7558 1.7077 0.0749  0.0578  0.0710  795  GLN A OE1   
5250 N  NE2   . GLN A 692 ? 1.7807 1.8278 1.7993 0.0694  0.0573  0.0755  795  GLN A NE2   
5251 N  N     . ASN A 693 ? 1.1327 1.2304 1.1961 0.0492  0.0232  0.0435  796  ASN A N     
5252 C  CA    . ASN A 693 ? 1.1884 1.2952 1.2714 0.0414  0.0191  0.0416  796  ASN A CA    
5253 C  C     . ASN A 693 ? 1.2133 1.3287 1.2979 0.0392  0.0108  0.0341  796  ASN A C     
5254 O  O     . ASN A 693 ? 1.2220 1.3427 1.3039 0.0418  0.0117  0.0342  796  ASN A O     
5255 C  CB    . ASN A 693 ? 1.2416 1.3580 1.3421 0.0384  0.0259  0.0488  796  ASN A CB    
5256 C  CG    . ASN A 693 ? 1.3592 1.4676 1.4617 0.0379  0.0341  0.0565  796  ASN A CG    
5257 O  OD1   . ASN A 693 ? 1.3373 1.4315 1.4252 0.0418  0.0355  0.0572  796  ASN A OD1   
5258 N  ND2   . ASN A 693 ? 1.4291 1.5475 1.5500 0.0332  0.0396  0.0626  796  ASN A ND2   
5259 N  N     . ASN A 694 ? 1.1480 1.2636 1.2356 0.0349  0.0034  0.0278  797  ASN A N     
5260 C  CA    . ASN A 694 ? 1.1141 1.2381 1.2035 0.0324  -0.0042 0.0208  797  ASN A CA    
5261 C  C     . ASN A 694 ? 1.0366 1.1720 1.1444 0.0257  -0.0066 0.0208  797  ASN A C     
5262 O  O     . ASN A 694 ? 1.0223 1.1559 1.1391 0.0204  -0.0081 0.0200  797  ASN A O     
5263 C  CB    . ASN A 694 ? 1.1132 1.2322 1.1946 0.0324  -0.0106 0.0137  797  ASN A CB    
5264 C  CG    . ASN A 694 ? 1.1153 1.2417 1.1928 0.0316  -0.0167 0.0073  797  ASN A CG    
5265 O  OD1   . ASN A 694 ? 1.0355 1.1704 1.1187 0.0297  -0.0175 0.0075  797  ASN A OD1   
5266 N  ND2   . ASN A 694 ? 1.0956 1.2195 1.1636 0.0334  -0.0208 0.0021  797  ASN A ND2   
5267 N  N     . GLU A 695 ? 1.0171 1.1636 1.1296 0.0262  -0.0072 0.0217  798  GLU A N     
5268 C  CA    . GLU A 695 ? 1.0071 1.1677 1.1372 0.0208  -0.0098 0.0225  798  GLU A CA    
5269 C  C     . GLU A 695 ? 0.9597 1.1268 1.0882 0.0187  -0.0183 0.0156  798  GLU A C     
5270 O  O     . GLU A 695 ? 0.9290 1.0955 1.0467 0.0229  -0.0190 0.0141  798  GLU A O     
5271 C  CB    . GLU A 695 ? 1.0157 1.1859 1.1534 0.0244  -0.0034 0.0303  798  GLU A CB    
5272 C  CG    . GLU A 695 ? 1.0768 1.2423 1.2171 0.0264  0.0061  0.0379  798  GLU A CG    
5273 C  CD    . GLU A 695 ? 1.2234 1.3945 1.3639 0.0336  0.0140  0.0451  798  GLU A CD    
5274 O  OE1   . GLU A 695 ? 1.2578 1.4239 1.3839 0.0400  0.0143  0.0435  798  GLU A OE1   
5275 O  OE2   . GLU A 695 ? 1.2289 1.4090 1.3836 0.0329  0.0204  0.0522  798  GLU A OE2   
5276 N  N     . ILE A 696 ? 0.9523 1.1243 1.0904 0.0118  -0.0244 0.0112  799  ILE A N     
5277 C  CA    . ILE A 696 ? 0.9433 1.1212 1.0791 0.0095  -0.0325 0.0043  799  ILE A CA    
5278 C  C     . ILE A 696 ? 0.8943 1.0862 1.0465 0.0029  -0.0372 0.0041  799  ILE A C     
5279 O  O     . ILE A 696 ? 0.8993 1.0914 1.0630 -0.0032 -0.0367 0.0052  799  ILE A O     
5280 C  CB    . ILE A 696 ? 0.8959 1.0630 1.0217 0.0084  -0.0364 -0.0034 799  ILE A CB    
5281 C  CG1   . ILE A 696 ? 0.9216 1.0780 1.0327 0.0147  -0.0325 -0.0029 799  ILE A CG1   
5282 C  CG2   . ILE A 696 ? 0.8984 1.0720 1.0209 0.0065  -0.0438 -0.0102 799  ILE A CG2   
5283 C  CD1   . ILE A 696 ? 0.8997 1.0477 1.0023 0.0153  -0.0357 -0.0094 799  ILE A CD1   
5284 N  N     . ILE A 697 ? 0.8645 1.0681 1.0172 0.0037  -0.0420 0.0030  800  ILE A N     
5285 C  CA    . ILE A 697 ? 0.8944 1.1138 1.0613 -0.0022 -0.0483 0.0022  800  ILE A CA    
5286 C  C     . ILE A 697 ? 0.8951 1.1118 1.0555 -0.0068 -0.0567 -0.0073 800  ILE A C     
5287 O  O     . ILE A 697 ? 0.8763 1.0898 1.0232 -0.0030 -0.0588 -0.0111 800  ILE A O     
5288 C  CB    . ILE A 697 ? 0.8711 1.1057 1.0418 0.0030  -0.0485 0.0077  800  ILE A CB    
5289 C  CG1   . ILE A 697 ? 0.9018 1.1400 1.0803 0.0080  -0.0396 0.0172  800  ILE A CG1   
5290 C  CG2   . ILE A 697 ? 0.8928 1.1454 1.0761 -0.0026 -0.0570 0.0059  800  ILE A CG2   
5291 C  CD1   . ILE A 697 ? 0.9026 1.1534 1.0832 0.0155  -0.0384 0.0232  800  ILE A CD1   
5292 N  N     . PHE A 698 ? 0.8989 1.1163 1.0684 -0.0154 -0.0610 -0.0114 801  PHE A N     
5293 C  CA    . PHE A 698 ? 0.9196 1.1338 1.0828 -0.0201 -0.0689 -0.0210 801  PHE A CA    
5294 C  C     . PHE A 698 ? 1.0125 1.2457 1.1856 -0.0250 -0.0769 -0.0219 801  PHE A C     
5295 O  O     . PHE A 698 ? 0.9322 1.1750 1.1215 -0.0323 -0.0788 -0.0201 801  PHE A O     
5296 C  CB    . PHE A 698 ? 0.8958 1.0947 1.0595 -0.0263 -0.0687 -0.0258 801  PHE A CB    
5297 C  CG    . PHE A 698 ? 0.9605 1.1545 1.1173 -0.0313 -0.0764 -0.0363 801  PHE A CG    
5298 C  CD1   . PHE A 698 ? 0.9905 1.1739 1.1305 -0.0260 -0.0770 -0.0425 801  PHE A CD1   
5299 C  CD2   . PHE A 698 ? 1.0279 1.2283 1.1948 -0.0414 -0.0830 -0.0401 801  PHE A CD2   
5300 C  CE1   . PHE A 698 ? 1.0607 1.2387 1.1928 -0.0295 -0.0832 -0.0523 801  PHE A CE1   
5301 C  CE2   . PHE A 698 ? 1.0721 1.2659 1.2302 -0.0459 -0.0902 -0.0505 801  PHE A CE2   
5302 C  CZ    . PHE A 698 ? 1.0547 1.2367 1.1947 -0.0393 -0.0899 -0.0566 801  PHE A CZ    
5303 N  N     . LYS A 699 ? 0.9137 1.1529 1.0770 -0.0211 -0.0816 -0.0245 802  LYS A N     
5304 C  CA    . LYS A 699 ? 0.9072 1.1655 1.0772 -0.0234 -0.0894 -0.0244 802  LYS A CA    
5305 C  C     . LYS A 699 ? 0.9731 1.2284 1.1340 -0.0287 -0.0981 -0.0349 802  LYS A C     
5306 O  O     . LYS A 699 ? 0.9751 1.2206 1.1191 -0.0245 -0.0980 -0.0397 802  LYS A O     
5307 C  CB    . LYS A 699 ? 0.9249 1.1917 1.0891 -0.0140 -0.0877 -0.0181 802  LYS A CB    
5308 C  CG    . LYS A 699 ? 1.0492 1.3389 1.2250 -0.0139 -0.0936 -0.0136 802  LYS A CG    
5309 C  CD    . LYS A 699 ? 1.0987 1.3925 1.2668 -0.0031 -0.0904 -0.0065 802  LYS A CD    
5310 C  CE    . LYS A 699 ? 1.2375 1.5552 1.4185 -0.0009 -0.0954 -0.0003 802  LYS A CE    
5311 N  NZ    . LYS A 699 ? 1.2329 1.5635 1.4361 -0.0029 -0.0920 0.0061  802  LYS A NZ    
5312 N  N     . ASN A 700 ? 0.9504 1.2146 1.1222 -0.0381 -0.1054 -0.0386 803  ASN A N     
5313 C  CA    . ASN A 700 ? 0.9542 1.2145 1.1168 -0.0442 -0.1141 -0.0495 803  ASN A CA    
5314 C  C     . ASN A 700 ? 1.0194 1.3024 1.1877 -0.0467 -0.1240 -0.0493 803  ASN A C     
5315 O  O     . ASN A 700 ? 1.0919 1.3924 1.2791 -0.0517 -0.1267 -0.0445 803  ASN A O     
5316 C  CB    . ASN A 700 ? 0.9307 1.1779 1.0986 -0.0547 -0.1150 -0.0557 803  ASN A CB    
5317 C  CG    . ASN A 700 ? 0.9809 1.2175 1.1348 -0.0598 -0.1225 -0.0683 803  ASN A CG    
5318 O  OD1   . ASN A 700 ? 0.9800 1.2241 1.1232 -0.0572 -0.1287 -0.0722 803  ASN A OD1   
5319 N  ND2   . ASN A 700 ? 1.0064 1.2237 1.1587 -0.0665 -0.1213 -0.0745 803  ASN A ND2   
5320 N  N     . GLY A 701 ? 1.0102 1.2940 1.1621 -0.0429 -0.1291 -0.0540 804  GLY A N     
5321 C  CA    . GLY A 701 ? 1.0579 1.3620 1.2111 -0.0442 -0.1393 -0.0544 804  GLY A CA    
5322 C  C     . GLY A 701 ? 1.1477 1.4608 1.2917 -0.0330 -0.1382 -0.0475 804  GLY A C     
5323 O  O     . GLY A 701 ? 1.2107 1.5378 1.3501 -0.0323 -0.1468 -0.0486 804  GLY A O     
5324 N  N     . ASP A 702 ? 1.0867 1.3917 1.2268 -0.0243 -0.1282 -0.0406 805  ASP A N     
5325 C  CA    . ASP A 702 ? 1.1509 1.4606 1.2810 -0.0141 -0.1260 -0.0337 805  ASP A CA    
5326 C  C     . ASP A 702 ? 1.1379 1.4285 1.2482 -0.0094 -0.1195 -0.0366 805  ASP A C     
5327 O  O     . ASP A 702 ? 1.1223 1.3981 1.2317 -0.0104 -0.1129 -0.0389 805  ASP A O     
5328 C  CB    . ASP A 702 ? 1.2507 1.5686 1.3937 -0.0077 -0.1196 -0.0219 805  ASP A CB    
5329 C  CG    . ASP A 702 ? 1.4673 1.8104 1.6287 -0.0092 -0.1265 -0.0169 805  ASP A CG    
5330 O  OD1   . ASP A 702 ? 1.3995 1.7557 1.5575 -0.0104 -0.1364 -0.0196 805  ASP A OD1   
5331 O  OD2   . ASP A 702 ? 1.5153 1.8662 1.6945 -0.0089 -0.1219 -0.0102 805  ASP A OD2   
5332 N  N     . ASP A 703 ? 1.2122 1.5046 1.3069 -0.0042 -0.1213 -0.0361 806  ASP A N     
5333 C  CA    . ASP A 703 ? 1.1820 1.4595 1.2588 -0.0002 -0.1150 -0.0380 806  ASP A CA    
5334 C  C     . ASP A 703 ? 1.1965 1.4672 1.2743 0.0057  -0.1053 -0.0295 806  ASP A C     
5335 O  O     . ASP A 703 ? 1.2464 1.5232 1.3244 0.0115  -0.1040 -0.0210 806  ASP A O     
5336 C  CB    . ASP A 703 ? 1.1279 1.4096 1.1877 0.0030  -0.1192 -0.0391 806  ASP A CB    
5337 C  CG    . ASP A 703 ? 1.2223 1.4906 1.2645 0.0055  -0.1128 -0.0419 806  ASP A CG    
5338 O  OD1   . ASP A 703 ? 1.3507 1.6079 1.3939 0.0035  -0.1076 -0.0461 806  ASP A OD1   
5339 O  OD2   . ASP A 703 ? 1.2258 1.4955 1.2534 0.0095  -0.1129 -0.0395 806  ASP A OD2   
5340 N  N     . LEU A 704 ? 1.1867 1.4442 1.2641 0.0046  -0.0986 -0.0317 807  LEU A N     
5341 C  CA    . LEU A 704 ? 1.1308 1.3803 1.2077 0.0091  -0.0898 -0.0251 807  LEU A CA    
5342 C  C     . LEU A 704 ? 1.1061 1.3459 1.1660 0.0119  -0.0849 -0.0255 807  LEU A C     
5343 O  O     . LEU A 704 ? 1.0889 1.3197 1.1463 0.0140  -0.0779 -0.0221 807  LEU A O     
5344 C  CB    . LEU A 704 ? 1.0602 1.3021 1.1470 0.0065  -0.0856 -0.0263 807  LEU A CB    
5345 C  CG    . LEU A 704 ? 1.0971 1.3478 1.2024 0.0035  -0.0877 -0.0235 807  LEU A CG    
5346 C  CD1   . LEU A 704 ? 1.0424 1.2831 1.1546 0.0011  -0.0827 -0.0244 807  LEU A CD1   
5347 C  CD2   . LEU A 704 ? 1.1194 1.3799 1.2313 0.0091  -0.0858 -0.0136 807  LEU A CD2   
5348 N  N     . ARG A 705 ? 1.1069 1.3487 1.1548 0.0114  -0.0884 -0.0298 808  ARG A N     
5349 C  CA    . ARG A 705 ? 1.1151 1.3495 1.1477 0.0132  -0.0832 -0.0295 808  ARG A CA    
5350 C  C     . ARG A 705 ? 1.0778 1.3102 1.1044 0.0179  -0.0794 -0.0203 808  ARG A C     
5351 O  O     . ARG A 705 ? 1.0387 1.2615 1.0571 0.0185  -0.0727 -0.0179 808  ARG A O     
5352 C  CB    . ARG A 705 ? 1.1475 1.3850 1.1682 0.0119  -0.0871 -0.0359 808  ARG A CB    
5353 C  CG    . ARG A 705 ? 1.1392 1.3745 1.1617 0.0084  -0.0890 -0.0457 808  ARG A CG    
5354 C  CD    . ARG A 705 ? 1.2628 1.5001 1.2709 0.0084  -0.0915 -0.0519 808  ARG A CD    
5355 N  NE    . ARG A 705 ? 1.2932 1.5392 1.2975 0.0086  -0.0991 -0.0514 808  ARG A NE    
5356 C  CZ    . ARG A 705 ? 1.2637 1.5124 1.2532 0.0095  -0.1020 -0.0551 808  ARG A CZ    
5357 N  NH1   . ARG A 705 ? 1.3405 1.5846 1.3182 0.0103  -0.0971 -0.0595 808  ARG A NH1   
5358 N  NH2   . ARG A 705 ? 1.2565 1.5142 1.2429 0.0099  -0.1100 -0.0542 808  ARG A NH2   
5359 N  N     . GLN A 706 ? 1.1436 1.3848 1.1739 0.0214  -0.0837 -0.0149 809  GLN A N     
5360 C  CA    . GLN A 706 ? 1.1576 1.3953 1.1816 0.0275  -0.0798 -0.0054 809  GLN A CA    
5361 C  C     . GLN A 706 ? 1.1828 1.4111 1.2125 0.0295  -0.0725 -0.0008 809  GLN A C     
5362 O  O     . GLN A 706 ? 1.1575 1.3742 1.1768 0.0327  -0.0662 0.0044  809  GLN A O     
5363 C  CB    . GLN A 706 ? 1.2292 1.4809 1.2579 0.0321  -0.0865 -0.0004 809  GLN A CB    
5364 C  CG    . GLN A 706 ? 1.2701 1.5299 1.2886 0.0316  -0.0937 -0.0036 809  GLN A CG    
5365 C  CD    . GLN A 706 ? 1.2778 1.5444 1.3018 0.0246  -0.1004 -0.0141 809  GLN A CD    
5366 O  OE1   . GLN A 706 ? 1.2042 1.4723 1.2429 0.0204  -0.1013 -0.0177 809  GLN A OE1   
5367 N  NE2   . GLN A 706 ? 1.3683 1.6371 1.3790 0.0234  -0.1048 -0.0191 809  GLN A NE2   
5368 N  N     . ASP A 707 ? 1.1852 1.4169 1.2301 0.0274  -0.0730 -0.0028 810  ASP A N     
5369 C  CA    . ASP A 707 ? 1.0645 1.2870 1.1134 0.0293  -0.0659 0.0010  810  ASP A CA    
5370 C  C     . ASP A 707 ? 1.0379 1.2466 1.0770 0.0260  -0.0605 -0.0029 810  ASP A C     
5371 O  O     . ASP A 707 ? 1.1104 1.3073 1.1427 0.0282  -0.0541 0.0009  810  ASP A O     
5372 C  CB    . ASP A 707 ? 1.1521 1.3823 1.2193 0.0276  -0.0675 0.0004  810  ASP A CB    
5373 C  CG    . ASP A 707 ? 1.4115 1.6576 1.4911 0.0311  -0.0718 0.0058  810  ASP A CG    
5374 O  OD1   . ASP A 707 ? 1.4155 1.6729 1.4948 0.0301  -0.0793 0.0042  810  ASP A OD1   
5375 O  OD2   . ASP A 707 ? 1.3187 1.5669 1.4081 0.0350  -0.0678 0.0118  810  ASP A OD2   
5376 N  N     . MET A 708 ? 0.9488 1.1589 0.9868 0.0209  -0.0630 -0.0106 811  MET A N     
5377 C  CA    . MET A 708 ? 0.9102 1.1112 0.9401 0.0179  -0.0586 -0.0143 811  MET A CA    
5378 C  C     . MET A 708 ? 1.0062 1.1993 1.0212 0.0184  -0.0543 -0.0108 811  MET A C     
5379 O  O     . MET A 708 ? 1.0596 1.2422 1.0689 0.0174  -0.0489 -0.0094 811  MET A O     
5380 C  CB    . MET A 708 ? 0.8854 1.0913 0.9155 0.0141  -0.0621 -0.0226 811  MET A CB    
5381 C  CG    . MET A 708 ? 0.9256 1.1331 0.9676 0.0125  -0.0643 -0.0269 811  MET A CG    
5382 S  SD    . MET A 708 ? 1.0048 1.2142 1.0435 0.0099  -0.0667 -0.0367 811  MET A SD    
5383 C  CE    . MET A 708 ? 0.9206 1.1260 0.9486 0.0094  -0.0607 -0.0367 811  MET A CE    
5384 N  N     . LEU A 709 ? 1.0003 1.1975 1.0077 0.0196  -0.0568 -0.0093 812  LEU A N     
5385 C  CA    . LEU A 709 ? 0.9753 1.1637 0.9672 0.0194  -0.0522 -0.0057 812  LEU A CA    
5386 C  C     . LEU A 709 ? 0.9585 1.1349 0.9459 0.0238  -0.0473 0.0022  812  LEU A C     
5387 O  O     . LEU A 709 ? 0.9530 1.1160 0.9301 0.0214  -0.0414 0.0036  812  LEU A O     
5388 C  CB    . LEU A 709 ? 1.0531 1.2483 1.0369 0.0207  -0.0559 -0.0050 812  LEU A CB    
5389 C  CG    . LEU A 709 ? 0.9704 1.1564 0.9369 0.0200  -0.0509 -0.0009 812  LEU A CG    
5390 C  CD1   . LEU A 709 ? 0.9739 1.1572 0.9361 0.0129  -0.0465 -0.0060 812  LEU A CD1   
5391 C  CD2   . LEU A 709 ? 1.0262 1.2195 0.9844 0.0230  -0.0550 0.0010  812  LEU A CD2   
5392 N  N     . THR A 710 ? 0.9740 1.1550 0.9691 0.0300  -0.0495 0.0071  813  THR A N     
5393 C  CA    . THR A 710 ? 1.0055 1.1748 0.9961 0.0361  -0.0441 0.0148  813  THR A CA    
5394 C  C     . THR A 710 ? 0.9788 1.1371 0.9710 0.0342  -0.0388 0.0132  813  THR A C     
5395 O  O     . THR A 710 ? 0.9817 1.1231 0.9620 0.0353  -0.0325 0.0164  813  THR A O     
5396 C  CB    . THR A 710 ? 1.0434 1.2242 1.0445 0.0439  -0.0476 0.0205  813  THR A CB    
5397 O  OG1   . THR A 710 ? 1.2269 1.4217 1.2461 0.0415  -0.0522 0.0162  813  THR A OG1   
5398 C  CG2   . THR A 710 ? 1.0539 1.2435 1.0494 0.0472  -0.0527 0.0234  813  THR A CG2   
5399 N  N     . LEU A 711 ? 0.9610 1.1273 0.9662 0.0313  -0.0411 0.0082  814  LEU A N     
5400 C  CA    . LEU A 711 ? 0.9515 1.1080 0.9569 0.0297  -0.0366 0.0066  814  LEU A CA    
5401 C  C     . LEU A 711 ? 0.9478 1.0949 0.9415 0.0230  -0.0340 0.0022  814  LEU A C     
5402 O  O     . LEU A 711 ? 1.0084 1.1420 0.9944 0.0220  -0.0292 0.0027  814  LEU A O     
5403 C  CB    . LEU A 711 ? 0.9593 1.1262 0.9804 0.0284  -0.0397 0.0030  814  LEU A CB    
5404 C  CG    . LEU A 711 ? 0.9353 1.1106 0.9697 0.0339  -0.0405 0.0079  814  LEU A CG    
5405 C  CD1   . LEU A 711 ? 0.9058 1.0932 0.9555 0.0304  -0.0452 0.0037  814  LEU A CD1   
5406 C  CD2   . LEU A 711 ? 0.9293 1.0936 0.9614 0.0388  -0.0335 0.0128  814  LEU A CD2   
5407 N  N     . GLN A 712 ? 0.8901 1.0446 0.8821 0.0181  -0.0370 -0.0021 815  GLN A N     
5408 C  CA    . GLN A 712 ? 0.9196 1.0685 0.9021 0.0114  -0.0344 -0.0056 815  GLN A CA    
5409 C  C     . GLN A 712 ? 0.9157 1.0489 0.8825 0.0106  -0.0292 -0.0008 815  GLN A C     
5410 O  O     . GLN A 712 ? 0.9449 1.0674 0.9035 0.0052  -0.0253 -0.0023 815  GLN A O     
5411 C  CB    . GLN A 712 ? 0.8866 1.0483 0.8710 0.0076  -0.0379 -0.0107 815  GLN A CB    
5412 C  CG    . GLN A 712 ? 0.9523 1.1126 0.9294 0.0003  -0.0349 -0.0140 815  GLN A CG    
5413 C  CD    . GLN A 712 ? 0.9901 1.1604 0.9641 -0.0020 -0.0361 -0.0163 815  GLN A CD    
5414 O  OE1   . GLN A 712 ? 1.0678 1.2439 1.0424 0.0019  -0.0394 -0.0153 815  GLN A OE1   
5415 N  NE2   . GLN A 712 ? 0.9240 1.0974 0.8946 -0.0084 -0.0334 -0.0193 815  GLN A NE2   
5416 N  N     . ILE A 713 ? 0.9498 1.0810 0.9116 0.0158  -0.0291 0.0050  816  ILE A N     
5417 C  CA    . ILE A 713 ? 0.9813 1.0946 0.9265 0.0161  -0.0236 0.0105  816  ILE A CA    
5418 C  C     . ILE A 713 ? 0.8960 0.9922 0.8364 0.0199  -0.0187 0.0136  816  ILE A C     
5419 O  O     . ILE A 713 ? 0.8813 0.9587 0.8076 0.0161  -0.0133 0.0144  816  ILE A O     
5420 C  CB    . ILE A 713 ? 0.9375 1.0538 0.8780 0.0224  -0.0251 0.0166  816  ILE A CB    
5421 C  CG1   . ILE A 713 ? 0.9010 1.0313 0.8418 0.0180  -0.0290 0.0129  816  ILE A CG1   
5422 C  CG2   . ILE A 713 ? 0.8764 0.9710 0.7987 0.0247  -0.0187 0.0236  816  ILE A CG2   
5423 C  CD1   . ILE A 713 ? 1.0787 1.2177 1.0183 0.0247  -0.0332 0.0173  816  ILE A CD1   
5424 N  N     . ILE A 714 ? 0.9294 1.0316 0.8812 0.0270  -0.0201 0.0152  817  ILE A N     
5425 C  CA    . ILE A 714 ? 0.9940 1.0809 0.9413 0.0318  -0.0148 0.0180  817  ILE A CA    
5426 C  C     . ILE A 714 ? 0.9489 1.0263 0.8909 0.0240  -0.0126 0.0121  817  ILE A C     
5427 O  O     . ILE A 714 ? 1.0863 1.1430 1.0141 0.0234  -0.0072 0.0130  817  ILE A O     
5428 C  CB    . ILE A 714 ? 1.0126 1.1118 0.9756 0.0401  -0.0166 0.0208  817  ILE A CB    
5429 C  CG1   . ILE A 714 ? 0.9187 1.0249 0.8844 0.0491  -0.0180 0.0280  817  ILE A CG1   
5430 C  CG2   . ILE A 714 ? 0.9617 1.0474 0.9212 0.0440  -0.0108 0.0219  817  ILE A CG2   
5431 C  CD1   . ILE A 714 ? 0.9544 1.0750 0.9370 0.0567  -0.0195 0.0315  817  ILE A CD1   
5432 N  N     . ARG A 715 ? 0.8435 0.9354 0.7960 0.0181  -0.0170 0.0058  818  ARG A N     
5433 C  CA    . ARG A 715 ? 0.9230 1.0095 0.8714 0.0109  -0.0161 0.0002  818  ARG A CA    
5434 C  C     . ARG A 715 ? 0.9531 1.0276 0.8867 0.0022  -0.0134 -0.0013 818  ARG A C     
5435 O  O     . ARG A 715 ? 1.0986 1.1583 1.0214 -0.0023 -0.0104 -0.0033 818  ARG A O     
5436 C  CB    . ARG A 715 ? 0.9781 1.0835 0.9405 0.0077  -0.0214 -0.0055 818  ARG A CB    
5437 C  CG    . ARG A 715 ? 0.9483 1.0521 0.9078 0.0011  -0.0216 -0.0110 818  ARG A CG    
5438 C  CD    . ARG A 715 ? 0.9938 1.1155 0.9671 0.0006  -0.0264 -0.0155 818  ARG A CD    
5439 N  NE    . ARG A 715 ? 1.1407 1.2663 1.1244 0.0077  -0.0274 -0.0135 818  ARG A NE    
5440 N  N     . ILE A 716 ? 0.9699 1.0504 0.9021 -0.0007 -0.0143 -0.0003 819  ILE A N     
5441 C  CA    . ILE A 716 ? 0.9699 1.0403 0.8891 -0.0100 -0.0111 -0.0010 819  ILE A CA    
5442 C  C     . ILE A 716 ? 0.9621 1.0055 0.8634 -0.0081 -0.0048 0.0042  819  ILE A C     
5443 O  O     . ILE A 716 ? 0.8818 0.9089 0.7704 -0.0164 -0.0013 0.0022  819  ILE A O     
5444 C  CB    . ILE A 716 ? 0.9213 1.0054 0.8430 -0.0126 -0.0129 -0.0006 819  ILE A CB    
5445 C  CG1   . ILE A 716 ? 0.9010 1.0086 0.8378 -0.0151 -0.0181 -0.0069 819  ILE A CG1   
5446 C  CG2   . ILE A 716 ? 0.7957 0.8679 0.7031 -0.0221 -0.0081 0.0005  819  ILE A CG2   
5447 C  CD1   . ILE A 716 ? 0.9729 1.0945 0.9117 -0.0168 -0.0195 -0.0074 819  ILE A CD1   
5448 N  N     . MET A 717 ? 1.0129 1.0509 0.9126 0.0031  -0.0035 0.0108  820  MET A N     
5449 C  CA    . MET A 717 ? 1.0476 1.0585 0.9296 0.0074  0.0031  0.0164  820  MET A CA    
5450 C  C     . MET A 717 ? 1.1023 1.0964 0.9773 0.0072  0.0064  0.0135  820  MET A C     
5451 O  O     . MET A 717 ? 1.1116 1.0797 0.9681 0.0036  0.0118  0.0139  820  MET A O     
5452 C  CB    . MET A 717 ? 1.0415 1.0546 0.9261 0.0214  0.0033  0.0244  820  MET A CB    
5453 C  CG    . MET A 717 ? 1.0165 1.0425 0.9033 0.0225  0.0002  0.0278  820  MET A CG    
5454 S  SD    . MET A 717 ? 1.1848 1.2184 1.0772 0.0391  -0.0015 0.0369  820  MET A SD    
5455 C  CE    . MET A 717 ? 1.1026 1.1015 0.9729 0.0468  0.0080  0.0442  820  MET A CE    
5456 N  N     . GLU A 718 ? 1.1422 1.1494 1.0304 0.0109  0.0033  0.0106  821  GLU A N     
5457 C  CA    . GLU A 718 ? 1.1518 1.1444 1.0326 0.0112  0.0063  0.0078  821  GLU A CA    
5458 C  C     . GLU A 718 ? 1.1819 1.1665 1.0532 -0.0027 0.0058  0.0007  821  GLU A C     
5459 O  O     . GLU A 718 ? 1.2070 1.1680 1.0614 -0.0053 0.0100  -0.0010 821  GLU A O     
5460 C  CB    . GLU A 718 ? 1.2313 1.2415 1.1287 0.0173  0.0031  0.0066  821  GLU A CB    
5461 C  CG    . GLU A 718 ? 1.2620 1.2585 1.1514 0.0190  0.0063  0.0041  821  GLU A CG    
5462 C  CD    . GLU A 718 ? 1.2855 1.2997 1.1912 0.0241  0.0036  0.0035  821  GLU A CD    
5463 O  OE1   . GLU A 718 ? 1.2632 1.3000 1.1861 0.0227  -0.0019 0.0027  821  GLU A OE1   
5464 O  OE2   . GLU A 718 ? 1.3009 1.3050 1.2010 0.0294  0.0074  0.0039  821  GLU A OE2   
5465 N  N     . ASN A 719 ? 1.0819 1.0867 0.9638 -0.0117 0.0007  -0.0036 822  ASN A N     
5466 C  CA    . ASN A 719 ? 1.0581 1.0603 0.9336 -0.0256 -0.0003 -0.0100 822  ASN A CA    
5467 C  C     . ASN A 719 ? 1.1505 1.1303 1.0079 -0.0337 0.0047  -0.0084 822  ASN A C     
5468 O  O     . ASN A 719 ? 1.3046 1.2711 1.1505 -0.0445 0.0058  -0.0131 822  ASN A O     
5469 C  CB    . ASN A 719 ? 1.1056 1.1367 0.9979 -0.0316 -0.0062 -0.0141 822  ASN A CB    
5470 C  CG    . ASN A 719 ? 1.2774 1.3118 1.1669 -0.0451 -0.0081 -0.0206 822  ASN A CG    
5471 O  OD1   . ASN A 719 ? 1.4919 1.5310 1.3840 -0.0462 -0.0113 -0.0252 822  ASN A OD1   
5472 N  ND2   . ASN A 719 ? 1.3812 1.4143 1.2658 -0.0557 -0.0063 -0.0208 822  ASN A ND2   
5473 N  N     . ILE A 720 ? 1.1952 1.1701 1.0492 -0.0290 0.0077  -0.0019 823  ILE A N     
5474 C  CA    . ILE A 720 ? 1.2195 1.1690 1.0541 -0.0352 0.0137  0.0010  823  ILE A CA    
5475 C  C     . ILE A 720 ? 1.2308 1.1471 1.0459 -0.0310 0.0194  0.0021  823  ILE A C     
5476 O  O     . ILE A 720 ? 1.2926 1.1863 1.0911 -0.0418 0.0227  -0.0012 823  ILE A O     
5477 C  CB    . ILE A 720 ? 1.2178 1.1698 1.0522 -0.0289 0.0155  0.0088  823  ILE A CB    
5478 C  CG1   . ILE A 720 ? 1.1647 1.1450 1.0134 -0.0355 0.0111  0.0068  823  ILE A CG1   
5479 C  CG2   . ILE A 720 ? 1.0976 1.0172 0.9089 -0.0319 0.0230  0.0137  823  ILE A CG2   
5480 C  CD1   . ILE A 720 ? 1.1893 1.1683 1.0328 -0.0524 0.0127  0.0029  823  ILE A CD1   
5481 N  N     . TRP A 721 ? 1.2345 1.1475 1.0513 -0.0154 0.0209  0.0065  824  TRP A N     
5482 C  CA    . TRP A 721 ? 1.2518 1.1335 1.0498 -0.0088 0.0273  0.0079  824  TRP A CA    
5483 C  C     . TRP A 721 ? 1.3027 1.1763 1.0942 -0.0165 0.0262  -0.0005 824  TRP A C     
5484 O  O     . TRP A 721 ? 1.3644 1.2067 1.1339 -0.0201 0.0312  -0.0026 824  TRP A O     
5485 C  CB    . TRP A 721 ? 1.2385 1.1251 1.0438 0.0100  0.0289  0.0145  824  TRP A CB    
5486 C  CG    . TRP A 721 ? 1.2297 1.1207 1.0379 0.0192  0.0299  0.0233  824  TRP A CG    
5487 C  CD1   . TRP A 721 ? 1.2082 1.0841 1.0030 0.0157  0.0332  0.0275  824  TRP A CD1   
5488 C  CD2   . TRP A 721 ? 1.1877 1.1004 1.0127 0.0331  0.0274  0.0292  824  TRP A CD2   
5489 N  NE1   . TRP A 721 ? 1.1789 1.0657 0.9802 0.0276  0.0325  0.0358  824  TRP A NE1   
5490 C  CE2   . TRP A 721 ? 1.1468 1.0572 0.9673 0.0380  0.0286  0.0366  824  TRP A CE2   
5491 C  CE3   . TRP A 721 ? 1.1792 1.1132 1.0227 0.0412  0.0243  0.0290  824  TRP A CE3   
5492 C  CZ2   . TRP A 721 ? 1.1172 1.0474 0.9513 0.0507  0.0257  0.0433  824  TRP A CZ2   
5493 C  CZ3   . TRP A 721 ? 1.1906 1.1438 1.0485 0.0527  0.0220  0.0356  824  TRP A CZ3   
5494 C  CH2   . TRP A 721 ? 1.1520 1.1040 1.0054 0.0574  0.0222  0.0424  824  TRP A CH2   
5495 N  N     . GLN A 722 ? 1.2694 1.1698 1.0783 -0.0187 0.0197  -0.0053 825  GLN A N     
5496 C  CA    . GLN A 722 ? 1.2890 1.1843 1.0920 -0.0240 0.0179  -0.0127 825  GLN A CA    
5497 C  C     . GLN A 722 ? 1.3003 1.1836 1.0904 -0.0420 0.0170  -0.0193 825  GLN A C     
5498 O  O     . GLN A 722 ? 1.3930 1.2507 1.1635 -0.0464 0.0197  -0.0236 825  GLN A O     
5499 C  CB    . GLN A 722 ? 1.2691 1.1964 1.0938 -0.0220 0.0111  -0.0154 825  GLN A CB    
5500 C  CG    . GLN A 722 ? 1.3458 1.2677 1.1657 -0.0170 0.0112  -0.0187 825  GLN A CG    
5501 C  CD    . GLN A 722 ? 1.3435 1.2524 1.1590 -0.0008 0.0176  -0.0125 825  GLN A CD    
5502 O  OE1   . GLN A 722 ? 1.4469 1.3273 1.2418 0.0025  0.0236  -0.0128 825  GLN A OE1   
5503 N  NE2   . GLN A 722 ? 1.2649 1.1949 1.0999 0.0094  0.0165  -0.0071 825  GLN A NE2   
5504 N  N     . ASN A 723 ? 1.2648 1.1664 1.0652 -0.0531 0.0136  -0.0203 826  ASN A N     
5505 C  CA    . ASN A 723 ? 1.2928 1.1886 1.0848 -0.0717 0.0123  -0.0265 826  ASN A CA    
5506 C  C     . ASN A 723 ? 1.3332 1.1921 1.1011 -0.0780 0.0196  -0.0246 826  ASN A C     
5507 O  O     . ASN A 723 ? 1.3606 1.2087 1.1180 -0.0946 0.0193  -0.0302 826  ASN A O     
5508 C  CB    . ASN A 723 ? 1.1829 1.1109 0.9942 -0.0807 0.0076  -0.0273 826  ASN A CB    
5509 C  CG    . ASN A 723 ? 1.3528 1.3140 1.1848 -0.0776 0.0000  -0.0311 826  ASN A CG    
5510 O  OD1   . ASN A 723 ? 1.4630 1.4337 1.2969 -0.0868 -0.0047 -0.0377 826  ASN A OD1   
5511 N  ND2   . ASN A 723 ? 1.2951 1.2737 1.1422 -0.0647 -0.0013 -0.0268 826  ASN A ND2   
5512 N  N     . GLN A 724 ? 1.3177 1.1569 1.0763 -0.0654 0.0261  -0.0168 827  GLN A N     
5513 C  CA    . GLN A 724 ? 1.3377 1.1370 1.0706 -0.0690 0.0340  -0.0144 827  GLN A CA    
5514 C  C     . GLN A 724 ? 1.4740 1.2398 1.1852 -0.0621 0.0386  -0.0167 827  GLN A C     
5515 O  O     . GLN A 724 ? 1.4922 1.2209 1.1788 -0.0683 0.0446  -0.0175 827  GLN A O     
5516 C  CB    . GLN A 724 ? 1.4415 1.2354 1.1734 -0.0582 0.0391  -0.0039 827  GLN A CB    
5517 C  CG    . GLN A 724 ? 1.6721 1.4908 1.4182 -0.0662 0.0365  -0.0013 827  GLN A CG    
5518 C  CD    . GLN A 724 ? 1.5315 1.3387 1.2705 -0.0569 0.0421  0.0090  827  GLN A CD    
5519 O  OE1   . GLN A 724 ? 1.6360 1.4135 1.3576 -0.0459 0.0483  0.0143  827  GLN A OE1   
5520 N  NE2   . GLN A 724 ? 1.4393 1.2699 1.1907 -0.0604 0.0399  0.0121  827  GLN A NE2   
5521 N  N     . GLY A 725 ? 1.4393 1.2160 1.1581 -0.0496 0.0365  -0.0177 828  GLY A N     
5522 C  CA    . GLY A 725 ? 1.4601 1.2073 1.1590 -0.0405 0.0417  -0.0193 828  GLY A CA    
5523 C  C     . GLY A 725 ? 1.5055 1.2489 1.2061 -0.0181 0.0473  -0.0106 828  GLY A C     
5524 O  O     . GLY A 725 ? 1.5652 1.2794 1.2462 -0.0087 0.0539  -0.0104 828  GLY A O     
5525 N  N     . LEU A 726 ? 1.5078 1.2805 1.2311 -0.0091 0.0448  -0.0037 829  LEU A N     
5526 C  CA    . LEU A 726 ? 1.4478 1.2234 1.1770 0.0116  0.0489  0.0049  829  LEU A CA    
5527 C  C     . LEU A 726 ? 1.5036 1.3112 1.2552 0.0181  0.0438  0.0037  829  LEU A C     
5528 O  O     . LEU A 726 ? 1.5114 1.3519 1.2860 0.0152  0.0370  0.0040  829  LEU A O     
5529 C  CB    . LEU A 726 ? 1.4390 1.2237 1.1763 0.0168  0.0494  0.0137  829  LEU A CB    
5530 C  CG    . LEU A 726 ? 1.5892 1.3436 1.3051 0.0099  0.0546  0.0162  829  LEU A CG    
5531 C  CD1   . LEU A 726 ? 1.4203 1.1877 1.1452 0.0167  0.0544  0.0256  829  LEU A CD1   
5532 C  CD2   . LEU A 726 ? 1.6794 1.3898 1.3668 0.0175  0.0640  0.0174  829  LEU A CD2   
5533 N  N     . ASP A 727 ? 1.5479 1.3440 1.2914 0.0270  0.0477  0.0023  830  ASP A N     
5534 C  CA    . ASP A 727 ? 1.4973 1.3199 1.2595 0.0334  0.0443  0.0018  830  ASP A CA    
5535 C  C     . ASP A 727 ? 1.4880 1.3273 1.2671 0.0502  0.0467  0.0114  830  ASP A C     
5536 O  O     . ASP A 727 ? 1.5932 1.4223 1.3670 0.0646  0.0536  0.0158  830  ASP A O     
5537 C  CB    . ASP A 727 ? 1.6745 1.4782 1.4197 0.0354  0.0478  -0.0036 830  ASP A CB    
5538 C  CG    . ASP A 727 ? 1.6904 1.5208 1.4526 0.0367  0.0430  -0.0059 830  ASP A CG    
5539 O  OD1   . ASP A 727 ? 1.6222 1.4820 1.4093 0.0423  0.0399  -0.0009 830  ASP A OD1   
5540 O  OD2   . ASP A 727 ? 1.8612 1.6822 1.6109 0.0320  0.0422  -0.0126 830  ASP A OD2   
5541 N  N     . LEU A 728 ? 1.3902 1.2566 1.1900 0.0482  0.0409  0.0146  831  LEU A N     
5542 C  CA    . LEU A 728 ? 1.3184 1.2072 1.1381 0.0613  0.0406  0.0227  831  LEU A CA    
5543 C  C     . LEU A 728 ? 1.2670 1.1898 1.1117 0.0571  0.0329  0.0200  831  LEU A C     
5544 O  O     . LEU A 728 ? 1.2774 1.2153 1.1308 0.0461  0.0262  0.0163  831  LEU A O     
5545 C  CB    . LEU A 728 ? 1.3165 1.2060 1.1367 0.0633  0.0402  0.0288  831  LEU A CB    
5546 C  CG    . LEU A 728 ? 1.3332 1.1866 1.1272 0.0667  0.0479  0.0321  831  LEU A CG    
5547 C  CD1   . LEU A 728 ? 1.2966 1.1549 1.0931 0.0704  0.0469  0.0396  831  LEU A CD1   
5548 C  CD2   . LEU A 728 ? 1.3859 1.2192 1.1679 0.0822  0.0567  0.0359  831  LEU A CD2   
5549 N  N     . ARG A 729 ? 1.2018 1.1357 1.0573 0.0661  0.0346  0.0221  832  ARG A N     
5550 C  CA    . ARG A 729 ? 1.2987 1.2596 1.1748 0.0621  0.0285  0.0194  832  ARG A CA    
5551 C  C     . ARG A 729 ? 1.2014 1.1897 1.1011 0.0664  0.0242  0.0247  832  ARG A C     
5552 O  O     . ARG A 729 ? 1.2208 1.2178 1.1307 0.0777  0.0274  0.0312  832  ARG A O     
5553 C  CB    . ARG A 729 ? 1.2734 1.2313 1.1480 0.0683  0.0328  0.0191  832  ARG A CB    
5554 C  CG    . ARG A 729 ? 1.3082 1.2841 1.1951 0.0612  0.0270  0.0142  832  ARG A CG    
5555 C  CD    . ARG A 729 ? 1.4312 1.3990 1.3107 0.0665  0.0320  0.0136  832  ARG A CD    
5556 N  NE    . ARG A 729 ? 1.5524 1.4895 1.4045 0.0672  0.0378  0.0106  832  ARG A NE    
5557 C  CZ    . ARG A 729 ? 1.5902 1.5133 1.4256 0.0563  0.0346  0.0028  832  ARG A CZ    
5558 N  NH1   . ARG A 729 ? 1.5535 1.4920 1.3977 0.0446  0.0261  -0.0023 832  ARG A NH1   
5559 N  NH2   . ARG A 729 ? 1.5591 1.4523 1.3684 0.0572  0.0402  -0.0001 832  ARG A NH2   
5560 N  N     . MET A 730 ? 1.0911 1.0937 0.9993 0.0573  0.0171  0.0218  833  MET A N     
5561 C  CA    . MET A 730 ? 1.0778 1.1071 1.0077 0.0590  0.0115  0.0246  833  MET A CA    
5562 C  C     . MET A 730 ? 1.0071 1.0552 0.9537 0.0554  0.0072  0.0210  833  MET A C     
5563 O  O     . MET A 730 ? 1.0956 1.1379 1.0365 0.0499  0.0071  0.0157  833  MET A O     
5564 C  CB    . MET A 730 ? 1.1384 1.1725 1.0673 0.0516  0.0065  0.0231  833  MET A CB    
5565 C  CG    . MET A 730 ? 1.1256 1.1371 1.0346 0.0527  0.0110  0.0261  833  MET A CG    
5566 S  SD    . MET A 730 ? 1.2574 1.2664 1.1664 0.0691  0.0155  0.0368  833  MET A SD    
5567 C  CE    . MET A 730 ? 1.1292 1.1686 1.0574 0.0685  0.0067  0.0390  833  MET A CE    
5568 N  N     . LEU A 731 ? 0.9603 1.0305 0.9269 0.0585  0.0035  0.0240  834  LEU A N     
5569 C  CA    . LEU A 731 ? 0.9839 1.0706 0.9668 0.0554  -0.0002 0.0214  834  LEU A CA    
5570 C  C     . LEU A 731 ? 0.9082 1.0138 0.9044 0.0498  -0.0081 0.0189  834  LEU A C     
5571 O  O     . LEU A 731 ? 0.8903 1.0121 0.9020 0.0530  -0.0108 0.0223  834  LEU A O     
5572 C  CB    . LEU A 731 ? 0.9931 1.0870 0.9876 0.0639  0.0042  0.0272  834  LEU A CB    
5573 C  CG    . LEU A 731 ? 0.9161 1.0217 0.9243 0.0609  0.0025  0.0253  834  LEU A CG    
5574 C  CD1   . LEU A 731 ? 1.0920 1.1868 1.0885 0.0545  0.0017  0.0188  834  LEU A CD1   
5575 C  CD2   . LEU A 731 ? 0.9332 1.0417 0.9489 0.0693  0.0092  0.0317  834  LEU A CD2   
5576 N  N     . PRO A 732 ? 0.8049 0.9095 0.7955 0.0414  -0.0121 0.0128  835  PRO A N     
5577 C  CA    . PRO A 732 ? 0.8449 0.9661 0.8462 0.0365  -0.0191 0.0096  835  PRO A CA    
5578 C  C     . PRO A 732 ? 0.8065 0.9391 0.8211 0.0338  -0.0225 0.0059  835  PRO A C     
5579 O  O     . PRO A 732 ? 0.8476 0.9805 0.8603 0.0284  -0.0246 0.0004  835  PRO A O     
5580 C  CB    . PRO A 732 ? 0.9683 1.0822 0.9565 0.0294  -0.0200 0.0052  835  PRO A CB    
5581 C  CG    . PRO A 732 ? 0.9151 1.0136 0.8913 0.0274  -0.0158 0.0031  835  PRO A CG    
5582 C  CD    . PRO A 732 ? 0.9168 1.0052 0.8903 0.0358  -0.0101 0.0086  835  PRO A CD    
5583 N  N     . TYR A 733 ? 0.8662 1.0089 0.8952 0.0377  -0.0228 0.0095  836  TYR A N     
5584 C  CA    . TYR A 733 ? 0.9188 1.0694 0.9599 0.0353  -0.0249 0.0071  836  TYR A CA    
5585 C  C     . TYR A 733 ? 0.9100 1.0699 0.9560 0.0294  -0.0317 0.0010  836  TYR A C     
5586 O  O     . TYR A 733 ? 0.8848 1.0487 0.9277 0.0277  -0.0351 -0.0004 836  TYR A O     
5587 C  CB    . TYR A 733 ? 0.9222 1.0824 0.9786 0.0394  -0.0235 0.0126  836  TYR A CB    
5588 C  CG    . TYR A 733 ? 0.9576 1.1314 1.0235 0.0406  -0.0277 0.0153  836  TYR A CG    
5589 C  CD1   . TYR A 733 ? 0.9537 1.1267 1.0159 0.0473  -0.0248 0.0213  836  TYR A CD1   
5590 C  CD2   . TYR A 733 ? 0.9404 1.1275 1.0181 0.0356  -0.0346 0.0117  836  TYR A CD2   
5591 C  CE1   . TYR A 733 ? 0.9926 1.1798 1.0633 0.0493  -0.0293 0.0242  836  TYR A CE1   
5592 C  CE2   . TYR A 733 ? 0.9661 1.1668 1.0517 0.0364  -0.0394 0.0138  836  TYR A CE2   
5593 C  CZ    . TYR A 733 ? 0.9921 1.1940 1.0746 0.0434  -0.0370 0.0203  836  TYR A CZ    
5594 O  OH    . TYR A 733 ? 0.9743 1.1914 1.0644 0.0450  -0.0425 0.0227  836  TYR A OH    
5595 N  N     . GLY A 734 ? 0.9618 1.1239 1.0141 0.0270  -0.0332 -0.0023 837  GLY A N     
5596 C  CA    . GLY A 734 ? 0.9140 1.0825 0.9692 0.0226  -0.0387 -0.0086 837  GLY A CA    
5597 C  C     . GLY A 734 ? 0.9219 1.1016 0.9878 0.0212  -0.0436 -0.0090 837  GLY A C     
5598 O  O     . GLY A 734 ? 1.0342 1.2195 1.1108 0.0227  -0.0434 -0.0047 837  GLY A O     
5599 N  N     . CYS A 735 ? 0.9318 1.1159 0.9948 0.0182  -0.0482 -0.0143 838  CYS A N     
5600 C  CA    . CYS A 735 ? 0.9312 1.1253 1.0015 0.0162  -0.0540 -0.0164 838  CYS A CA    
5601 C  C     . CYS A 735 ? 0.8448 1.0399 0.9092 0.0134  -0.0575 -0.0239 838  CYS A C     
5602 O  O     . CYS A 735 ? 0.8681 1.0615 0.9219 0.0134  -0.0562 -0.0251 838  CYS A O     
5603 C  CB    . CYS A 735 ? 0.9498 1.1499 1.0190 0.0186  -0.0552 -0.0117 838  CYS A CB    
5604 S  SG    . CYS A 735 ? 1.1374 1.3516 1.2141 0.0160  -0.0637 -0.0143 838  CYS A SG    
5605 N  N     . LEU A 736 ? 0.7466 0.9438 0.8174 0.0109  -0.0612 -0.0287 839  LEU A N     
5606 C  CA    . LEU A 736 ? 0.8574 1.0543 0.9224 0.0097  -0.0636 -0.0362 839  LEU A CA    
5607 C  C     . LEU A 736 ? 0.9669 1.1683 1.0362 0.0067  -0.0696 -0.0408 839  LEU A C     
5608 O  O     . LEU A 736 ? 0.9683 1.1673 1.0467 0.0045  -0.0711 -0.0418 839  LEU A O     
5609 C  CB    . LEU A 736 ? 0.8470 1.0369 0.9117 0.0108  -0.0609 -0.0387 839  LEU A CB    
5610 C  CG    . LEU A 736 ? 0.8548 1.0445 0.9142 0.0113  -0.0625 -0.0462 839  LEU A CG    
5611 C  CD1   . LEU A 736 ? 0.8621 1.0565 0.9120 0.0120  -0.0607 -0.0472 839  LEU A CD1   
5612 C  CD2   . LEU A 736 ? 0.8633 1.0456 0.9252 0.0135  -0.0607 -0.0479 839  LEU A CD2   
5613 N  N     . SER A 737 ? 0.9453 1.1523 1.0073 0.0063  -0.0731 -0.0437 840  SER A N     
5614 C  CA    . SER A 737 ? 0.8693 1.0795 0.9320 0.0033  -0.0794 -0.0498 840  SER A CA    
5615 C  C     . SER A 737 ? 0.8360 1.0384 0.8951 0.0032  -0.0791 -0.0576 840  SER A C     
5616 O  O     . SER A 737 ? 0.8819 1.0823 0.9330 0.0062  -0.0756 -0.0597 840  SER A O     
5617 C  CB    . SER A 737 ? 0.9627 1.1804 1.0156 0.0038  -0.0827 -0.0506 840  SER A CB    
5618 O  OG    . SER A 737 ? 0.9783 1.1989 1.0301 0.0008  -0.0896 -0.0571 840  SER A OG    
5619 N  N     . ILE A 738 ? 0.8151 1.0129 0.8803 -0.0002 -0.0824 -0.0617 841  ILE A N     
5620 C  CA    . ILE A 738 ? 0.9164 1.1034 0.9777 0.0006  -0.0816 -0.0687 841  ILE A CA    
5621 C  C     . ILE A 738 ? 0.9453 1.1303 1.0003 -0.0022 -0.0874 -0.0775 841  ILE A C     
5622 O  O     . ILE A 738 ? 0.8757 1.0495 0.9268 -0.0016 -0.0871 -0.0841 841  ILE A O     
5623 C  CB    . ILE A 738 ? 0.9534 1.1308 1.0244 -0.0006 -0.0791 -0.0664 841  ILE A CB    
5624 C  CG1   . ILE A 738 ? 0.9533 1.1320 1.0350 -0.0077 -0.0836 -0.0658 841  ILE A CG1   
5625 C  CG2   . ILE A 738 ? 0.9276 1.1061 1.0023 0.0028  -0.0734 -0.0582 841  ILE A CG2   
5626 C  CD1   . ILE A 738 ? 0.9834 1.1514 1.0741 -0.0100 -0.0806 -0.0635 841  ILE A CD1   
5627 N  N     . GLY A 739 ? 1.0521 1.2470 1.1047 -0.0048 -0.0927 -0.0779 842  GLY A N     
5628 C  CA    . GLY A 739 ? 0.9697 1.1628 1.0140 -0.0077 -0.0988 -0.0868 842  GLY A CA    
5629 C  C     . GLY A 739 ? 0.9798 1.1861 1.0246 -0.0110 -0.1057 -0.0851 842  GLY A C     
5630 O  O     . GLY A 739 ? 1.0333 1.2497 1.0787 -0.0083 -0.1044 -0.0777 842  GLY A O     
5631 N  N     . ASP A 740 ? 1.0357 1.2409 1.0793 -0.0168 -0.1132 -0.0922 843  ASP A N     
5632 C  CA    . ASP A 740 ? 1.0853 1.3043 1.1280 -0.0200 -0.1215 -0.0920 843  ASP A CA    
5633 C  C     . ASP A 740 ? 1.0391 1.2696 1.1008 -0.0238 -0.1238 -0.0837 843  ASP A C     
5634 O  O     . ASP A 740 ? 1.0667 1.2969 1.1399 -0.0314 -0.1280 -0.0860 843  ASP A O     
5635 C  CB    . ASP A 740 ? 1.1693 1.3828 1.2029 -0.0255 -0.1293 -0.1035 843  ASP A CB    
5636 C  CG    . ASP A 740 ? 1.1350 1.3634 1.1628 -0.0273 -0.1384 -0.1043 843  ASP A CG    
5637 O  OD1   . ASP A 740 ? 1.2058 1.4475 1.2345 -0.0228 -0.1377 -0.0956 843  ASP A OD1   
5638 O  OD2   . ASP A 740 ? 1.1970 1.4229 1.2183 -0.0332 -0.1465 -0.1136 843  ASP A OD2   
5639 N  N     . CYS A 741 ? 1.0544 1.2948 1.1193 -0.0186 -0.1204 -0.0739 844  CYS A N     
5640 C  CA    . CYS A 741 ? 1.1034 1.3564 1.1854 -0.0196 -0.1212 -0.0648 844  CYS A CA    
5641 C  C     . CYS A 741 ? 1.0401 1.2863 1.1373 -0.0231 -0.1166 -0.0626 844  CYS A C     
5642 O  O     . CYS A 741 ? 1.0149 1.2705 1.1283 -0.0281 -0.1194 -0.0592 844  CYS A O     
5643 C  CB    . CYS A 741 ? 1.0573 1.3266 1.1446 -0.0245 -0.1319 -0.0660 844  CYS A CB    
5644 S  SG    . CYS A 741 ? 1.2185 1.4988 1.2889 -0.0183 -0.1368 -0.0645 844  CYS A SG    
5645 N  N     . VAL A 742 ? 0.9571 1.1879 1.0490 -0.0203 -0.1093 -0.0641 845  VAL A N     
5646 C  CA    . VAL A 742 ? 1.0237 1.2463 1.1268 -0.0216 -0.1034 -0.0606 845  VAL A CA    
5647 C  C     . VAL A 742 ? 0.9932 1.2101 1.0910 -0.0140 -0.0948 -0.0552 845  VAL A C     
5648 O  O     . VAL A 742 ? 1.0455 1.2584 1.1299 -0.0096 -0.0930 -0.0581 845  VAL A O     
5649 C  CB    . VAL A 742 ? 0.9650 1.1718 1.0664 -0.0266 -0.1041 -0.0690 845  VAL A CB    
5650 C  CG1   . VAL A 742 ? 0.9629 1.1744 1.0727 -0.0366 -0.1122 -0.0734 845  VAL A CG1   
5651 C  CG2   . VAL A 742 ? 0.9826 1.1792 1.0661 -0.0225 -0.1036 -0.0771 845  VAL A CG2   
5652 N  N     . GLY A 743 ? 0.9346 1.1518 1.0428 -0.0128 -0.0896 -0.0475 846  GLY A N     
5653 C  CA    . GLY A 743 ? 0.9644 1.1760 1.0667 -0.0063 -0.0821 -0.0427 846  GLY A CA    
5654 C  C     . GLY A 743 ? 0.8995 1.1083 1.0124 -0.0057 -0.0763 -0.0357 846  GLY A C     
5655 O  O     . GLY A 743 ? 0.8678 1.0799 0.9937 -0.0103 -0.0774 -0.0338 846  GLY A O     
5656 N  N     . LEU A 744 ? 0.8707 1.0736 0.9772 -0.0003 -0.0700 -0.0319 847  LEU A N     
5657 C  CA    . LEU A 744 ? 0.9091 1.1074 1.0214 0.0018  -0.0636 -0.0255 847  LEU A CA    
5658 C  C     . LEU A 744 ? 0.8965 1.0987 1.0060 0.0069  -0.0597 -0.0185 847  LEU A C     
5659 O  O     . LEU A 744 ? 0.9111 1.1127 1.0094 0.0096  -0.0596 -0.0194 847  LEU A O     
5660 C  CB    . LEU A 744 ? 0.8476 1.0327 0.9527 0.0040  -0.0597 -0.0278 847  LEU A CB    
5661 C  CG    . LEU A 744 ? 0.8492 1.0269 0.9523 0.0012  -0.0629 -0.0354 847  LEU A CG    
5662 C  CD1   . LEU A 744 ? 0.8375 1.0039 0.9330 0.0056  -0.0589 -0.0365 847  LEU A CD1   
5663 C  CD2   . LEU A 744 ? 0.8367 1.0134 0.9518 -0.0051 -0.0649 -0.0356 847  LEU A CD2   
5664 N  N     . ILE A 745 ? 0.8938 1.0992 1.0130 0.0081  -0.0557 -0.0115 848  ILE A N     
5665 C  CA    . ILE A 745 ? 0.9153 1.1220 1.0315 0.0141  -0.0508 -0.0046 848  ILE A CA    
5666 C  C     . ILE A 745 ? 0.8986 1.0950 1.0127 0.0171  -0.0432 -0.0008 848  ILE A C     
5667 O  O     . ILE A 745 ? 0.8808 1.0767 1.0046 0.0150  -0.0410 0.0013  848  ILE A O     
5668 C  CB    . ILE A 745 ? 0.9735 1.1952 1.1024 0.0149  -0.0522 0.0012  848  ILE A CB    
5669 C  CG1   . ILE A 745 ? 0.8772 1.1103 1.0085 0.0113  -0.0610 -0.0030 848  ILE A CG1   
5670 C  CG2   . ILE A 745 ? 0.9815 1.2020 1.1043 0.0228  -0.0467 0.0080  848  ILE A CG2   
5671 C  CD1   . ILE A 745 ? 0.9681 1.1989 1.0842 0.0147  -0.0628 -0.0046 848  ILE A CD1   
5672 N  N     . GLU A 746 ? 0.9418 1.1293 1.0422 0.0214  -0.0393 0.0001  849  GLU A N     
5673 C  CA    . GLU A 746 ? 0.9912 1.1687 1.0868 0.0249  -0.0325 0.0035  849  GLU A CA    
5674 C  C     . GLU A 746 ? 0.9173 1.0986 1.0198 0.0293  -0.0269 0.0115  849  GLU A C     
5675 O  O     . GLU A 746 ? 0.9294 1.1157 1.0313 0.0327  -0.0266 0.0147  849  GLU A O     
5676 C  CB    . GLU A 746 ? 1.0210 1.1882 1.0994 0.0271  -0.0308 0.0012  849  GLU A CB    
5677 C  CG    . GLU A 746 ? 0.9231 1.0799 0.9936 0.0313  -0.0240 0.0050  849  GLU A CG    
5678 C  CD    . GLU A 746 ? 1.0464 1.1936 1.0997 0.0321  -0.0231 0.0024  849  GLU A CD    
5679 O  OE1   . GLU A 746 ? 1.0966 1.2457 1.1454 0.0286  -0.0275 -0.0028 849  GLU A OE1   
5680 O  OE2   . GLU A 746 ? 1.0484 1.1861 1.0924 0.0358  -0.0177 0.0054  849  GLU A OE2   
5681 N  N     . VAL A 747 ? 0.9407 1.1195 1.0490 0.0299  -0.0218 0.0153  850  VAL A N     
5682 C  CA    . VAL A 747 ? 0.9513 1.1341 1.0662 0.0348  -0.0149 0.0233  850  VAL A CA    
5683 C  C     . VAL A 747 ? 0.9131 1.0817 1.0111 0.0414  -0.0081 0.0252  850  VAL A C     
5684 O  O     . VAL A 747 ? 0.9593 1.1163 1.0469 0.0411  -0.0066 0.0229  850  VAL A O     
5685 C  CB    . VAL A 747 ? 0.9390 1.1267 1.0690 0.0316  -0.0119 0.0269  850  VAL A CB    
5686 C  CG1   . VAL A 747 ? 0.9476 1.1404 1.0840 0.0376  -0.0034 0.0356  850  VAL A CG1   
5687 C  CG2   . VAL A 747 ? 0.9247 1.1255 1.0709 0.0238  -0.0191 0.0242  850  VAL A CG2   
5688 N  N     . VAL A 748 ? 0.8295 0.9983 0.9235 0.0476  -0.0043 0.0295  851  VAL A N     
5689 C  CA    . VAL A 748 ? 1.0726 1.2264 1.1500 0.0541  0.0031  0.0316  851  VAL A CA    
5690 C  C     . VAL A 748 ? 1.1087 1.2657 1.1941 0.0593  0.0116  0.0391  851  VAL A C     
5691 O  O     . VAL A 748 ? 1.0660 1.2390 1.1693 0.0604  0.0126  0.0443  851  VAL A O     
5692 C  CB    . VAL A 748 ? 1.0629 1.2108 1.1284 0.0586  0.0036  0.0319  851  VAL A CB    
5693 C  CG1   . VAL A 748 ? 1.1057 1.2679 1.1845 0.0633  0.0044  0.0380  851  VAL A CG1   
5694 C  CG2   . VAL A 748 ? 1.0792 1.2081 1.1248 0.0642  0.0109  0.0326  851  VAL A CG2   
5695 N  N     . ARG A 749 ? 1.1257 1.2690 1.1982 0.0624  0.0178  0.0398  852  ARG A N     
5696 C  CA    . ARG A 749 ? 1.2568 1.4019 1.3351 0.0671  0.0268  0.0468  852  ARG A CA    
5697 C  C     . ARG A 749 ? 1.2750 1.4172 1.3472 0.0772  0.0351  0.0523  852  ARG A C     
5698 O  O     . ARG A 749 ? 1.2760 1.4066 1.3321 0.0809  0.0349  0.0498  852  ARG A O     
5699 C  CB    . ARG A 749 ? 1.3170 1.4482 1.3823 0.0667  0.0297  0.0454  852  ARG A CB    
5700 C  CG    . ARG A 749 ? 1.3422 1.4765 1.4154 0.0587  0.0236  0.0420  852  ARG A CG    
5701 C  CD    . ARG A 749 ? 1.3602 1.4794 1.4153 0.0591  0.0234  0.0387  852  ARG A CD    
5702 N  NE    . ARG A 749 ? 1.5533 1.6733 1.6160 0.0548  0.0218  0.0389  852  ARG A NE    
5703 C  CZ    . ARG A 749 ? 1.6749 1.7915 1.7391 0.0568  0.0288  0.0449  852  ARG A CZ    
5704 N  NH1   . ARG A 749 ? 1.7633 1.8766 1.8219 0.0633  0.0382  0.0509  852  ARG A NH1   
5705 N  NH2   . ARG A 749 ? 1.4857 1.6007 1.5557 0.0526  0.0270  0.0450  852  ARG A NH2   
5706 N  N     . ASN A 750 ? 1.2124 1.3647 1.2975 0.0817  0.0430  0.0601  853  ASN A N     
5707 C  CA    . ASN A 750 ? 1.2616 1.4122 1.3422 0.0932  0.0528  0.0664  853  ASN A CA    
5708 C  C     . ASN A 750 ? 1.2266 1.3834 1.3097 0.0978  0.0500  0.0673  853  ASN A C     
5709 O  O     . ASN A 750 ? 1.2406 1.3859 1.3095 0.1077  0.0563  0.0694  853  ASN A O     
5710 C  CB    . ASN A 750 ? 1.2467 1.3725 1.2995 0.0992  0.0595  0.0645  853  ASN A CB    
5711 C  CG    . ASN A 750 ? 1.2417 1.3616 1.2903 0.0967  0.0630  0.0649  853  ASN A CG    
5712 O  OD1   . ASN A 750 ? 1.3717 1.4958 1.4256 0.1018  0.0726  0.0719  853  ASN A OD1   
5713 N  ND2   . ASN A 750 ? 1.1881 1.2989 1.2271 0.0893  0.0557  0.0581  853  ASN A ND2   
5714 N  N     . SER A 751 ? 1.1944 1.3678 1.2941 0.0913  0.0408  0.0657  854  SER A N     
5715 C  CA    . SER A 751 ? 1.1625 1.3437 1.2653 0.0955  0.0371  0.0672  854  SER A CA    
5716 C  C     . SER A 751 ? 1.1410 1.3513 1.2719 0.0967  0.0366  0.0741  854  SER A C     
5717 O  O     . SER A 751 ? 1.1360 1.3612 1.2855 0.0883  0.0338  0.0743  854  SER A O     
5718 C  CB    . SER A 751 ? 1.1588 1.3361 1.2553 0.0873  0.0261  0.0595  854  SER A CB    
5719 O  OG    . SER A 751 ? 1.1453 1.3350 1.2569 0.0765  0.0186  0.0559  854  SER A OG    
5720 N  N     . HIS A 752 ? 1.1317 1.3498 1.2652 0.1071  0.0394  0.0799  855  HIS A N     
5721 C  CA    . HIS A 752 ? 1.1443 1.3930 1.3049 0.1097  0.0387  0.0871  855  HIS A CA    
5722 C  C     . HIS A 752 ? 1.1586 1.4146 1.3187 0.1161  0.0333  0.0890  855  HIS A C     
5723 O  O     . HIS A 752 ? 1.1535 1.3891 1.2916 0.1244  0.0363  0.0885  855  HIS A O     
5724 C  CB    . HIS A 752 ? 1.1996 1.4557 1.3680 0.1200  0.0518  0.0961  855  HIS A CB    
5725 C  CG    . HIS A 752 ? 1.1680 1.4110 1.3298 0.1167  0.0593  0.0952  855  HIS A CG    
5726 N  ND1   . HIS A 752 ? 1.1523 1.4103 1.3340 0.1074  0.0595  0.0969  855  HIS A ND1   
5727 C  CD2   . HIS A 752 ? 1.2036 1.4190 1.3399 0.1212  0.0666  0.0928  855  HIS A CD2   
5728 C  CE1   . HIS A 752 ? 1.2813 1.5216 1.4496 0.1073  0.0671  0.0963  855  HIS A CE1   
5729 N  NE2   . HIS A 752 ? 1.2664 1.4816 1.4072 0.1156  0.0711  0.0936  855  HIS A NE2   
5730 N  N     . THR A 753 ? 1.1924 1.4769 1.3758 0.1121  0.0252  0.0911  856  THR A N     
5731 C  CA    . THR A 753 ? 1.2128 1.5074 1.3969 0.1189  0.0195  0.0938  856  THR A CA    
5732 C  C     . THR A 753 ? 1.2712 1.5745 1.4594 0.1361  0.0289  0.1042  856  THR A C     
5733 O  O     . THR A 753 ? 1.3142 1.6228 1.5107 0.1413  0.0390  0.1095  856  THR A O     
5734 C  CB    . THR A 753 ? 1.1975 1.5207 1.4042 0.1091  0.0070  0.0923  856  THR A CB    
5735 O  OG1   . THR A 753 ? 1.2592 1.6130 1.4945 0.1100  0.0093  0.0995  856  THR A OG1   
5736 C  CG2   . THR A 753 ? 1.1452 1.4604 1.3501 0.0927  -0.0004 0.0824  856  THR A CG2   
5737 N  N     . ILE A 754 ? 1.3164 1.6208 1.4979 0.1457  0.0259  0.1074  857  ILE A N     
5738 C  CA    . ILE A 754 ? 1.3374 1.6494 1.5215 0.1642  0.0346  0.1177  857  ILE A CA    
5739 C  C     . ILE A 754 ? 1.3765 1.7296 1.5953 0.1657  0.0344  0.1253  857  ILE A C     
5740 O  O     . ILE A 754 ? 1.4422 1.8038 1.6689 0.1777  0.0456  0.1333  857  ILE A O     
5741 C  CB    . ILE A 754 ? 1.4218 1.7255 1.5906 0.1740  0.0306  0.1199  857  ILE A CB    
5742 C  CG1   . ILE A 754 ? 1.4203 1.6824 1.5549 0.1716  0.0324  0.1127  857  ILE A CG1   
5743 C  CG2   . ILE A 754 ? 1.4779 1.7906 1.6501 0.1947  0.0394  0.1312  857  ILE A CG2   
5744 C  CD1   . ILE A 754 ? 1.3051 1.5385 1.4203 0.1783  0.0458  0.1125  857  ILE A CD1   
5745 N  N     . MET A 755 ? 1.3133 1.6929 1.5532 0.1533  0.0219  0.1228  858  MET A N     
5746 C  CA    . MET A 755 ? 1.2954 1.7162 1.5702 0.1519  0.0204  0.1294  858  MET A CA    
5747 C  C     . MET A 755 ? 1.3383 1.7619 1.6254 0.1457  0.0298  0.1304  858  MET A C     
5748 O  O     . MET A 755 ? 1.3695 1.8197 1.6795 0.1517  0.0366  0.1391  858  MET A O     
5749 C  CB    . MET A 755 ? 1.2417 1.6861 1.5330 0.1377  0.0040  0.1246  858  MET A CB    
5750 C  CG    . MET A 755 ? 1.2310 1.7213 1.5587 0.1361  0.0000  0.1314  858  MET A CG    
5751 S  SD    . MET A 755 ? 1.3502 1.8649 1.6931 0.1188  -0.0203 0.1242  858  MET A SD    
5752 C  CE    . MET A 755 ? 1.3034 1.7932 1.6388 0.0973  -0.0219 0.1121  858  MET A CE    
5753 N  N     . GLN A 756 ? 1.2862 1.6834 1.5584 0.1343  0.0307  0.1222  859  GLN A N     
5754 C  CA    . GLN A 756 ? 1.3304 1.7256 1.6096 0.1298  0.0407  0.1237  859  GLN A CA    
5755 C  C     . GLN A 756 ? 1.3815 1.7620 1.6469 0.1467  0.0566  0.1302  859  GLN A C     
5756 O  O     . GLN A 756 ? 1.4831 1.8787 1.7642 0.1503  0.0668  0.1373  859  GLN A O     
5757 C  CB    . GLN A 756 ? 1.2837 1.6531 1.5480 0.1151  0.0372  0.1136  859  GLN A CB    
5758 C  CG    . GLN A 756 ? 1.1981 1.5804 1.4761 0.0979  0.0231  0.1068  859  GLN A CG    
5759 C  CD    . GLN A 756 ? 1.1680 1.5227 1.4285 0.0863  0.0201  0.0971  859  GLN A CD    
5760 O  OE1   . GLN A 756 ? 1.2208 1.5504 1.4624 0.0897  0.0286  0.0960  859  GLN A OE1   
5761 N  NE2   . GLN A 756 ? 1.2189 1.5785 1.4850 0.0731  0.0079  0.0898  859  GLN A NE2   
5762 N  N     . ILE A 757 ? 1.3849 1.7353 1.6204 0.1568  0.0593  0.1277  860  ILE A N     
5763 C  CA    . ILE A 757 ? 1.4118 1.7440 1.6302 0.1733  0.0742  0.1328  860  ILE A CA    
5764 C  C     . ILE A 757 ? 1.4646 1.8250 1.7020 0.1895  0.0807  0.1443  860  ILE A C     
5765 O  O     . ILE A 757 ? 1.4897 1.8522 1.7291 0.2005  0.0945  0.1510  860  ILE A O     
5766 C  CB    . ILE A 757 ? 1.3623 1.6549 1.5441 0.1787  0.0744  0.1268  860  ILE A CB    
5767 C  CG1   . ILE A 757 ? 1.3119 1.5783 1.4757 0.1641  0.0704  0.1163  860  ILE A CG1   
5768 C  CG2   . ILE A 757 ? 1.3468 1.6203 1.5098 0.1974  0.0892  0.1321  860  ILE A CG2   
5769 N  N     . GLN A 758 ? 1.3829 1.7668 1.6346 0.1919  0.0709  0.1472  861  GLN A N     
5770 C  CA    . GLN A 758 ? 1.4399 1.8542 1.7113 0.2083  0.0758  0.1587  861  GLN A CA    
5771 C  C     . GLN A 758 ? 1.4892 1.9413 1.7958 0.2036  0.0803  0.1652  861  GLN A C     
5772 O  O     . GLN A 758 ? 1.5180 1.9863 1.8357 0.2187  0.0923  0.1750  861  GLN A O     
5773 C  CB    . GLN A 758 ? 1.5139 1.9466 1.7928 0.2105  0.0625  0.1601  861  GLN A CB    
5774 C  CG    . GLN A 758 ? 1.6709 2.1368 1.9697 0.2291  0.0660  0.1724  861  GLN A CG    
5775 C  CD    . GLN A 758 ? 1.7021 2.2195 2.0434 0.2206  0.0601  0.1773  861  GLN A CD    
5776 O  OE1   . GLN A 758 ? 1.6943 2.2212 2.0490 0.1998  0.0514  0.1708  861  GLN A OE1   
5777 N  NE2   . GLN A 758 ? 1.6545 2.2055 2.0171 0.2366  0.0648  0.1889  861  GLN A NE2   
5778 N  N     . CYS A 759 ? 1.4670 1.9329 1.7913 0.1829  0.0714  0.1601  862  CYS A N     
5779 C  CA    . CYS A 759 ? 1.4786 1.9785 1.8362 0.1756  0.0757  0.1659  862  CYS A CA    
5780 C  C     . CYS A 759 ? 1.5089 1.9911 1.8577 0.1775  0.0918  0.1678  862  CYS A C     
5781 O  O     . CYS A 759 ? 1.5402 2.0493 1.9137 0.1782  0.1006  0.1759  862  CYS A O     
5782 C  CB    . CYS A 759 ? 1.4135 1.9294 1.7901 0.1522  0.0614  0.1593  862  CYS A CB    
5783 S  SG    . CYS A 759 ? 1.5118 2.0570 1.9039 0.1487  0.0420  0.1578  862  CYS A SG    
5784 N  N     . LYS A 760 ? 1.5113 1.9501 1.8256 0.1780  0.0956  0.1607  863  LYS A N     
5785 C  CA    . LYS A 760 ? 1.6032 2.0219 1.9043 0.1804  0.1102  0.1618  863  LYS A CA    
5786 C  C     . LYS A 760 ? 1.6295 2.0375 1.9151 0.2035  0.1255  0.1687  863  LYS A C     
5787 O  O     . LYS A 760 ? 1.5700 1.9417 1.8241 0.2097  0.1339  0.1651  863  LYS A O     
5788 C  CB    . LYS A 760 ? 1.5475 1.9267 1.8193 0.1695  0.1060  0.1507  863  LYS A CB    
5789 C  CG    . LYS A 760 ? 1.5248 1.9114 1.8106 0.1475  0.0943  0.1444  863  LYS A CG    
5790 C  CD    . LYS A 760 ? 1.5165 1.8676 1.7736 0.1391  0.0863  0.1329  863  LYS A CD    
5791 C  CE    . LYS A 760 ? 1.4801 1.7971 1.7076 0.1451  0.0973  0.1309  863  LYS A CE    
5792 N  NZ    . LYS A 760 ? 1.2908 1.5766 1.4919 0.1373  0.0891  0.1199  863  LYS A NZ    
5793 N  N     . GLY A 761 ? 1.6446 2.0847 1.9520 0.2168  0.1291  0.1785  864  GLY A N     
5794 C  CA    . GLY A 761 ? 1.6070 2.0395 1.9016 0.2406  0.1440  0.1858  864  GLY A CA    
5795 C  C     . GLY A 761 ? 1.5329 2.0018 1.8513 0.2554  0.1434  0.1957  864  GLY A C     
5796 O  O     . GLY A 761 ? 1.4248 1.8793 1.7252 0.2724  0.1447  0.1973  864  GLY A O     
5797 N  N     . ASN A 770 ? 1.5544 1.9975 1.8146 0.3556  0.1406  0.2196  873  ASN A N     
5798 C  CA    . ASN A 770 ? 1.5365 1.9891 1.8056 0.3328  0.1213  0.2120  873  ASN A CA    
5799 C  C     . ASN A 770 ? 1.6310 2.0327 1.8601 0.3272  0.1158  0.2020  873  ASN A C     
5800 O  O     . ASN A 770 ? 1.6696 2.0594 1.8933 0.3055  0.1060  0.1916  873  ASN A O     
5801 C  CB    . ASN A 770 ? 1.5500 2.0502 1.8497 0.3372  0.1092  0.2198  873  ASN A CB    
5802 C  CG    . ASN A 770 ? 1.5997 2.1238 1.9202 0.3116  0.0907  0.2129  873  ASN A CG    
5803 O  OD1   . ASN A 770 ? 1.6413 2.1377 1.9451 0.2928  0.0846  0.2015  873  ASN A OD1   
5804 N  ND2   . ASN A 770 ? 1.4529 2.0291 1.8098 0.3109  0.0814  0.2196  873  ASN A ND2   
5805 N  N     . SER A 771 ? 1.5866 1.9581 1.7875 0.3471  0.1229  0.2053  874  SER A N     
5806 C  CA    . SER A 771 ? 1.5453 1.8688 1.7083 0.3422  0.1186  0.1969  874  SER A CA    
5807 C  C     . SER A 771 ? 1.5086 1.7857 1.6405 0.3364  0.1286  0.1879  874  SER A C     
5808 O  O     . SER A 771 ? 1.5182 1.7680 1.6312 0.3191  0.1214  0.1772  874  SER A O     
5809 C  CB    . SER A 771 ? 1.4858 1.7940 1.6304 0.3648  0.1217  0.2045  874  SER A CB    
5810 O  OG    . SER A 771 ? 1.4767 1.8270 1.6476 0.3694  0.1104  0.2123  874  SER A OG    
5811 N  N     . HIS A 772 ? 1.4693 1.7378 1.5951 0.3509  0.1450  0.1920  875  HIS A N     
5812 C  CA    . HIS A 772 ? 1.4790 1.7048 1.5743 0.3468  0.1548  0.1836  875  HIS A CA    
5813 C  C     . HIS A 772 ? 1.4677 1.7061 1.5776 0.3264  0.1524  0.1774  875  HIS A C     
5814 O  O     . HIS A 772 ? 1.4441 1.6530 1.5321 0.3236  0.1609  0.1715  875  HIS A O     
5815 C  CB    . HIS A 772 ? 1.4126 1.6227 1.4930 0.3713  0.1740  0.1902  875  HIS A CB    
5816 C  CG    . HIS A 772 ? 1.4623 1.6437 1.5167 0.3916  0.1787  0.1943  875  HIS A CG    
5817 N  ND1   . HIS A 772 ? 1.5525 1.7581 1.6221 0.4032  0.1725  0.2033  875  HIS A ND1   
5818 C  CD2   . HIS A 772 ? 1.4491 1.5780 1.4619 0.4025  0.1892  0.1906  875  HIS A CD2   
5819 C  CE1   . HIS A 772 ? 1.4866 1.6550 1.5250 0.4210  0.1794  0.2057  875  HIS A CE1   
5820 N  NE2   . HIS A 772 ? 1.4347 1.5554 1.4382 0.4204  0.1897  0.1978  875  HIS A NE2   
5821 N  N     . THR A 773 ? 1.4615 1.7416 1.6065 0.3122  0.1410  0.1786  876  THR A N     
5822 C  CA    . THR A 773 ? 1.4187 1.7099 1.5777 0.2931  0.1390  0.1734  876  THR A CA    
5823 C  C     . THR A 773 ? 1.4150 1.6693 1.5474 0.2754  0.1321  0.1604  876  THR A C     
5824 O  O     . THR A 773 ? 1.3924 1.6331 1.5167 0.2670  0.1370  0.1554  876  THR A O     
5825 C  CB    . THR A 773 ? 1.4500 1.7915 1.6511 0.2813  0.1276  0.1770  876  THR A CB    
5826 O  OG1   . THR A 773 ? 1.5386 1.8848 1.7408 0.2756  0.1123  0.1744  876  THR A OG1   
5827 C  CG2   . THR A 773 ? 1.5191 1.9019 1.7505 0.2968  0.1359  0.1900  876  THR A CG2   
5828 N  N     . LEU A 774 ? 1.4210 1.6599 1.5397 0.2699  0.1210  0.1553  877  LEU A N     
5829 C  CA    . LEU A 774 ? 1.3652 1.5715 1.4598 0.2535  0.1145  0.1433  877  LEU A CA    
5830 C  C     . LEU A 774 ? 1.4151 1.5763 1.4726 0.2603  0.1260  0.1389  877  LEU A C     
5831 O  O     . LEU A 774 ? 1.4038 1.5456 1.4474 0.2479  0.1255  0.1305  877  LEU A O     
5832 C  CB    . LEU A 774 ? 1.3357 1.5366 1.4238 0.2476  0.1015  0.1399  877  LEU A CB    
5833 C  CG    . LEU A 774 ? 1.2064 1.3742 1.2691 0.2319  0.0950  0.1282  877  LEU A CG    
5834 C  CD1   . LEU A 774 ? 1.0791 1.2601 1.1564 0.2124  0.0879  0.1214  877  LEU A CD1   
5835 C  CD2   . LEU A 774 ? 1.2842 1.4450 1.3379 0.2298  0.0851  0.1268  877  LEU A CD2   
5836 N  N     . HIS A 775 ? 1.4298 1.5735 1.4703 0.2801  0.1361  0.1442  878  HIS A N     
5837 C  CA    . HIS A 775 ? 1.4067 1.5057 1.4101 0.2871  0.1474  0.1396  878  HIS A CA    
5838 C  C     . HIS A 775 ? 1.4971 1.5985 1.5023 0.2880  0.1580  0.1396  878  HIS A C     
5839 O  O     . HIS A 775 ? 1.5275 1.5985 1.5075 0.2807  0.1606  0.1312  878  HIS A O     
5840 C  CB    . HIS A 775 ? 1.4040 1.4849 1.3902 0.3100  0.1571  0.1463  878  HIS A CB    
5841 C  CG    . HIS A 775 ? 1.4661 1.4954 1.4099 0.3163  0.1674  0.1403  878  HIS A CG    
5842 N  ND1   . HIS A 775 ? 1.5333 1.5387 1.4562 0.3381  0.1792  0.1455  878  HIS A ND1   
5843 C  CD2   . HIS A 775 ? 1.4700 1.4666 1.3877 0.3034  0.1672  0.1292  878  HIS A CD2   
5844 C  CE1   . HIS A 775 ? 1.5608 1.5192 1.4456 0.3376  0.1860  0.1373  878  HIS A CE1   
5845 N  NE2   . HIS A 775 ? 1.5385 1.4920 1.4200 0.3164  0.1785  0.1273  878  HIS A NE2   
5846 N  N     . GLN A 776 ? 1.5232 1.6618 1.5582 0.2965  0.1641  0.1492  879  GLN A N     
5847 C  CA    . GLN A 776 ? 1.5008 1.6446 1.5396 0.2969  0.1747  0.1504  879  GLN A CA    
5848 C  C     . GLN A 776 ? 1.5534 1.7043 1.6015 0.2741  0.1657  0.1434  879  GLN A C     
5849 O  O     . GLN A 776 ? 1.5750 1.7134 1.6117 0.2711  0.1727  0.1406  879  GLN A O     
5850 C  CB    . GLN A 776 ? 1.4865 1.6718 1.5580 0.3106  0.1835  0.1632  879  GLN A CB    
5851 C  CG    . GLN A 776 ? 1.5374 1.7136 1.5969 0.3370  0.1971  0.1710  879  GLN A CG    
5852 C  CD    . GLN A 776 ? 1.7324 1.8733 1.7596 0.3480  0.2134  0.1686  879  GLN A CD    
5853 O  OE1   . GLN A 776 ? 1.6349 1.7645 1.6528 0.3366  0.2152  0.1627  879  GLN A OE1   
5854 N  NE2   . GLN A 776 ? 1.7812 1.9036 1.7897 0.3711  0.2255  0.1732  879  GLN A NE2   
5855 N  N     . TRP A 777 ? 1.4351 1.6049 1.5021 0.2588  0.1503  0.1407  880  TRP A N     
5856 C  CA    . TRP A 777 ? 1.3980 1.5746 1.4745 0.2382  0.1417  0.1344  880  TRP A CA    
5857 C  C     . TRP A 777 ? 1.4159 1.5524 1.4581 0.2295  0.1399  0.1234  880  TRP A C     
5858 O  O     . TRP A 777 ? 1.3848 1.5196 1.4269 0.2182  0.1389  0.1193  880  TRP A O     
5859 C  CB    . TRP A 777 ? 1.3716 1.5743 1.4727 0.2251  0.1258  0.1333  880  TRP A CB    
5860 C  CG    . TRP A 777 ? 1.3580 1.5704 1.4719 0.2052  0.1173  0.1277  880  TRP A CG    
5861 C  CD1   . TRP A 777 ? 1.3383 1.5805 1.4809 0.1982  0.1180  0.1321  880  TRP A CD1   
5862 C  CD2   . TRP A 777 ? 1.3556 1.5474 1.4537 0.1899  0.1070  0.1170  880  TRP A CD2   
5863 N  NE1   . TRP A 777 ? 1.3481 1.5868 1.4923 0.1802  0.1091  0.1247  880  TRP A NE1   
5864 C  CE2   . TRP A 777 ? 1.3681 1.5773 1.4857 0.1755  0.1022  0.1155  880  TRP A CE2   
5865 C  CE3   . TRP A 777 ? 1.3471 1.5077 1.4169 0.1870  0.1019  0.1089  880  TRP A CE3   
5866 C  CZ2   . TRP A 777 ? 1.4207 1.6174 1.5300 0.1601  0.0926  0.1063  880  TRP A CZ2   
5867 C  CZ3   . TRP A 777 ? 1.3734 1.5245 1.4369 0.1708  0.0922  0.0998  880  TRP A CZ3   
5868 C  CH2   . TRP A 777 ? 1.3675 1.5367 1.4505 0.1584  0.0877  0.0986  880  TRP A CH2   
5869 N  N     . LEU A 778 ? 1.4681 1.5723 1.4812 0.2344  0.1395  0.1186  881  LEU A N     
5870 C  CA    . LEU A 778 ? 1.4855 1.5527 1.4662 0.2256  0.1375  0.1079  881  LEU A CA    
5871 C  C     . LEU A 778 ? 1.5482 1.5905 1.5038 0.2357  0.1514  0.1073  881  LEU A C     
5872 O  O     . LEU A 778 ? 1.5376 1.5633 1.4770 0.2268  0.1507  0.1004  881  LEU A O     
5873 C  CB    . LEU A 778 ? 1.4862 1.5284 1.4459 0.2244  0.1312  0.1028  881  LEU A CB    
5874 C  CG    . LEU A 778 ? 1.3415 1.4000 1.3172 0.2109  0.1161  0.1001  881  LEU A CG    
5875 C  CD1   . LEU A 778 ? 1.2798 1.3107 1.2318 0.2113  0.1125  0.0962  881  LEU A CD1   
5876 C  CD2   . LEU A 778 ? 1.3102 1.3744 1.2920 0.1921  0.1070  0.0927  881  LEU A CD2   
5877 N  N     . LYS A 779 ? 1.7305 1.7699 1.6816 0.2552  0.1642  0.1146  882  LYS A N     
5878 C  CA    . LYS A 779 ? 1.6638 1.6788 1.5894 0.2665  0.1786  0.1141  882  LYS A CA    
5879 C  C     . LYS A 779 ? 1.6455 1.6798 1.5854 0.2626  0.1837  0.1170  882  LYS A C     
5880 O  O     . LYS A 779 ? 1.8218 1.8332 1.7371 0.2641  0.1910  0.1130  882  LYS A O     
5881 C  CB    . LYS A 779 ? 1.6598 1.6709 1.5804 0.2898  0.1919  0.1223  882  LYS A CB    
5882 C  CG    . LYS A 779 ? 1.8947 1.8754 1.7838 0.3035  0.2077  0.1211  882  LYS A CG    
5883 C  CD    . LYS A 779 ? 1.8250 1.7603 1.6736 0.2940  0.2040  0.1080  882  LYS A CD    
5884 C  CE    . LYS A 779 ? 1.9638 1.8648 1.7768 0.3087  0.2194  0.1059  882  LYS A CE    
5885 N  NZ    . LYS A 779 ? 2.0301 1.9164 1.8318 0.3301  0.2302  0.1114  882  LYS A NZ    
5886 N  N     . ASP A 780 ? 1.5472 1.6225 1.5256 0.2571  0.1799  0.1239  883  ASP A N     
5887 C  CA    . ASP A 780 ? 1.5265 1.6193 1.5192 0.2513  0.1843  0.1270  883  ASP A CA    
5888 C  C     . ASP A 780 ? 1.5753 1.6544 1.5570 0.2330  0.1743  0.1175  883  ASP A C     
5889 O  O     . ASP A 780 ? 1.4859 1.5586 1.4586 0.2311  0.1803  0.1171  883  ASP A O     
5890 C  CB    . ASP A 780 ? 1.5090 1.6486 1.5463 0.2489  0.1825  0.1365  883  ASP A CB    
5891 C  CG    . ASP A 780 ? 1.5903 1.7491 1.6418 0.2681  0.1931  0.1471  883  ASP A CG    
5892 O  OD1   . ASP A 780 ? 1.6460 1.7850 1.6753 0.2849  0.2072  0.1492  883  ASP A OD1   
5893 O  OD2   . ASP A 780 ? 1.5525 1.7464 1.6369 0.2669  0.1873  0.1532  883  ASP A OD2   
5894 N  N     . LYS A 781 ? 1.5274 1.6024 1.5091 0.2202  0.1595  0.1104  884  LYS A N     
5895 C  CA    . LYS A 781 ? 1.4819 1.5473 1.4558 0.2033  0.1490  0.1017  884  LYS A CA    
5896 C  C     . LYS A 781 ? 1.4996 1.5263 1.4354 0.2013  0.1463  0.0914  884  LYS A C     
5897 O  O     . LYS A 781 ? 1.4667 1.4854 1.3951 0.1876  0.1363  0.0836  884  LYS A O     
5898 C  CB    . LYS A 781 ? 1.3559 1.4443 1.3560 0.1893  0.1344  0.1003  884  LYS A CB    
5899 C  CG    . LYS A 781 ? 1.3285 1.4557 1.3666 0.1906  0.1355  0.1099  884  LYS A CG    
5900 C  CD    . LYS A 781 ? 1.3080 1.4557 1.3696 0.1742  0.1215  0.1071  884  LYS A CD    
5901 C  CE    . LYS A 781 ? 1.2920 1.4356 1.3519 0.1622  0.1193  0.1034  884  LYS A CE    
5902 N  NZ    . LYS A 781 ? 1.3402 1.5058 1.4259 0.1477  0.1080  0.1022  884  LYS A NZ    
5903 N  N     . ASN A 782 ? 1.5610 1.5636 1.4727 0.2146  0.1550  0.0911  885  ASN A N     
5904 C  CA    . ASN A 782 ? 1.5962 1.5597 1.4696 0.2126  0.1539  0.0811  885  ASN A CA    
5905 C  C     . ASN A 782 ? 1.6810 1.6215 1.5292 0.2299  0.1695  0.0832  885  ASN A C     
5906 O  O     . ASN A 782 ? 1.7015 1.6436 1.5531 0.2445  0.1775  0.0896  885  ASN A O     
5907 C  CB    . ASN A 782 ? 1.6059 1.5577 1.4731 0.2073  0.1445  0.0762  885  ASN A CB    
5908 C  CG    . ASN A 782 ? 1.4214 1.3948 1.3115 0.1910  0.1296  0.0737  885  ASN A CG    
5909 O  OD1   . ASN A 782 ? 1.2798 1.2437 1.1598 0.1775  0.1207  0.0653  885  ASN A OD1   
5910 N  ND2   . ASN A 782 ? 1.3983 1.4018 1.3192 0.1925  0.1267  0.0808  885  ASN A ND2   
5911 N  N     . LYS A 783 ? 1.8515 1.7705 1.6733 0.2291  0.1737  0.0779  886  LYS A N     
5912 C  CA    . LYS A 783 ? 1.6816 1.5775 1.4768 0.2455  0.1891  0.0791  886  LYS A CA    
5913 C  C     . LYS A 783 ? 1.8157 1.6784 1.5836 0.2540  0.1924  0.0749  886  LYS A C     
5914 O  O     . LYS A 783 ? 1.9634 1.8200 1.7318 0.2459  0.1823  0.0708  886  LYS A O     
5915 C  CB    . LYS A 783 ? 1.6814 1.5586 1.4501 0.2410  0.1906  0.0727  886  LYS A CB    
5916 C  CG    . LYS A 783 ? 1.8800 1.7848 1.6704 0.2363  0.1914  0.0784  886  LYS A CG    
5917 C  CD    . LYS A 783 ? 1.7169 1.6316 1.5178 0.2168  0.1751  0.0728  886  LYS A CD    
5918 C  CE    . LYS A 783 ? 1.6707 1.6065 1.4877 0.2129  0.1768  0.0783  886  LYS A CE    
5919 N  NZ    . LYS A 783 ? 1.5827 1.5250 1.4066 0.1958  0.1618  0.0726  886  LYS A NZ    
5920 N  N     . GLY A 784 ? 1.7797 1.6190 1.5220 0.2705  0.2071  0.0759  887  GLY A N     
5921 C  CA    . GLY A 784 ? 1.7968 1.6004 1.5104 0.2799  0.2118  0.0720  887  GLY A CA    
5922 C  C     . GLY A 784 ? 1.8368 1.6056 1.5198 0.2648  0.2013  0.0585  887  GLY A C     
5923 O  O     . GLY A 784 ? 1.8587 1.6024 1.5255 0.2662  0.2003  0.0552  887  GLY A O     
5924 N  N     . GLU A 785 ? 1.8054 1.5729 1.4804 0.2501  0.1934  0.0510  888  GLU A N     
5925 C  CA    . GLU A 785 ? 1.8918 1.6323 1.5420 0.2338  0.1819  0.0383  888  GLU A CA    
5926 C  C     . GLU A 785 ? 1.8694 1.6316 1.5457 0.2171  0.1664  0.0373  888  GLU A C     
5927 O  O     . GLU A 785 ? 1.8580 1.6002 1.5210 0.2078  0.1593  0.0306  888  GLU A O     
5928 C  CB    . GLU A 785 ? 1.8299 1.5598 1.4585 0.2265  0.1799  0.0307  888  GLU A CB    
5929 C  CG    . GLU A 785 ? 2.0660 1.7691 1.6620 0.2422  0.1949  0.0298  888  GLU A CG    
5930 C  CD    . GLU A 785 ? 2.0676 1.7621 1.6417 0.2354  0.1922  0.0227  888  GLU A CD    
5931 O  OE1   . GLU A 785 ? 1.9791 1.6922 1.5670 0.2198  0.1792  0.0200  888  GLU A OE1   
5932 O  OE2   . GLU A 785 ? 1.8958 1.5645 1.4378 0.2465  0.2033  0.0200  888  GLU A OE2   
5933 N  N     . ILE A 786 ? 1.7790 1.5810 1.4917 0.2128  0.1614  0.0440  889  ILE A N     
5934 C  CA    . ILE A 786 ? 1.6885 1.5126 1.4269 0.1985  0.1476  0.0436  889  ILE A CA    
5935 C  C     . ILE A 786 ? 1.6865 1.5211 1.4431 0.2057  0.1487  0.0508  889  ILE A C     
5936 O  O     . ILE A 786 ? 1.6501 1.4988 1.4237 0.1950  0.1377  0.0501  889  ILE A O     
5937 C  CB    . ILE A 786 ? 1.6290 1.4887 1.3971 0.1908  0.1417  0.0472  889  ILE A CB    
5938 C  CG1   . ILE A 786 ? 1.6302 1.4815 1.3807 0.1902  0.1449  0.0438  889  ILE A CG1   
5939 C  CG2   . ILE A 786 ? 1.7170 1.5906 1.5004 0.1731  0.1260  0.0424  889  ILE A CG2   
5940 C  CD1   . ILE A 786 ? 1.6301 1.5113 1.4057 0.1820  0.1391  0.0470  889  ILE A CD1   
5941 N  N     . TYR A 787 ? 1.6974 1.5258 1.4500 0.2245  0.1617  0.0578  890  TYR A N     
5942 C  CA    . TYR A 787 ? 1.6137 1.4535 1.3833 0.2335  0.1629  0.0657  890  TYR A CA    
5943 C  C     . TYR A 787 ? 1.5786 1.3948 1.3324 0.2253  0.1553  0.0598  890  TYR A C     
5944 O  O     . TYR A 787 ? 1.5947 1.4297 1.3695 0.2207  0.1474  0.0632  890  TYR A O     
5945 C  CB    . TYR A 787 ? 1.6248 1.4565 1.3866 0.2566  0.1792  0.0735  890  TYR A CB    
5946 C  CG    . TYR A 787 ? 1.5042 1.3434 1.2784 0.2689  0.1814  0.0819  890  TYR A CG    
5947 C  CD1   . TYR A 787 ? 1.4595 1.3423 1.2733 0.2725  0.1789  0.0920  890  TYR A CD1   
5948 C  CD2   . TYR A 787 ? 1.4752 1.2772 1.2207 0.2770  0.1860  0.0798  890  TYR A CD2   
5949 C  CE1   . TYR A 787 ? 1.4304 1.3220 1.2553 0.2845  0.1802  0.1000  890  TYR A CE1   
5950 C  CE2   . TYR A 787 ? 1.4714 1.2797 1.2269 0.2896  0.1881  0.0883  890  TYR A CE2   
5951 C  CZ    . TYR A 787 ? 1.4456 1.3000 1.2411 0.2937  0.1849  0.0985  890  TYR A CZ    
5952 O  OH    . TYR A 787 ? 1.5394 1.4018 1.3447 0.3069  0.1862  0.1073  890  TYR A OH    
5953 N  N     . ASP A 788 ? 1.5673 1.3419 1.2836 0.2227  0.1577  0.0509  891  ASP A N     
5954 C  CA    . ASP A 788 ? 1.5860 1.3353 1.2855 0.2139  0.1517  0.0454  891  ASP A CA    
5955 C  C     . ASP A 788 ? 1.6264 1.3929 1.3409 0.1923  0.1362  0.0399  891  ASP A C     
5956 O  O     . ASP A 788 ? 1.6013 1.3646 1.3179 0.1857  0.1301  0.0396  891  ASP A O     
5957 C  CB    . ASP A 788 ? 1.6148 1.3149 1.2702 0.2141  0.1577  0.0361  891  ASP A CB    
5958 C  CG    . ASP A 788 ? 1.6732 1.3459 1.3090 0.2350  0.1719  0.0413  891  ASP A CG    
5959 O  OD1   . ASP A 788 ? 1.6520 1.3462 1.3099 0.2496  0.1765  0.0525  891  ASP A OD1   
5960 O  OD2   . ASP A 788 ? 1.7300 1.3595 1.3279 0.2370  0.1782  0.0339  891  ASP A OD2   
5961 N  N     . ALA A 789 ? 1.6772 1.4617 1.4014 0.1819  0.1301  0.0360  892  ALA A N     
5962 C  CA    . ALA A 789 ? 1.5430 1.3466 1.2833 0.1632  0.1160  0.0314  892  ALA A CA    
5963 C  C     . ALA A 789 ? 1.5715 1.4138 1.3494 0.1638  0.1108  0.0396  892  ALA A C     
5964 O  O     . ALA A 789 ? 1.6547 1.5090 1.4445 0.1512  0.1003  0.0372  892  ALA A O     
5965 C  CB    . ALA A 789 ? 1.6002 1.4095 1.3375 0.1534  0.1113  0.0250  892  ALA A CB    
5966 N  N     . ALA A 790 ? 1.6164 1.4791 1.4131 0.1779  0.1182  0.0491  893  ALA A N     
5967 C  CA    . ALA A 790 ? 1.4605 1.3609 1.2930 0.1779  0.1129  0.0566  893  ALA A CA    
5968 C  C     . ALA A 790 ? 1.4032 1.3020 1.2386 0.1840  0.1124  0.0615  893  ALA A C     
5969 O  O     . ALA A 790 ? 1.4262 1.3454 1.2808 0.1762  0.1028  0.0626  893  ALA A O     
5970 C  CB    . ALA A 790 ? 1.5031 1.4282 1.3561 0.1891  0.1206  0.0650  893  ALA A CB    
5971 N  N     . ILE A 791 ? 1.4580 1.3322 1.2737 0.1988  0.1227  0.0648  894  ILE A N     
5972 C  CA    . ILE A 791 ? 1.4321 1.3019 1.2477 0.2061  0.1227  0.0702  894  ILE A CA    
5973 C  C     . ILE A 791 ? 1.4536 1.3012 1.2519 0.1916  0.1148  0.0628  894  ILE A C     
5974 O  O     . ILE A 791 ? 1.4659 1.3202 1.2718 0.1907  0.1098  0.0665  894  ILE A O     
5975 C  CB    . ILE A 791 ? 1.4658 1.3131 1.2634 0.2274  0.1369  0.0762  894  ILE A CB    
5976 C  CG1   . ILE A 791 ? 1.5332 1.3379 1.2932 0.2276  0.1446  0.0679  894  ILE A CG1   
5977 C  CG2   . ILE A 791 ? 1.3723 1.2515 1.1953 0.2429  0.1440  0.0863  894  ILE A CG2   
5978 C  CD1   . ILE A 791 ? 1.5711 1.3339 1.2991 0.2217  0.1438  0.0616  894  ILE A CD1   
5979 N  N     . ASP A 792 ? 1.4887 1.3107 1.2635 0.1798  0.1135  0.0526  895  ASP A N     
5980 C  CA    . ASP A 792 ? 1.4675 1.2716 1.2281 0.1639  0.1060  0.0454  895  ASP A CA    
5981 C  C     . ASP A 792 ? 1.4165 1.2537 1.2038 0.1497  0.0933  0.0443  895  ASP A C     
5982 O  O     . ASP A 792 ? 1.4236 1.2623 1.2139 0.1442  0.0880  0.0453  895  ASP A O     
5983 C  CB    . ASP A 792 ? 1.4520 1.2252 1.1835 0.1539  0.1068  0.0344  895  ASP A CB    
5984 C  CG    . ASP A 792 ? 1.4103 1.1606 1.1240 0.1382  0.1011  0.0273  895  ASP A CG    
5985 O  OD1   . ASP A 792 ? 1.4056 1.1278 1.1006 0.1433  0.1064  0.0294  895  ASP A OD1   
5986 O  OD2   . ASP A 792 ? 1.4326 1.1930 1.1511 0.1210  0.0916  0.0201  895  ASP A OD2   
5987 N  N     . LEU A 793 ? 1.3865 1.2493 1.1924 0.1443  0.0888  0.0424  896  LEU A N     
5988 C  CA    . LEU A 793 ? 1.3415 1.2356 1.1730 0.1325  0.0776  0.0416  896  LEU A CA    
5989 C  C     . LEU A 793 ? 1.3319 1.2510 1.1868 0.1400  0.0756  0.0504  896  LEU A C     
5990 O  O     . LEU A 793 ? 1.3832 1.3192 1.2518 0.1308  0.0666  0.0496  896  LEU A O     
5991 C  CB    . LEU A 793 ? 1.3535 1.2676 1.1991 0.1280  0.0749  0.0392  896  LEU A CB    
5992 C  CG    . LEU A 793 ? 1.3440 1.2893 1.2156 0.1169  0.0641  0.0379  896  LEU A CG    
5993 C  CD1   . LEU A 793 ? 1.3409 1.2794 1.2046 0.1021  0.0557  0.0306  896  LEU A CD1   
5994 C  CD2   . LEU A 793 ? 1.2850 1.2441 1.1663 0.1146  0.0636  0.0365  896  LEU A CD2   
5995 N  N     . PHE A 794 ? 1.3447 1.2673 1.2042 0.1569  0.0839  0.0589  897  PHE A N     
5996 C  CA    . PHE A 794 ? 1.3202 1.2683 1.2020 0.1648  0.0816  0.0677  897  PHE A CA    
5997 C  C     . PHE A 794 ? 1.3754 1.3066 1.2434 0.1662  0.0803  0.0696  897  PHE A C     
5998 O  O     . PHE A 794 ? 1.3496 1.3005 1.2326 0.1625  0.0723  0.0720  897  PHE A O     
5999 C  CB    . PHE A 794 ? 1.3011 1.2603 1.1929 0.1830  0.0911  0.0767  897  PHE A CB    
6000 C  CG    . PHE A 794 ? 1.2334 1.2260 1.1528 0.1905  0.0876  0.0858  897  PHE A CG    
6001 C  CD1   . PHE A 794 ? 1.1954 1.2252 1.1458 0.1853  0.0818  0.0876  897  PHE A CD1   
6002 C  CD2   . PHE A 794 ? 1.3279 1.3144 1.2415 0.2027  0.0899  0.0927  897  PHE A CD2   
6003 C  CE1   . PHE A 794 ? 1.2166 1.2783 1.1925 0.1909  0.0776  0.0953  897  PHE A CE1   
6004 C  CE2   . PHE A 794 ? 1.3705 1.3900 1.3095 0.2098  0.0856  0.1011  897  PHE A CE2   
6005 C  CZ    . PHE A 794 ? 1.3075 1.3654 1.2780 0.2034  0.0791  0.1020  897  PHE A CZ    
6006 N  N     . THR A 795 ? 1.5247 1.4180 1.3628 0.1715  0.0881  0.0684  898  THR A N     
6007 C  CA    . THR A 795 ? 1.5588 1.4319 1.3811 0.1733  0.0883  0.0709  898  THR A CA    
6008 C  C     . THR A 795 ? 1.5564 1.4271 1.3753 0.1538  0.0788  0.0638  898  THR A C     
6009 O  O     . THR A 795 ? 1.5554 1.4302 1.3766 0.1525  0.0746  0.0673  898  THR A O     
6010 C  CB    . THR A 795 ? 1.5805 1.4095 1.3694 0.1827  0.0997  0.0706  898  THR A CB    
6011 O  OG1   . THR A 795 ? 1.7302 1.5364 1.5001 0.1709  0.1006  0.0601  898  THR A OG1   
6012 C  CG2   . THR A 795 ? 1.6735 1.5059 1.4659 0.2048  0.1101  0.0790  898  THR A CG2   
6013 N  N     . ARG A 796 ? 1.4186 1.2839 1.2321 0.1390  0.0755  0.0541  899  ARG A N     
6014 C  CA    . ARG A 796 ? 1.3812 1.2458 1.1921 0.1208  0.0672  0.0473  899  ARG A CA    
6015 C  C     . ARG A 796 ? 1.3197 1.2228 1.1595 0.1147  0.0572  0.0484  899  ARG A C     
6016 O  O     . ARG A 796 ? 1.2954 1.2015 1.1355 0.1053  0.0514  0.0470  899  ARG A O     
6017 C  CB    . ARG A 796 ? 1.3810 1.2310 1.1784 0.1078  0.0662  0.0369  899  ARG A CB    
6018 C  CG    . ARG A 796 ? 1.4833 1.2933 1.2497 0.1124  0.0756  0.0342  899  ARG A CG    
6019 C  CD    . ARG A 796 ? 1.4991 1.2979 1.2528 0.0994  0.0733  0.0236  899  ARG A CD    
6020 N  NE    . ARG A 796 ? 1.6117 1.3915 1.3492 0.0829  0.0695  0.0167  899  ARG A NE    
6021 C  CZ    . ARG A 796 ? 1.6343 1.3749 1.3423 0.0812  0.0754  0.0140  899  ARG A CZ    
6022 N  NH1   . ARG A 796 ? 1.5942 1.3082 1.2837 0.0960  0.0856  0.0172  899  ARG A NH1   
6023 N  NH2   . ARG A 796 ? 1.7234 1.4507 1.4200 0.0640  0.0713  0.0079  899  ARG A NH2   
6024 N  N     . SER A 797 ? 1.3202 1.2518 1.1834 0.1197  0.0554  0.0509  900  SER A N     
6025 C  CA    . SER A 797 ? 1.2446 1.2107 1.1341 0.1144  0.0461  0.0517  900  SER A CA    
6026 C  C     . SER A 797 ? 1.2462 1.2249 1.1447 0.1237  0.0446  0.0602  900  SER A C     
6027 O  O     . SER A 797 ? 1.2258 1.2230 1.1360 0.1170  0.0364  0.0597  900  SER A O     
6028 C  CB    . SER A 797 ? 1.2010 1.1916 1.1120 0.1156  0.0450  0.0517  900  SER A CB    
6029 O  OG    . SER A 797 ? 1.2134 1.2094 1.1311 0.1310  0.0522  0.0596  900  SER A OG    
6030 N  N     . CYS A 798 ? 1.2645 1.2340 1.1570 0.1397  0.0524  0.0680  901  CYS A N     
6031 C  CA    . CYS A 798 ? 1.2494 1.2303 1.1485 0.1500  0.0508  0.0768  901  CYS A CA    
6032 C  C     . CYS A 798 ? 1.2604 1.2202 1.1398 0.1449  0.0493  0.0764  901  CYS A C     
6033 O  O     . CYS A 798 ? 1.2851 1.2613 1.1729 0.1440  0.0427  0.0796  901  CYS A O     
6034 C  CB    . CYS A 798 ? 1.2489 1.2249 1.1458 0.1700  0.0602  0.0858  901  CYS A CB    
6035 S  SG    . CYS A 798 ? 1.5898 1.6077 1.5211 0.1790  0.0595  0.0916  901  CYS A SG    
6036 N  N     . ALA A 799 ? 1.2708 1.1937 1.1230 0.1411  0.0556  0.0724  902  ALA A N     
6037 C  CA    . ALA A 799 ? 1.2811 1.1814 1.1134 0.1350  0.0554  0.0723  902  ALA A CA    
6038 C  C     . ALA A 799 ? 1.2920 1.2108 1.1346 0.1183  0.0456  0.0668  902  ALA A C     
6039 O  O     . ALA A 799 ? 1.2340 1.1514 1.0714 0.1161  0.0430  0.0699  902  ALA A O     
6040 C  CB    . ALA A 799 ? 1.3063 1.1642 1.1088 0.1306  0.0633  0.0673  902  ALA A CB    
6041 N  N     . GLY A 800 ? 1.2285 1.1643 1.0850 0.1074  0.0406  0.0590  903  GLY A N     
6042 C  CA    . GLY A 800 ? 1.2110 1.1651 1.0777 0.0930  0.0318  0.0536  903  GLY A CA    
6043 C  C     . GLY A 800 ? 1.2060 1.1916 1.0933 0.0973  0.0247  0.0583  903  GLY A C     
6044 O  O     . GLY A 800 ? 1.3148 1.3052 1.2003 0.0921  0.0203  0.0588  903  GLY A O     
6045 N  N     . TYR A 801 ? 1.1799 1.1876 1.0868 0.1063  0.0234  0.0618  904  TYR A N     
6046 C  CA    . TYR A 801 ? 1.1664 1.2055 1.0938 0.1092  0.0156  0.0654  904  TYR A CA    
6047 C  C     . TYR A 801 ? 1.2807 1.3174 1.2013 0.1217  0.0168  0.0749  904  TYR A C     
6048 O  O     . TYR A 801 ? 1.2284 1.2851 1.1581 0.1215  0.0094  0.0771  904  TYR A O     
6049 C  CB    . TYR A 801 ? 1.0730 1.1371 1.0242 0.1133  0.0140  0.0660  904  TYR A CB    
6050 C  CG    . TYR A 801 ? 1.1165 1.1912 1.0788 0.1004  0.0095  0.0573  904  TYR A CG    
6051 C  CD1   . TYR A 801 ? 1.0933 1.1908 1.0706 0.0920  0.0003  0.0534  904  TYR A CD1   
6052 C  CD2   . TYR A 801 ? 1.0799 1.1407 1.0361 0.0972  0.0146  0.0528  904  TYR A CD2   
6053 C  CE1   . TYR A 801 ? 1.0985 1.2039 1.0847 0.0816  -0.0033 0.0458  904  TYR A CE1   
6054 C  CE2   . TYR A 801 ? 1.0145 1.0847 0.9798 0.0867  0.0105  0.0456  904  TYR A CE2   
6055 C  CZ    . TYR A 801 ? 1.0073 1.0994 0.9878 0.0792  0.0018  0.0423  904  TYR A CZ    
6056 O  OH    . TYR A 801 ? 0.9489 1.0486 0.9375 0.0701  -0.0018 0.0356  904  TYR A OH    
6057 N  N     . CYS A 802 ? 1.2315 1.2431 1.1351 0.1330  0.0258  0.0806  905  CYS A N     
6058 C  CA    . CYS A 802 ? 1.2489 1.2542 1.1426 0.1456  0.0275  0.0903  905  CYS A CA    
6059 C  C     . CYS A 802 ? 1.2357 1.2274 1.1128 0.1366  0.0251  0.0891  905  CYS A C     
6060 O  O     . CYS A 802 ? 1.2618 1.2629 1.1386 0.1424  0.0213  0.0954  905  CYS A O     
6061 C  CB    . CYS A 802 ? 1.2865 1.2631 1.1626 0.1600  0.0389  0.0961  905  CYS A CB    
6062 S  SG    . CYS A 802 ? 1.6290 1.5957 1.4917 0.1790  0.0422  0.1095  905  CYS A SG    
6063 N  N     . VAL A 803 ? 1.2247 1.1957 1.0883 0.1222  0.0274  0.0812  906  VAL A N     
6064 C  CA    . VAL A 803 ? 1.2050 1.1638 1.0536 0.1121  0.0261  0.0800  906  VAL A CA    
6065 C  C     . VAL A 803 ? 1.2103 1.1988 1.0758 0.1007  0.0163  0.0744  906  VAL A C     
6066 O  O     . VAL A 803 ? 1.1418 1.1357 1.0031 0.0990  0.0127  0.0770  906  VAL A O     
6067 C  CB    . VAL A 803 ? 1.1605 1.0850 0.9875 0.1011  0.0330  0.0742  906  VAL A CB    
6068 C  CG1   . VAL A 803 ? 1.1463 1.0641 0.9628 0.0870  0.0313  0.0716  906  VAL A CG1   
6069 C  CG2   . VAL A 803 ? 1.2104 1.1001 1.0154 0.1129  0.0432  0.0802  906  VAL A CG2   
6070 N  N     . ALA A 804 ? 1.1858 1.1929 1.0693 0.0936  0.0120  0.0669  907  ALA A N     
6071 C  CA    . ALA A 804 ? 1.1909 1.2229 1.0887 0.0829  0.0034  0.0606  907  ALA A CA    
6072 C  C     . ALA A 804 ? 1.1324 1.1911 1.0438 0.0902  -0.0040 0.0654  907  ALA A C     
6073 O  O     . ALA A 804 ? 1.0407 1.1094 0.9512 0.0849  -0.0092 0.0640  907  ALA A O     
6074 C  CB    . ALA A 804 ? 1.0841 1.1277 0.9971 0.0756  0.0012  0.0525  907  ALA A CB    
6075 N  N     . THR A 805 ? 1.1551 1.2267 1.0792 0.1023  -0.0045 0.0709  908  THR A N     
6076 C  CA    . THR A 805 ? 1.1434 1.2432 1.0822 0.1083  -0.0127 0.0749  908  THR A CA    
6077 C  C     . THR A 805 ? 1.1150 1.2080 1.0383 0.1164  -0.0128 0.0831  908  THR A C     
6078 O  O     . THR A 805 ? 1.1275 1.2411 1.0567 0.1168  -0.0210 0.0842  908  THR A O     
6079 C  CB    . THR A 805 ? 1.0996 1.2171 1.0576 0.1187  -0.0128 0.0793  908  THR A CB    
6080 O  OG1   . THR A 805 ? 1.1044 1.2014 1.0504 0.1314  -0.0035 0.0867  908  THR A OG1   
6081 C  CG2   . THR A 805 ? 1.0620 1.1892 1.0364 0.1102  -0.0136 0.0716  908  THR A CG2   
6082 N  N     . PHE A 806 ? 1.1303 1.1935 1.0324 0.1228  -0.0039 0.0888  909  PHE A N     
6083 C  CA    . PHE A 806 ? 1.1104 1.1637 0.9953 0.1312  -0.0030 0.0976  909  PHE A CA    
6084 C  C     . PHE A 806 ? 1.1831 1.2313 1.0557 0.1188  -0.0054 0.0938  909  PHE A C     
6085 O  O     . PHE A 806 ? 1.2573 1.3171 1.1267 0.1223  -0.0107 0.0980  909  PHE A O     
6086 C  CB    . PHE A 806 ? 1.1551 1.1738 1.0188 0.1414  0.0081  0.1047  909  PHE A CB    
6087 C  CG    . PHE A 806 ? 1.2151 1.2158 1.0563 0.1483  0.0108  0.1136  909  PHE A CG    
6088 C  CD1   . PHE A 806 ? 1.2718 1.2878 1.1157 0.1642  0.0069  0.1238  909  PHE A CD1   
6089 C  CD2   . PHE A 806 ? 1.1850 1.1542 1.0024 0.1387  0.0171  0.1122  909  PHE A CD2   
6090 C  CE1   . PHE A 806 ? 1.3359 1.3345 1.1576 0.1715  0.0094  0.1328  909  PHE A CE1   
6091 C  CE2   . PHE A 806 ? 1.2652 1.2160 1.0608 0.1447  0.0204  0.1211  909  PHE A CE2   
6092 C  CZ    . PHE A 806 ? 1.3447 1.3094 1.1416 0.1618  0.0166  0.1316  909  PHE A CZ    
6093 N  N     . ILE A 807 ? 1.1466 1.1790 1.0123 0.1046  -0.0014 0.0859  910  ILE A N     
6094 C  CA    . ILE A 807 ? 1.0910 1.1192 0.9457 0.0926  -0.0022 0.0824  910  ILE A CA    
6095 C  C     . ILE A 807 ? 1.0954 1.1561 0.9665 0.0876  -0.0125 0.0771  910  ILE A C     
6096 O  O     . ILE A 807 ? 1.2301 1.2963 1.0932 0.0866  -0.0156 0.0791  910  ILE A O     
6097 C  CB    . ILE A 807 ? 1.0921 1.1001 0.9390 0.0783  0.0038  0.0749  910  ILE A CB    
6098 C  CG1   . ILE A 807 ? 1.1210 1.0931 0.9479 0.0826  0.0139  0.0797  910  ILE A CG1   
6099 C  CG2   . ILE A 807 ? 1.0976 1.1061 0.9366 0.0654  0.0031  0.0712  910  ILE A CG2   
6100 C  CD1   . ILE A 807 ? 1.0951 1.0475 0.9141 0.0681  0.0191  0.0719  910  ILE A CD1   
6101 N  N     . LEU A 808 ? 1.0262 1.1071 0.9188 0.0844  -0.0176 0.0702  911  LEU A N     
6102 C  CA    . LEU A 808 ? 1.0871 1.1956 0.9944 0.0787  -0.0270 0.0639  911  LEU A CA    
6103 C  C     . LEU A 808 ? 1.1431 1.2749 1.0607 0.0889  -0.0352 0.0689  911  LEU A C     
6104 O  O     . LEU A 808 ? 1.2136 1.3660 1.1392 0.0846  -0.0435 0.0641  911  LEU A O     
6105 C  CB    . LEU A 808 ? 1.0649 1.1833 0.9900 0.0706  -0.0289 0.0546  911  LEU A CB    
6106 C  CG    . LEU A 808 ? 1.0570 1.1587 0.9752 0.0594  -0.0231 0.0482  911  LEU A CG    
6107 C  CD1   . LEU A 808 ? 1.1524 1.2654 1.0882 0.0541  -0.0256 0.0404  911  LEU A CD1   
6108 C  CD2   . LEU A 808 ? 0.9111 1.0112 0.8184 0.0502  -0.0232 0.0449  911  LEU A CD2   
6109 N  N     . GLY A 809 ? 1.1273 1.2566 1.0445 0.1023  -0.0332 0.0781  912  GLY A N     
6110 C  CA    . GLY A 809 ? 1.1827 1.3371 1.1114 0.1123  -0.0414 0.0834  912  GLY A CA    
6111 C  C     . GLY A 809 ? 1.2247 1.4079 1.1789 0.1069  -0.0500 0.0762  912  GLY A C     
6112 O  O     . GLY A 809 ? 1.2946 1.4989 1.2548 0.1046  -0.0596 0.0736  912  GLY A O     
6113 N  N     . ILE A 810 ? 1.2527 1.4357 1.2208 0.1045  -0.0466 0.0729  913  ILE A N     
6114 C  CA    . ILE A 810 ? 1.2503 1.4569 1.2421 0.0982  -0.0533 0.0663  913  ILE A CA    
6115 C  C     . ILE A 810 ? 1.2344 1.4667 1.2431 0.1078  -0.0595 0.0727  913  ILE A C     
6116 O  O     . ILE A 810 ? 1.2723 1.5042 1.2741 0.1204  -0.0584 0.0824  913  ILE A O     
6117 C  CB    . ILE A 810 ? 1.1996 1.3963 1.1989 0.0929  -0.0469 0.0616  913  ILE A CB    
6118 C  CG1   . ILE A 810 ? 1.1217 1.2882 1.1003 0.0892  -0.0380 0.0601  913  ILE A CG1   
6119 C  CG2   . ILE A 810 ? 1.2789 1.4901 1.2935 0.0813  -0.0529 0.0517  913  ILE A CG2   
6120 N  N     . GLY A 811 ? 1.2323 1.4874 1.2635 0.1020  -0.0659 0.0677  914  GLY A N     
6121 C  CA    . GLY A 811 ? 1.2475 1.5303 1.2983 0.1092  -0.0720 0.0734  914  GLY A CA    
6122 C  C     . GLY A 811 ? 1.2439 1.5233 1.2994 0.1220  -0.0634 0.0829  914  GLY A C     
6123 O  O     . GLY A 811 ? 1.2640 1.5206 1.3116 0.1230  -0.0531 0.0830  914  GLY A O     
6124 N  N     . ASP A 812 ? 1.2448 1.5482 1.3132 0.1325  -0.0680 0.0910  915  ASP A N     
6125 C  CA    . ASP A 812 ? 1.2426 1.5452 1.3151 0.1475  -0.0598 0.1012  915  ASP A CA    
6126 C  C     . ASP A 812 ? 1.2336 1.5390 1.3238 0.1439  -0.0534 0.0989  915  ASP A C     
6127 O  O     . ASP A 812 ? 1.3134 1.6388 1.4240 0.1333  -0.0592 0.0932  915  ASP A O     
6128 C  CB    . ASP A 812 ? 1.3036 1.6370 1.3893 0.1595  -0.0672 0.1103  915  ASP A CB    
6129 C  CG    . ASP A 812 ? 1.4109 1.7406 1.4769 0.1653  -0.0729 0.1142  915  ASP A CG    
6130 O  OD1   . ASP A 812 ? 1.4071 1.7113 1.4504 0.1588  -0.0709 0.1094  915  ASP A OD1   
6131 O  OD2   . ASP A 812 ? 1.5270 1.8802 1.6001 0.1768  -0.0792 0.1225  915  ASP A OD2   
6132 N  N     . ARG A 813 ? 1.2321 1.5153 1.3125 0.1528  -0.0412 0.1035  916  ARG A N     
6133 C  CA    . ARG A 813 ? 1.1769 1.4585 1.2693 0.1511  -0.0334 0.1021  916  ARG A CA    
6134 C  C     . ARG A 813 ? 1.1400 1.4496 1.2556 0.1628  -0.0320 0.1111  916  ARG A C     
6135 O  O     . ARG A 813 ? 1.1726 1.4892 1.2862 0.1780  -0.0313 0.1206  916  ARG A O     
6136 C  CB    . ARG A 813 ? 1.1800 1.4237 1.2490 0.1549  -0.0209 0.1019  916  ARG A CB    
6137 C  CG    . ARG A 813 ? 1.1504 1.3736 1.2093 0.1396  -0.0196 0.0910  916  ARG A CG    
6138 C  CD    . ARG A 813 ? 1.1325 1.3559 1.1841 0.1281  -0.0287 0.0842  916  ARG A CD    
6139 N  NE    . ARG A 813 ? 1.1298 1.3767 1.2015 0.1162  -0.0375 0.0774  916  ARG A NE    
6140 C  CZ    . ARG A 813 ? 1.1792 1.4272 1.2471 0.1048  -0.0449 0.0695  916  ARG A CZ    
6141 N  NH1   . ARG A 813 ? 1.2949 1.5246 1.3412 0.1029  -0.0447 0.0676  916  ARG A NH1   
6142 N  NH2   . ARG A 813 ? 1.1850 1.4521 1.2706 0.0949  -0.0522 0.0634  916  ARG A NH2   
6143 N  N     . HIS A 814 ? 1.1349 1.4610 1.2726 0.1559  -0.0311 0.1086  917  HIS A N     
6144 C  CA    . HIS A 814 ? 1.1412 1.4957 1.3036 0.1654  -0.0284 0.1170  917  HIS A CA    
6145 C  C     . HIS A 814 ? 1.1588 1.5079 1.3301 0.1606  -0.0191 0.1146  917  HIS A C     
6146 O  O     . HIS A 814 ? 1.1586 1.4805 1.3147 0.1521  -0.0150 0.1072  917  HIS A O     
6147 C  CB    . HIS A 814 ? 1.1132 1.5085 1.3012 0.1601  -0.0419 0.1176  917  HIS A CB    
6148 C  CG    . HIS A 814 ? 1.1246 1.5255 1.3201 0.1399  -0.0512 0.1064  917  HIS A CG    
6149 N  ND1   . HIS A 814 ? 1.1222 1.5268 1.3331 0.1285  -0.0484 0.1016  917  HIS A ND1   
6150 C  CD2   . HIS A 814 ? 1.1303 1.5322 1.3188 0.1297  -0.0626 0.0991  917  HIS A CD2   
6151 C  CE1   . HIS A 814 ? 1.1322 1.5389 1.3451 0.1124  -0.0578 0.0919  917  HIS A CE1   
6152 N  NE2   . HIS A 814 ? 1.1367 1.5421 1.3362 0.1129  -0.0664 0.0899  917  HIS A NE2   
6153 N  N     . ASN A 815 ? 1.1159 1.4923 1.3123 0.1663  -0.0158 0.1214  918  ASN A N     
6154 C  CA    . ASN A 815 ? 1.1842 1.5560 1.3881 0.1646  -0.0052 0.1213  918  ASN A CA    
6155 C  C     . ASN A 815 ? 1.1856 1.5571 1.3975 0.1449  -0.0094 0.1117  918  ASN A C     
6156 O  O     . ASN A 815 ? 1.2092 1.5690 1.4206 0.1423  -0.0005 0.1103  918  ASN A O     
6157 C  CB    . ASN A 815 ? 1.2238 1.6288 1.4548 0.1753  -0.0005 0.1317  918  ASN A CB    
6158 C  CG    . ASN A 815 ? 1.3066 1.7544 1.5686 0.1664  -0.0130 0.1323  918  ASN A CG    
6159 O  OD1   . ASN A 815 ? 1.2988 1.7523 1.5586 0.1583  -0.0259 0.1273  918  ASN A OD1   
6160 N  ND2   . ASN A 815 ? 1.1849 1.6630 1.4756 0.1676  -0.0092 0.1384  918  ASN A ND2   
6161 N  N     . SER A 816 ? 1.1491 1.5320 1.3670 0.1319  -0.0224 0.1051  919  SER A N     
6162 C  CA    . SER A 816 ? 1.1472 1.5258 1.3694 0.1140  -0.0265 0.0955  919  SER A CA    
6163 C  C     . SER A 816 ? 1.1637 1.5126 1.3601 0.1068  -0.0296 0.0862  919  SER A C     
6164 O  O     . SER A 816 ? 1.1684 1.5088 1.3645 0.0939  -0.0314 0.0782  919  SER A O     
6165 C  CB    . SER A 816 ? 1.1507 1.5626 1.3987 0.1028  -0.0385 0.0935  919  SER A CB    
6166 O  OG    . SER A 816 ? 1.2053 1.6475 1.4805 0.1070  -0.0355 0.1018  919  SER A OG    
6167 N  N     . ASN A 817 ? 1.2054 1.5385 1.3804 0.1148  -0.0298 0.0874  920  ASN A N     
6168 C  CA    . ASN A 817 ? 1.1364 1.4422 1.2872 0.1084  -0.0315 0.0795  920  ASN A CA    
6169 C  C     . ASN A 817 ? 1.1724 1.4463 1.3028 0.1116  -0.0203 0.0785  920  ASN A C     
6170 O  O     . ASN A 817 ? 1.2505 1.5036 1.3641 0.1040  -0.0210 0.0711  920  ASN A O     
6171 C  CB    . ASN A 817 ? 1.1076 1.4118 1.2446 0.1138  -0.0373 0.0814  920  ASN A CB    
6172 C  CG    . ASN A 817 ? 1.2671 1.5941 1.4150 0.1053  -0.0508 0.0773  920  ASN A CG    
6173 O  OD1   . ASN A 817 ? 1.4957 1.8406 1.6629 0.0953  -0.0561 0.0732  920  ASN A OD1   
6174 N  ND2   . ASN A 817 ? 1.3185 1.6435 1.4525 0.1091  -0.0563 0.0783  920  ASN A ND2   
6175 N  N     . ILE A 818 ? 1.1444 1.4148 1.2758 0.1228  -0.0100 0.0854  921  ILE A N     
6176 C  CA    . ILE A 818 ? 1.1518 1.3907 1.2612 0.1275  0.0007  0.0848  921  ILE A CA    
6177 C  C     . ILE A 818 ? 1.1644 1.4039 1.2831 0.1248  0.0076  0.0841  921  ILE A C     
6178 O  O     . ILE A 818 ? 1.1651 1.4271 1.3051 0.1289  0.0102  0.0901  921  ILE A O     
6179 C  CB    . ILE A 818 ? 1.1516 1.3801 1.2487 0.1446  0.0083  0.0934  921  ILE A CB    
6180 C  CG1   . ILE A 818 ? 1.1142 1.3450 1.2037 0.1482  0.0012  0.0956  921  ILE A CG1   
6181 C  CG2   . ILE A 818 ? 1.1526 1.3448 1.2234 0.1479  0.0186  0.0912  921  ILE A CG2   
6182 C  CD1   . ILE A 818 ? 1.0970 1.3199 1.1760 0.1665  0.0079  0.1053  921  ILE A CD1   
6183 N  N     . MET A 819 ? 1.1056 1.3214 1.2086 0.1179  0.0107  0.0773  922  MET A N     
6184 C  CA    . MET A 819 ? 1.1156 1.3282 1.2229 0.1152  0.0172  0.0764  922  MET A CA    
6185 C  C     . MET A 819 ? 1.1901 1.3720 1.2722 0.1214  0.0271  0.0756  922  MET A C     
6186 O  O     . MET A 819 ? 1.2157 1.3754 1.2759 0.1210  0.0265  0.0719  922  MET A O     
6187 C  CB    . MET A 819 ? 1.0736 1.2886 1.1868 0.1002  0.0104  0.0683  922  MET A CB    
6188 C  CG    . MET A 819 ? 1.1214 1.3631 1.2569 0.0923  0.0003  0.0673  922  MET A CG    
6189 S  SD    . MET A 819 ? 1.1754 1.4180 1.3193 0.0771  -0.0042 0.0595  922  MET A SD    
6190 C  CE    . MET A 819 ? 1.1189 1.3591 1.2687 0.0813  0.0078  0.0650  922  MET A CE    
6191 N  N     . VAL A 820 ? 1.1881 1.3685 1.2729 0.1265  0.0363  0.0789  923  VAL A N     
6192 C  CA    . VAL A 820 ? 1.2008 1.3527 1.2614 0.1329  0.0462  0.0781  923  VAL A CA    
6193 C  C     . VAL A 820 ? 1.2043 1.3529 1.2659 0.1269  0.0497  0.0752  923  VAL A C     
6194 O  O     . VAL A 820 ? 1.1796 1.3495 1.2630 0.1246  0.0503  0.0786  923  VAL A O     
6195 C  CB    . VAL A 820 ? 1.1894 1.3397 1.2473 0.1501  0.0567  0.0869  923  VAL A CB    
6196 C  CG1   . VAL A 820 ? 1.2147 1.3316 1.2438 0.1564  0.0667  0.0847  923  VAL A CG1   
6197 C  CG2   . VAL A 820 ? 1.1866 1.3424 1.2451 0.1573  0.0529  0.0911  923  VAL A CG2   
6198 N  N     . LYS A 821 ? 1.2353 1.3572 1.2728 0.1239  0.0518  0.0690  924  LYS A N     
6199 C  CA    . LYS A 821 ? 1.2567 1.3725 1.2905 0.1198  0.0554  0.0664  924  LYS A CA    
6200 C  C     . LYS A 821 ? 1.3240 1.4299 1.3485 0.1321  0.0684  0.0718  924  LYS A C     
6201 O  O     . LYS A 821 ? 1.3212 1.4237 1.3413 0.1441  0.0748  0.0770  924  LYS A O     
6202 C  CB    . LYS A 821 ? 1.2368 1.3318 1.2499 0.1106  0.0504  0.0571  924  LYS A CB    
6203 C  CG    . LYS A 821 ? 1.1873 1.2922 1.2092 0.0987  0.0386  0.0515  924  LYS A CG    
6204 C  CD    . LYS A 821 ? 1.1257 1.2128 1.1286 0.0905  0.0347  0.0429  924  LYS A CD    
6205 C  CE    . LYS A 821 ? 1.0722 1.1545 1.0711 0.0891  0.0379  0.0417  924  LYS A CE    
6206 N  N     . ASP A 822 ? 1.3434 1.4440 1.3635 0.1300  0.0728  0.0707  925  ASP A N     
6207 C  CA    . ASP A 822 ? 1.3894 1.4793 1.3980 0.1415  0.0857  0.0753  925  ASP A CA    
6208 C  C     . ASP A 822 ? 1.4519 1.5096 1.4278 0.1475  0.0899  0.0709  925  ASP A C     
6209 O  O     . ASP A 822 ? 1.3370 1.3851 1.3029 0.1608  0.1003  0.0754  925  ASP A O     
6210 C  CB    . ASP A 822 ? 1.4852 1.5757 1.4945 0.1373  0.0889  0.0751  925  ASP A CB    
6211 C  CG    . ASP A 822 ? 1.4904 1.6101 1.5313 0.1326  0.0878  0.0809  925  ASP A CG    
6212 O  OD1   . ASP A 822 ? 1.4672 1.6083 1.5300 0.1318  0.0834  0.0842  925  ASP A OD1   
6213 O  OD2   . ASP A 822 ? 1.3465 1.4673 1.3897 0.1293  0.0911  0.0821  925  ASP A OD2   
6214 N  N     . ASP A 823 ? 1.2949 1.3355 1.2536 0.1377  0.0821  0.0619  926  ASP A N     
6215 C  CA    . ASP A 823 ? 1.2678 1.2766 1.1949 0.1405  0.0851  0.0567  926  ASP A CA    
6216 C  C     . ASP A 823 ? 1.2877 1.2887 1.2097 0.1473  0.0863  0.0590  926  ASP A C     
6217 O  O     . ASP A 823 ? 1.2906 1.2629 1.1859 0.1521  0.0914  0.0562  926  ASP A O     
6218 C  CB    . ASP A 823 ? 1.2709 1.2678 1.1844 0.1267  0.0757  0.0468  926  ASP A CB    
6219 C  CG    . ASP A 823 ? 1.3666 1.3806 1.2974 0.1158  0.0641  0.0444  926  ASP A CG    
6220 O  OD1   . ASP A 823 ? 1.3880 1.4199 1.3382 0.1188  0.0627  0.0497  926  ASP A OD1   
6221 O  OD2   . ASP A 823 ? 1.2693 1.2798 1.1943 0.1047  0.0563  0.0371  926  ASP A OD2   
6222 N  N     . GLY A 824 ? 1.3396 1.3639 1.2850 0.1479  0.0818  0.0641  927  GLY A N     
6223 C  CA    . GLY A 824 ? 1.3162 1.3350 1.2575 0.1551  0.0823  0.0673  927  GLY A CA    
6224 C  C     . GLY A 824 ? 1.2933 1.3120 1.2344 0.1442  0.0714  0.0627  927  GLY A C     
6225 O  O     . GLY A 824 ? 1.2797 1.2866 1.2106 0.1493  0.0721  0.0646  927  GLY A O     
6226 N  N     . GLN A 825 ? 1.3852 1.4159 1.3363 0.1303  0.0620  0.0571  928  GLN A N     
6227 C  CA    . GLN A 825 ? 1.4161 1.4486 1.3675 0.1201  0.0522  0.0527  928  GLN A CA    
6228 C  C     . GLN A 825 ? 1.2261 1.2869 1.2026 0.1215  0.0466  0.0581  928  GLN A C     
6229 O  O     . GLN A 825 ? 1.2130 1.2983 1.2125 0.1204  0.0447  0.0607  928  GLN A O     
6230 C  CB    . GLN A 825 ? 1.3126 1.3460 1.2632 0.1059  0.0450  0.0444  928  GLN A CB    
6231 C  CG    . GLN A 825 ? 1.1953 1.2307 1.1455 0.0952  0.0358  0.0394  928  GLN A CG    
6232 C  CD    . GLN A 825 ? 1.3797 1.4167 1.3288 0.0828  0.0295  0.0315  928  GLN A CD    
6233 O  OE1   . GLN A 825 ? 1.3593 1.3935 1.3058 0.0823  0.0317  0.0296  928  GLN A OE1   
6234 N  NE2   . GLN A 825 ? 1.2230 1.2650 1.1739 0.0736  0.0219  0.0272  928  GLN A NE2   
6235 N  N     . LEU A 826 ? 1.2571 1.3141 1.2284 0.1235  0.0439  0.0598  929  LEU A N     
6236 C  CA    . LEU A 826 ? 1.2000 1.2824 1.1915 0.1258  0.0381  0.0650  929  LEU A CA    
6237 C  C     . LEU A 826 ? 1.0862 1.1747 1.0798 0.1132  0.0276  0.0592  929  LEU A C     
6238 O  O     . LEU A 826 ? 1.0491 1.1181 1.0245 0.1057  0.0263  0.0532  929  LEU A O     
6239 C  CB    . LEU A 826 ? 1.1531 1.2283 1.1368 0.1401  0.0433  0.0727  929  LEU A CB    
6240 C  CG    . LEU A 826 ? 1.1311 1.2343 1.1354 0.1462  0.0382  0.0799  929  LEU A CG    
6241 C  CD1   . LEU A 826 ? 1.2120 1.3156 1.2165 0.1645  0.0470  0.0897  929  LEU A CD1   
6242 C  CD2   . LEU A 826 ? 1.1433 1.2431 1.1397 0.1411  0.0305  0.0783  929  LEU A CD2   
6243 N  N     . PHE A 827 ? 1.0689 1.1850 1.0847 0.1105  0.0201  0.0607  930  PHE A N     
6244 C  CA    . PHE A 827 ? 1.1012 1.2251 1.1197 0.0997  0.0103  0.0554  930  PHE A CA    
6245 C  C     . PHE A 827 ? 1.0666 1.2197 1.1072 0.1011  0.0033  0.0593  930  PHE A C     
6246 O  O     . PHE A 827 ? 1.0806 1.2498 1.1365 0.1091  0.0057  0.0659  930  PHE A O     
6247 C  CB    . PHE A 827 ? 1.0260 1.1489 1.0457 0.0874  0.0068  0.0470  930  PHE A CB    
6248 C  CG    . PHE A 827 ? 1.0176 1.1571 1.0566 0.0858  0.0067  0.0474  930  PHE A CG    
6249 C  CD1   . PHE A 827 ? 1.1049 1.2377 1.1425 0.0914  0.0150  0.0502  930  PHE A CD1   
6250 C  CD2   . PHE A 827 ? 0.9065 1.0668 0.9639 0.0785  -0.0013 0.0449  930  PHE A CD2   
6251 C  CE1   . PHE A 827 ? 1.0748 1.2221 1.1297 0.0896  0.0158  0.0514  930  PHE A CE1   
6252 C  CE2   . PHE A 827 ? 0.9938 1.1670 1.0682 0.0761  -0.0009 0.0455  930  PHE A CE2   
6253 C  CZ    . PHE A 827 ? 1.0465 1.2136 1.1201 0.0815  0.0079  0.0492  930  PHE A CZ    
6254 N  N     . HIS A 828 ? 1.0558 1.2163 1.0976 0.0931  -0.0054 0.0550  931  HIS A N     
6255 C  CA    . HIS A 828 ? 1.0821 1.2690 1.1419 0.0923  -0.0138 0.0568  931  HIS A CA    
6256 C  C     . HIS A 828 ? 1.0690 1.2671 1.1401 0.0797  -0.0211 0.0489  931  HIS A C     
6257 O  O     . HIS A 828 ? 1.0463 1.2313 1.1087 0.0722  -0.0204 0.0423  931  HIS A O     
6258 C  CB    . HIS A 828 ? 1.0523 1.2373 1.1011 0.0955  -0.0178 0.0591  931  HIS A CB    
6259 C  CG    . HIS A 828 ? 1.0393 1.2099 1.0745 0.1086  -0.0104 0.0671  931  HIS A CG    
6260 N  ND1   . HIS A 828 ? 1.1538 1.3246 1.1941 0.1195  -0.0027 0.0736  931  HIS A ND1   
6261 C  CD2   . HIS A 828 ? 1.0426 1.1965 1.0583 0.1131  -0.0089 0.0700  931  HIS A CD2   
6262 C  CE1   . HIS A 828 ? 1.1401 1.2943 1.1642 0.1308  0.0031  0.0797  931  HIS A CE1   
6263 N  NE2   . HIS A 828 ? 1.0920 1.2348 1.1006 0.1269  -0.0005 0.0779  931  HIS A NE2   
6264 N  N     . ILE A 829 ? 1.1282 1.3508 1.2185 0.0774  -0.0283 0.0495  932  ILE A N     
6265 C  CA    . ILE A 829 ? 1.1815 1.4135 1.2830 0.0660  -0.0346 0.0423  932  ILE A CA    
6266 C  C     . ILE A 829 ? 1.1453 1.3935 1.2525 0.0614  -0.0452 0.0393  932  ILE A C     
6267 O  O     . ILE A 829 ? 1.2603 1.5070 1.3654 0.0525  -0.0504 0.0314  932  ILE A O     
6268 C  CB    . ILE A 829 ? 1.0757 1.3196 1.1969 0.0648  -0.0320 0.0445  932  ILE A CB    
6269 C  CG1   . ILE A 829 ? 1.1927 1.4589 1.3312 0.0720  -0.0324 0.0528  932  ILE A CG1   
6270 C  CG2   . ILE A 829 ? 1.1236 1.3493 1.2362 0.0675  -0.0221 0.0454  932  ILE A CG2   
6271 C  CD1   . ILE A 829 ? 1.1210 1.4027 1.2817 0.0690  -0.0302 0.0552  932  ILE A CD1   
6272 N  N     . ASP A 830 ? 1.1634 1.4273 1.2771 0.0681  -0.0485 0.0455  933  ASP A N     
6273 C  CA    . ASP A 830 ? 1.2830 1.5661 1.4045 0.0636  -0.0595 0.0429  933  ASP A CA    
6274 C  C     . ASP A 830 ? 1.2136 1.4856 1.3164 0.0595  -0.0637 0.0368  933  ASP A C     
6275 O  O     . ASP A 830 ? 1.4314 1.7039 1.5349 0.0500  -0.0687 0.0284  933  ASP A O     
6276 C  CB    . ASP A 830 ? 1.4211 1.7240 1.5517 0.0732  -0.0623 0.0516  933  ASP A CB    
6277 C  CG    . ASP A 830 ? 1.3422 1.6681 1.4827 0.0681  -0.0747 0.0488  933  ASP A CG    
6278 O  OD1   . ASP A 830 ? 1.2809 1.6193 1.4374 0.0582  -0.0798 0.0436  933  ASP A OD1   
6279 O  OD2   . ASP A 830 ? 1.5417 1.8720 1.6727 0.0737  -0.0794 0.0517  933  ASP A OD2   
6280 N  N     . PHE A 831 ? 1.2515 1.5130 1.3373 0.0669  -0.0611 0.0413  934  PHE A N     
6281 C  CA    . PHE A 831 ? 1.2972 1.5481 1.3643 0.0636  -0.0636 0.0370  934  PHE A CA    
6282 C  C     . PHE A 831 ? 1.3727 1.6413 1.4447 0.0583  -0.0747 0.0322  934  PHE A C     
6283 O  O     . PHE A 831 ? 1.3377 1.6044 1.4076 0.0495  -0.0781 0.0234  934  PHE A O     
6284 C  CB    . PHE A 831 ? 1.2250 1.4567 1.2819 0.0563  -0.0587 0.0300  934  PHE A CB    
6285 C  CG    . PHE A 831 ? 1.2099 1.4225 1.2588 0.0603  -0.0487 0.0336  934  PHE A CG    
6286 C  CD1   . PHE A 831 ? 1.2061 1.4112 1.2473 0.0706  -0.0435 0.0421  934  PHE A CD1   
6287 C  CD2   . PHE A 831 ? 1.1424 1.3439 1.1902 0.0545  -0.0447 0.0282  934  PHE A CD2   
6288 C  CE1   . PHE A 831 ? 1.1342 1.3194 1.1659 0.0741  -0.0342 0.0444  934  PHE A CE1   
6289 C  CE2   . PHE A 831 ? 1.0457 1.2294 1.0844 0.0577  -0.0362 0.0307  934  PHE A CE2   
6290 C  CZ    . PHE A 831 ? 1.0346 1.2094 1.0648 0.0672  -0.0309 0.0384  934  PHE A CZ    
6291 N  N     . GLY A 832 ? 1.3703 1.6564 1.4484 0.0646  -0.0802 0.0381  935  GLY A N     
6292 C  CA    . GLY A 832 ? 1.4711 1.7753 1.5529 0.0603  -0.0916 0.0339  935  GLY A CA    
6293 C  C     . GLY A 832 ? 1.4955 1.7897 1.5555 0.0589  -0.0938 0.0303  935  GLY A C     
6294 O  O     . GLY A 832 ? 1.4633 1.7555 1.5197 0.0501  -0.0974 0.0210  935  GLY A O     
6295 N  N     . HIS A 833 ? 1.5475 1.8345 1.5922 0.0680  -0.0909 0.0381  936  HIS A N     
6296 C  CA    . HIS A 833 ? 1.5141 1.7913 1.5370 0.0674  -0.0916 0.0365  936  HIS A CA    
6297 C  C     . HIS A 833 ? 1.5201 1.7750 1.5253 0.0744  -0.0815 0.0441  936  HIS A C     
6298 O  O     . HIS A 833 ? 1.6652 1.9186 1.6719 0.0844  -0.0778 0.0532  936  HIS A O     
6299 C  CB    . HIS A 833 ? 1.6623 1.9582 1.6826 0.0711  -0.1022 0.0384  936  HIS A CB    
6300 C  CG    . HIS A 833 ? 1.6606 1.9747 1.6929 0.0622  -0.1128 0.0291  936  HIS A CG    
6301 N  ND1   . HIS A 833 ? 1.6531 1.9612 1.6893 0.0514  -0.1123 0.0185  936  HIS A ND1   
6302 C  CD2   . HIS A 833 ? 1.5955 1.9328 1.6361 0.0623  -0.1244 0.0285  936  HIS A CD2   
6303 C  CE1   . HIS A 833 ? 1.6097 1.9339 1.6550 0.0452  -0.1225 0.0116  936  HIS A CE1   
6304 N  NE2   . HIS A 833 ? 1.5828 1.9256 1.6313 0.0508  -0.1304 0.0171  936  HIS A NE2   
6305 N  N     . PHE A 834 ? 1.4233 1.6609 1.4119 0.0689  -0.0768 0.0401  937  PHE A N     
6306 C  CA    . PHE A 834 ? 1.3992 1.6135 1.3693 0.0726  -0.0672 0.0460  937  PHE A CA    
6307 C  C     . PHE A 834 ? 1.4164 1.6279 1.3670 0.0764  -0.0689 0.0506  937  PHE A C     
6308 O  O     . PHE A 834 ? 1.4417 1.6697 1.3926 0.0761  -0.0776 0.0483  937  PHE A O     
6309 C  CB    . PHE A 834 ? 1.3749 1.5728 1.3406 0.0631  -0.0603 0.0393  937  PHE A CB    
6310 C  CG    . PHE A 834 ? 1.3408 1.5461 1.3073 0.0534  -0.0646 0.0293  937  PHE A CG    
6311 C  CD1   . PHE A 834 ? 1.3559 1.5556 1.3054 0.0504  -0.0634 0.0281  937  PHE A CD1   
6312 C  CD2   . PHE A 834 ? 1.2776 1.4945 1.2609 0.0479  -0.0691 0.0215  937  PHE A CD2   
6313 C  CE1   . PHE A 834 ? 1.3330 1.5397 1.2828 0.0429  -0.0665 0.0190  937  PHE A CE1   
6314 C  CE2   . PHE A 834 ? 1.2816 1.5033 1.2643 0.0404  -0.0724 0.0123  937  PHE A CE2   
6315 C  CZ    . PHE A 834 ? 1.3309 1.5481 1.2969 0.0384  -0.0711 0.0110  937  PHE A CZ    
6316 N  N     . LEU A 835 ? 1.4196 1.6088 1.3519 0.0798  -0.0602 0.0570  938  LEU A N     
6317 C  CA    . LEU A 835 ? 1.3861 1.5682 1.2973 0.0844  -0.0595 0.0634  938  LEU A CA    
6318 C  C     . LEU A 835 ? 1.4827 1.6815 1.3973 0.0968  -0.0670 0.0714  938  LEU A C     
6319 O  O     . LEU A 835 ? 1.5502 1.7565 1.4789 0.1042  -0.0677 0.0756  938  LEU A O     
6320 C  CB    . LEU A 835 ? 1.4233 1.6085 1.3259 0.0750  -0.0617 0.0560  938  LEU A CB    
6321 C  CG    . LEU A 835 ? 1.3934 1.5650 1.2937 0.0635  -0.0543 0.0489  938  LEU A CG    
6322 C  CD1   . LEU A 835 ? 1.3870 1.5675 1.2832 0.0555  -0.0573 0.0408  938  LEU A CD1   
6323 C  CD2   . LEU A 835 ? 1.4078 1.5529 1.2903 0.0637  -0.0435 0.0557  938  LEU A CD2   
6324 N  N     . ASP A 836 ? 1.5114 1.7177 1.4134 0.0997  -0.0725 0.0737  939  ASP A N     
6325 C  CA    . ASP A 836 ? 1.7042 1.9289 1.6091 0.1115  -0.0809 0.0812  939  ASP A CA    
6326 C  C     . ASP A 836 ? 1.7943 2.0489 1.7240 0.1080  -0.0923 0.0741  939  ASP A C     
6327 O  O     . ASP A 836 ? 1.7118 1.9713 1.6517 0.0963  -0.0945 0.0630  939  ASP A O     
6328 C  CB    . ASP A 836 ? 1.7736 1.9977 1.6560 0.1152  -0.0841 0.0854  939  ASP A CB    
6329 C  CG    . ASP A 836 ? 1.7990 2.0378 1.6797 0.1301  -0.0911 0.0960  939  ASP A CG    
6330 O  OD1   . ASP A 836 ? 1.8079 2.0352 1.6849 0.1417  -0.0851 0.1067  939  ASP A OD1   
6331 O  OD2   . ASP A 836 ? 1.8494 2.1112 1.7319 0.1306  -0.1029 0.0934  939  ASP A OD2   
6332 N  N     . HIS A 837 ? 1.8219 2.0965 1.7613 0.1183  -0.0995 0.0810  940  HIS A N     
6333 C  CA    . HIS A 837 ? 1.7994 2.1042 1.7630 0.1147  -0.1109 0.0754  940  HIS A CA    
6334 C  C     . HIS A 837 ? 1.8287 2.1457 1.7879 0.1053  -0.1210 0.0654  940  HIS A C     
6335 O  O     . HIS A 837 ? 1.8244 2.1339 1.7613 0.1067  -0.1217 0.0664  940  HIS A O     
6336 C  CB    . HIS A 837 ? 1.7903 2.1167 1.7642 0.1284  -0.1170 0.0859  940  HIS A CB    
6337 C  CG    . HIS A 837 ? 1.7945 2.1229 1.7479 0.1391  -0.1214 0.0943  940  HIS A CG    
6338 N  ND1   . HIS A 837 ? 1.8118 2.1234 1.7493 0.1534  -0.1136 0.1072  940  HIS A ND1   
6339 C  CD2   . HIS A 837 ? 1.7381 2.0820 1.6826 0.1379  -0.1327 0.0917  940  HIS A CD2   
6340 C  CE1   . HIS A 837 ? 1.7594 2.0764 1.6794 0.1610  -0.1198 0.1130  940  HIS A CE1   
6341 N  NE2   . HIS A 837 ? 1.7401 2.0774 1.6639 0.1518  -0.1316 0.1037  940  HIS A NE2   
6342 N  N     . ARG A 846 ? 1.7303 1.7733 1.4970 0.2506  -0.0151 0.1961  949  ARG A N     
6343 C  CA    . ARG A 846 ? 1.6945 1.7860 1.4934 0.2517  -0.0284 0.1918  949  ARG A CA    
6344 C  C     . ARG A 846 ? 1.6407 1.7479 1.4583 0.2291  -0.0333 0.1756  949  ARG A C     
6345 O  O     . ARG A 846 ? 1.6081 1.7504 1.4427 0.2233  -0.0458 0.1700  949  ARG A O     
6346 C  CB    . ARG A 846 ? 1.8013 1.9213 1.5987 0.2617  -0.0407 0.1990  949  ARG A CB    
6347 C  CG    . ARG A 846 ? 1.8957 2.0232 1.6914 0.2877  -0.0413 0.2145  949  ARG A CG    
6348 C  CD    . ARG A 846 ? 1.9953 2.0764 1.7567 0.3002  -0.0280 0.2266  949  ARG A CD    
6349 N  NE    . ARG A 846 ? 1.9954 2.0568 1.7292 0.2922  -0.0272 0.2278  949  ARG A NE    
6350 C  CZ    . ARG A 846 ? 2.0905 2.1626 1.8105 0.3028  -0.0343 0.2372  949  ARG A CZ    
6351 N  NH1   . ARG A 846 ? 2.0927 2.1964 1.8240 0.3220  -0.0437 0.2463  949  ARG A NH1   
6352 N  NH2   . ARG A 846 ? 2.1686 2.2207 1.8629 0.2940  -0.0318 0.2378  949  ARG A NH2   
6353 N  N     . GLU A 847 ? 1.5815 1.6618 1.3949 0.2166  -0.0236 0.1681  950  GLU A N     
6354 C  CA    . GLU A 847 ? 1.5528 1.6466 1.3846 0.1973  -0.0272 0.1535  950  GLU A CA    
6355 C  C     . GLU A 847 ? 1.5251 1.6409 1.3854 0.2002  -0.0294 0.1501  950  GLU A C     
6356 O  O     . GLU A 847 ? 1.5075 1.6154 1.3691 0.2142  -0.0231 0.1573  950  GLU A O     
6357 C  CB    . GLU A 847 ? 1.5065 1.5652 1.3225 0.1824  -0.0167 0.1469  950  GLU A CB    
6358 C  CG    . GLU A 847 ? 1.4671 1.5162 1.2648 0.1707  -0.0169 0.1445  950  GLU A CG    
6359 C  CD    . GLU A 847 ? 1.5658 1.5929 1.3354 0.1821  -0.0123 0.1575  950  GLU A CD    
6360 O  OE1   . GLU A 847 ? 1.6270 1.6401 1.3888 0.1989  -0.0073 0.1680  950  GLU A OE1   
6361 O  OE2   . GLU A 847 ? 1.4904 1.5138 1.2450 0.1749  -0.0131 0.1575  950  GLU A OE2   
6362 N  N     . ARG A 848 ? 1.5141 1.6568 1.3965 0.1871  -0.0377 0.1392  951  ARG A N     
6363 C  CA    . ARG A 848 ? 1.5361 1.7039 1.4474 0.1883  -0.0409 0.1362  951  ARG A CA    
6364 C  C     . ARG A 848 ? 1.5680 1.7125 1.4798 0.1840  -0.0299 0.1319  951  ARG A C     
6365 O  O     . ARG A 848 ? 1.5644 1.6886 1.4667 0.1699  -0.0255 0.1237  951  ARG A O     
6366 C  CB    . ARG A 848 ? 1.6746 1.8747 1.6068 0.1748  -0.0530 0.1258  951  ARG A CB    
6367 C  CG    . ARG A 848 ? 1.7000 1.9274 1.6629 0.1743  -0.0567 0.1227  951  ARG A CG    
6368 C  CD    . ARG A 848 ? 1.7146 1.9733 1.6960 0.1621  -0.0697 0.1137  951  ARG A CD    
6369 N  NE    . ARG A 848 ? 1.7990 2.0804 1.7792 0.1687  -0.0808 0.1185  951  ARG A NE    
6370 C  CZ    . ARG A 848 ? 1.9868 2.2649 1.9498 0.1639  -0.0859 0.1160  951  ARG A CZ    
6371 N  NH1   . ARG A 848 ? 1.8447 2.0992 1.7917 0.1522  -0.0809 0.1088  951  ARG A NH1   
6372 N  NH2   . ARG A 848 ? 1.9593 2.2594 1.9210 0.1712  -0.0964 0.1209  951  ARG A NH2   
6373 N  N     . VAL A 849 ? 1.4086 1.5573 1.3313 0.1966  -0.0254 0.1375  952  VAL A N     
6374 C  CA    . VAL A 849 ? 1.3213 1.4519 1.2462 0.1940  -0.0156 0.1334  952  VAL A CA    
6375 C  C     . VAL A 849 ? 1.2968 1.4604 1.2533 0.1897  -0.0211 0.1284  952  VAL A C     
6376 O  O     . VAL A 849 ? 1.2861 1.4704 1.2591 0.2027  -0.0214 0.1353  952  VAL A O     
6377 C  CB    . VAL A 849 ? 1.3032 1.4086 1.2134 0.2120  -0.0042 0.1436  952  VAL A CB    
6378 C  CG1   . VAL A 849 ? 1.3757 1.4626 1.2868 0.2091  0.0056  0.1385  952  VAL A CG1   
6379 C  CG2   . VAL A 849 ? 1.3128 1.3828 1.1905 0.2153  0.0014  0.1489  952  VAL A CG2   
6380 N  N     . PRO A 850 ? 1.2808 1.4511 1.2471 0.1721  -0.0250 0.1169  953  PRO A N     
6381 C  CA    . PRO A 850 ? 1.2741 1.4750 1.2699 0.1674  -0.0303 0.1125  953  PRO A CA    
6382 C  C     . PRO A 850 ? 1.2754 1.4699 1.2791 0.1732  -0.0208 0.1142  953  PRO A C     
6383 O  O     . PRO A 850 ? 1.2325 1.4543 1.2600 0.1783  -0.0229 0.1172  953  PRO A O     
6384 C  CB    . PRO A 850 ? 1.2292 1.4311 1.2271 0.1479  -0.0356 0.1001  953  PRO A CB    
6385 C  CG    . PRO A 850 ? 1.2083 1.3753 1.1794 0.1427  -0.0288 0.0976  953  PRO A CG    
6386 C  CD    . PRO A 850 ? 1.2374 1.3895 1.1889 0.1562  -0.0252 0.1080  953  PRO A CD    
6387 N  N     . PHE A 851 ? 1.4054 1.5651 1.3897 0.1721  -0.0103 0.1121  954  PHE A N     
6388 C  CA    . PHE A 851 ? 1.3022 1.4518 1.2893 0.1785  -0.0003 0.1135  954  PHE A CA    
6389 C  C     . PHE A 851 ? 1.4246 1.5593 1.3984 0.1985  0.0080  0.1248  954  PHE A C     
6390 O  O     . PHE A 851 ? 1.5794 1.6795 1.5260 0.2014  0.0145  0.1264  954  PHE A O     
6391 C  CB    . PHE A 851 ? 1.3114 1.4316 1.2837 0.1663  0.0059  0.1045  954  PHE A CB    
6392 C  CG    . PHE A 851 ? 1.4599 1.5755 1.4385 0.1691  0.0139  0.1033  954  PHE A CG    
6393 C  CD1   . PHE A 851 ? 1.4466 1.5855 1.4453 0.1809  0.0157  0.1099  954  PHE A CD1   
6394 C  CD2   . PHE A 851 ? 1.3825 1.4718 1.3468 0.1600  0.0197  0.0958  954  PHE A CD2   
6395 C  CE1   . PHE A 851 ? 1.3869 1.5215 1.3904 0.1838  0.0240  0.1093  954  PHE A CE1   
6396 C  CE2   . PHE A 851 ? 1.3262 1.4106 1.2941 0.1631  0.0271  0.0947  954  PHE A CE2   
6397 C  CZ    . PHE A 851 ? 1.4408 1.5471 1.4277 0.1752  0.0297  0.1016  954  PHE A CZ    
6398 N  N     . VAL A 852 ? 1.4070 1.5676 1.4002 0.2124  0.0080  0.1327  955  VAL A N     
6399 C  CA    . VAL A 852 ? 1.4429 1.5946 1.4261 0.2341  0.0150  0.1446  955  VAL A CA    
6400 C  C     . VAL A 852 ? 1.4662 1.5946 1.4409 0.2441  0.0291  0.1465  955  VAL A C     
6401 O  O     . VAL A 852 ? 1.5094 1.6193 1.4686 0.2623  0.0373  0.1553  955  VAL A O     
6402 C  CB    . VAL A 852 ? 1.3710 1.5665 1.3800 0.2456  0.0071  0.1533  955  VAL A CB    
6403 C  CG1   . VAL A 852 ? 1.4370 1.6597 1.4742 0.2488  0.0100  0.1544  955  VAL A CG1   
6404 C  CG2   . VAL A 852 ? 1.3504 1.5376 1.3449 0.2672  0.0106  0.1660  955  VAL A CG2   
6405 N  N     . LEU A 853 ? 1.4500 1.5768 1.4323 0.2337  0.0324  0.1386  956  LEU A N     
6406 C  CA    . LEU A 853 ? 1.5510 1.6563 1.5244 0.2424  0.0456  0.1394  956  LEU A CA    
6407 C  C     . LEU A 853 ? 1.5153 1.6398 1.5021 0.2646  0.0513  0.1511  956  LEU A C     
6408 O  O     . LEU A 853 ? 1.5025 1.6045 1.4704 0.2821  0.0596  0.1587  956  LEU A O     
6409 C  CB    . LEU A 853 ? 1.5267 1.5809 1.4630 0.2430  0.0544  0.1370  956  LEU A CB    
6410 C  CG    . LEU A 853 ? 1.5052 1.5344 1.4271 0.2232  0.0548  0.1246  956  LEU A CG    
6411 C  CD1   . LEU A 853 ? 1.4644 1.5011 1.3986 0.2188  0.0587  0.1193  956  LEU A CD1   
6412 C  CD2   . LEU A 853 ? 1.5140 1.5561 1.4417 0.2051  0.0428  0.1182  956  LEU A CD2   
6413 N  N     . THR A 854 ? 1.5398 1.7057 1.5594 0.2641  0.0472  0.1528  957  THR A N     
6414 C  CA    . THR A 854 ? 1.4560 1.6471 1.4931 0.2843  0.0521  0.1642  957  THR A CA    
6415 C  C     . THR A 854 ? 1.4362 1.5996 1.4578 0.2982  0.0686  0.1667  957  THR A C     
6416 O  O     . THR A 854 ? 1.4300 1.5573 1.4293 0.2904  0.0752  0.1587  957  THR A O     
6417 C  CB    . THR A 854 ? 1.4642 1.7053 1.5407 0.2774  0.0446  0.1645  957  THR A CB    
6418 O  OG1   . THR A 854 ? 1.3867 1.6232 1.4686 0.2643  0.0489  0.1564  957  THR A OG1   
6419 C  CG2   . THR A 854 ? 1.4470 1.7137 1.5367 0.2636  0.0281  0.1611  957  THR A CG2   
6420 N  N     . GLN A 855 ? 1.4485 1.6306 1.4823 0.3196  0.0751  0.1778  958  GLN A N     
6421 C  CA    . GLN A 855 ? 1.4081 1.5652 1.4268 0.3362  0.0917  0.1813  958  GLN A CA    
6422 C  C     . GLN A 855 ? 1.4272 1.5832 1.4524 0.3258  0.0979  0.1740  958  GLN A C     
6423 O  O     . GLN A 855 ? 1.4725 1.5956 1.4757 0.3337  0.1110  0.1725  958  GLN A O     
6424 C  CB    . GLN A 855 ? 1.3768 1.5617 1.4122 0.3617  0.0970  0.1953  958  GLN A CB    
6425 C  CG    . GLN A 855 ? 1.5070 1.6824 1.5274 0.3785  0.0951  0.2044  958  GLN A CG    
6426 C  CD    . GLN A 855 ? 1.3897 1.5972 1.4269 0.3690  0.0777  0.2055  958  GLN A CD    
6427 O  OE1   . GLN A 855 ? 1.3385 1.5738 1.3979 0.3490  0.0668  0.1986  958  GLN A OE1   
6428 N  NE2   . GLN A 855 ? 1.2919 1.4942 1.3168 0.3840  0.0753  0.2142  958  GLN A NE2   
6429 N  N     . ASP A 856 ? 1.4099 1.5996 1.4631 0.3085  0.0888  0.1694  959  ASP A N     
6430 C  CA    . ASP A 856 ? 1.4156 1.6025 1.4732 0.2977  0.0942  0.1626  959  ASP A CA    
6431 C  C     . ASP A 856 ? 1.4373 1.5781 1.4623 0.2846  0.0959  0.1512  959  ASP A C     
6432 O  O     . ASP A 856 ? 1.4661 1.5844 1.4770 0.2855  0.1061  0.1475  959  ASP A O     
6433 C  CB    . ASP A 856 ? 1.4526 1.6824 1.5454 0.2811  0.0835  0.1602  959  ASP A CB    
6434 C  CG    . ASP A 856 ? 1.6761 1.9542 1.8040 0.2923  0.0831  0.1710  959  ASP A CG    
6435 O  OD1   . ASP A 856 ? 1.6512 1.9452 1.7847 0.3039  0.0781  0.1786  959  ASP A OD1   
6436 O  OD2   . ASP A 856 ? 1.6522 1.9533 1.8024 0.2894  0.0876  0.1723  959  ASP A OD2   
6437 N  N     . PHE A 857 ? 1.4395 1.5669 1.4522 0.2724  0.0859  0.1456  960  PHE A N     
6438 C  CA    . PHE A 857 ? 1.4030 1.4894 1.3863 0.2592  0.0868  0.1350  960  PHE A CA    
6439 C  C     . PHE A 857 ? 1.4030 1.4443 1.3513 0.2726  0.0986  0.1365  960  PHE A C     
6440 O  O     . PHE A 857 ? 1.4784 1.4862 1.4034 0.2666  0.1046  0.1288  960  PHE A O     
6441 C  CB    . PHE A 857 ? 1.4297 1.5169 1.4110 0.2428  0.0736  0.1294  960  PHE A CB    
6442 C  CG    . PHE A 857 ? 1.4080 1.5363 1.4209 0.2297  0.0616  0.1272  960  PHE A CG    
6443 C  CD1   . PHE A 857 ? 1.4173 1.5531 1.4409 0.2151  0.0598  0.1197  960  PHE A CD1   
6444 C  CD2   . PHE A 857 ? 1.4163 1.5739 1.4463 0.2322  0.0519  0.1326  960  PHE A CD2   
6445 C  CE1   . PHE A 857 ? 1.4508 1.6207 1.5016 0.2029  0.0491  0.1174  960  PHE A CE1   
6446 C  CE2   . PHE A 857 ? 1.3931 1.5861 1.4503 0.2193  0.0406  0.1297  960  PHE A CE2   
6447 C  CZ    . PHE A 857 ? 1.3919 1.5899 1.4593 0.2046  0.0395  0.1220  960  PHE A CZ    
6448 N  N     . LEU A 858 ? 1.4496 1.4886 1.3927 0.2910  0.1019  0.1463  961  LEU A N     
6449 C  CA    . LEU A 858 ? 1.4676 1.4608 1.3758 0.3049  0.1137  0.1482  961  LEU A CA    
6450 C  C     . LEU A 858 ? 1.5344 1.5143 1.4351 0.3167  0.1279  0.1485  961  LEU A C     
6451 O  O     . LEU A 858 ? 1.5523 1.4867 1.4198 0.3193  0.1371  0.1439  961  LEU A O     
6452 C  CB    . LEU A 858 ? 1.4586 1.4550 1.3648 0.3243  0.1143  0.1600  961  LEU A CB    
6453 C  CG    . LEU A 858 ? 1.4174 1.4186 1.3228 0.3152  0.1020  0.1604  961  LEU A CG    
6454 C  CD1   . LEU A 858 ? 1.4783 1.4849 1.3820 0.3372  0.1032  0.1735  961  LEU A CD1   
6455 C  CD2   . LEU A 858 ? 1.3939 1.3501 1.2670 0.2995  0.1019  0.1510  961  LEU A CD2   
6456 N  N     . ILE A 859 ? 1.4800 1.4985 1.4105 0.3234  0.1301  0.1537  962  ILE A N     
6457 C  CA    . ILE A 859 ? 1.4691 1.4779 1.3936 0.3341  0.1441  0.1541  962  ILE A CA    
6458 C  C     . ILE A 859 ? 1.4824 1.4652 1.3893 0.3162  0.1448  0.1414  962  ILE A C     
6459 O  O     . ILE A 859 ? 1.5582 1.5048 1.4372 0.3225  0.1562  0.1378  962  ILE A O     
6460 C  CB    . ILE A 859 ? 1.4984 1.5585 1.4619 0.3421  0.1456  0.1624  962  ILE A CB    
6461 C  CG1   . ILE A 859 ? 1.4939 1.5789 1.4727 0.3632  0.1463  0.1757  962  ILE A CG1   
6462 C  CG2   . ILE A 859 ? 1.4541 1.5060 1.4122 0.3504  0.1601  0.1621  962  ILE A CG2   
6463 C  CD1   . ILE A 859 ? 1.5371 1.5910 1.4904 0.3890  0.1617  0.1822  962  ILE A CD1   
6464 N  N     . VAL A 860 ? 1.4428 1.4429 1.3644 0.2940  0.1325  0.1343  963  VAL A N     
6465 C  CA    . VAL A 860 ? 1.4426 1.4227 1.3501 0.2773  0.1321  0.1229  963  VAL A CA    
6466 C  C     . VAL A 860 ? 1.4918 1.4230 1.3610 0.2709  0.1327  0.1148  963  VAL A C     
6467 O  O     . VAL A 860 ? 1.5051 1.4059 1.3504 0.2669  0.1386  0.1073  963  VAL A O     
6468 C  CB    . VAL A 860 ? 1.3599 1.3721 1.2938 0.2569  0.1189  0.1181  963  VAL A CB    
6469 C  CG1   . VAL A 860 ? 1.3265 1.3215 1.2476 0.2419  0.1189  0.1076  963  VAL A CG1   
6470 C  CG2   . VAL A 860 ? 1.3773 1.4375 1.3495 0.2620  0.1179  0.1263  963  VAL A CG2   
6471 N  N     . ILE A 861 ? 1.5148 1.4377 1.3773 0.2692  0.1266  0.1163  964  ILE A N     
6472 C  CA    . ILE A 861 ? 1.5183 1.3962 1.3463 0.2606  0.1267  0.1090  964  ILE A CA    
6473 C  C     . ILE A 861 ? 1.5537 1.3887 1.3490 0.2767  0.1411  0.1101  964  ILE A C     
6474 O  O     . ILE A 861 ? 1.5469 1.3433 1.3127 0.2683  0.1445  0.1010  964  ILE A O     
6475 C  CB    . ILE A 861 ? 1.4640 1.3447 1.2933 0.2561  0.1178  0.1119  964  ILE A CB    
6476 C  CG1   . ILE A 861 ? 1.4136 1.3286 1.2685 0.2371  0.1036  0.1076  964  ILE A CG1   
6477 C  CG2   . ILE A 861 ? 1.3916 1.2231 1.1839 0.2507  0.1208  0.1068  964  ILE A CG2   
6478 C  CD1   . ILE A 861 ? 1.4520 1.3737 1.3094 0.2329  0.0947  0.1105  964  ILE A CD1   
6479 N  N     . SER A 862 ? 1.5625 1.4037 1.3621 0.3000  0.1496  0.1210  965  SER A N     
6480 C  CA    . SER A 862 ? 1.6261 1.4259 1.3941 0.3182  0.1642  0.1230  965  SER A CA    
6481 C  C     . SER A 862 ? 1.6604 1.4649 1.4305 0.3307  0.1757  0.1240  965  SER A C     
6482 O  O     . SER A 862 ? 1.7136 1.4903 1.4618 0.3503  0.1892  0.1275  965  SER A O     
6483 C  CB    . SER A 862 ? 1.7307 1.5293 1.4976 0.3387  0.1677  0.1351  965  SER A CB    
6484 O  OG    . SER A 862 ? 1.8090 1.5626 1.5422 0.3567  0.1821  0.1369  965  SER A OG    
6485 N  N     . LYS A 863 ? 1.6377 1.4752 1.4323 0.3203  0.1715  0.1211  966  LYS A N     
6486 C  CA    . LYS A 863 ? 1.6583 1.5028 1.4561 0.3299  0.1823  0.1220  966  LYS A CA    
6487 C  C     . LYS A 863 ? 1.7069 1.5699 1.5181 0.3570  0.1928  0.1354  966  LYS A C     
6488 O  O     . LYS A 863 ? 1.7582 1.6522 1.5941 0.3627  0.1869  0.1443  966  LYS A O     
6489 C  CB    . LYS A 863 ? 1.6798 1.4752 1.4376 0.3265  0.1900  0.1115  966  LYS A CB    
6490 C  CG    . LYS A 863 ? 1.5987 1.3734 1.3409 0.3010  0.1788  0.0989  966  LYS A CG    
6491 C  CD    . LYS A 863 ? 1.6050 1.3301 1.3058 0.2984  0.1862  0.0885  966  LYS A CD    
6492 C  CE    . LYS A 863 ? 1.6114 1.3130 1.2946 0.2744  0.1755  0.0770  966  LYS A CE    
6493 N  NZ    . LYS A 863 ? 1.6826 1.3400 1.3275 0.2689  0.1807  0.0657  966  LYS A NZ    
6494 N  N     . GLY A 864 ? 1.6768 1.5229 1.4724 0.3745  0.2083  0.1373  967  GLY A N     
6495 C  CA    . GLY A 864 ? 1.8591 1.7179 1.6633 0.4022  0.2196  0.1501  967  GLY A CA    
6496 C  C     . GLY A 864 ? 1.8707 1.7002 1.6537 0.4141  0.2206  0.1542  967  GLY A C     
6497 O  O     . GLY A 864 ? 1.9671 1.7427 1.7092 0.4174  0.2277  0.1483  967  GLY A O     
6498 N  N     . ALA A 865 ? 1.7855 1.6486 1.5947 0.4203  0.2133  0.1642  968  ALA A N     
6499 C  CA    . ALA A 865 ? 1.8597 1.6974 1.6502 0.4298  0.2122  0.1688  968  ALA A CA    
6500 C  C     . ALA A 865 ? 1.9409 1.8127 1.7548 0.4554  0.2158  0.1845  968  ALA A C     
6501 O  O     . ALA A 865 ? 1.8880 1.8160 1.7431 0.4545  0.2091  0.1908  968  ALA A O     
6502 C  CB    . ALA A 865 ? 1.9129 1.7524 1.7065 0.4061  0.1955  0.1634  968  ALA A CB    
6503 N  N     . GLN A 866 ? 2.0059 1.8431 1.7928 0.4780  0.2262  0.1906  969  GLN A N     
6504 C  CA    . GLN A 866 ? 2.1506 2.0177 1.9568 0.5044  0.2293  0.2063  969  GLN A CA    
6505 C  C     . GLN A 866 ? 2.2759 2.1699 2.1009 0.4967  0.2130  0.2114  969  GLN A C     
6506 O  O     . GLN A 866 ? 2.3329 2.2824 2.1963 0.5031  0.2064  0.2209  969  GLN A O     
6507 C  CB    . GLN A 866 ? 2.2575 2.0752 2.0261 0.5317  0.2456  0.2114  969  GLN A CB    
6508 C  CG    . GLN A 866 ? 2.3073 2.1517 2.0919 0.5614  0.2491  0.2283  969  GLN A CG    
6509 C  CD    . GLN A 866 ? 2.3495 2.1394 2.0932 0.5885  0.2650  0.2331  969  GLN A CD    
6510 O  OE1   . GLN A 866 ? 2.3993 2.1293 2.1015 0.5841  0.2736  0.2231  969  GLN A OE1   
6511 N  NE2   . GLN A 866 ? 2.3074 2.1174 2.0622 0.6169  0.2689  0.2484  969  GLN A NE2   
6512 N  N     . GLU A 867 ? 2.4844 2.3401 2.2825 0.4823  0.2064  0.2051  970  GLU A N     
6513 C  CA    . GLU A 867 ? 2.4910 2.3660 2.3010 0.4754  0.1920  0.2096  970  GLU A CA    
6514 C  C     . GLU A 867 ? 2.4735 2.3411 2.2803 0.4427  0.1787  0.1972  970  GLU A C     
6515 O  O     . GLU A 867 ? 2.5713 2.4429 2.3786 0.4353  0.1679  0.1992  970  GLU A O     
6516 C  CB    . GLU A 867 ? 2.5956 2.4325 2.3753 0.4955  0.1979  0.2182  970  GLU A CB    
6517 C  CG    . GLU A 867 ? 2.6005 2.4461 2.3836 0.5307  0.2105  0.2321  970  GLU A CG    
6518 C  CD    . GLU A 867 ? 2.6113 2.5257 2.4395 0.5416  0.2016  0.2444  970  GLU A CD    
6519 O  OE1   . GLU A 867 ? 2.7242 2.6714 2.5743 0.5235  0.1851  0.2431  970  GLU A OE1   
6520 O  OE2   . GLU A 867 ? 2.6478 2.5841 2.4893 0.5682  0.2111  0.2553  970  GLU A OE2   
6521 N  N     . CYS A 868 ? 2.1385 1.9953 1.9408 0.4240  0.1795  0.1848  971  CYS A N     
6522 C  CA    . CYS A 868 ? 2.0499 1.9027 1.8512 0.3935  0.1674  0.1727  971  CYS A CA    
6523 C  C     . CYS A 868 ? 2.0401 1.8421 1.8045 0.3849  0.1666  0.1681  971  CYS A C     
6524 O  O     . CYS A 868 ? 1.9352 1.7046 1.6781 0.3666  0.1669  0.1562  971  CYS A O     
6525 C  CB    . CYS A 868 ? 1.9359 1.8447 1.7767 0.3817  0.1516  0.1751  971  CYS A CB    
6526 S  SG    . CYS A 868 ? 1.7958 1.7665 1.6827 0.3868  0.1511  0.1799  971  CYS A SG    
6527 N  N     . THR A 869 ? 2.1387 1.9344 1.8958 0.3975  0.1656  0.1778  972  THR A N     
6528 C  CA    . THR A 869 ? 2.0729 1.8202 1.7951 0.3901  0.1659  0.1752  972  THR A CA    
6529 C  C     . THR A 869 ? 2.0721 1.7596 1.7535 0.4025  0.1820  0.1734  972  THR A C     
6530 O  O     . THR A 869 ? 2.1143 1.7981 1.7940 0.4148  0.1923  0.1726  972  THR A O     
6531 C  CB    . THR A 869 ? 2.0840 1.8451 1.8114 0.4003  0.1596  0.1870  972  THR A CB    
6532 O  OG1   . THR A 869 ? 2.2198 1.9892 1.9507 0.4315  0.1682  0.2005  972  THR A OG1   
6533 C  CG2   . THR A 869 ? 1.8621 1.6793 1.6268 0.3860  0.1431  0.1869  972  THR A CG2   
6534 N  N     . LYS A 870 ? 2.0627 1.7018 1.7100 0.3992  0.1846  0.1728  973  LYS A N     
6535 C  CA    . LYS A 870 ? 2.0612 1.6350 1.6643 0.4063  0.1988  0.1692  973  LYS A CA    
6536 C  C     . LYS A 870 ? 2.0260 1.5855 1.6207 0.3987  0.2049  0.1570  973  LYS A C     
6537 O  O     . LYS A 870 ? 2.0879 1.6183 1.6620 0.4166  0.2187  0.1576  973  LYS A O     
6538 C  CB    . LYS A 870 ? 2.1442 1.7008 1.7336 0.4401  0.2109  0.1832  973  LYS A CB    
6539 C  CG    . LYS A 870 ? 2.2050 1.8032 1.8219 0.4650  0.2161  0.1920  973  LYS A CG    
6540 C  CD    . LYS A 870 ? 2.3285 1.9021 1.9263 0.4991  0.2294  0.2051  973  LYS A CD    
6541 C  CE    . LYS A 870 ? 2.3889 2.0057 2.0151 0.5242  0.2356  0.2140  973  LYS A CE    
6542 N  NZ    . LYS A 870 ? 2.4128 2.1026 2.0880 0.5214  0.2216  0.2208  973  LYS A NZ    
6543 N  N     . THR A 871 ? 1.9398 1.5195 1.5495 0.3721  0.1946  0.1459  974  THR A N     
6544 C  CA    . THR A 871 ? 1.8853 1.4554 1.4884 0.3616  0.1979  0.1338  974  THR A CA    
6545 C  C     . THR A 871 ? 1.8531 1.4032 1.4429 0.3305  0.1895  0.1203  974  THR A C     
6546 O  O     . THR A 871 ? 1.8395 1.4105 1.4445 0.3143  0.1777  0.1201  974  THR A O     
6547 C  CB    . THR A 871 ? 1.8578 1.4855 1.5010 0.3633  0.1937  0.1352  974  THR A CB    
6548 O  OG1   . THR A 871 ? 1.9494 1.6014 1.6089 0.3916  0.2008  0.1487  974  THR A OG1   
6549 C  CG2   . THR A 871 ? 1.8469 1.4621 1.4800 0.3556  0.1987  0.1240  974  THR A CG2   
6550 N  N     . ARG A 872 ? 1.8562 1.3661 1.4168 0.3225  0.1958  0.1089  975  ARG A N     
6551 C  CA    . ARG A 872 ? 1.8654 1.3576 1.4135 0.2929  0.1879  0.0956  975  ARG A CA    
6552 C  C     . ARG A 872 ? 1.7804 1.3244 1.3645 0.2743  0.1741  0.0911  975  ARG A C     
6553 O  O     . ARG A 872 ? 1.7949 1.3411 1.3809 0.2512  0.1642  0.0847  975  ARG A O     
6554 C  CB    . ARG A 872 ? 1.9864 1.4315 1.4990 0.2889  0.1964  0.0840  975  ARG A CB    
6555 C  CG    . ARG A 872 ? 2.1101 1.4942 1.5807 0.3029  0.2097  0.0859  975  ARG A CG    
6556 C  CD    . ARG A 872 ? 2.2943 1.6325 1.7291 0.2967  0.2169  0.0726  975  ARG A CD    
6557 N  NE    . ARG A 872 ? 2.4062 1.6822 1.7985 0.3103  0.2302  0.0736  975  ARG A NE    
6558 C  CZ    . ARG A 872 ? 2.4099 1.6362 1.7641 0.3085  0.2385  0.0629  975  ARG A CZ    
6559 N  NH1   . ARG A 872 ? 2.3910 1.6229 1.7434 0.2939  0.2346  0.0504  975  ARG A NH1   
6560 N  NH2   . ARG A 872 ? 2.3495 1.5180 1.6651 0.3218  0.2510  0.0646  975  ARG A NH2   
6561 N  N     . GLU A 873 ? 1.7396 1.3250 1.3522 0.2840  0.1739  0.0946  976  GLU A N     
6562 C  CA    . GLU A 873 ? 1.7234 1.3579 1.3709 0.2680  0.1612  0.0916  976  GLU A CA    
6563 C  C     . GLU A 873 ? 1.6723 1.3360 1.3423 0.2625  0.1506  0.0980  976  GLU A C     
6564 O  O     . GLU A 873 ? 1.5866 1.2695 1.2702 0.2416  0.1392  0.0920  976  GLU A O     
6565 C  CB    . GLU A 873 ? 1.6830 1.3547 1.3565 0.2810  0.1644  0.0959  976  GLU A CB    
6566 C  CG    . GLU A 873 ? 1.7469 1.4070 1.4088 0.2753  0.1686  0.0862  976  GLU A CG    
6567 C  CD    . GLU A 873 ? 1.7843 1.3903 1.4048 0.2857  0.1819  0.0823  976  GLU A CD    
6568 O  OE1   . GLU A 873 ? 1.8001 1.3857 1.4072 0.3056  0.1913  0.0904  976  GLU A OE1   
6569 O  OE2   . GLU A 873 ? 1.7407 1.3238 1.3407 0.2743  0.1828  0.0711  976  GLU A OE2   
6570 N  N     . PHE A 874 ? 1.6639 1.3316 1.3371 0.2817  0.1542  0.1101  977  PHE A N     
6571 C  CA    . PHE A 874 ? 1.5906 1.2837 1.2815 0.2779  0.1443  0.1165  977  PHE A CA    
6572 C  C     . PHE A 874 ? 1.6310 1.2868 1.2951 0.2640  0.1425  0.1130  977  PHE A C     
6573 O  O     . PHE A 874 ? 1.5805 1.2555 1.2572 0.2492  0.1320  0.1122  977  PHE A O     
6574 C  CB    . PHE A 874 ? 1.6411 1.3527 1.3440 0.3040  0.1481  0.1312  977  PHE A CB    
6575 C  CG    . PHE A 874 ? 1.6090 1.3519 1.3319 0.3017  0.1372  0.1383  977  PHE A CG    
6576 C  CD1   . PHE A 874 ? 1.4941 1.2884 1.2530 0.2916  0.1252  0.1373  977  PHE A CD1   
6577 C  CD2   . PHE A 874 ? 1.6288 1.3482 1.3327 0.3099  0.1390  0.1459  977  PHE A CD2   
6578 C  CE1   . PHE A 874 ? 1.4776 1.2997 1.2528 0.2895  0.1149  0.1430  977  PHE A CE1   
6579 C  CE2   . PHE A 874 ? 1.6406 1.3888 1.3609 0.3084  0.1288  0.1525  977  PHE A CE2   
6580 C  CZ    . PHE A 874 ? 1.5600 1.3599 1.3158 0.2981  0.1165  0.1506  977  PHE A CZ    
6581 N  N     . GLU A 875 ? 1.6752 1.2771 1.3020 0.2681  0.1531  0.1108  978  GLU A N     
6582 C  CA    . GLU A 875 ? 1.6786 1.2423 1.2790 0.2529  0.1524  0.1071  978  GLU A CA    
6583 C  C     . GLU A 875 ? 1.6606 1.2293 1.2643 0.2235  0.1434  0.0939  978  GLU A C     
6584 O  O     . GLU A 875 ? 1.6489 1.2168 1.2516 0.2070  0.1369  0.0923  978  GLU A O     
6585 C  CB    . GLU A 875 ? 1.7916 1.2940 1.3502 0.2628  0.1661  0.1066  978  GLU A CB    
6586 C  CG    . GLU A 875 ? 1.8367 1.3282 1.3876 0.2928  0.1757  0.1207  978  GLU A CG    
6587 C  CD    . GLU A 875 ? 1.9279 1.3531 1.4340 0.3016  0.1894  0.1200  978  GLU A CD    
6588 O  OE1   . GLU A 875 ? 2.0209 1.4075 1.5013 0.2814  0.1902  0.1089  978  GLU A OE1   
6589 O  OE2   . GLU A 875 ? 1.8734 1.2850 1.3699 0.3288  0.1995  0.1303  978  GLU A OE2   
6590 N  N     . ARG A 876 ? 1.6878 1.2625 1.2953 0.2172  0.1432  0.0846  979  ARG A N     
6591 C  CA    . ARG A 876 ? 1.6522 1.2388 1.2670 0.1912  0.1337  0.0729  979  ARG A CA    
6592 C  C     . ARG A 876 ? 1.5429 1.1839 1.1957 0.1838  0.1215  0.0749  979  ARG A C     
6593 O  O     . ARG A 876 ? 1.5493 1.2011 1.2087 0.1626  0.1128  0.0674  979  ARG A O     
6594 C  CB    . ARG A 876 ? 1.7148 1.2932 1.3221 0.1881  0.1367  0.0632  979  ARG A CB    
6595 C  CG    . ARG A 876 ? 1.8240 1.3508 1.3935 0.1759  0.1414  0.0528  979  ARG A CG    
6596 C  CD    . ARG A 876 ? 1.9689 1.4473 1.5057 0.1939  0.1550  0.0574  979  ARG A CD    
6597 N  NE    . ARG A 876 ? 2.2194 1.6969 1.7537 0.2146  0.1640  0.0594  979  ARG A NE    
6598 C  CZ    . ARG A 876 ? 2.2142 1.6680 1.7280 0.2124  0.1688  0.0498  979  ARG A CZ    
6599 N  NH1   . ARG A 876 ? 2.2198 1.6490 1.7137 0.1900  0.1648  0.0371  979  ARG A NH1   
6600 N  NH2   . ARG A 876 ? 2.0976 1.5538 1.6109 0.2331  0.1779  0.0530  979  ARG A NH2   
6601 N  N     . PHE A 877 ? 1.5141 1.1897 1.1917 0.2007  0.1206  0.0846  980  PHE A N     
6602 C  CA    . PHE A 877 ? 1.4546 1.1785 1.1658 0.1937  0.1089  0.0866  980  PHE A CA    
6603 C  C     . PHE A 877 ? 1.5015 1.2240 1.2099 0.1890  0.1042  0.0914  980  PHE A C     
6604 O  O     . PHE A 877 ? 1.4150 1.1630 1.1398 0.1740  0.0942  0.0883  980  PHE A O     
6605 C  CB    . PHE A 877 ? 1.4458 1.2077 1.1847 0.2118  0.1090  0.0950  980  PHE A CB    
6606 C  CG    . PHE A 877 ? 1.3845 1.1940 1.1564 0.2062  0.0972  0.0977  980  PHE A CG    
6607 C  CD1   . PHE A 877 ? 1.3779 1.2152 1.1705 0.1909  0.0890  0.0901  980  PHE A CD1   
6608 C  CD2   . PHE A 877 ? 1.3970 1.2221 1.1776 0.2166  0.0942  0.1078  980  PHE A CD2   
6609 C  CE1   . PHE A 877 ? 1.3852 1.2632 1.2061 0.1856  0.0783  0.0918  980  PHE A CE1   
6610 C  CE2   . PHE A 877 ? 1.3882 1.2557 1.1972 0.2109  0.0828  0.1093  980  PHE A CE2   
6611 C  CZ    . PHE A 877 ? 1.3983 1.2913 1.2271 0.1951  0.0751  0.1010  980  PHE A CZ    
6612 N  N     . GLN A 878 ? 1.5126 1.2047 1.1991 0.2023  0.1119  0.0994  981  GLN A N     
6613 C  CA    . GLN A 878 ? 1.4729 1.1582 1.1519 0.1980  0.1088  0.1045  981  GLN A CA    
6614 C  C     . GLN A 878 ? 1.4786 1.1401 1.1408 0.1734  0.1067  0.0949  981  GLN A C     
6615 O  O     . GLN A 878 ? 1.5426 1.2174 1.2113 0.1615  0.0999  0.0954  981  GLN A O     
6616 C  CB    . GLN A 878 ? 1.5138 1.1679 1.1704 0.2191  0.1186  0.1157  981  GLN A CB    
6617 C  CG    . GLN A 878 ? 1.5527 1.2369 1.2290 0.2440  0.1193  0.1273  981  GLN A CG    
6618 C  CD    . GLN A 878 ? 1.6558 1.3083 1.3088 0.2664  0.1292  0.1389  981  GLN A CD    
6619 O  OE1   . GLN A 878 ? 1.6784 1.2818 1.2997 0.2698  0.1400  0.1370  981  GLN A OE1   
6620 N  NE2   . GLN A 878 ? 1.7102 1.3899 1.3778 0.2820  0.1254  0.1508  981  GLN A NE2   
6621 N  N     . GLU A 879 ? 1.4895 1.1166 1.1300 0.1653  0.1125  0.0861  982  GLU A N     
6622 C  CA    . GLU A 879 ? 1.5266 1.1338 1.1530 0.1407  0.1102  0.0765  982  GLU A CA    
6623 C  C     . GLU A 879 ? 1.4709 1.1190 1.1243 0.1228  0.0985  0.0688  982  GLU A C     
6624 O  O     . GLU A 879 ? 1.4972 1.1475 1.1504 0.1046  0.0936  0.0650  982  GLU A O     
6625 C  CB    . GLU A 879 ? 1.6071 1.1703 1.2046 0.1362  0.1180  0.0680  982  GLU A CB    
6626 C  CG    . GLU A 879 ? 1.6987 1.2095 1.2615 0.1475  0.1299  0.0735  982  GLU A CG    
6627 C  CD    . GLU A 879 ? 1.8907 1.3563 1.4231 0.1407  0.1369  0.0634  982  GLU A CD    
6628 O  OE1   . GLU A 879 ? 1.8624 1.3404 1.4019 0.1289  0.1323  0.0528  982  GLU A OE1   
6629 O  OE2   . GLU A 879 ? 2.0094 1.4261 1.5097 0.1472  0.1469  0.0660  982  GLU A OE2   
6630 N  N     . MET A 880 ? 1.4091 1.0897 1.0857 0.1280  0.0946  0.0667  983  MET A N     
6631 C  CA    . MET A 880 ? 1.4244 1.1428 1.1262 0.1129  0.0840  0.0599  983  MET A CA    
6632 C  C     . MET A 880 ? 1.4187 1.1683 1.1401 0.1107  0.0763  0.0652  983  MET A C     
6633 O  O     . MET A 880 ? 1.3790 1.1469 1.1113 0.0941  0.0688  0.0593  983  MET A O     
6634 C  CB    . MET A 880 ? 1.3982 1.1423 1.1195 0.1204  0.0825  0.0579  983  MET A CB    
6635 C  CG    . MET A 880 ? 1.3140 1.0324 1.0174 0.1188  0.0883  0.0503  983  MET A CG    
6636 S  SD    . MET A 880 ? 1.4521 1.2037 1.1793 0.1242  0.0858  0.0477  983  MET A SD    
6637 C  CE    . MET A 880 ? 1.4461 1.2143 1.1878 0.1503  0.0914  0.0611  983  MET A CE    
6638 N  N     . CYS A 881 ? 1.5067 1.2631 1.2320 0.1279  0.0780  0.0762  984  CYS A N     
6639 C  CA    . CYS A 881 ? 1.4538 1.2384 1.1948 0.1267  0.0705  0.0813  984  CYS A CA    
6640 C  C     . CYS A 881 ? 1.3968 1.1582 1.1181 0.1158  0.0718  0.0822  984  CYS A C     
6641 O  O     . CYS A 881 ? 1.3431 1.1249 1.0749 0.1034  0.0648  0.0800  984  CYS A O     
6642 C  CB    . CYS A 881 ? 1.3796 1.1808 1.1311 0.1487  0.0711  0.0929  984  CYS A CB    
6643 S  SG    . CYS A 881 ? 1.4157 1.2529 1.1962 0.1602  0.0688  0.0931  984  CYS A SG    
6644 N  N     . TYR A 882 ? 1.4293 1.1470 1.1214 0.1202  0.0814  0.0856  985  TYR A N     
6645 C  CA    . TYR A 882 ? 1.3904 1.0827 1.0621 0.1093  0.0840  0.0874  985  TYR A CA    
6646 C  C     . TYR A 882 ? 1.3686 1.0615 1.0408 0.0838  0.0802  0.0761  985  TYR A C     
6647 O  O     . TYR A 882 ? 1.3729 1.0748 1.0473 0.0717  0.0768  0.0764  985  TYR A O     
6648 C  CB    . TYR A 882 ? 1.5342 1.1750 1.1727 0.1182  0.0958  0.0923  985  TYR A CB    
6649 C  CG    . TYR A 882 ? 1.5470 1.1846 1.1829 0.1452  0.1006  0.1044  985  TYR A CG    
6650 C  CD1   . TYR A 882 ? 1.5038 1.1813 1.1630 0.1579  0.0939  0.1123  985  TYR A CD1   
6651 C  CD2   . TYR A 882 ? 1.6115 1.2063 1.2212 0.1583  0.1118  0.1076  985  TYR A CD2   
6652 C  CE1   . TYR A 882 ? 1.5469 1.2251 1.2054 0.1829  0.0978  0.1237  985  TYR A CE1   
6653 C  CE2   . TYR A 882 ? 1.6168 1.2103 1.2248 0.1845  0.1167  0.1191  985  TYR A CE2   
6654 C  CZ    . TYR A 882 ? 1.5760 1.2127 1.2094 0.1967  0.1094  0.1274  985  TYR A CZ    
6655 O  OH    . TYR A 882 ? 1.5872 1.2261 1.2206 0.2230  0.1137  0.1392  985  TYR A OH    
6656 N  N     . LYS A 883 ? 1.4293 1.1138 1.0993 0.0759  0.0809  0.0663  986  LYS A N     
6657 C  CA    . LYS A 883 ? 1.3752 1.0622 1.0463 0.0522  0.0769  0.0556  986  LYS A CA    
6658 C  C     . LYS A 883 ? 1.3055 1.0403 1.0068 0.0449  0.0664  0.0522  986  LYS A C     
6659 O  O     . LYS A 883 ? 1.2793 1.0231 0.9841 0.0275  0.0627  0.0476  986  LYS A O     
6660 C  CB    . LYS A 883 ? 1.4113 1.0791 1.0719 0.0472  0.0794  0.0462  986  LYS A CB    
6661 C  CG    . LYS A 883 ? 1.5357 1.1513 1.1627 0.0517  0.0900  0.0474  986  LYS A CG    
6662 C  CD    . LYS A 883 ? 1.5702 1.1692 1.1868 0.0489  0.0919  0.0377  986  LYS A CD    
6663 C  CE    . LYS A 883 ? 1.6517 1.1962 1.2329 0.0549  0.1030  0.0385  986  LYS A CE    
6664 N  NZ    . LYS A 883 ? 1.8790 1.4073 1.4485 0.0548  0.1052  0.0293  986  LYS A NZ    
6665 N  N     . ALA A 884 ? 1.2646 1.0303 0.9880 0.0578  0.0619  0.0544  987  ALA A N     
6666 C  CA    . ALA A 884 ? 1.2247 1.0332 0.9754 0.0519  0.0522  0.0513  987  ALA A CA    
6667 C  C     . ALA A 884 ? 1.2451 1.0677 1.0002 0.0522  0.0492  0.0577  987  ALA A C     
6668 O  O     . ALA A 884 ? 1.1921 1.0375 0.9595 0.0403  0.0432  0.0535  987  ALA A O     
6669 C  CB    . ALA A 884 ? 1.2245 1.0593 0.9964 0.0647  0.0487  0.0520  987  ALA A CB    
6670 N  N     . TYR A 885 ? 1.2650 1.0744 1.0094 0.0666  0.0535  0.0680  988  TYR A N     
6671 C  CA    . TYR A 885 ? 1.2318 1.0534 0.9777 0.0686  0.0508  0.0749  988  TYR A CA    
6672 C  C     . TYR A 885 ? 1.2458 1.0515 0.9771 0.0512  0.0532  0.0728  988  TYR A C     
6673 O  O     . TYR A 885 ? 1.2325 1.0616 0.9743 0.0425  0.0479  0.0711  988  TYR A O     
6674 C  CB    . TYR A 885 ? 1.2578 1.0656 0.9925 0.0887  0.0554  0.0870  988  TYR A CB    
6675 C  CG    . TYR A 885 ? 1.3014 1.1182 1.0334 0.0924  0.0530  0.0953  988  TYR A CG    
6676 C  CD1   . TYR A 885 ? 1.3084 1.1649 1.0623 0.0972  0.0437  0.0967  988  TYR A CD1   
6677 C  CD2   . TYR A 885 ? 1.4057 1.1899 1.1117 0.0909  0.0601  0.1016  988  TYR A CD2   
6678 C  CE1   . TYR A 885 ? 1.2994 1.1640 1.0488 0.1010  0.0410  0.1040  988  TYR A CE1   
6679 C  CE2   . TYR A 885 ? 1.3246 1.1164 1.0262 0.0949  0.0582  0.1098  988  TYR A CE2   
6680 C  CZ    . TYR A 885 ? 1.3300 1.1627 1.0531 0.1003  0.0484  0.1108  988  TYR A CZ    
6681 O  OH    . TYR A 885 ? 1.4094 1.2497 1.1263 0.1046  0.0460  0.1186  988  TYR A OH    
6682 N  N     . LEU A 886 ? 1.2367 1.0023 0.9434 0.0457  0.0616  0.0726  989  LEU A N     
6683 C  CA    . LEU A 886 ? 1.2516 1.0008 0.9443 0.0276  0.0648  0.0708  989  LEU A CA    
6684 C  C     . LEU A 886 ? 1.2412 1.0107 0.9483 0.0078  0.0596  0.0593  989  LEU A C     
6685 O  O     . LEU A 886 ? 1.2546 1.0254 0.9588 -0.0075 0.0601  0.0578  989  LEU A O     
6686 C  CB    . LEU A 886 ? 1.3664 1.0651 1.0285 0.0258  0.0752  0.0730  989  LEU A CB    
6687 C  CG    . LEU A 886 ? 1.4307 1.1043 1.0745 0.0452  0.0818  0.0857  989  LEU A CG    
6688 C  CD1   . LEU A 886 ? 1.5619 1.1816 1.1732 0.0415  0.0927  0.0870  989  LEU A CD1   
6689 C  CD2   . LEU A 886 ? 1.4203 1.1099 1.0665 0.0487  0.0797  0.0946  989  LEU A CD2   
6690 N  N     . ALA A 887 ? 1.2438 1.0297 0.9660 0.0083  0.0548  0.0516  990  ALA A N     
6691 C  CA    . ALA A 887 ? 1.2318 1.0406 0.9691 -0.0082 0.0490  0.0414  990  ALA A CA    
6692 C  C     . ALA A 887 ? 1.2096 1.0579 0.9687 -0.0090 0.0418  0.0416  990  ALA A C     
6693 O  O     . ALA A 887 ? 1.2135 1.0751 0.9782 -0.0238 0.0397  0.0371  990  ALA A O     
6694 C  CB    . ALA A 887 ? 1.2706 1.0845 1.0162 -0.0058 0.0461  0.0342  990  ALA A CB    
6695 N  N     . ILE A 888 ? 1.2096 1.0772 0.9811 0.0066  0.0379  0.0466  991  ILE A N     
6696 C  CA    . ILE A 888 ? 1.1691 1.0713 0.9587 0.0066  0.0310  0.0465  991  ILE A CA    
6697 C  C     . ILE A 888 ? 1.1590 1.0556 0.9367 0.0037  0.0340  0.0529  991  ILE A C     
6698 O  O     . ILE A 888 ? 1.1565 1.0747 0.9429 -0.0043 0.0306  0.0504  991  ILE A O     
6699 C  CB    . ILE A 888 ? 1.1554 1.0787 0.9607 0.0230  0.0258  0.0498  991  ILE A CB    
6700 C  CG1   . ILE A 888 ? 1.0714 0.9997 0.8879 0.0253  0.0240  0.0440  991  ILE A CG1   
6701 C  CG2   . ILE A 888 ? 1.1377 1.0946 0.9599 0.0225  0.0183  0.0487  991  ILE A CG2   
6702 C  CD1   . ILE A 888 ? 1.0934 1.0403 0.9235 0.0122  0.0192  0.0340  991  ILE A CD1   
6703 N  N     . ARG A 889 ? 1.1900 1.0567 0.9465 0.0107  0.0409  0.0615  992  ARG A N     
6704 C  CA    . ARG A 889 ? 1.1627 1.0202 0.9048 0.0080  0.0448  0.0687  992  ARG A CA    
6705 C  C     . ARG A 889 ? 1.2201 1.0717 0.9567 -0.0128 0.0483  0.0637  992  ARG A C     
6706 O  O     . ARG A 889 ? 1.3480 1.2100 1.0835 -0.0186 0.0488  0.0663  992  ARG A O     
6707 C  CB    . ARG A 889 ? 1.1246 0.9465 0.8430 0.0199  0.0524  0.0791  992  ARG A CB    
6708 C  CG    . ARG A 889 ? 1.2968 1.1044 0.9969 0.0184  0.0575  0.0880  992  ARG A CG    
6709 C  CD    . ARG A 889 ? 1.3380 1.1106 1.0150 0.0332  0.0647  0.0990  992  ARG A CD    
6710 N  NE    . ARG A 889 ? 1.3646 1.1217 1.0222 0.0325  0.0701  0.1086  992  ARG A NE    
6711 C  CZ    . ARG A 889 ? 1.4907 1.2134 1.1263 0.0201  0.0794  0.1107  992  ARG A CZ    
6712 N  NH1   . ARG A 889 ? 1.4685 1.1684 1.0981 0.0067  0.0837  0.1033  992  ARG A NH1   
6713 N  NH2   . ARG A 889 ? 1.5119 1.2223 1.1302 0.0208  0.0843  0.1205  992  ARG A NH2   
6714 N  N     . GLN A 890 ? 1.2303 1.0669 0.9637 -0.0245 0.0506  0.0565  993  GLN A N     
6715 C  CA    . GLN A 890 ? 1.2609 1.0952 0.9916 -0.0456 0.0533  0.0513  993  GLN A CA    
6716 C  C     . GLN A 890 ? 1.1422 1.0174 0.8965 -0.0535 0.0463  0.0443  993  GLN A C     
6717 O  O     . GLN A 890 ? 1.1714 1.0527 0.9265 -0.0694 0.0483  0.0416  993  GLN A O     
6718 C  CB    . GLN A 890 ? 1.3669 1.1758 1.0880 -0.0557 0.0563  0.0447  993  GLN A CB    
6719 C  CG    . GLN A 890 ? 1.5563 1.3547 1.2696 -0.0783 0.0605  0.0409  993  GLN A CG    
6720 C  CD    . GLN A 890 ? 1.6962 1.4821 1.4069 -0.0900 0.0596  0.0312  993  GLN A CD    
6721 O  OE1   . GLN A 890 ? 1.7703 1.5485 1.4802 -0.0801 0.0576  0.0284  993  GLN A OE1   
6722 N  NE2   . GLN A 890 ? 1.6228 1.4081 1.3323 -0.1114 0.0611  0.0261  993  GLN A NE2   
6723 N  N     . HIS A 891 ? 1.1172 1.0200 0.8906 -0.0427 0.0386  0.0415  994  HIS A N     
6724 C  CA    . HIS A 891 ? 1.1348 1.0747 0.9297 -0.0476 0.0320  0.0351  994  HIS A CA    
6725 C  C     . HIS A 891 ? 1.1377 1.0989 0.9398 -0.0361 0.0280  0.0396  994  HIS A C     
6726 O  O     . HIS A 891 ? 1.1379 1.1277 0.9585 -0.0329 0.0211  0.0346  994  HIS A O     
6727 C  CB    . HIS A 891 ? 1.2896 1.2440 1.1009 -0.0468 0.0259  0.0266  994  HIS A CB    
6728 C  CG    . HIS A 891 ? 1.2540 1.1915 1.0589 -0.0588 0.0283  0.0209  994  HIS A CG    
6729 N  ND1   . HIS A 891 ? 1.2957 1.1998 1.0831 -0.0561 0.0331  0.0229  994  HIS A ND1   
6730 C  CD2   . HIS A 891 ? 1.2499 1.1995 1.0628 -0.0733 0.0263  0.0130  994  HIS A CD2   
6731 C  CE1   . HIS A 891 ? 1.2784 1.1737 1.0623 -0.0693 0.0335  0.0158  994  HIS A CE1   
6732 N  NE2   . HIS A 891 ? 1.2010 1.1248 1.0009 -0.0800 0.0291  0.0100  994  HIS A NE2   
6733 N  N     . ALA A 892 ? 1.1725 1.1188 0.9586 -0.0297 0.0323  0.0490  995  ALA A N     
6734 C  CA    . ALA A 892 ? 1.0913 1.0561 0.8816 -0.0178 0.0278  0.0535  995  ALA A CA    
6735 C  C     . ALA A 892 ? 1.0699 1.0634 0.8712 -0.0251 0.0247  0.0487  995  ALA A C     
6736 O  O     . ALA A 892 ? 1.0732 1.0910 0.8871 -0.0175 0.0177  0.0465  995  ALA A O     
6737 C  CB    . ALA A 892 ? 1.1023 1.0442 0.8707 -0.0102 0.0334  0.0651  995  ALA A CB    
6738 N  N     . ASN A 893 ? 1.0760 1.0671 0.8729 -0.0401 0.0302  0.0469  996  ASN A N     
6739 C  CA    . ASN A 893 ? 1.0537 1.0718 0.8602 -0.0464 0.0288  0.0429  996  ASN A CA    
6740 C  C     . ASN A 893 ? 1.0966 1.1428 0.9260 -0.0451 0.0207  0.0331  996  ASN A C     
6741 O  O     . ASN A 893 ? 1.0576 1.1274 0.8955 -0.0422 0.0169  0.0303  996  ASN A O     
6742 C  CB    . ASN A 893 ? 1.0284 1.0406 0.8289 -0.0637 0.0365  0.0424  996  ASN A CB    
6743 C  CG    . ASN A 893 ? 1.2005 1.1846 0.9772 -0.0660 0.0454  0.0526  996  ASN A CG    
6744 O  OD1   . ASN A 893 ? 1.2105 1.1760 0.9739 -0.0538 0.0459  0.0602  996  ASN A OD1   
6745 N  ND2   . ASN A 893 ? 1.2628 1.2439 1.0342 -0.0815 0.0528  0.0533  996  ASN A ND2   
6746 N  N     . LEU A 894 ? 1.1205 1.1629 0.9583 -0.0468 0.0183  0.0280  997  LEU A N     
6747 C  CA    . LEU A 894 ? 0.9999 1.0664 0.8582 -0.0454 0.0113  0.0194  997  LEU A CA    
6748 C  C     . LEU A 894 ? 1.0714 1.1507 0.9376 -0.0314 0.0044  0.0198  997  LEU A C     
6749 O  O     . LEU A 894 ? 0.9799 1.0821 0.8575 -0.0298 -0.0002 0.0151  997  LEU A O     
6750 C  CB    . LEU A 894 ? 1.0986 1.1556 0.9611 -0.0494 0.0106  0.0149  997  LEU A CB    
6751 C  CG    . LEU A 894 ? 1.0135 1.0898 0.8948 -0.0453 0.0034  0.0077  997  LEU A CG    
6752 C  CD1   . LEU A 894 ? 1.1070 1.2103 1.0016 -0.0510 0.0010  0.0015  997  LEU A CD1   
6753 C  CD2   . LEU A 894 ? 1.1432 1.2062 1.0241 -0.0485 0.0036  0.0045  997  LEU A CD2   
6754 N  N     . PHE A 895 ? 0.9832 1.0481 0.8436 -0.0212 0.0036  0.0254  998  PHE A N     
6755 C  CA    . PHE A 895 ? 1.0172 1.0958 0.8868 -0.0090 -0.0034 0.0259  998  PHE A CA    
6756 C  C     . PHE A 895 ? 1.0802 1.1709 0.9452 -0.0053 -0.0054 0.0285  998  PHE A C     
6757 O  O     . PHE A 895 ? 1.0460 1.1565 0.9220 -0.0006 -0.0122 0.0245  998  PHE A O     
6758 C  CB    . PHE A 895 ? 0.9934 1.0557 0.8582 0.0013  -0.0029 0.0321  998  PHE A CB    
6759 C  CG    . PHE A 895 ? 1.0759 1.1263 0.9441 -0.0007 -0.0010 0.0292  998  PHE A CG    
6760 C  CD1   . PHE A 895 ? 1.0328 1.0976 0.9181 0.0013  -0.0062 0.0233  998  PHE A CD1   
6761 C  CD2   . PHE A 895 ? 1.0807 1.1039 0.9332 -0.0049 0.0061  0.0322  998  PHE A CD2   
6762 C  CE1   . PHE A 895 ? 1.0440 1.0978 0.9307 -0.0001 -0.0043 0.0208  998  PHE A CE1   
6763 C  CE2   . PHE A 895 ? 1.0687 1.0801 0.9221 -0.0067 0.0077  0.0288  998  PHE A CE2   
6764 C  CZ    . PHE A 895 ? 1.1685 1.1959 1.0389 -0.0040 0.0025  0.0233  998  PHE A CZ    
6765 N  N     . ILE A 896 ? 1.0478 1.1255 0.8952 -0.0075 0.0006  0.0351  999  ILE A N     
6766 C  CA    . ILE A 896 ? 1.0685 1.1571 0.9089 -0.0045 -0.0006 0.0377  999  ILE A CA    
6767 C  C     . ILE A 896 ? 1.1185 1.2295 0.9692 -0.0113 -0.0023 0.0292  999  ILE A C     
6768 O  O     . ILE A 896 ? 1.0634 1.1916 0.9178 -0.0061 -0.0079 0.0263  999  ILE A O     
6769 C  CB    . ILE A 896 ? 1.1242 1.1924 0.9423 -0.0067 0.0077  0.0469  999  ILE A CB    
6770 C  CG1   . ILE A 896 ? 1.0362 1.0821 0.8428 0.0033  0.0091  0.0560  999  ILE A CG1   
6771 C  CG2   . ILE A 896 ? 1.1047 1.1849 0.9141 -0.0045 0.0072  0.0493  999  ILE A CG2   
6772 N  N     . ASN A 897 ? 1.0593 1.1708 0.9147 -0.0228 0.0022  0.0248  1000 ASN A N     
6773 C  CA    . ASN A 897 ? 1.0273 1.1612 0.8940 -0.0279 0.0010  0.0168  1000 ASN A CA    
6774 C  C     . ASN A 897 ? 1.0419 1.1914 0.9262 -0.0224 -0.0073 0.0091  1000 ASN A C     
6775 O  O     . ASN A 897 ? 1.0547 1.2224 0.9457 -0.0211 -0.0102 0.0034  1000 ASN A O     
6776 C  CB    . ASN A 897 ? 1.0331 1.1662 0.9025 -0.0413 0.0072  0.0143  1000 ASN A CB    
6777 C  CG    . ASN A 897 ? 1.2594 1.3834 1.1134 -0.0491 0.0161  0.0206  1000 ASN A CG    
6778 O  OD1   . ASN A 897 ? 1.3577 1.4823 1.2001 -0.0444 0.0177  0.0254  1000 ASN A OD1   
6779 N  ND2   . ASN A 897 ? 1.3067 1.4221 1.1596 -0.0616 0.0219  0.0207  1000 ASN A ND2   
6780 N  N     . LEU A 898 ? 1.0122 1.1538 0.9033 -0.0188 -0.0105 0.0090  1001 LEU A N     
6781 C  CA    . LEU A 898 ? 1.0061 1.1608 0.9132 -0.0137 -0.0178 0.0028  1001 LEU A CA    
6782 C  C     . LEU A 898 ? 1.0171 1.1796 0.9240 -0.0045 -0.0241 0.0037  1001 LEU A C     
6783 O  O     . LEU A 898 ? 1.0570 1.2338 0.9747 -0.0021 -0.0298 -0.0028 1001 LEU A O     
6784 C  CB    . LEU A 898 ? 1.0807 1.2248 0.9942 -0.0126 -0.0186 0.0030  1001 LEU A CB    
6785 C  CG    . LEU A 898 ? 1.1035 1.2433 1.0196 -0.0219 -0.0148 -0.0004 1001 LEU A CG    
6786 C  CD1   . LEU A 898 ? 0.9646 1.0918 0.8837 -0.0195 -0.0153 0.0002  1001 LEU A CD1   
6787 C  CD2   . LEU A 898 ? 0.9896 1.1495 0.9183 -0.0256 -0.0170 -0.0083 1001 LEU A CD2   
6788 N  N     . PHE A 899 ? 1.0791 1.2322 0.9735 0.0008  -0.0235 0.0115  1002 PHE A N     
6789 C  CA    . PHE A 899 ? 1.1514 1.3141 1.0447 0.0090  -0.0303 0.0125  1002 PHE A CA    
6790 C  C     . PHE A 899 ? 1.0529 1.2267 0.9384 0.0074  -0.0304 0.0095  1002 PHE A C     
6791 O  O     . PHE A 899 ? 1.0206 1.2075 0.9098 0.0113  -0.0372 0.0048  1002 PHE A O     
6792 C  CB    . PHE A 899 ? 1.0980 1.2485 0.9802 0.0166  -0.0299 0.0226  1002 PHE A CB    
6793 C  CG    . PHE A 899 ? 1.1066 1.2527 0.9988 0.0223  -0.0325 0.0249  1002 PHE A CG    
6794 C  CD1   . PHE A 899 ? 1.1323 1.2935 1.0401 0.0265  -0.0405 0.0209  1002 PHE A CD1   
6795 C  CD2   . PHE A 899 ? 1.1598 1.2859 1.0450 0.0234  -0.0263 0.0313  1002 PHE A CD2   
6796 C  CE1   . PHE A 899 ? 1.0900 1.2489 1.0078 0.0318  -0.0420 0.0236  1002 PHE A CE1   
6797 C  CE2   . PHE A 899 ? 1.0613 1.1838 0.9551 0.0298  -0.0277 0.0336  1002 PHE A CE2   
6798 C  CZ    . PHE A 899 ? 1.0843 1.2244 0.9950 0.0340  -0.0353 0.0301  1002 PHE A CZ    
6799 N  N     . SER A 900 ? 0.9870 1.1552 0.8612 0.0013  -0.0225 0.0120  1003 SER A N     
6800 C  CA    . SER A 900 ? 1.0943 1.2726 0.9593 0.0003  -0.0209 0.0101  1003 SER A CA    
6801 C  C     . SER A 900 ? 1.1232 1.3189 1.0009 -0.0011 -0.0243 -0.0007 1003 SER A C     
6802 O  O     . SER A 900 ? 1.2396 1.4455 1.1125 0.0024  -0.0275 -0.0045 1003 SER A O     
6803 C  CB    . SER A 900 ? 1.0554 1.2252 0.9085 -0.0076 -0.0105 0.0150  1003 SER A CB    
6804 O  OG    . SER A 900 ? 1.1155 1.2667 0.9531 -0.0053 -0.0069 0.0254  1003 SER A OG    
6805 N  N     . MET A 901 ? 1.0090 1.2069 0.9014 -0.0056 -0.0236 -0.0056 1004 MET A N     
6806 C  CA    . MET A 901 ? 0.9868 1.1995 0.8911 -0.0060 -0.0262 -0.0152 1004 MET A CA    
6807 C  C     . MET A 901 ? 0.9699 1.1874 0.8820 0.0005  -0.0355 -0.0203 1004 MET A C     
6808 O  O     . MET A 901 ? 0.9629 1.1900 0.8824 0.0014  -0.0379 -0.0283 1004 MET A O     
6809 C  CB    . MET A 901 ? 1.0434 1.2569 0.9601 -0.0122 -0.0229 -0.0180 1004 MET A CB    
6810 C  CG    . MET A 901 ? 1.0717 1.2825 0.9824 -0.0208 -0.0141 -0.0141 1004 MET A CG    
6811 S  SD    . MET A 901 ? 1.2185 1.4285 1.1421 -0.0289 -0.0118 -0.0163 1004 MET A SD    
6812 C  CE    . MET A 901 ? 1.1049 1.3371 1.0434 -0.0270 -0.0141 -0.0260 1004 MET A CE    
6813 N  N     . MET A 902 ? 0.9897 1.2009 0.9006 0.0050  -0.0404 -0.0156 1005 MET A N     
6814 C  CA    . MET A 902 ? 1.0873 1.3041 1.0072 0.0097  -0.0493 -0.0197 1005 MET A CA    
6815 C  C     . MET A 902 ? 1.2023 1.4247 1.1116 0.0143  -0.0551 -0.0199 1005 MET A C     
6816 O  O     . MET A 902 ? 1.2035 1.4315 1.1197 0.0170  -0.0633 -0.0235 1005 MET A O     
6817 C  CB    . MET A 902 ? 1.0915 1.3012 1.0203 0.0117  -0.0515 -0.0147 1005 MET A CB    
6818 C  CG    . MET A 902 ? 1.0241 1.2276 0.9626 0.0077  -0.0470 -0.0152 1005 MET A CG    
6819 S  SD    . MET A 902 ? 1.0855 1.2981 1.0388 0.0055  -0.0494 -0.0256 1005 MET A SD    
6820 C  CE    . MET A 902 ? 1.0292 1.2465 0.9925 0.0101  -0.0587 -0.0279 1005 MET A CE    
6821 N  N     . LEU A 903 ? 1.2685 1.4898 1.1608 0.0147  -0.0511 -0.0161 1006 LEU A N     
6822 C  CA    . LEU A 903 ? 1.3295 1.5558 1.2090 0.0197  -0.0569 -0.0158 1006 LEU A CA    
6823 C  C     . LEU A 903 ? 1.4531 1.6893 1.3338 0.0200  -0.0622 -0.0269 1006 LEU A C     
6824 O  O     . LEU A 903 ? 1.4213 1.6627 1.2985 0.0234  -0.0710 -0.0294 1006 LEU A O     
6825 C  CB    . LEU A 903 ? 1.2952 1.5167 1.1545 0.0201  -0.0501 -0.0087 1006 LEU A CB    
6826 C  CG    . LEU A 903 ? 1.2600 1.4682 1.1137 0.0209  -0.0454 0.0030  1006 LEU A CG    
6827 C  CD1   . LEU A 903 ? 1.4033 1.6048 1.2364 0.0199  -0.0372 0.0098  1006 LEU A CD1   
6828 C  CD2   . LEU A 903 ? 1.3093 1.5175 1.1643 0.0283  -0.0536 0.0080  1006 LEU A CD2   
6829 N  N     . GLY A 904 ? 1.8383 2.0770 1.7234 0.0167  -0.0573 -0.0336 1007 GLY A N     
6830 C  CA    . GLY A 904 ? 1.8517 2.0968 1.7370 0.0179  -0.0612 -0.0445 1007 GLY A CA    
6831 C  C     . GLY A 904 ? 1.8092 2.0548 1.7093 0.0180  -0.0698 -0.0505 1007 GLY A C     
6832 O  O     . GLY A 904 ? 1.8828 2.1308 1.7816 0.0188  -0.0740 -0.0598 1007 GLY A O     
6833 N  N     . SER A 905 ? 1.4512 1.6935 1.3644 0.0170  -0.0718 -0.0454 1008 SER A N     
6834 C  CA    . SER A 905 ? 1.3934 1.6366 1.3217 0.0164  -0.0790 -0.0498 1008 SER A CA    
6835 C  C     . SER A 905 ? 1.4537 1.7020 1.3789 0.0182  -0.0889 -0.0495 1008 SER A C     
6836 O  O     . SER A 905 ? 1.5070 1.7577 1.4192 0.0212  -0.0902 -0.0441 1008 SER A O     
6837 C  CB    . SER A 905 ? 1.3435 1.5822 1.2868 0.0150  -0.0763 -0.0442 1008 SER A CB    
6838 O  OG    . SER A 905 ? 1.3183 1.5532 1.2625 0.0128  -0.0676 -0.0432 1008 SER A OG    
6839 N  N     . GLY A 906 ? 1.3707 1.6212 1.3084 0.0163  -0.0960 -0.0549 1009 GLY A N     
6840 C  CA    . GLY A 906 ? 1.3608 1.6188 1.2985 0.0166  -0.1065 -0.0558 1009 GLY A CA    
6841 C  C     . GLY A 906 ? 1.4000 1.6627 1.3469 0.0188  -0.1089 -0.0455 1009 GLY A C     
6842 O  O     . GLY A 906 ? 1.3793 1.6513 1.3328 0.0185  -0.1180 -0.0455 1009 GLY A O     
6843 N  N     . MET A 907 ? 1.4468 1.7035 1.3944 0.0210  -0.1006 -0.0369 1010 MET A N     
6844 C  CA    . MET A 907 ? 1.3777 1.6361 1.3324 0.0246  -0.1009 -0.0266 1010 MET A CA    
6845 C  C     . MET A 907 ? 1.3843 1.6512 1.3284 0.0296  -0.1074 -0.0215 1010 MET A C     
6846 O  O     . MET A 907 ? 1.4449 1.7080 1.3705 0.0325  -0.1042 -0.0182 1010 MET A O     
6847 C  CB    . MET A 907 ? 1.4797 1.7264 1.4312 0.0259  -0.0902 -0.0193 1010 MET A CB    
6848 C  CG    . MET A 907 ? 1.4873 1.7264 1.4447 0.0212  -0.0835 -0.0244 1010 MET A CG    
6849 S  SD    . MET A 907 ? 1.3471 1.5857 1.3268 0.0192  -0.0843 -0.0259 1010 MET A SD    
6850 C  CE    . MET A 907 ? 1.1804 1.4142 1.1625 0.0242  -0.0805 -0.0137 1010 MET A CE    
6851 N  N     . PRO A 908 ? 1.4283 1.7075 1.3835 0.0308  -0.1165 -0.0202 1011 PRO A N     
6852 C  CA    . PRO A 908 ? 1.3810 1.6708 1.3263 0.0365  -0.1238 -0.0149 1011 PRO A CA    
6853 C  C     . PRO A 908 ? 1.3957 1.6794 1.3315 0.0445  -0.1176 -0.0021 1011 PRO A C     
6854 O  O     . PRO A 908 ? 1.4157 1.7036 1.3363 0.0502  -0.1211 0.0029  1011 PRO A O     
6855 C  CB    . PRO A 908 ? 1.3475 1.6539 1.3124 0.0351  -0.1340 -0.0158 1011 PRO A CB    
6856 C  CG    . PRO A 908 ? 1.3688 1.6714 1.3492 0.0269  -0.1330 -0.0248 1011 PRO A CG    
6857 C  CD    . PRO A 908 ? 1.4202 1.7059 1.3977 0.0268  -0.1206 -0.0234 1011 PRO A CD    
6858 N  N     . GLU A 909 ? 1.3856 1.6581 1.3283 0.0455  -0.1085 0.0034  1012 GLU A N     
6859 C  CA    . GLU A 909 ? 1.4159 1.6777 1.3482 0.0526  -0.1014 0.0151  1012 GLU A CA    
6860 C  C     . GLU A 909 ? 1.3898 1.6334 1.3073 0.0495  -0.0904 0.0154  1012 GLU A C     
6861 O  O     . GLU A 909 ? 1.3800 1.6097 1.2908 0.0528  -0.0824 0.0237  1012 GLU A O     
6862 C  CB    . GLU A 909 ? 1.3874 1.6484 1.3360 0.0565  -0.0987 0.0216  1012 GLU A CB    
6863 C  CG    . GLU A 909 ? 1.4553 1.7089 1.4179 0.0499  -0.0931 0.0162  1012 GLU A CG    
6864 C  CD    . GLU A 909 ? 1.4761 1.7425 1.4554 0.0433  -0.1004 0.0065  1012 GLU A CD    
6865 O  OE1   . GLU A 909 ? 1.4123 1.6945 1.4046 0.0450  -0.1083 0.0075  1012 GLU A OE1   
6866 O  OE2   . GLU A 909 ? 1.5697 1.8304 1.5487 0.0364  -0.0982 -0.0021 1012 GLU A OE2   
6867 N  N     . LEU A 910 ? 1.4030 1.6464 1.3154 0.0430  -0.0896 0.0063  1013 LEU A N     
6868 C  CA    . LEU A 910 ? 1.3621 1.5926 1.2617 0.0393  -0.0796 0.0063  1013 LEU A CA    
6869 C  C     . LEU A 910 ? 1.3920 1.6279 1.2784 0.0370  -0.0814 -0.0005 1013 LEU A C     
6870 O  O     . LEU A 910 ? 1.3438 1.5785 1.2310 0.0315  -0.0773 -0.0080 1013 LEU A O     
6871 C  CB    . LEU A 910 ? 1.3256 1.5491 1.2380 0.0332  -0.0733 0.0020  1013 LEU A CB    
6872 C  CG    . LEU A 910 ? 1.2637 1.4727 1.1769 0.0340  -0.0654 0.0099  1013 LEU A CG    
6873 C  CD1   . LEU A 910 ? 1.2494 1.4536 1.1736 0.0274  -0.0605 0.0043  1013 LEU A CD1   
6874 C  CD2   . LEU A 910 ? 1.2361 1.4327 1.1290 0.0351  -0.0581 0.0175  1013 LEU A CD2   
6875 N  N     . GLN A 911 ? 1.4547 1.6974 1.3281 0.0421  -0.0876 0.0021  1014 GLN A N     
6876 C  CA    . GLN A 911 ? 1.4475 1.6945 1.3048 0.0412  -0.0892 -0.0038 1014 GLN A CA    
6877 C  C     . GLN A 911 ? 1.3852 1.6231 1.2200 0.0434  -0.0808 0.0039  1014 GLN A C     
6878 O  O     . GLN A 911 ? 1.3191 1.5552 1.1440 0.0398  -0.0749 -0.0006 1014 GLN A O     
6879 C  CB    . GLN A 911 ? 1.4395 1.7004 1.2944 0.0446  -0.1024 -0.0072 1014 GLN A CB    
6880 C  CG    . GLN A 911 ? 1.4954 1.7657 1.3712 0.0404  -0.1109 -0.0164 1014 GLN A CG    
6881 C  CD    . GLN A 911 ? 1.6380 1.9051 1.5171 0.0339  -0.1082 -0.0285 1014 GLN A CD    
6882 O  OE1   . GLN A 911 ? 1.4962 1.7564 1.3866 0.0305  -0.1009 -0.0297 1014 GLN A OE1   
6883 N  NE2   . GLN A 911 ? 1.6364 1.9083 1.5047 0.0330  -0.1141 -0.0376 1014 GLN A NE2   
6884 N  N     . SER A 912 ? 1.4642 1.6958 1.2906 0.0495  -0.0795 0.0158  1015 SER A N     
6885 C  CA    . SER A 912 ? 1.5969 1.8176 1.4006 0.0518  -0.0714 0.0247  1015 SER A CA    
6886 C  C     . SER A 912 ? 1.6648 1.8678 1.4699 0.0496  -0.0603 0.0328  1015 SER A C     
6887 O  O     . SER A 912 ? 1.5944 1.7941 1.4163 0.0487  -0.0602 0.0330  1015 SER A O     
6888 C  CB    . SER A 912 ? 1.6764 1.9013 1.4647 0.0616  -0.0784 0.0329  1015 SER A CB    
6889 O  OG    . SER A 912 ? 1.6376 1.8620 1.4363 0.0680  -0.0821 0.0405  1015 SER A OG    
6890 N  N     . PHE A 913 ? 1.8480 2.0387 1.6340 0.0483  -0.0506 0.0394  1016 PHE A N     
6891 C  CA    . PHE A 913 ? 1.7480 1.9189 1.5310 0.0456  -0.0400 0.0477  1016 PHE A CA    
6892 C  C     . PHE A 913 ? 1.7071 1.8676 1.4848 0.0553  -0.0416 0.0592  1016 PHE A C     
6893 O  O     . PHE A 913 ? 1.7719 1.9130 1.5464 0.0541  -0.0333 0.0661  1016 PHE A O     
6894 C  CB    . PHE A 913 ? 1.7870 1.9478 1.5510 0.0402  -0.0288 0.0518  1016 PHE A CB    
6895 C  CG    . PHE A 913 ? 1.9079 2.0757 1.6803 0.0297  -0.0235 0.0423  1016 PHE A CG    
6896 C  CD1   . PHE A 913 ? 1.9629 2.1464 1.7325 0.0294  -0.0264 0.0342  1016 PHE A CD1   
6897 C  CD2   . PHE A 913 ? 1.8724 2.0316 1.6550 0.0206  -0.0157 0.0413  1016 PHE A CD2   
6898 C  CE1   . PHE A 913 ? 1.9344 2.1255 1.7121 0.0213  -0.0210 0.0259  1016 PHE A CE1   
6899 C  CE2   . PHE A 913 ? 1.7358 1.9043 1.5274 0.0118  -0.0113 0.0331  1016 PHE A CE2   
6900 C  CZ    . PHE A 913 ? 1.8105 1.9953 1.6001 0.0127  -0.0136 0.0257  1016 PHE A CZ    
6901 N  N     . ASP A 914 ? 1.6341 1.8070 1.4105 0.0651  -0.0521 0.0614  1017 ASP A N     
6902 C  CA    . ASP A 914 ? 1.6247 1.7910 1.3981 0.0761  -0.0542 0.0726  1017 ASP A CA    
6903 C  C     . ASP A 914 ? 1.6160 1.7842 1.4127 0.0770  -0.0566 0.0706  1017 ASP A C     
6904 O  O     . ASP A 914 ? 1.5881 1.7426 1.3829 0.0837  -0.0526 0.0798  1017 ASP A O     
6905 C  CB    . ASP A 914 ? 1.6979 1.8804 1.4630 0.0864  -0.0655 0.0758  1017 ASP A CB    
6906 C  CG    . ASP A 914 ? 1.6533 1.8356 1.3943 0.0860  -0.0638 0.0768  1017 ASP A CG    
6907 O  OD1   . ASP A 914 ? 1.6444 1.8085 1.3699 0.0817  -0.0518 0.0814  1017 ASP A OD1   
6908 O  OD2   . ASP A 914 ? 1.5292 1.7296 1.2663 0.0896  -0.0743 0.0727  1017 ASP A OD2   
6909 N  N     . ASP A 915 ? 1.7533 1.9370 1.5707 0.0708  -0.0624 0.0591  1018 ASP A N     
6910 C  CA    . ASP A 915 ? 1.5991 1.7844 1.4383 0.0707  -0.0636 0.0572  1018 ASP A CA    
6911 C  C     . ASP A 915 ? 1.5246 1.6884 1.3636 0.0649  -0.0520 0.0584  1018 ASP A C     
6912 O  O     . ASP A 915 ? 1.6224 1.7769 1.4677 0.0692  -0.0492 0.0632  1018 ASP A O     
6913 C  CB    . ASP A 915 ? 1.5696 1.7742 1.4288 0.0647  -0.0717 0.0448  1018 ASP A CB    
6914 C  CG    . ASP A 915 ? 1.7367 1.9620 1.5958 0.0686  -0.0840 0.0420  1018 ASP A CG    
6915 O  OD1   . ASP A 915 ? 1.9099 2.1405 1.7637 0.0784  -0.0889 0.0505  1018 ASP A OD1   
6916 O  OD2   . ASP A 915 ? 1.7128 1.9488 1.5765 0.0622  -0.0889 0.0312  1018 ASP A OD2   
6917 N  N     . ILE A 916 ? 1.4330 1.5894 1.2647 0.0551  -0.0451 0.0540  1019 ILE A N     
6918 C  CA    . ILE A 916 ? 1.3909 1.5280 1.2217 0.0479  -0.0348 0.0547  1019 ILE A CA    
6919 C  C     . ILE A 916 ? 1.3916 1.5048 1.2040 0.0532  -0.0272 0.0668  1019 ILE A C     
6920 O  O     . ILE A 916 ? 1.3452 1.4398 1.1575 0.0504  -0.0202 0.0688  1019 ILE A O     
6921 C  CB    . ILE A 916 ? 1.3709 1.5095 1.1989 0.0362  -0.0297 0.0476  1019 ILE A CB    
6922 C  CG1   . ILE A 916 ? 1.3247 1.4853 1.1685 0.0330  -0.0372 0.0360  1019 ILE A CG1   
6923 C  CG2   . ILE A 916 ? 1.2733 1.3958 1.1033 0.0271  -0.0207 0.0468  1019 ILE A CG2   
6924 C  CD1   . ILE A 916 ? 1.2670 1.4315 1.1107 0.0232  -0.0321 0.0288  1019 ILE A CD1   
6925 N  N     . ALA A 917 ? 1.4127 1.5246 1.2082 0.0614  -0.0285 0.0751  1020 ALA A N     
6926 C  CA    . ALA A 917 ? 1.3710 1.4584 1.1471 0.0680  -0.0211 0.0876  1020 ALA A CA    
6927 C  C     . ALA A 917 ? 1.3058 1.3863 1.0889 0.0787  -0.0223 0.0932  1020 ALA A C     
6928 O  O     . ALA A 917 ? 1.3145 1.3708 1.0819 0.0848  -0.0151 0.1032  1020 ALA A O     
6929 C  CB    . ALA A 917 ? 1.3917 1.4812 1.1476 0.0758  -0.0231 0.0957  1020 ALA A CB    
6930 N  N     . TYR A 918 ? 1.3100 1.4104 1.1156 0.0813  -0.0305 0.0874  1021 TYR A N     
6931 C  CA    . TYR A 918 ? 1.2961 1.3928 1.1099 0.0920  -0.0309 0.0929  1021 TYR A CA    
6932 C  C     . TYR A 918 ? 1.2969 1.3669 1.1077 0.0876  -0.0204 0.0932  1021 TYR A C     
6933 O  O     . TYR A 918 ? 1.3107 1.3606 1.1112 0.0970  -0.0148 0.1021  1021 TYR A O     
6934 C  CB    . TYR A 918 ? 1.3271 1.4522 1.1670 0.0936  -0.0412 0.0861  1021 TYR A CB    
6935 C  CG    . TYR A 918 ? 1.3600 1.4873 1.2098 0.1063  -0.0424 0.0928  1021 TYR A CG    
6936 C  CD1   . TYR A 918 ? 1.3173 1.4544 1.1633 0.1206  -0.0476 0.1024  1021 TYR A CD1   
6937 C  CD2   . TYR A 918 ? 1.3611 1.4822 1.2241 0.1046  -0.0382 0.0898  1021 TYR A CD2   
6938 C  CE1   . TYR A 918 ? 1.3624 1.5043 1.2189 0.1331  -0.0482 0.1090  1021 TYR A CE1   
6939 C  CE2   . TYR A 918 ? 1.3062 1.4303 1.1784 0.1169  -0.0382 0.0962  1021 TYR A CE2   
6940 C  CZ    . TYR A 918 ? 1.3584 1.4936 1.2281 0.1313  -0.0430 0.1059  1021 TYR A CZ    
6941 O  OH    . TYR A 918 ? 1.3271 1.4678 1.2073 0.1444  -0.0425 0.1127  1021 TYR A OH    
6942 N  N     . ILE A 919 ? 1.2499 1.3189 1.0687 0.0737  -0.0178 0.0833  1022 ILE A N     
6943 C  CA    . ILE A 919 ? 1.2095 1.2538 1.0243 0.0680  -0.0087 0.0825  1022 ILE A CA    
6944 C  C     . ILE A 919 ? 1.2006 1.2147 0.9897 0.0658  0.0012  0.0900  1022 ILE A C     
6945 O  O     . ILE A 919 ? 1.1716 1.1592 0.9517 0.0653  0.0089  0.0926  1022 ILE A O     
6946 C  CB    . ILE A 919 ? 1.2085 1.2608 1.0371 0.0535  -0.0090 0.0704  1022 ILE A CB    
6947 C  CG1   . ILE A 919 ? 1.1710 1.2295 0.9936 0.0425  -0.0081 0.0663  1022 ILE A CG1   
6948 C  CG2   . ILE A 919 ? 1.1643 1.2419 1.0170 0.0558  -0.0177 0.0637  1022 ILE A CG2   
6949 N  N     . ARG A 920 ? 1.2616 1.2777 1.0374 0.0643  0.0015  0.0935  1023 ARG A N     
6950 C  CA    . ARG A 920 ? 1.2271 1.2134 0.9772 0.0629  0.0113  0.1023  1023 ARG A CA    
6951 C  C     . ARG A 920 ? 1.1916 1.1590 0.9283 0.0795  0.0138  0.1144  1023 ARG A C     
6952 O  O     . ARG A 920 ? 1.1847 1.1189 0.9015 0.0791  0.0237  0.1211  1023 ARG A O     
6953 C  CB    . ARG A 920 ? 1.2317 1.2265 0.9705 0.0586  0.0113  0.1041  1023 ARG A CB    
6954 C  CG    . ARG A 920 ? 1.4121 1.3769 1.1257 0.0524  0.0229  0.1116  1023 ARG A CG    
6955 C  CD    . ARG A 920 ? 1.3638 1.3397 1.0673 0.0478  0.0234  0.1130  1023 ARG A CD    
6956 N  NE    . ARG A 920 ? 1.2802 1.2278 0.9602 0.0406  0.0354  0.1208  1023 ARG A NE    
6957 N  N     . LYS A 921 ? 1.1322 1.1202 0.8796 0.0939  0.0052  0.1174  1024 LYS A N     
6958 C  CA    . LYS A 921 ? 1.2237 1.1979 0.9616 0.1117  0.0070  0.1290  1024 LYS A CA    
6959 C  C     . LYS A 921 ? 1.2991 1.2588 1.0444 0.1146  0.0116  0.1274  1024 LYS A C     
6960 O  O     . LYS A 921 ? 1.3022 1.2297 1.0297 0.1211  0.0205  0.1349  1024 LYS A O     
6961 C  CB    . LYS A 921 ? 1.2805 1.2859 1.0291 0.1256  -0.0045 0.1327  1024 LYS A CB    
6962 C  CG    . LYS A 921 ? 1.5150 1.5388 1.2576 0.1230  -0.0108 0.1324  1024 LYS A CG    
6963 C  CD    . LYS A 921 ? 1.5540 1.6092 1.3078 0.1362  -0.0234 0.1353  1024 LYS A CD    
6964 C  CE    . LYS A 921 ? 1.4804 1.5537 1.2266 0.1334  -0.0304 0.1338  1024 LYS A CE    
6965 N  NZ    . LYS A 921 ? 1.4076 1.4948 1.1656 0.1167  -0.0328 0.1198  1024 LYS A NZ    
6966 N  N     . THR A 922 ? 1.2516 1.2332 1.0215 0.1104  0.0059  0.1178  1025 THR A N     
6967 C  CA    . THR A 922 ? 1.2368 1.2075 1.0142 0.1142  0.0099  0.1162  1025 THR A CA    
6968 C  C     . THR A 922 ? 1.2412 1.1773 1.0036 0.1028  0.0204  0.1129  1025 THR A C     
6969 O  O     . THR A 922 ? 1.2872 1.2010 1.0437 0.1086  0.0268  0.1149  1025 THR A O     
6970 C  CB    . THR A 922 ? 1.2069 1.2086 1.0131 0.1105  0.0018  0.1066  1025 THR A CB    
6971 O  OG1   . THR A 922 ? 1.1943 1.2056 1.0071 0.0933  -0.0005 0.0959  1025 THR A OG1   
6972 C  CG2   . THR A 922 ? 1.2304 1.2652 1.0520 0.1217  -0.0087 0.1099  1025 THR A CG2   
6973 N  N     . LEU A 923 ? 1.1935 1.1249 0.9492 0.0864  0.0224  0.1078  1026 LEU A N     
6974 C  CA    . LEU A 923 ? 1.2113 1.1113 0.9526 0.0735  0.0318  0.1047  1026 LEU A CA    
6975 C  C     . LEU A 923 ? 1.2999 1.1653 1.0121 0.0752  0.0410  0.1147  1026 LEU A C     
6976 O  O     . LEU A 923 ? 1.2799 1.1136 0.9771 0.0656  0.0496  0.1134  1026 LEU A O     
6977 C  CB    . LEU A 923 ? 1.2050 1.1196 0.9562 0.0541  0.0297  0.0939  1026 LEU A CB    
6978 C  CG    . LEU A 923 ? 1.1680 1.1085 0.9447 0.0496  0.0228  0.0830  1026 LEU A CG    
6979 C  CD1   . LEU A 923 ? 1.0748 1.0323 0.8604 0.0332  0.0205  0.0739  1026 LEU A CD1   
6980 C  CD2   . LEU A 923 ? 1.0257 0.9469 0.8019 0.0495  0.0272  0.0799  1026 LEU A CD2   
6981 N  N     . ALA A 924 ? 1.2837 1.1534 0.9867 0.0867  0.0393  0.1246  1027 ALA A N     
6982 C  CA    . ALA A 924 ? 1.2526 1.0891 0.9265 0.0905  0.0481  0.1359  1027 ALA A CA    
6983 C  C     . ALA A 924 ? 1.3024 1.1204 0.9635 0.0699  0.0555  0.1325  1027 ALA A C     
6984 O  O     . ALA A 924 ? 1.3772 1.1567 1.0175 0.0648  0.0656  0.1359  1027 ALA A O     
6985 C  CB    . ALA A 924 ? 1.3152 1.1181 0.9743 0.1041  0.0554  0.1432  1027 ALA A CB    
6986 N  N     . LEU A 925 ? 1.1848 1.0310 0.8586 0.0577  0.0505  0.1256  1028 LEU A N     
6987 C  CA    . LEU A 925 ? 1.3082 1.1449 0.9757 0.0370  0.0568  0.1211  1028 LEU A CA    
6988 C  C     . LEU A 925 ? 1.4276 1.2353 1.0669 0.0352  0.0664  0.1321  1028 LEU A C     
6989 O  O     . LEU A 925 ? 1.4109 1.1987 1.0403 0.0182  0.0746  0.1304  1028 LEU A O     
6990 C  CB    . LEU A 925 ? 1.2931 1.1687 0.9807 0.0275  0.0496  0.1121  1028 LEU A CB    
6991 C  CG    . LEU A 925 ? 1.2642 1.1667 0.9791 0.0266  0.0409  0.1006  1028 LEU A CG    
6992 C  CD1   . LEU A 925 ? 1.2231 1.1588 0.9546 0.0164  0.0354  0.0918  1028 LEU A CD1   
6993 C  CD2   . LEU A 925 ? 1.2928 1.1750 1.0088 0.0180  0.0454  0.0948  1028 LEU A CD2   
6994 N  N     . ASP A 926 ? 1.5284 1.3336 1.1546 0.0519  0.0655  0.1437  1029 ASP A N     
6995 C  CA    . ASP A 926 ? 1.5405 1.3174 1.1382 0.0516  0.0749  0.1555  1029 ASP A CA    
6996 C  C     . ASP A 926 ? 1.6126 1.3412 1.1869 0.0561  0.0853  0.1633  1029 ASP A C     
6997 O  O     . ASP A 926 ? 1.6706 1.3688 1.2190 0.0537  0.0948  0.1731  1029 ASP A O     
6998 C  CB    . ASP A 926 ? 1.5833 1.3770 1.1743 0.0685  0.0694  0.1652  1029 ASP A CB    
6999 C  CG    . ASP A 926 ? 1.7288 1.5665 1.3387 0.0641  0.0597  0.1575  1029 ASP A CG    
7000 O  OD1   . ASP A 926 ? 1.6373 1.4927 1.2666 0.0493  0.0575  0.1450  1029 ASP A OD1   
7001 O  OD2   . ASP A 926 ? 1.8857 1.7396 1.4902 0.0759  0.0543  0.1637  1029 ASP A OD2   
7002 N  N     . LYS A 927 ? 1.6283 1.3475 1.2095 0.0625  0.0843  0.1593  1030 LYS A N     
7003 C  CA    . LYS A 927 ? 1.6047 1.2768 1.1630 0.0684  0.0941  0.1657  1030 LYS A CA    
7004 C  C     . LYS A 927 ? 1.5802 1.2312 1.1389 0.0488  0.0995  0.1550  1030 LYS A C     
7005 O  O     . LYS A 927 ? 1.5592 1.2366 1.1399 0.0345  0.0940  0.1427  1030 LYS A O     
7006 C  CB    . LYS A 927 ? 1.5544 1.2285 1.1168 0.0930  0.0901  0.1705  1030 LYS A CB    
7007 C  CG    . LYS A 927 ? 1.7492 1.4517 1.3160 0.1125  0.0821  0.1796  1030 LYS A CG    
7008 C  CD    . LYS A 927 ? 1.7508 1.4431 1.3125 0.1379  0.0822  0.1888  1030 LYS A CD    
7009 C  CE    . LYS A 927 ? 1.8166 1.5167 1.3979 0.1405  0.0796  0.1797  1030 LYS A CE    
7010 N  NZ    . LYS A 927 ? 1.9236 1.6114 1.4987 0.1656  0.0818  0.1891  1030 LYS A NZ    
7011 N  N     . THR A 928 ? 1.6183 1.2203 1.1512 0.0487  0.1102  0.1600  1031 THR A N     
7012 C  CA    . THR A 928 ? 1.6278 1.2052 1.1573 0.0308  0.1153  0.1500  1031 THR A CA    
7013 C  C     . THR A 928 ? 1.5966 1.1866 1.1439 0.0384  0.1093  0.1409  1031 THR A C     
7014 O  O     . THR A 928 ? 1.5554 1.1674 1.1151 0.0585  0.1029  0.1439  1031 THR A O     
7015 C  CB    . THR A 928 ? 1.6634 1.1814 1.1579 0.0293  0.1286  0.1576  1031 THR A CB    
7016 O  OG1   . THR A 928 ? 1.6879 1.1846 1.1691 0.0552  0.1310  0.1666  1031 THR A OG1   
7017 C  CG2   . THR A 928 ? 1.7160 1.2205 1.1920 0.0213  0.1355  0.1676  1031 THR A CG2   
7018 N  N     . GLU A 929 ? 1.6564 1.2327 1.2046 0.0216  0.1114  0.1297  1032 GLU A N     
7019 C  CA    . GLU A 929 ? 1.5735 1.1606 1.1370 0.0271  0.1063  0.1206  1032 GLU A CA    
7020 C  C     . GLU A 929 ? 1.5484 1.1064 1.0962 0.0500  0.1113  0.1277  1032 GLU A C     
7021 O  O     . GLU A 929 ? 1.4917 1.0710 1.0558 0.0652  0.1059  0.1261  1032 GLU A O     
7022 C  CB    . GLU A 929 ? 1.5879 1.1634 1.1518 0.0039  0.1077  0.1076  1032 GLU A CB    
7023 C  CG    . GLU A 929 ? 1.6450 1.2441 1.2302 0.0053  0.1003  0.0965  1032 GLU A CG    
7024 C  CD    . GLU A 929 ? 1.6367 1.2302 1.2235 -0.0185 0.1000  0.0836  1032 GLU A CD    
7025 O  OE1   . GLU A 929 ? 1.6264 1.1856 1.1923 -0.0341 0.1074  0.0833  1032 GLU A OE1   
7026 O  OE2   . GLU A 929 ? 1.6747 1.2985 1.2837 -0.0220 0.0922  0.0740  1032 GLU A OE2   
7027 N  N     . GLN A 930 ? 1.6467 1.1557 1.1628 0.0530  0.1222  0.1360  1033 GLN A N     
7028 C  CA    . GLN A 930 ? 1.6285 1.1083 1.1276 0.0773  0.1280  0.1444  1033 GLN A CA    
7029 C  C     . GLN A 930 ? 1.6319 1.1426 1.1430 0.1021  0.1222  0.1553  1033 GLN A C     
7030 O  O     . GLN A 930 ? 1.6075 1.1266 1.1264 0.1223  0.1205  0.1574  1033 GLN A O     
7031 C  CB    . GLN A 930 ? 1.7145 1.1341 1.1754 0.0751  0.1411  0.1520  1033 GLN A CB    
7032 C  CG    . GLN A 930 ? 1.7780 1.1667 1.2179 0.1034  0.1481  0.1644  1033 GLN A CG    
7033 C  CD    . GLN A 930 ? 1.6929 1.0533 1.1236 0.1111  0.1530  0.1583  1033 GLN A CD    
7034 O  OE1   . GLN A 930 ? 1.7338 1.1227 1.1850 0.1244  0.1473  0.1548  1033 GLN A OE1   
7035 N  NE2   . GLN A 930 ? 1.5859 0.8888 0.9846 0.1026  0.1641  0.1570  1033 GLN A NE2   
7036 N  N     . GLU A 931 ? 1.6063 1.1355 1.1192 0.1006  0.1192  0.1624  1034 GLU A N     
7037 C  CA    . GLU A 931 ? 1.6055 1.1646 1.1283 0.1231  0.1128  0.1727  1034 GLU A CA    
7038 C  C     . GLU A 931 ? 1.5371 1.1515 1.0964 0.1251  0.0999  0.1646  1034 GLU A C     
7039 O  O     . GLU A 931 ? 1.5342 1.1711 1.1057 0.1459  0.0946  0.1700  1034 GLU A O     
7040 C  CB    . GLU A 931 ? 1.6916 1.2524 1.2026 0.1203  0.1135  0.1822  1034 GLU A CB    
7041 C  CG    . GLU A 931 ? 1.7175 1.2227 1.1910 0.1210  0.1267  0.1928  1034 GLU A CG    
7042 C  CD    . GLU A 931 ? 1.7689 1.2747 1.2310 0.1112  0.1286  0.1997  1034 GLU A CD    
7043 O  OE1   . GLU A 931 ? 1.7435 1.2900 1.2265 0.0991  0.1206  0.1936  1034 GLU A OE1   
7044 O  OE2   . GLU A 931 ? 1.8781 1.3428 1.3095 0.1161  0.1387  0.2116  1034 GLU A OE2   
7045 N  N     . ALA A 932 ? 1.5057 1.1429 1.0830 0.1038  0.0948  0.1520  1035 ALA A N     
7046 C  CA    . ALA A 932 ? 1.4596 1.1461 1.0702 0.1046  0.0831  0.1440  1035 ALA A CA    
7047 C  C     . ALA A 932 ? 1.4935 1.1807 1.1142 0.1158  0.0827  0.1401  1035 ALA A C     
7048 O  O     . ALA A 932 ? 1.4852 1.2102 1.1312 0.1245  0.0741  0.1381  1035 ALA A O     
7049 C  CB    . ALA A 932 ? 1.4355 1.1422 1.0607 0.0801  0.0789  0.1317  1035 ALA A CB    
7050 N  N     . LEU A 933 ? 1.5222 1.1674 1.1231 0.1154  0.0923  0.1390  1036 LEU A N     
7051 C  CA    . LEU A 933 ? 1.4588 1.1012 1.0658 0.1280  0.0935  0.1363  1036 LEU A CA    
7052 C  C     . LEU A 933 ? 1.4824 1.1244 1.0858 0.1562  0.0953  0.1492  1036 LEU A C     
7053 O  O     . LEU A 933 ? 1.4663 1.1371 1.0908 0.1696  0.0904  0.1492  1036 LEU A O     
7054 C  CB    . LEU A 933 ? 1.4949 1.0910 1.0794 0.1183  0.1032  0.1300  1036 LEU A CB    
7055 C  CG    . LEU A 933 ? 1.4651 1.0598 1.0562 0.1268  0.1044  0.1241  1036 LEU A CG    
7056 C  CD1   . LEU A 933 ? 1.4097 1.0512 1.0337 0.1183  0.0939  0.1140  1036 LEU A CD1   
7057 C  CD2   . LEU A 933 ? 1.6903 1.2355 1.2548 0.1168  0.1138  0.1176  1036 LEU A CD2   
7058 N  N     . GLU A 934 ? 1.5173 1.1276 1.0945 0.1655  0.1024  0.1609  1037 GLU A N     
7059 C  CA    . GLU A 934 ? 1.5415 1.1532 1.1147 0.1935  0.1036  0.1745  1037 GLU A CA    
7060 C  C     . GLU A 934 ? 1.5315 1.1984 1.1329 0.2020  0.0910  0.1780  1037 GLU A C     
7061 O  O     . GLU A 934 ? 1.5322 1.2183 1.1447 0.2237  0.0884  0.1851  1037 GLU A O     
7062 C  CB    . GLU A 934 ? 1.5554 1.1232 1.0942 0.2004  0.1131  0.1867  1037 GLU A CB    
7063 C  CG    . GLU A 934 ? 1.6099 1.1182 1.1176 0.1920  0.1261  0.1837  1037 GLU A CG    
7064 C  CD    . GLU A 934 ? 1.8119 1.2758 1.2851 0.1956  0.1355  0.1956  1037 GLU A CD    
7065 O  OE1   . GLU A 934 ? 1.9170 1.3984 1.3908 0.1989  0.1313  0.2045  1037 GLU A OE1   
7066 O  OE2   . GLU A 934 ? 1.8465 1.2566 1.2907 0.1950  0.1472  0.1961  1037 GLU A OE2   
7067 N  N     . TYR A 935 ? 1.4692 1.1624 1.0822 0.1851  0.0831  0.1730  1038 TYR A N     
7068 C  CA    . TYR A 935 ? 1.4636 1.2086 1.1029 0.1903  0.0704  0.1740  1038 TYR A CA    
7069 C  C     . TYR A 935 ? 1.4489 1.2279 1.1188 0.1929  0.0639  0.1662  1038 TYR A C     
7070 O  O     . TYR A 935 ? 1.4733 1.2799 1.1591 0.2105  0.0585  0.1720  1038 TYR A O     
7071 C  CB    . TYR A 935 ? 1.4581 1.2199 1.1013 0.1704  0.0647  0.1685  1038 TYR A CB    
7072 C  CG    . TYR A 935 ? 1.4352 1.2501 1.1078 0.1697  0.0510  0.1643  1038 TYR A CG    
7073 C  CD1   . TYR A 935 ? 1.4088 1.2482 1.0854 0.1854  0.0438  0.1736  1038 TYR A CD1   
7074 C  CD2   . TYR A 935 ? 1.4481 1.2877 1.1434 0.1532  0.0452  0.1507  1038 TYR A CD2   
7075 C  CE1   . TYR A 935 ? 1.4103 1.2963 1.1124 0.1834  0.0310  0.1689  1038 TYR A CE1   
7076 C  CE2   . TYR A 935 ? 1.4129 1.2973 1.1333 0.1522  0.0332  0.1465  1038 TYR A CE2   
7077 C  CZ    . TYR A 935 ? 1.4101 1.3170 1.1336 0.1667  0.0261  0.1551  1038 TYR A CZ    
7078 O  OH    . TYR A 935 ? 1.4183 1.3680 1.1655 0.1644  0.0138  0.1500  1038 TYR A OH    
7079 N  N     . PHE A 936 ? 1.4534 1.2312 1.1319 0.1752  0.0643  0.1533  1039 PHE A N     
7080 C  CA    . PHE A 936 ? 1.4336 1.2409 1.1395 0.1764  0.0591  0.1459  1039 PHE A CA    
7081 C  C     . PHE A 936 ? 1.4143 1.2118 1.1187 0.1979  0.0650  0.1524  1039 PHE A C     
7082 O  O     . PHE A 936 ? 1.3673 1.1982 1.0963 0.2075  0.0596  0.1527  1039 PHE A O     
7083 C  CB    . PHE A 936 ? 1.3824 1.1830 1.0921 0.1551  0.0602  0.1320  1039 PHE A CB    
7084 C  CG    . PHE A 936 ? 1.3357 1.1602 1.0694 0.1563  0.0566  0.1249  1039 PHE A CG    
7085 C  CD1   . PHE A 936 ? 1.3144 1.1833 1.0770 0.1521  0.0457  0.1203  1039 PHE A CD1   
7086 C  CD2   . PHE A 936 ? 1.3197 1.1205 1.0457 0.1616  0.0645  0.1228  1039 PHE A CD2   
7087 C  CE1   . PHE A 936 ? 1.2613 1.1506 1.0453 0.1528  0.0432  0.1144  1039 PHE A CE1   
7088 C  CE2   . PHE A 936 ? 1.2619 1.0844 1.0090 0.1629  0.0620  0.1169  1039 PHE A CE2   
7089 C  CZ    . PHE A 936 ? 1.2615 1.1283 1.0379 0.1583  0.0514  0.1131  1039 PHE A CZ    
7090 N  N     . MET A 937 ? 1.4266 1.1780 1.1022 0.2055  0.0766  0.1578  1040 MET A N     
7091 C  CA    . MET A 937 ? 1.5168 1.2559 1.1882 0.2279  0.0836  0.1646  1040 MET A CA    
7092 C  C     . MET A 937 ? 1.6044 1.3702 1.2859 0.2511  0.0792  0.1777  1040 MET A C     
7093 O  O     . MET A 937 ? 1.6395 1.4140 1.3299 0.2701  0.0819  0.1827  1040 MET A O     
7094 C  CB    . MET A 937 ? 1.5927 1.2722 1.2275 0.2309  0.0973  0.1673  1040 MET A CB    
7095 C  CG    . MET A 937 ? 1.6086 1.2606 1.2332 0.2105  0.1022  0.1541  1040 MET A CG    
7096 S  SD    . MET A 937 ? 1.7019 1.2814 1.2822 0.2143  0.1183  0.1566  1040 MET A SD    
7097 C  CE    . MET A 937 ? 1.9036 1.4808 1.4843 0.2475  0.1250  0.1658  1040 MET A CE    
7098 N  N     . LYS A 938 ? 1.7764 1.5568 1.4568 0.2503  0.0724  0.1836  1041 LYS A N     
7099 C  CA    . LYS A 938 ? 1.7235 1.5292 1.4115 0.2725  0.0674  0.1964  1041 LYS A CA    
7100 C  C     . LYS A 938 ? 1.6913 1.5552 1.4173 0.2728  0.0544  0.1930  1041 LYS A C     
7101 O  O     . LYS A 938 ? 1.7378 1.6254 1.4792 0.2921  0.0526  0.2002  1041 LYS A O     
7102 C  CB    . LYS A 938 ? 1.7706 1.5664 1.4388 0.2727  0.0656  0.2048  1041 LYS A CB    
7103 C  CG    . LYS A 938 ? 1.8237 1.6415 1.4950 0.2973  0.0606  0.2193  1041 LYS A CG    
7104 C  CD    . LYS A 938 ? 1.7906 1.5916 1.4367 0.2991  0.0607  0.2287  1041 LYS A CD    
7105 C  CE    . LYS A 938 ? 1.9294 1.7520 1.5772 0.3254  0.0555  0.2438  1041 LYS A CE    
7106 N  NZ    . LYS A 938 ? 2.3467 2.1523 1.9678 0.3285  0.0557  0.2540  1041 LYS A NZ    
7107 N  N     . GLN A 939 ? 1.5727 1.4605 1.3145 0.2517  0.0456  0.1822  1042 GLN A N     
7108 C  CA    . GLN A 939 ? 1.5637 1.5036 1.3402 0.2503  0.0334  0.1781  1042 GLN A CA    
7109 C  C     . GLN A 939 ? 1.5014 1.4525 1.2977 0.2544  0.0364  0.1740  1042 GLN A C     
7110 O  O     . GLN A 939 ? 1.4723 1.4630 1.2954 0.2626  0.0294  0.1762  1042 GLN A O     
7111 C  CB    . GLN A 939 ? 1.5245 1.4826 1.3109 0.2271  0.0247  0.1668  1042 GLN A CB    
7112 C  CG    . GLN A 939 ? 1.5155 1.4841 1.2936 0.2260  0.0174  0.1715  1042 GLN A CG    
7113 C  CD    . GLN A 939 ? 1.6007 1.5261 1.3447 0.2227  0.0264  0.1759  1042 GLN A CD    
7114 O  OE1   . GLN A 939 ? 1.7065 1.6031 1.4386 0.2079  0.0337  0.1687  1042 GLN A OE1   
7115 N  NE2   . GLN A 939 ? 1.5709 1.4916 1.2988 0.2362  0.0258  0.1880  1042 GLN A NE2   
7116 N  N     . MET A 940 ? 1.5584 1.4755 1.3417 0.2482  0.0466  0.1680  1043 MET A N     
7117 C  CA    . MET A 940 ? 1.5404 1.4637 1.3381 0.2545  0.0512  0.1653  1043 MET A CA    
7118 C  C     . MET A 940 ? 1.5337 1.4558 1.3294 0.2816  0.0572  0.1781  1043 MET A C     
7119 O  O     . MET A 940 ? 1.5329 1.4859 1.3532 0.2916  0.0556  0.1801  1043 MET A O     
7120 C  CB    . MET A 940 ? 1.5044 1.3892 1.2847 0.2421  0.0606  0.1559  1043 MET A CB    
7121 C  CG    . MET A 940 ? 1.3993 1.2899 1.1857 0.2162  0.0547  0.1428  1043 MET A CG    
7122 S  SD    . MET A 940 ? 1.3626 1.3072 1.1894 0.2080  0.0431  0.1354  1043 MET A SD    
7123 C  CE    . MET A 940 ? 1.4649 1.4372 1.2996 0.1992  0.0303  0.1358  1043 MET A CE    
7124 N  N     . ASN A 941 ? 1.5996 1.4866 1.3664 0.2941  0.0646  0.1873  1044 ASN A N     
7125 C  CA    . ASN A 941 ? 1.6536 1.5387 1.4169 0.3221  0.0706  0.2006  1044 ASN A CA    
7126 C  C     . ASN A 941 ? 1.6633 1.5992 1.4519 0.3342  0.0589  0.2093  1044 ASN A C     
7127 O  O     . ASN A 941 ? 1.6950 1.6551 1.5009 0.3532  0.0598  0.2166  1044 ASN A O     
7128 C  CB    . ASN A 941 ? 1.7183 1.5509 1.4425 0.3319  0.0811  0.2086  1044 ASN A CB    
7129 C  CG    . ASN A 941 ? 1.8085 1.6315 1.5250 0.3623  0.0897  0.2219  1044 ASN A CG    
7130 O  OD1   . ASN A 941 ? 1.8507 1.6483 1.5580 0.3708  0.1011  0.2207  1044 ASN A OD1   
7131 N  ND2   . ASN A 941 ? 1.8072 1.6506 1.5267 0.3796  0.0842  0.2348  1044 ASN A ND2   
7132 N  N     . ASP A 942 ? 1.6632 1.6171 1.4546 0.3231  0.0477  0.2084  1045 ASP A N     
7133 C  CA    . ASP A 942 ? 1.5772 1.5792 1.3908 0.3330  0.0352  0.2156  1045 ASP A CA    
7134 C  C     . ASP A 942 ? 1.5302 1.5812 1.3830 0.3262  0.0265  0.2089  1045 ASP A C     
7135 O  O     . ASP A 942 ? 1.5433 1.6327 1.4188 0.3409  0.0209  0.2163  1045 ASP A O     
7136 C  CB    . ASP A 942 ? 1.6086 1.6142 1.4118 0.3220  0.0260  0.2154  1045 ASP A CB    
7137 C  CG    . ASP A 942 ? 1.7358 1.6968 1.5012 0.3308  0.0342  0.2247  1045 ASP A CG    
7138 O  OD1   . ASP A 942 ? 1.7774 1.7138 1.5280 0.3515  0.0443  0.2347  1045 ASP A OD1   
7139 O  OD2   . ASP A 942 ? 1.7452 1.6950 1.4953 0.3174  0.0311  0.2224  1045 ASP A OD2   
7140 N  N     . ALA A 943 ? 1.5544 1.6051 1.4158 0.3039  0.0254  0.1951  1046 ALA A N     
7141 C  CA    . ALA A 943 ? 1.5026 1.5952 1.3992 0.2960  0.0182  0.1884  1046 ALA A CA    
7142 C  C     . ALA A 943 ? 1.4992 1.5947 1.4080 0.3089  0.0275  0.1912  1046 ALA A C     
7143 O  O     . ALA A 943 ? 1.4535 1.5900 1.3938 0.3097  0.0221  0.1909  1046 ALA A O     
7144 C  CB    . ALA A 943 ? 1.4325 1.5215 1.3325 0.2696  0.0148  0.1735  1046 ALA A CB    
7145 N  N     . HIS A 944 ? 1.5166 1.5692 1.4006 0.3186  0.0416  0.1938  1047 HIS A N     
7146 C  CA    . HIS A 944 ? 1.5404 1.5910 1.4318 0.3315  0.0521  0.1961  1047 HIS A CA    
7147 C  C     . HIS A 944 ? 1.6003 1.6464 1.4841 0.3608  0.0594  0.2108  1047 HIS A C     
7148 O  O     . HIS A 944 ? 1.6713 1.7167 1.5605 0.3749  0.0691  0.2141  1047 HIS A O     
7149 C  CB    . HIS A 944 ? 1.5737 1.5786 1.4425 0.3213  0.0635  0.1867  1047 HIS A CB    
7150 C  CG    . HIS A 944 ? 1.5274 1.5366 1.4037 0.2943  0.0573  0.1726  1047 HIS A CG    
7151 N  ND1   . HIS A 944 ? 1.5733 1.5490 1.4336 0.2822  0.0648  0.1629  1047 HIS A ND1   
7152 C  CD2   . HIS A 944 ? 1.4992 1.5418 1.3966 0.2779  0.0443  0.1666  1047 HIS A CD2   
7153 C  CE1   . HIS A 944 ? 1.5852 1.5750 1.4574 0.2603  0.0567  0.1521  1047 HIS A CE1   
7154 N  NE2   . HIS A 944 ? 1.5272 1.5563 1.4215 0.2575  0.0447  0.1541  1047 HIS A NE2   
7155 N  N     . HIS A 945 ? 1.6194 1.6621 1.4898 0.3710  0.0553  0.2201  1048 HIS A N     
7156 C  CA    . HIS A 945 ? 1.6563 1.6970 1.5194 0.4006  0.0611  0.2354  1048 HIS A CA    
7157 C  C     . HIS A 945 ? 1.6508 1.6380 1.4836 0.4137  0.0790  0.2376  1048 HIS A C     
7158 O  O     . HIS A 945 ? 1.6710 1.6596 1.5052 0.4384  0.0874  0.2474  1048 HIS A O     
7159 C  CB    . HIS A 945 ? 1.6608 1.7583 1.5620 0.4147  0.0557  0.2423  1048 HIS A CB    
7160 C  CG    . HIS A 945 ? 1.7256 1.8755 1.6570 0.4009  0.0379  0.2391  1048 HIS A CG    
7161 N  ND1   . HIS A 945 ? 1.7724 1.9765 1.7429 0.4033  0.0311  0.2407  1048 HIS A ND1   
7162 C  CD2   . HIS A 945 ? 1.6483 1.8039 1.5756 0.3843  0.0258  0.2342  1048 HIS A CD2   
7163 C  CE1   . HIS A 945 ? 1.7516 1.9909 1.7401 0.3882  0.0151  0.2363  1048 HIS A CE1   
7164 N  NE2   . HIS A 945 ? 1.6973 1.9080 1.6596 0.3771  0.0117  0.2323  1048 HIS A NE2   
7165 N  N     . GLY A 946 ? 1.6628 1.6027 1.4679 0.3970  0.0849  0.2283  1049 GLY A N     
7166 C  CA    . GLY A 946 ? 1.7437 1.6275 1.5162 0.4053  0.1010  0.2282  1049 GLY A CA    
7167 C  C     . GLY A 946 ? 1.8417 1.7027 1.6082 0.3832  0.1053  0.2130  1049 GLY A C     
7168 O  O     . GLY A 946 ? 1.8042 1.6920 1.5917 0.3619  0.0962  0.2029  1049 GLY A O     
7169 N  N     . GLY A 947 ? 1.8346 1.6439 1.5706 0.3890  0.1195  0.2113  1050 GLY A N     
7170 C  CA    . GLY A 947 ? 1.8035 1.5862 1.5291 0.3703  0.1246  0.1973  1050 GLY A CA    
7171 C  C     . GLY A 947 ? 1.8234 1.5696 1.5243 0.3465  0.1231  0.1885  1050 GLY A C     
7172 O  O     . GLY A 947 ? 1.8130 1.5294 1.4991 0.3323  0.1284  0.1774  1050 GLY A O     
7173 N  N     . TRP A 948 ? 1.8779 1.6265 1.5738 0.3414  0.1160  0.1931  1051 TRP A N     
7174 C  CA    . TRP A 948 ? 1.8844 1.6021 1.5586 0.3187  0.1147  0.1860  1051 TRP A CA    
7175 C  C     . TRP A 948 ? 2.0271 1.7086 1.6708 0.3295  0.1201  0.1968  1051 TRP A C     
7176 O  O     . TRP A 948 ? 2.0249 1.7106 1.6650 0.3198  0.1135  0.1991  1051 TRP A O     
7177 C  CB    . TRP A 948 ? 1.7647 1.5232 1.4638 0.2973  0.1003  0.1792  1051 TRP A CB    
7178 C  CG    . TRP A 948 ? 1.6765 1.4705 1.4054 0.2865  0.0946  0.1692  1051 TRP A CG    
7179 C  CD1   . TRP A 948 ? 1.6406 1.4770 1.3997 0.2983  0.0909  0.1724  1051 TRP A CD1   
7180 C  CD2   . TRP A 948 ? 1.6268 1.4178 1.3586 0.2618  0.0918  0.1550  1051 TRP A CD2   
7181 N  NE1   . TRP A 948 ? 1.6018 1.4589 1.3809 0.2823  0.0868  0.1613  1051 TRP A NE1   
7182 C  CE2   . TRP A 948 ? 1.5879 1.4181 1.3505 0.2606  0.0870  0.1506  1051 TRP A CE2   
7183 C  CE3   . TRP A 948 ? 1.6018 1.3620 1.3137 0.2406  0.0931  0.1460  1051 TRP A CE3   
7184 C  CZ2   . TRP A 948 ? 1.5054 1.3428 1.2777 0.2403  0.0834  0.1379  1051 TRP A CZ2   
7185 C  CZ3   . TRP A 948 ? 1.5439 1.3143 1.2671 0.2205  0.0889  0.1332  1051 TRP A CZ3   
7186 C  CH2   . TRP A 948 ? 1.4778 1.2856 1.2301 0.2212  0.0842  0.1294  1051 TRP A CH2   
7187 N  N     . THR A 949 ? 2.1830 1.8271 1.8031 0.3505  0.1328  0.2041  1052 THR A N     
7188 C  CA    . THR A 949 ? 2.3611 1.9659 1.9496 0.3633  0.1395  0.2156  1052 THR A CA    
7189 C  C     . THR A 949 ? 2.5535 2.0944 2.1039 0.3480  0.1496  0.2086  1052 THR A C     
7190 O  O     . THR A 949 ? 2.5764 2.1042 2.1157 0.3280  0.1463  0.2057  1052 THR A O     
7191 C  CB    . THR A 949 ? 2.3438 1.9446 1.9278 0.3978  0.1477  0.2292  1052 THR A CB    
7192 O  OG1   . THR A 949 ? 2.4000 1.9774 1.9763 0.4046  0.1588  0.2235  1052 THR A OG1   
7193 C  CG2   . THR A 949 ? 2.1952 1.8618 1.8176 0.4121  0.1367  0.2371  1052 THR A CG2   
7194 N  N     . THR A 950 ? 2.8907 2.3919 2.4207 0.3571  0.1621  0.2059  1053 THR A N     
7195 C  CA    . THR A 950 ? 2.9411 2.3794 2.4340 0.3424  0.1721  0.1979  1053 THR A CA    
7196 C  C     . THR A 950 ? 2.9258 2.3216 2.3866 0.3426  0.1771  0.2068  1053 THR A C     
7197 O  O     . THR A 950 ? 2.9418 2.2983 2.3793 0.3205  0.1804  0.1996  1053 THR A O     
7198 C  CB    . THR A 950 ? 2.8954 2.3414 2.3976 0.3094  0.1656  0.1810  1053 THR A CB    
7199 O  OG1   . THR A 950 ? 2.8128 2.2832 2.3269 0.2909  0.1550  0.1809  1053 THR A OG1   
7200 C  CG2   . THR A 950 ? 2.7917 2.2818 2.3263 0.3091  0.1601  0.1733  1053 THR A CG2   
7201 N  N     . LYS A 951 ? 2.7159 2.1196 2.1752 0.3674  0.1776  0.2229  1054 LYS A N     
7202 C  CA    . LYS A 951 ? 2.6295 1.9922 2.0569 0.3709  0.1832  0.2334  1054 LYS A CA    
7203 C  C     . LYS A 951 ? 2.5510 1.8733 1.9511 0.4032  0.1965  0.2462  1054 LYS A C     
7204 O  O     . LYS A 951 ? 2.5404 1.8256 1.9227 0.4098  0.2076  0.2412  1054 LYS A O     
7205 C  CB    . LYS A 951 ? 2.5505 1.9563 1.9961 0.3704  0.1711  0.2423  1054 LYS A CB    
7206 C  CG    . LYS A 951 ? 2.4911 1.9288 1.9573 0.3385  0.1593  0.2306  1054 LYS A CG    
7207 C  CD    . LYS A 951 ? 2.3613 1.8341 1.8390 0.3394  0.1489  0.2398  1054 LYS A CD    
7208 C  CE    . LYS A 951 ? 2.3525 1.8543 1.8485 0.3087  0.1385  0.2282  1054 LYS A CE    
7209 N  NZ    . LYS A 951 ? 2.3095 1.8431 1.8136 0.3094  0.1288  0.2365  1054 LYS A NZ    
7210 N  N     . THR B 4   ? 2.0534 1.9890 1.6156 0.2712  -0.0016 0.1489  3    THR B N     
7211 C  CA    . THR B 4   ? 2.0027 1.9227 1.5620 0.2630  0.0133  0.1505  3    THR B CA    
7212 C  C     . THR B 4   ? 2.0156 1.9096 1.5585 0.2719  0.0292  0.1673  3    THR B C     
7213 O  O     . THR B 4   ? 2.0009 1.8880 1.5247 0.2860  0.0272  0.1772  3    THR B O     
7214 C  CB    . THR B 4   ? 1.9147 1.8373 1.5087 0.2475  0.0189  0.1437  3    THR B CB    
7215 O  OG1   . THR B 4   ? 1.9467 1.8620 1.5614 0.2484  0.0231  0.1500  3    THR B OG1   
7216 C  CG2   . THR B 4   ? 1.8317 1.7783 1.4402 0.2379  0.0048  0.1275  3    THR B CG2   
7217 N  N     . SER B 5   ? 1.9866 1.8669 1.5371 0.2637  0.0453  0.1710  4    SER B N     
7218 C  CA    . SER B 5   ? 2.0046 1.8605 1.5430 0.2694  0.0627  0.1872  4    SER B CA    
7219 C  C     . SER B 5   ? 2.0871 1.9353 1.6576 0.2573  0.0752  0.1898  4    SER B C     
7220 O  O     . SER B 5   ? 1.9786 1.8301 1.5619 0.2464  0.0825  0.1850  4    SER B O     
7221 C  CB    . SER B 5   ? 1.9336 1.7815 1.4424 0.2730  0.0712  0.1905  4    SER B CB    
7222 O  OG    . SER B 5   ? 1.8330 1.6850 1.3087 0.2852  0.0600  0.1900  4    SER B OG    
7223 N  N     . ALA B 6   ? 2.2784 2.1162 1.8611 0.2595  0.0776  0.1972  5    ALA B N     
7224 C  CA    . ALA B 6   ? 2.0824 1.9120 1.6948 0.2474  0.0884  0.1995  5    ALA B CA    
7225 C  C     . ALA B 6   ? 2.0666 1.8793 1.6726 0.2447  0.1080  0.2115  5    ALA B C     
7226 O  O     . ALA B 6   ? 1.9380 1.7323 1.5206 0.2548  0.1165  0.2252  5    ALA B O     
7227 C  CB    . ALA B 6   ? 1.9474 1.7663 1.5698 0.2514  0.0862  0.2046  5    ALA B CB    
7228 N  N     . VAL B 7   ? 1.9932 1.8128 1.6200 0.2316  0.1156  0.2069  6    VAL B N     
7229 C  CA    . VAL B 7   ? 1.9967 1.8057 1.6207 0.2282  0.1344  0.2171  6    VAL B CA    
7230 C  C     . VAL B 7   ? 2.0698 1.8645 1.7154 0.2202  0.1463  0.2269  6    VAL B C     
7231 O  O     . VAL B 7   ? 2.1130 1.9125 1.7859 0.2110  0.1405  0.2204  6    VAL B O     
7232 C  CB    . VAL B 7   ? 1.8885 1.7133 1.5244 0.2191  0.1368  0.2077  6    VAL B CB    
7233 C  CG1   . VAL B 7   ? 1.8420 1.6583 1.4722 0.2182  0.1566  0.2187  6    VAL B CG1   
7234 C  CG2   . VAL B 7   ? 1.7895 1.6271 1.4059 0.2249  0.1232  0.1959  6    VAL B CG2   
7235 N  N     . PRO B 8   ? 2.0644 1.8407 1.6980 0.2228  0.1630  0.2423  7    PRO B N     
7236 C  CA    . PRO B 8   ? 2.2429 2.0061 1.8991 0.2120  0.1755  0.2512  7    PRO B CA    
7237 C  C     . PRO B 8   ? 2.4197 2.1979 2.1073 0.1961  0.1830  0.2466  7    PRO B C     
7238 O  O     . PRO B 8   ? 2.4737 2.2716 2.1666 0.1940  0.1774  0.2357  7    PRO B O     
7239 C  CB    . PRO B 8   ? 2.2028 1.9431 1.8328 0.2204  0.1914  0.2694  7    PRO B CB    
7240 C  CG    . PRO B 8   ? 2.1210 1.8686 1.7222 0.2310  0.1917  0.2688  7    PRO B CG    
7241 C  CD    . PRO B 8   ? 2.0453 1.8102 1.6420 0.2359  0.1707  0.2529  7    PRO B CD    
7242 N  N     . SER B 9   ? 2.4446 2.2133 2.1526 0.1849  0.1955  0.2550  8    SER B N     
7243 C  CA    . SER B 9   ? 2.4664 2.2506 2.2075 0.1690  0.2030  0.2521  8    SER B CA    
7244 C  C     . SER B 9   ? 2.5028 2.3070 2.2674 0.1618  0.1868  0.2348  8    SER B C     
7245 O  O     . SER B 9   ? 2.4491 2.2500 2.2130 0.1645  0.1731  0.2278  8    SER B O     
7246 C  CB    . SER B 9   ? 2.3686 2.1614 2.1010 0.1715  0.2161  0.2574  8    SER B CB    
7247 O  OG    . SER B 9   ? 2.3473 2.1530 2.0629 0.1805  0.2063  0.2470  8    SER B OG    
7248 N  N     . ASP B 10  ? 2.6336 2.4586 2.4185 0.1535  0.1886  0.2284  9    ASP B N     
7249 C  CA    . ASP B 10  ? 2.5864 2.4306 2.3930 0.1465  0.1746  0.2129  9    ASP B CA    
7250 C  C     . ASP B 10  ? 2.4984 2.3628 2.3171 0.1423  0.1796  0.2090  9    ASP B C     
7251 O  O     . ASP B 10  ? 2.5027 2.3672 2.3199 0.1423  0.1951  0.2187  9    ASP B O     
7252 C  CB    . ASP B 10  ? 2.6323 2.4747 2.4678 0.1333  0.1713  0.2102  9    ASP B CB    
7253 C  CG    . ASP B 10  ? 2.6653 2.5040 2.5207 0.1212  0.1870  0.2208  9    ASP B CG    
7254 O  OD1   . ASP B 10  ? 2.6628 2.4994 2.5089 0.1241  0.2016  0.2318  9    ASP B OD1   
7255 O  OD2   . ASP B 10  ? 2.7004 2.5390 2.5807 0.1084  0.1849  0.2181  9    ASP B OD2   
7256 N  N     . ASN B 11  ? 2.3273 2.2087 2.1577 0.1394  0.1670  0.1951  10   ASN B N     
7257 C  CA    . ASN B 11  ? 2.2138 2.1141 2.0557 0.1363  0.1697  0.1898  10   ASN B CA    
7258 C  C     . ASN B 11  ? 2.1823 2.0791 1.9964 0.1477  0.1788  0.1946  10   ASN B C     
7259 O  O     . ASN B 11  ? 2.0691 1.9702 1.8879 0.1470  0.1936  0.2022  10   ASN B O     
7260 C  CB    . ASN B 11  ? 2.2732 2.1843 2.1488 0.1231  0.1793  0.1942  10   ASN B CB    
7261 C  CG    . ASN B 11  ? 2.2509 2.1843 2.1446 0.1191  0.1772  0.1859  10   ASN B CG    
7262 O  OD1   . ASN B 11  ? 2.1626 2.1002 2.0401 0.1272  0.1739  0.1798  10   ASN B OD1   
7263 N  ND2   . ASN B 11  ? 2.2618 2.2089 2.1887 0.1066  0.1790  0.1857  10   ASN B ND2   
7264 N  N     . LEU B 12  ? 2.0672 1.9570 1.8518 0.1584  0.1695  0.1897  11   LEU B N     
7265 C  CA    . LEU B 12  ? 1.7919 1.6758 1.5451 0.1698  0.1763  0.1930  11   LEU B CA    
7266 C  C     . LEU B 12  ? 1.6281 1.5255 1.3854 0.1692  0.1778  0.1851  11   LEU B C     
7267 O  O     . LEU B 12  ? 1.6486 1.5587 1.4231 0.1630  0.1671  0.1737  11   LEU B O     
7268 C  CB    . LEU B 12  ? 1.7190 1.5939 1.4407 0.1803  0.1636  0.1885  11   LEU B CB    
7269 C  CG    . LEU B 12  ? 1.8872 1.7511 1.6069 0.1819  0.1572  0.1929  11   LEU B CG    
7270 C  CD1   . LEU B 12  ? 1.8575 1.7198 1.5511 0.1917  0.1418  0.1859  11   LEU B CD1   
7271 C  CD2   . LEU B 12  ? 2.0156 1.8623 1.7261 0.1852  0.1730  0.2097  11   LEU B CD2   
7272 N  N     . PRO B 13  ? 1.5327 1.4268 1.2733 0.1762  0.1916  0.1913  12   PRO B N     
7273 C  CA    . PRO B 13  ? 1.4660 1.3693 1.2049 0.1781  0.1933  0.1836  12   PRO B CA    
7274 C  C     . PRO B 13  ? 1.4244 1.3253 1.1408 0.1826  0.1772  0.1697  12   PRO B C     
7275 O  O     . PRO B 13  ? 1.4782 1.3682 1.1671 0.1894  0.1701  0.1692  12   PRO B O     
7276 C  CB    . PRO B 13  ? 1.3595 1.2555 1.0787 0.1871  0.2121  0.1944  12   PRO B CB    
7277 C  CG    . PRO B 13  ? 1.3980 1.2777 1.0957 0.1927  0.2155  0.2049  12   PRO B CG    
7278 C  CD    . PRO B 13  ? 1.4573 1.3379 1.1791 0.1832  0.2074  0.2061  12   PRO B CD    
7279 N  N     . THR B 14  ? 1.3572 1.2689 1.0859 0.1783  0.1711  0.1588  13   THR B N     
7280 C  CA    . THR B 14  ? 1.3101 1.2207 1.0211 0.1799  0.1561  0.1449  13   THR B CA    
7281 C  C     . THR B 14  ? 1.3170 1.2246 1.0117 0.1854  0.1630  0.1405  13   THR B C     
7282 O  O     . THR B 14  ? 1.2915 1.2078 1.0062 0.1828  0.1714  0.1413  13   THR B O     
7283 C  CB    . THR B 14  ? 1.3080 1.2313 1.0457 0.1696  0.1417  0.1350  13   THR B CB    
7284 O  OG1   . THR B 14  ? 1.3313 1.2550 1.0813 0.1658  0.1356  0.1388  13   THR B OG1   
7285 C  CG2   . THR B 14  ? 1.3026 1.2254 1.0228 0.1701  0.1270  0.1211  13   THR B CG2   
7286 N  N     . TYR B 15  ? 1.2918 1.1870 0.9497 0.1932  0.1593  0.1356  14   TYR B N     
7287 C  CA    . TYR B 15  ? 1.3741 1.2614 1.0095 0.1995  0.1657  0.1305  14   TYR B CA    
7288 C  C     . TYR B 15  ? 1.3618 1.2484 0.9875 0.1956  0.1495  0.1146  14   TYR B C     
7289 O  O     . TYR B 15  ? 1.4644 1.3468 1.0708 0.1957  0.1361  0.1087  14   TYR B O     
7290 C  CB    . TYR B 15  ? 1.4083 1.2797 1.0054 0.2113  0.1750  0.1368  14   TYR B CB    
7291 C  CG    . TYR B 15  ? 1.3662 1.2371 0.9702 0.2153  0.1926  0.1534  14   TYR B CG    
7292 C  CD1   . TYR B 15  ? 1.3937 1.2647 1.0053 0.2133  0.1907  0.1623  14   TYR B CD1   
7293 C  CD2   . TYR B 15  ? 1.3505 1.2202 0.9529 0.2213  0.2117  0.1605  14   TYR B CD2   
7294 C  CE1   . TYR B 15  ? 1.4005 1.2693 1.0180 0.2157  0.2073  0.1778  14   TYR B CE1   
7295 C  CE2   . TYR B 15  ? 1.3578 1.2283 0.9676 0.2239  0.2285  0.1761  14   TYR B CE2   
7296 C  CZ    . TYR B 15  ? 1.3458 1.2153 0.9629 0.2204  0.2261  0.1848  14   TYR B CZ    
7297 O  OH    . TYR B 15  ? 1.3048 1.1734 0.9289 0.2217  0.2432  0.2007  14   TYR B OH    
7298 N  N     . LYS B 16  ? 1.3910 1.2820 1.0303 0.1920  0.1508  0.1082  15   LYS B N     
7299 C  CA    . LYS B 16  ? 1.4562 1.3448 1.0868 0.1873  0.1371  0.0934  15   LYS B CA    
7300 C  C     . LYS B 16  ? 1.3495 1.2195 0.9408 0.1954  0.1416  0.0879  15   LYS B C     
7301 O  O     . LYS B 16  ? 1.3832 1.2472 0.9714 0.1987  0.1508  0.0856  15   LYS B O     
7302 C  CB    . LYS B 16  ? 1.4708 1.3712 1.1334 0.1798  0.1360  0.0896  15   LYS B CB    
7303 C  CG    . LYS B 16  ? 1.4756 1.3932 1.1745 0.1708  0.1295  0.0929  15   LYS B CG    
7304 C  CD    . LYS B 16  ? 1.5880 1.5172 1.3155 0.1638  0.1275  0.0886  15   LYS B CD    
7305 C  CE    . LYS B 16  ? 1.6966 1.6419 1.4580 0.1549  0.1208  0.0911  15   LYS B CE    
7306 N  NZ    . LYS B 16  ? 1.7071 1.6642 1.4948 0.1483  0.1180  0.0868  15   LYS B NZ    
7307 N  N     . LEU B 17  ? 1.2880 1.1482 0.8476 0.1993  0.1350  0.0855  16   LEU B N     
7308 C  CA    . LEU B 17  ? 1.4197 1.2606 0.9377 0.2064  0.1376  0.0791  16   LEU B CA    
7309 C  C     . LEU B 17  ? 1.3081 1.1444 0.8165 0.1987  0.1232  0.0630  16   LEU B C     
7310 O  O     . LEU B 17  ? 1.2779 1.1232 0.7923 0.1905  0.1064  0.0565  16   LEU B O     
7311 C  CB    . LEU B 17  ? 1.3952 1.2283 0.8819 0.2135  0.1354  0.0832  16   LEU B CB    
7312 C  CG    . LEU B 17  ? 1.2999 1.1368 0.7955 0.2199  0.1481  0.0999  16   LEU B CG    
7313 C  CD1   . LEU B 17  ? 1.3578 1.1856 0.8191 0.2275  0.1445  0.1034  16   LEU B CD1   
7314 C  CD2   . LEU B 17  ? 1.3159 1.1486 0.8152 0.2269  0.1699  0.1085  16   LEU B CD2   
7315 N  N     . VAL B 18  ? 1.3072 1.1292 0.8007 0.2014  0.1302  0.0568  17   VAL B N     
7316 C  CA    . VAL B 18  ? 1.3463 1.1605 0.8307 0.1935  0.1190  0.0419  17   VAL B CA    
7317 C  C     . VAL B 18  ? 1.3893 1.1798 0.8256 0.1987  0.1185  0.0333  17   VAL B C     
7318 O  O     . VAL B 18  ? 1.4022 1.1774 0.8169 0.2098  0.1338  0.0370  17   VAL B O     
7319 C  CB    . VAL B 18  ? 1.4225 1.2371 0.9290 0.1918  0.1267  0.0408  17   VAL B CB    
7320 C  CG1   . VAL B 18  ? 1.3961 1.2022 0.8947 0.1823  0.1145  0.0262  17   VAL B CG1   
7321 C  CG2   . VAL B 18  ? 1.3061 1.1444 0.8585 0.1876  0.1282  0.0502  17   VAL B CG2   
7322 N  N     . VAL B 19  ? 1.3885 1.1769 0.8083 0.1903  0.1010  0.0216  18   VAL B N     
7323 C  CA    . VAL B 19  ? 1.3977 1.1647 0.7711 0.1927  0.0970  0.0115  18   VAL B CA    
7324 C  C     . VAL B 19  ? 1.4675 1.2193 0.8318 0.1845  0.0926  -0.0026 18   VAL B C     
7325 O  O     . VAL B 19  ? 1.5722 1.3338 0.9520 0.1714  0.0780  -0.0106 18   VAL B O     
7326 C  CB    . VAL B 19  ? 1.3761 1.1523 0.7357 0.1889  0.0798  0.0083  18   VAL B CB    
7327 C  CG1   . VAL B 19  ? 1.4139 1.1688 0.7252 0.1897  0.0740  -0.0034 18   VAL B CG1   
7328 C  CG2   . VAL B 19  ? 1.3435 1.1313 0.7098 0.1981  0.0853  0.0233  18   VAL B CG2   
7329 N  N     . VAL B 20  ? 1.5223 1.2492 0.8608 0.1924  0.1057  -0.0055 19   VAL B N     
7330 C  CA    . VAL B 20  ? 1.5697 1.2771 0.8970 0.1864  0.1043  -0.0179 19   VAL B CA    
7331 C  C     . VAL B 20  ? 1.5684 1.2461 0.8433 0.1891  0.1033  -0.0293 19   VAL B C     
7332 O  O     . VAL B 20  ? 1.5250 1.1944 0.7726 0.2003  0.1105  -0.0252 19   VAL B O     
7333 C  CB    . VAL B 20  ? 1.5348 1.2375 0.8812 0.1937  0.1217  -0.0117 19   VAL B CB    
7334 C  CG1   . VAL B 20  ? 1.5249 1.2572 0.9222 0.1897  0.1212  -0.0014 19   VAL B CG1   
7335 C  CG2   . VAL B 20  ? 1.6634 1.3530 0.9895 0.2112  0.1416  -0.0034 19   VAL B CG2   
7336 N  N     . GLY B 21  ? 1.6453 1.3062 0.9053 0.1784  0.0945  -0.0438 20   GLY B N     
7337 C  CA    . GLY B 21  ? 1.5713 1.2024 0.7811 0.1780  0.0913  -0.0570 20   GLY B CA    
7338 C  C     . GLY B 21  ? 1.6739 1.2967 0.8778 0.1598  0.0751  -0.0728 20   GLY B C     
7339 O  O     . GLY B 21  ? 1.8329 1.4769 1.0708 0.1474  0.0644  -0.0731 20   GLY B O     
7340 N  N     . ASP B 22  ? 1.7414 1.3320 0.9000 0.1581  0.0737  -0.0861 21   ASP B N     
7341 C  CA    . ASP B 22  ? 1.7865 1.3633 0.9340 0.1402  0.0600  -0.1021 21   ASP B CA    
7342 C  C     . ASP B 22  ? 1.7925 1.3956 0.9485 0.1246  0.0371  -0.1075 21   ASP B C     
7343 O  O     . ASP B 22  ? 1.7235 1.3517 0.8880 0.1292  0.0318  -0.0997 21   ASP B O     
7344 C  CB    . ASP B 22  ? 1.9599 1.4934 1.0536 0.1423  0.0645  -0.1155 21   ASP B CB    
7345 C  CG    . ASP B 22  ? 2.0836 1.5893 1.1682 0.1576  0.0870  -0.1114 21   ASP B CG    
7346 O  OD1   . ASP B 22  ? 2.0424 1.5650 1.1642 0.1660  0.0984  -0.0980 21   ASP B OD1   
7347 O  OD2   . ASP B 22  ? 2.1296 1.5969 1.1698 0.1615  0.0931  -0.1218 21   ASP B OD2   
7348 N  N     . GLY B 23  ? 1.9519 1.5488 1.1053 0.1061  0.0239  -0.1208 22   GLY B N     
7349 C  CA    . GLY B 23  ? 1.9088 1.5323 1.0717 0.0903  0.0021  -0.1267 22   GLY B CA    
7350 C  C     . GLY B 23  ? 1.9866 1.6035 1.1079 0.0902  -0.0083 -0.1349 22   GLY B C     
7351 O  O     . GLY B 23  ? 2.2407 1.8234 1.3182 0.0954  -0.0018 -0.1426 22   GLY B O     
7352 N  N     . GLY B 24  ? 1.8951 1.5457 1.0298 0.0848  -0.0247 -0.1332 23   GLY B N     
7353 C  CA    . GLY B 24  ? 1.9704 1.6212 1.0691 0.0853  -0.0365 -0.1394 23   GLY B CA    
7354 C  C     . GLY B 24  ? 1.8205 1.4619 0.8944 0.1066  -0.0241 -0.1299 23   GLY B C     
7355 O  O     . GLY B 24  ? 1.8324 1.4709 0.8714 0.1089  -0.0328 -0.1348 23   GLY B O     
7356 N  N     . VAL B 25  ? 1.8198 1.4576 0.9106 0.1220  -0.0041 -0.1161 24   VAL B N     
7357 C  CA    . VAL B 25  ? 1.8424 1.4702 0.9100 0.1421  0.0101  -0.1062 24   VAL B CA    
7358 C  C     . VAL B 25  ? 1.7700 1.4292 0.8482 0.1482  0.0017  -0.0954 24   VAL B C     
7359 O  O     . VAL B 25  ? 1.8370 1.4897 0.8805 0.1579  0.0011  -0.0943 24   VAL B O     
7360 C  CB    . VAL B 25  ? 1.7567 1.3746 0.8431 0.1554  0.0338  -0.0943 24   VAL B CB    
7361 C  CG1   . VAL B 25  ? 1.7983 1.4197 0.8774 0.1749  0.0477  -0.0795 24   VAL B CG1   
7362 C  CG2   . VAL B 25  ? 1.7818 1.3602 0.8402 0.1560  0.0450  -0.1047 24   VAL B CG2   
7363 N  N     . GLY B 26  ? 1.6437 1.3359 0.7683 0.1434  -0.0048 -0.0872 25   GLY B N     
7364 C  CA    . GLY B 26  ? 1.6412 1.3623 0.7774 0.1493  -0.0130 -0.0768 25   GLY B CA    
7365 C  C     . GLY B 26  ? 1.5564 1.2964 0.7348 0.1580  -0.0015 -0.0593 25   GLY B C     
7366 O  O     . GLY B 26  ? 1.6321 1.3883 0.8155 0.1676  -0.0021 -0.0477 25   GLY B O     
7367 N  N     . LYS B 27  ? 1.6007 1.3379 0.8087 0.1547  0.0089  -0.0573 26   LYS B N     
7368 C  CA    . LYS B 27  ? 1.5024 1.2569 0.7512 0.1615  0.0197  -0.0417 26   LYS B CA    
7369 C  C     . LYS B 27  ? 1.4555 1.2432 0.7349 0.1567  0.0054  -0.0366 26   LYS B C     
7370 O  O     . LYS B 27  ? 1.4183 1.2192 0.7152 0.1662  0.0113  -0.0226 26   LYS B O     
7371 C  CB    . LYS B 27  ? 1.4489 1.1973 0.7243 0.1564  0.0295  -0.0427 26   LYS B CB    
7372 C  CG    . LYS B 27  ? 1.5271 1.2425 0.7747 0.1623  0.0446  -0.0473 26   LYS B CG    
7373 C  CD    . LYS B 27  ? 1.5825 1.2947 0.8587 0.1580  0.0529  -0.0472 26   LYS B CD    
7374 C  CE    . LYS B 27  ? 1.6924 1.4116 0.9827 0.1398  0.0368  -0.0589 26   LYS B CE    
7375 N  NZ    . LYS B 27  ? 1.7170 1.4132 0.9672 0.1312  0.0276  -0.0752 26   LYS B NZ    
7376 N  N     . SER B 28  ? 1.5053 1.3066 0.7915 0.1422  -0.0130 -0.0477 27   SER B N     
7377 C  CA    . SER B 28  ? 1.4662 1.3002 0.7821 0.1383  -0.0266 -0.0433 27   SER B CA    
7378 C  C     . SER B 28  ? 1.3972 1.2408 0.6921 0.1478  -0.0345 -0.0382 27   SER B C     
7379 O  O     . SER B 28  ? 1.3376 1.1981 0.6518 0.1560  -0.0334 -0.0257 27   SER B O     
7380 C  CB    . SER B 28  ? 1.5117 1.3589 0.8408 0.1201  -0.0433 -0.0565 27   SER B CB    
7381 O  OG    . SER B 28  ? 1.3325 1.1727 0.6841 0.1121  -0.0359 -0.0593 27   SER B OG    
7382 N  N     . ALA B 29  ? 1.4998 1.3313 0.7533 0.1470  -0.0425 -0.0478 28   ALA B N     
7383 C  CA    . ALA B 29  ? 1.5081 1.3496 0.7388 0.1559  -0.0520 -0.0437 28   ALA B CA    
7384 C  C     . ALA B 29  ? 1.4289 1.2615 0.6517 0.1745  -0.0354 -0.0272 28   ALA B C     
7385 O  O     . ALA B 29  ? 1.4271 1.2754 0.6523 0.1835  -0.0400 -0.0171 28   ALA B O     
7386 C  CB    . ALA B 29  ? 1.6317 1.4589 0.8165 0.1511  -0.0627 -0.0580 28   ALA B CB    
7387 N  N     . LEU B 30  ? 1.4387 1.2462 0.6523 0.1808  -0.0157 -0.0239 29   LEU B N     
7388 C  CA    . LEU B 30  ? 1.4435 1.2439 0.6541 0.1971  0.0020  -0.0075 29   LEU B CA    
7389 C  C     . LEU B 30  ? 1.4001 1.2216 0.6559 0.1989  0.0054  0.0061  29   LEU B C     
7390 O  O     . LEU B 30  ? 1.4029 1.2297 0.6582 0.2102  0.0097  0.0196  29   LEU B O     
7391 C  CB    . LEU B 30  ? 1.5010 1.2740 0.6983 0.2025  0.0228  -0.0069 29   LEU B CB    
7392 C  CG    . LEU B 30  ? 1.5215 1.2672 0.6666 0.2060  0.0246  -0.0171 29   LEU B CG    
7393 C  CD1   . LEU B 30  ? 1.5210 1.2416 0.6596 0.2109  0.0455  -0.0171 29   LEU B CD1   
7394 C  CD2   . LEU B 30  ? 1.6058 1.3486 0.7164 0.2195  0.0246  -0.0096 29   LEU B CD2   
7395 N  N     . THR B 31  ? 1.5186 1.3509 0.8122 0.1878  0.0037  0.0025  30   THR B N     
7396 C  CA    . THR B 31  ? 1.3216 1.1722 0.6577 0.1885  0.0072  0.0140  30   THR B CA    
7397 C  C     . THR B 31  ? 1.3108 1.1857 0.6575 0.1882  -0.0098 0.0161  30   THR B C     
7398 O  O     . THR B 31  ? 1.2984 1.1820 0.6610 0.1961  -0.0057 0.0292  30   THR B O     
7399 C  CB    . THR B 31  ? 1.3122 1.1669 0.6827 0.1770  0.0096  0.0088  30   THR B CB    
7400 O  OG1   . THR B 31  ? 1.3257 1.1575 0.6836 0.1784  0.0244  0.0062  30   THR B OG1   
7401 C  CG2   . THR B 31  ? 1.3235 1.1933 0.7355 0.1784  0.0157  0.0208  30   THR B CG2   
7402 N  N     . ILE B 32  ? 1.3167 1.2030 0.6549 0.1790  -0.0286 0.0035  31   ILE B N     
7403 C  CA    . ILE B 32  ? 1.3092 1.2210 0.6561 0.1798  -0.0452 0.0053  31   ILE B CA    
7404 C  C     . ILE B 32  ? 1.4339 1.3421 0.7513 0.1952  -0.0449 0.0151  31   ILE B C     
7405 O  O     . ILE B 32  ? 1.4797 1.4038 0.8091 0.2027  -0.0499 0.0248  31   ILE B O     
7406 C  CB    . ILE B 32  ? 1.3830 1.3094 0.7266 0.1658  -0.0652 -0.0107 31   ILE B CB    
7407 C  CG1   . ILE B 32  ? 1.2985 1.2262 0.6699 0.1506  -0.0642 -0.0195 31   ILE B CG1   
7408 C  CG2   . ILE B 32  ? 1.3020 1.2588 0.6581 0.1675  -0.0824 -0.0083 31   ILE B CG2   
7409 C  CD1   . ILE B 32  ? 1.2387 1.1832 0.6549 0.1497  -0.0608 -0.0117 31   ILE B CD1   
7410 N  N     . GLN B 33  ? 1.4186 1.3044 0.6956 0.2010  -0.0386 0.0131  32   GLN B N     
7411 C  CA    . GLN B 33  ? 1.4127 1.2926 0.6588 0.2165  -0.0364 0.0234  32   GLN B CA    
7412 C  C     . GLN B 33  ? 1.4070 1.2806 0.6685 0.2282  -0.0182 0.0418  32   GLN B C     
7413 O  O     . GLN B 33  ? 1.4964 1.3763 0.7534 0.2394  -0.0199 0.0535  32   GLN B O     
7414 C  CB    . GLN B 33  ? 1.5732 1.4288 0.7713 0.2197  -0.0325 0.0164  32   GLN B CB    
7415 C  CG    . GLN B 33  ? 1.4980 1.3479 0.6582 0.2353  -0.0327 0.0252  32   GLN B CG    
7416 C  CD    . GLN B 33  ? 1.5084 1.3812 0.6588 0.2348  -0.0563 0.0208  32   GLN B CD    
7417 O  OE1   . GLN B 33  ? 1.5168 1.3970 0.6573 0.2233  -0.0726 0.0051  32   GLN B OE1   
7418 N  NE2   . GLN B 33  ? 1.5091 1.3936 0.6626 0.2474  -0.0583 0.0350  32   GLN B NE2   
7419 N  N     . PHE B 34  ? 1.3844 1.2457 0.6643 0.2257  -0.0008 0.0447  33   PHE B N     
7420 C  CA    . PHE B 34  ? 1.4327 1.2879 0.7276 0.2349  0.0172  0.0618  33   PHE B CA    
7421 C  C     . PHE B 34  ? 1.4862 1.3609 0.8203 0.2334  0.0124  0.0694  33   PHE B C     
7422 O  O     . PHE B 34  ? 1.5317 1.4039 0.8698 0.2430  0.0208  0.0842  33   PHE B O     
7423 C  CB    . PHE B 34  ? 1.3836 1.2237 0.6891 0.2322  0.0363  0.0623  33   PHE B CB    
7424 C  CG    . PHE B 34  ? 1.4855 1.3220 0.8113 0.2389  0.0548  0.0791  33   PHE B CG    
7425 C  CD1   . PHE B 34  ? 1.5220 1.3474 0.8244 0.2522  0.0656  0.0926  33   PHE B CD1   
7426 C  CD2   . PHE B 34  ? 1.3845 1.2286 0.7523 0.2313  0.0615  0.0814  33   PHE B CD2   
7427 C  CE1   . PHE B 34  ? 1.5143 1.3362 0.8360 0.2567  0.0830  0.1082  33   PHE B CE1   
7428 C  CE2   . PHE B 34  ? 1.3556 1.1970 0.7426 0.2358  0.0779  0.0963  33   PHE B CE2   
7429 C  CZ    . PHE B 34  ? 1.4936 1.3240 0.8583 0.2480  0.0889  0.1097  33   PHE B CZ    
7430 N  N     . PHE B 35  ? 1.3688 1.2614 0.7306 0.2215  -0.0006 0.0595  34   PHE B N     
7431 C  CA    . PHE B 35  ? 1.3656 1.2759 0.7651 0.2196  -0.0047 0.0653  34   PHE B CA    
7432 C  C     . PHE B 35  ? 1.3480 1.2778 0.7442 0.2234  -0.0231 0.0648  34   PHE B C     
7433 O  O     . PHE B 35  ? 1.3452 1.2824 0.7579 0.2301  -0.0229 0.0754  34   PHE B O     
7434 C  CB    . PHE B 35  ? 1.3060 1.2255 0.7403 0.2052  -0.0065 0.0561  34   PHE B CB    
7435 C  CG    . PHE B 35  ? 1.2347 1.1413 0.6863 0.2032  0.0121  0.0610  34   PHE B CG    
7436 C  CD1   . PHE B 35  ? 1.2218 1.1312 0.7026 0.2051  0.0214  0.0723  34   PHE B CD1   
7437 C  CD2   . PHE B 35  ? 1.2859 1.1779 0.7245 0.1995  0.0202  0.0542  34   PHE B CD2   
7438 C  CE1   . PHE B 35  ? 1.2267 1.1274 0.7248 0.2026  0.0376  0.0768  34   PHE B CE1   
7439 C  CE2   . PHE B 35  ? 1.2537 1.1368 0.7094 0.1987  0.0371  0.0593  34   PHE B CE2   
7440 C  CZ    . PHE B 35  ? 1.1976 1.0866 0.6839 0.1999  0.0454  0.0707  34   PHE B CZ    
7441 N  N     . ALA B 36  ? 1.3751 1.3137 0.7508 0.2194  -0.0392 0.0529  35   ALA B N     
7442 C  CA    . ALA B 36  ? 1.4294 1.3915 0.8051 0.2222  -0.0581 0.0515  35   ALA B CA    
7443 C  C     . ALA B 36  ? 1.5640 1.5233 0.8972 0.2324  -0.0660 0.0526  35   ALA B C     
7444 O  O     . ALA B 36  ? 1.5851 1.5652 0.9159 0.2369  -0.0820 0.0528  35   ALA B O     
7445 C  CB    . ALA B 36  ? 1.3401 1.3233 0.7349 0.2066  -0.0738 0.0361  35   ALA B CB    
7446 N  N     . LYS B 37  ? 1.6412 1.5765 0.9405 0.2369  -0.0553 0.0534  36   LYS B N     
7447 C  CA    . LYS B 37  ? 1.7028 1.6326 0.9575 0.2473  -0.0616 0.0546  36   LYS B CA    
7448 C  C     . LYS B 37  ? 1.7490 1.6984 0.9915 0.2389  -0.0848 0.0394  36   LYS B C     
7449 O  O     . LYS B 37  ? 1.7342 1.6981 0.9595 0.2471  -0.0988 0.0417  36   LYS B O     
7450 C  CB    . LYS B 37  ? 1.9059 1.8370 1.1544 0.2647  -0.0589 0.0721  36   LYS B CB    
7451 C  CG    . LYS B 37  ? 2.0110 1.9231 1.2725 0.2715  -0.0362 0.0876  36   LYS B CG    
7452 C  CD    . LYS B 37  ? 2.0451 1.9306 1.2833 0.2719  -0.0185 0.0875  36   LYS B CD    
7453 C  CE    . LYS B 37  ? 2.0624 1.9337 1.3220 0.2747  0.0040  0.1011  36   LYS B CE    
7454 N  NZ    . LYS B 37  ? 1.9454 1.7947 1.1884 0.2740  0.0215  0.0999  36   LYS B NZ    
7455 N  N     . ILE B 38  ? 1.5488 1.4990 0.8003 0.2223  -0.0890 0.0240  37   ILE B N     
7456 C  CA    . ILE B 38  ? 1.5530 1.5213 0.7956 0.2109  -0.1104 0.0084  37   ILE B CA    
7457 C  C     . ILE B 38  ? 1.5048 1.4538 0.7342 0.1967  -0.1070 -0.0067 37   ILE B C     
7458 O  O     . ILE B 38  ? 1.4974 1.4331 0.7467 0.1907  -0.0932 -0.0073 37   ILE B O     
7459 C  CB    . ILE B 38  ? 1.4561 1.4584 0.7396 0.2032  -0.1245 0.0060  37   ILE B CB    
7460 C  CG1   . ILE B 38  ? 1.6009 1.6240 0.8773 0.1895  -0.1462 -0.0103 37   ILE B CG1   
7461 C  CG2   . ILE B 38  ? 1.5591 1.5591 0.8829 0.1942  -0.1131 0.0062  37   ILE B CG2   
7462 C  CD1   . ILE B 38  ? 1.6674 1.7264 0.9833 0.1821  -0.1599 -0.0126 37   ILE B CD1   
7463 N  N     . PHE B 39  ? 1.5498 1.4964 0.7441 0.1918  -0.1198 -0.0189 38   PHE B N     
7464 C  CA    . PHE B 39  ? 1.6091 1.5354 0.7857 0.1780  -0.1185 -0.0348 38   PHE B CA    
7465 C  C     . PHE B 39  ? 1.5367 1.4847 0.7381 0.1581  -0.1347 -0.0488 38   PHE B C     
7466 O  O     . PHE B 39  ? 1.5377 1.5159 0.7458 0.1547  -0.1539 -0.0517 38   PHE B O     
7467 C  CB    . PHE B 39  ? 1.5376 1.4464 0.6600 0.1822  -0.1233 -0.0416 38   PHE B CB    
7468 C  CG    . PHE B 39  ? 1.5593 1.4503 0.6605 0.1661  -0.1275 -0.0607 38   PHE B CG    
7469 C  CD1   . PHE B 39  ? 1.5604 1.4202 0.6576 0.1634  -0.1094 -0.0639 38   PHE B CD1   
7470 C  CD2   . PHE B 39  ? 1.6104 1.5157 0.6953 0.1538  -0.1497 -0.0753 38   PHE B CD2   
7471 C  CE1   . PHE B 39  ? 1.5838 1.4236 0.6595 0.1493  -0.1126 -0.0813 38   PHE B CE1   
7472 C  CE2   . PHE B 39  ? 1.7079 1.5938 0.7719 0.1379  -0.1534 -0.0932 38   PHE B CE2   
7473 C  CZ    . PHE B 39  ? 1.6738 1.5252 0.7322 0.1360  -0.1345 -0.0961 38   PHE B CZ    
7474 N  N     . VAL B 40  ? 1.4464 1.3798 0.6614 0.1455  -0.1266 -0.0568 39   VAL B N     
7475 C  CA    . VAL B 40  ? 1.5601 1.5097 0.7985 0.1254  -0.1390 -0.0697 39   VAL B CA    
7476 C  C     . VAL B 40  ? 1.5280 1.4554 0.7312 0.1124  -0.1440 -0.0870 39   VAL B C     
7477 O  O     . VAL B 40  ? 1.5442 1.4373 0.7284 0.1137  -0.1287 -0.0895 39   VAL B O     
7478 C  CB    . VAL B 40  ? 1.5558 1.5049 0.8359 0.1200  -0.1268 -0.0660 39   VAL B CB    
7479 C  CG1   . VAL B 40  ? 1.5623 1.5215 0.8592 0.0988  -0.1375 -0.0802 39   VAL B CG1   
7480 C  CG2   . VAL B 40  ? 1.3465 1.3198 0.6623 0.1304  -0.1249 -0.0511 39   VAL B CG2   
7481 N  N     . PRO B 41  ? 1.5402 1.4857 0.7337 0.0995  -0.1650 -0.0994 40   PRO B N     
7482 C  CA    . PRO B 41  ? 1.6143 1.5363 0.7712 0.0860  -0.1704 -0.1168 40   PRO B CA    
7483 C  C     . PRO B 41  ? 1.6853 1.6056 0.8622 0.0637  -0.1737 -0.1296 40   PRO B C     
7484 O  O     . PRO B 41  ? 1.6883 1.5823 0.8367 0.0516  -0.1748 -0.1439 40   PRO B O     
7485 C  CB    . PRO B 41  ? 1.6145 1.5593 0.7483 0.0849  -0.1925 -0.1223 40   PRO B CB    
7486 C  CG    . PRO B 41  ? 1.7101 1.7002 0.8863 0.0865  -0.2035 -0.1135 40   PRO B CG    
7487 C  CD    . PRO B 41  ? 1.5409 1.5281 0.7494 0.0998  -0.1846 -0.0971 40   PRO B CD    
7488 N  N     . ASP B 42  ? 1.6696 1.6160 0.8936 0.0580  -0.1749 -0.1247 41   ASP B N     
7489 C  CA    . ASP B 42  ? 1.6532 1.6026 0.8978 0.0363  -0.1795 -0.1361 41   ASP B CA    
7490 C  C     . ASP B 42  ? 1.6925 1.6050 0.9376 0.0348  -0.1597 -0.1368 41   ASP B C     
7491 O  O     . ASP B 42  ? 1.6895 1.5786 0.9245 0.0507  -0.1422 -0.1277 41   ASP B O     
7492 C  CB    . ASP B 42  ? 1.5955 1.5874 0.8891 0.0315  -0.1878 -0.1305 41   ASP B CB    
7493 C  CG    . ASP B 42  ? 1.6729 1.6714 0.9960 0.0488  -0.1739 -0.1131 41   ASP B CG    
7494 O  OD1   . ASP B 42  ? 1.6959 1.6722 1.0300 0.0506  -0.1568 -0.1093 41   ASP B OD1   
7495 O  OD2   . ASP B 42  ? 1.6582 1.6841 0.9933 0.0607  -0.1802 -0.1033 41   ASP B OD2   
7496 N  N     . TYR B 43  ? 1.7302 1.6386 0.9877 0.0153  -0.1624 -0.1474 42   TYR B N     
7497 C  CA    . TYR B 43  ? 1.7359 1.6096 0.9928 0.0116  -0.1459 -0.1498 42   TYR B CA    
7498 C  C     . TYR B 43  ? 1.7677 1.6609 1.0737 0.0081  -0.1408 -0.1423 42   TYR B C     
7499 O  O     . TYR B 43  ? 1.8119 1.7197 1.1380 -0.0098 -0.1497 -0.1495 42   TYR B O     
7500 C  CB    . TYR B 43  ? 1.7803 1.6286 1.0086 -0.0079 -0.1520 -0.1679 42   TYR B CB    
7501 C  CG    . TYR B 43  ? 1.7829 1.5972 1.0130 -0.0138 -0.1368 -0.1713 42   TYR B CG    
7502 C  CD1   . TYR B 43  ? 1.8064 1.5814 1.0114 -0.0001 -0.1183 -0.1685 42   TYR B CD1   
7503 C  CD2   . TYR B 43  ? 1.9084 1.7303 1.1644 -0.0326 -0.1408 -0.1768 42   TYR B CD2   
7504 C  CE1   . TYR B 43  ? 1.8995 1.6440 1.1058 -0.0040 -0.1046 -0.1710 42   TYR B CE1   
7505 C  CE2   . TYR B 43  ? 1.9652 1.7553 1.2215 -0.0371 -0.1271 -0.1792 42   TYR B CE2   
7506 C  CZ    . TYR B 43  ? 2.0512 1.8027 1.2825 -0.0223 -0.1093 -0.1763 42   TYR B CZ    
7507 O  OH    . TYR B 43  ? 2.0317 1.7522 1.2631 -0.0252 -0.0958 -0.1780 42   TYR B OH    
7508 N  N     . ASP B 44  ? 1.8363 1.7299 1.1612 0.0250  -0.1263 -0.1277 43   ASP B N     
7509 C  CA    . ASP B 44  ? 1.6622 1.5692 1.0304 0.0240  -0.1190 -0.1199 43   ASP B CA    
7510 C  C     . ASP B 44  ? 1.6094 1.4843 0.9744 0.0336  -0.0980 -0.1142 43   ASP B C     
7511 O  O     . ASP B 44  ? 1.5405 1.4128 0.9080 0.0509  -0.0865 -0.1020 43   ASP B O     
7512 C  CB    . ASP B 44  ? 1.6233 1.5658 1.0221 0.0348  -0.1226 -0.1072 43   ASP B CB    
7513 C  CG    . ASP B 44  ? 1.8510 1.8311 1.2644 0.0245  -0.1427 -0.1119 43   ASP B CG    
7514 O  OD1   . ASP B 44  ? 2.0763 2.0563 1.4695 0.0106  -0.1553 -0.1247 43   ASP B OD1   
7515 O  OD2   . ASP B 44  ? 1.8165 1.8267 1.2617 0.0301  -0.1456 -0.1030 43   ASP B OD2   
7516 N  N     . PRO B 45  ? 1.6668 1.5171 1.0262 0.0231  -0.0922 -0.1222 44   PRO B N     
7517 C  CA    . PRO B 45  ? 1.6484 1.4708 1.0072 0.0330  -0.0723 -0.1163 44   PRO B CA    
7518 C  C     . PRO B 45  ? 1.5639 1.4067 0.9646 0.0412  -0.0643 -0.1024 44   PRO B C     
7519 O  O     . PRO B 45  ? 1.4597 1.3276 0.8930 0.0322  -0.0715 -0.1017 44   PRO B O     
7520 C  CB    . PRO B 45  ? 1.7344 1.5326 1.0845 0.0175  -0.0713 -0.1279 44   PRO B CB    
7521 C  CG    . PRO B 45  ? 1.7645 1.5658 1.0929 0.0015  -0.0887 -0.1419 44   PRO B CG    
7522 C  CD    . PRO B 45  ? 1.7095 1.5535 1.0585 0.0019  -0.1032 -0.1373 44   PRO B CD    
7523 N  N     . THR B 46  ? 1.5017 1.3336 0.9009 0.0581  -0.0491 -0.0916 45   THR B N     
7524 C  CA    . THR B 46  ? 1.3938 1.2437 0.8297 0.0668  -0.0411 -0.0781 45   THR B CA    
7525 C  C     . THR B 46  ? 1.4892 1.3248 0.9410 0.0658  -0.0283 -0.0763 45   THR B C     
7526 O  O     . THR B 46  ? 1.5391 1.3448 0.9681 0.0689  -0.0179 -0.0796 45   THR B O     
7527 C  CB    . THR B 46  ? 1.4037 1.2522 0.8311 0.0849  -0.0318 -0.0665 45   THR B CB    
7528 O  OG1   . THR B 46  ? 1.6263 1.4858 1.0347 0.0868  -0.0438 -0.0682 45   THR B OG1   
7529 C  CG2   . THR B 46  ? 1.2735 1.1418 0.7393 0.0920  -0.0253 -0.0531 45   THR B CG2   
7530 N  N     . ILE B 47  ? 1.3549 1.2119 0.8450 0.0622  -0.0292 -0.0710 46   ILE B N     
7531 C  CA    . ILE B 47  ? 1.3679 1.2160 0.8766 0.0624  -0.0178 -0.0676 46   ILE B CA    
7532 C  C     . ILE B 47  ? 1.2989 1.1488 0.8210 0.0782  -0.0038 -0.0540 46   ILE B C     
7533 O  O     . ILE B 47  ? 1.3927 1.2211 0.9030 0.0867  0.0100  -0.0511 46   ILE B O     
7534 C  CB    . ILE B 47  ? 1.5571 1.4266 1.0984 0.0499  -0.0259 -0.0693 46   ILE B CB    
7535 C  CG1   . ILE B 47  ? 1.4223 1.2924 0.9510 0.0330  -0.0399 -0.0824 46   ILE B CG1   
7536 C  CG2   . ILE B 47  ? 1.3972 1.2562 0.9547 0.0504  -0.0147 -0.0659 46   ILE B CG2   
7537 C  CD1   . ILE B 47  ? 1.3054 1.2028 0.8655 0.0209  -0.0497 -0.0837 46   ILE B CD1   
7538 N  N     . GLU B 48  ? 1.2464 1.1218 0.7933 0.0820  -0.0071 -0.0456 47   GLU B N     
7539 C  CA    . GLU B 48  ? 1.2849 1.1633 0.8429 0.0958  0.0049  -0.0326 47   GLU B CA    
7540 C  C     . GLU B 48  ? 1.3039 1.2079 0.8817 0.0982  -0.0022 -0.0258 47   GLU B C     
7541 O  O     . GLU B 48  ? 1.2527 1.1757 0.8612 0.0931  -0.0067 -0.0239 47   GLU B O     
7542 C  CB    . GLU B 48  ? 1.2876 1.1634 0.8692 0.0980  0.0168  -0.0269 47   GLU B CB    
7543 C  CG    . GLU B 48  ? 1.3156 1.1985 0.9136 0.1098  0.0283  -0.0134 47   GLU B CG    
7544 C  CD    . GLU B 48  ? 1.4022 1.2753 1.0097 0.1153  0.0431  -0.0082 47   GLU B CD    
7545 O  OE1   . GLU B 48  ? 1.4220 1.2741 1.0096 0.1158  0.0482  -0.0139 47   GLU B OE1   
7546 O  OE2   . GLU B 48  ? 1.2952 1.1815 0.9299 0.1193  0.0494  0.0015  47   GLU B OE2   
7547 N  N     . ASP B 49  ? 1.3954 1.2988 0.9544 0.1067  -0.0030 -0.0219 48   ASP B N     
7548 C  CA    . ASP B 49  ? 1.3511 1.2752 0.9241 0.1111  -0.0091 -0.0147 48   ASP B CA    
7549 C  C     . ASP B 49  ? 1.3182 1.2368 0.8923 0.1244  0.0045  -0.0014 48   ASP B C     
7550 O  O     . ASP B 49  ? 1.4062 1.3057 0.9600 0.1317  0.0163  0.0012  48   ASP B O     
7551 C  CB    . ASP B 49  ? 1.3220 1.2526 0.8721 0.1099  -0.0233 -0.0205 48   ASP B CB    
7552 C  CG    . ASP B 49  ? 1.4432 1.3803 0.9916 0.0951  -0.0370 -0.0338 48   ASP B CG    
7553 O  OD1   . ASP B 49  ? 1.3508 1.2856 0.9146 0.0861  -0.0350 -0.0383 48   ASP B OD1   
7554 O  OD2   . ASP B 49  ? 1.4821 1.4272 1.0137 0.0922  -0.0498 -0.0397 48   ASP B OD2   
7555 N  N     . SER B 50  ? 1.1936 1.1287 0.7916 0.1276  0.0034  0.0071  49   SER B N     
7556 C  CA    . SER B 50  ? 1.2298 1.1611 0.8324 0.1384  0.0158  0.0203  49   SER B CA    
7557 C  C     . SER B 50  ? 1.2337 1.1737 0.8299 0.1452  0.0093  0.0263  49   SER B C     
7558 O  O     . SER B 50  ? 1.1511 1.1069 0.7532 0.1413  -0.0048 0.0218  49   SER B O     
7559 C  CB    . SER B 50  ? 1.2543 1.1937 0.8931 0.1360  0.0231  0.0265  49   SER B CB    
7560 O  OG    . SER B 50  ? 1.2087 1.1670 0.8716 0.1312  0.0127  0.0259  49   SER B OG    
7561 N  N     . TYR B 51  ? 1.2517 1.1815 0.8358 0.1561  0.0203  0.0370  50   TYR B N     
7562 C  CA    . TYR B 51  ? 1.3031 1.2370 0.8770 0.1647  0.0163  0.0446  50   TYR B CA    
7563 C  C     . TYR B 51  ? 1.2508 1.1787 0.8356 0.1724  0.0311  0.0591  50   TYR B C     
7564 O  O     . TYR B 51  ? 1.2262 1.1422 0.8091 0.1747  0.0458  0.0637  50   TYR B O     
7565 C  CB    . TYR B 51  ? 1.2131 1.1369 0.7461 0.1708  0.0124  0.0415  50   TYR B CB    
7566 C  CG    . TYR B 51  ? 1.1873 1.1158 0.7068 0.1619  -0.0025 0.0266  50   TYR B CG    
7567 C  CD1   . TYR B 51  ? 1.2062 1.1217 0.7149 0.1553  0.0006  0.0171  50   TYR B CD1   
7568 C  CD2   . TYR B 51  ? 1.1631 1.1091 0.6806 0.1602  -0.0196 0.0223  50   TYR B CD2   
7569 C  CE1   . TYR B 51  ? 1.2110 1.1289 0.7069 0.1456  -0.0127 0.0033  50   TYR B CE1   
7570 C  CE2   . TYR B 51  ? 1.1511 1.1032 0.6577 0.1504  -0.0333 0.0087  50   TYR B CE2   
7571 C  CZ    . TYR B 51  ? 1.2395 1.1764 0.7349 0.1424  -0.0298 -0.0009 50   TYR B CZ    
7572 O  OH    . TYR B 51  ? 1.2714 1.2124 0.7555 0.1312  -0.0432 -0.0146 50   TYR B OH    
7573 N  N     . LEU B 52  ? 1.2521 1.1883 0.8485 0.1763  0.0275  0.0666  51   LEU B N     
7574 C  CA    . LEU B 52  ? 1.3150 1.2453 0.9242 0.1815  0.0406  0.0803  51   LEU B CA    
7575 C  C     . LEU B 52  ? 1.4450 1.3711 1.0348 0.1927  0.0392  0.0896  51   LEU B C     
7576 O  O     . LEU B 52  ? 1.6090 1.5447 1.1910 0.1950  0.0250  0.0859  51   LEU B O     
7577 C  CB    . LEU B 52  ? 1.3441 1.2859 0.9917 0.1742  0.0393  0.0809  51   LEU B CB    
7578 C  CG    . LEU B 52  ? 1.3758 1.3118 1.0441 0.1738  0.0546  0.0916  51   LEU B CG    
7579 C  CD1   . LEU B 52  ? 1.3769 1.3244 1.0800 0.1633  0.0524  0.0868  51   LEU B CD1   
7580 C  CD2   . LEU B 52  ? 1.4406 1.3707 1.1069 0.1814  0.0584  0.1038  51   LEU B CD2   
7581 N  N     . LYS B 53  ? 1.4088 1.3212 0.9910 0.1999  0.0542  0.1022  52   LYS B N     
7582 C  CA    . LYS B 53  ? 1.4412 1.3460 1.0026 0.2115  0.0554  0.1129  52   LYS B CA    
7583 C  C     . LYS B 53  ? 1.4695 1.3611 1.0367 0.2151  0.0742  0.1276  52   LYS B C     
7584 O  O     . LYS B 53  ? 1.4182 1.3056 0.9943 0.2110  0.0871  0.1289  52   LYS B O     
7585 C  CB    . LYS B 53  ? 1.4135 1.3121 0.9341 0.2190  0.0507  0.1096  52   LYS B CB    
7586 C  CG    . LYS B 53  ? 1.5034 1.3941 0.9983 0.2323  0.0512  0.1209  52   LYS B CG    
7587 C  CD    . LYS B 53  ? 1.6853 1.5703 1.1386 0.2390  0.0460  0.1164  52   LYS B CD    
7588 C  CE    . LYS B 53  ? 1.4031 1.2755 0.8425 0.2368  0.0583  0.1126  52   LYS B CE    
7589 N  NZ    . LYS B 53  ? 1.4828 1.3429 0.9312 0.2397  0.0797  0.1258  52   LYS B NZ    
7590 N  N     . HIS B 54  ? 1.5463 1.4319 1.1089 0.2228  0.0759  0.1390  53   HIS B N     
7591 C  CA    . HIS B 54  ? 1.5533 1.4246 1.1173 0.2266  0.0937  0.1543  53   HIS B CA    
7592 C  C     . HIS B 54  ? 1.4867 1.3443 1.0111 0.2398  0.0985  0.1632  53   HIS B C     
7593 O  O     . HIS B 54  ? 1.4879 1.3457 0.9939 0.2482  0.0876  0.1645  53   HIS B O     
7594 C  CB    . HIS B 54  ? 1.5493 1.4201 1.1377 0.2247  0.0936  0.1615  53   HIS B CB    
7595 C  CG    . HIS B 54  ? 1.5751 1.4572 1.2018 0.2118  0.0914  0.1545  53   HIS B CG    
7596 N  ND1   . HIS B 54  ? 1.5886 1.4689 1.2397 0.2079  0.0929  0.1595  53   HIS B ND1   
7597 C  CD2   . HIS B 54  ? 1.6793 1.5735 1.3224 0.2022  0.0878  0.1429  53   HIS B CD2   
7598 C  CE1   . HIS B 54  ? 1.6014 1.4934 1.2823 0.1964  0.0899  0.1511  53   HIS B CE1   
7599 N  NE2   . HIS B 54  ? 1.5972 1.4982 1.2741 0.1930  0.0869  0.1413  53   HIS B NE2   
7600 N  N     . THR B 55  ? 1.4709 1.3174 0.9818 0.2424  0.1148  0.1694  54   THR B N     
7601 C  CA    . THR B 55  ? 1.4513 1.2833 0.9232 0.2551  0.1216  0.1786  54   THR B CA    
7602 C  C     . THR B 55  ? 1.4136 1.2331 0.8878 0.2565  0.1447  0.1929  54   THR B C     
7603 O  O     . THR B 55  ? 1.3988 1.2228 0.8999 0.2476  0.1548  0.1925  54   THR B O     
7604 C  CB    . THR B 55  ? 1.4432 1.2752 0.8828 0.2589  0.1152  0.1676  54   THR B CB    
7605 O  OG1   . THR B 55  ? 1.6085 1.4275 1.0076 0.2722  0.1183  0.1760  54   THR B OG1   
7606 C  CG2   . THR B 55  ? 1.3776 1.2075 0.8223 0.2537  0.1277  0.1632  54   THR B CG2   
7607 N  N     . GLU B 56  ? 1.5105 1.3153 0.9563 0.2678  0.1529  0.2061  55   GLU B N     
7608 C  CA    . GLU B 56  ? 1.4625 1.2548 0.9062 0.2700  0.1757  0.2211  55   GLU B CA    
7609 C  C     . GLU B 56  ? 1.4199 1.2053 0.8295 0.2778  0.1845  0.2201  55   GLU B C     
7610 O  O     . GLU B 56  ? 1.4940 1.2734 0.8657 0.2880  0.1765  0.2177  55   GLU B O     
7611 C  CB    . GLU B 56  ? 1.3895 1.1673 0.8226 0.2776  0.1814  0.2377  55   GLU B CB    
7612 C  CG    . GLU B 56  ? 1.5230 1.2890 0.9619 0.2766  0.2055  0.2542  55   GLU B CG    
7613 C  CD    . GLU B 56  ? 1.6642 1.4118 1.0858 0.2851  0.2120  0.2714  55   GLU B CD    
7614 O  OE1   . GLU B 56  ? 1.6583 1.4005 1.0510 0.2965  0.2000  0.2716  55   GLU B OE1   
7615 O  OE2   . GLU B 56  ? 1.7523 1.4911 1.1894 0.2804  0.2292  0.2849  55   GLU B OE2   
7616 N  N     . ILE B 57  ? 1.4512 1.2380 0.8738 0.2734  0.2007  0.2216  56   ILE B N     
7617 C  CA    . ILE B 57  ? 1.5183 1.2977 0.9109 0.2811  0.2120  0.2210  56   ILE B CA    
7618 C  C     . ILE B 57  ? 1.5693 1.3409 0.9646 0.2839  0.2371  0.2384  56   ILE B C     
7619 O  O     . ILE B 57  ? 1.5500 1.3298 0.9830 0.2743  0.2472  0.2436  56   ILE B O     
7620 C  CB    . ILE B 57  ? 1.4435 1.2327 0.8475 0.2747  0.2087  0.2055  56   ILE B CB    
7621 C  CG1   . ILE B 57  ? 1.4156 1.2133 0.8199 0.2700  0.1842  0.1886  56   ILE B CG1   
7622 C  CG2   . ILE B 57  ? 1.5394 1.3181 0.9091 0.2841  0.2211  0.2045  56   ILE B CG2   
7623 C  CD1   . ILE B 57  ? 1.4308 1.2351 0.8429 0.2637  0.1803  0.1732  56   ILE B CD1   
7624 N  N     . ASP B 58  ? 1.5540 1.3106 0.9090 0.2966  0.2470  0.2475  57   ASP B N     
7625 C  CA    . ASP B 58  ? 1.5976 1.3458 0.9502 0.3004  0.2719  0.2654  57   ASP B CA    
7626 C  C     . ASP B 58  ? 1.6488 1.3973 1.0337 0.2923  0.2776  0.2787  57   ASP B C     
7627 O  O     . ASP B 58  ? 1.5939 1.3464 1.0051 0.2857  0.2955  0.2886  57   ASP B O     
7628 C  CB    . ASP B 58  ? 1.5703 1.3258 0.9349 0.2983  0.2883  0.2635  57   ASP B CB    
7629 C  CG    . ASP B 58  ? 1.6315 1.3814 0.9590 0.3075  0.2855  0.2515  57   ASP B CG    
7630 O  OD1   . ASP B 58  ? 1.5882 1.3250 0.8724 0.3181  0.2788  0.2505  57   ASP B OD1   
7631 O  OD2   . ASP B 58  ? 1.6944 1.4524 1.0351 0.3045  0.2899  0.2428  57   ASP B OD2   
7632 N  N     . ASN B 59  ? 1.8064 1.5507 1.1894 0.2927  0.2620  0.2787  58   ASN B N     
7633 C  CA    . ASN B 59  ? 1.8937 1.6339 1.3026 0.2860  0.2650  0.2901  58   ASN B CA    
7634 C  C     . ASN B 59  ? 1.7636 1.5195 1.2238 0.2694  0.2652  0.2849  58   ASN B C     
7635 O  O     . ASN B 59  ? 1.7768 1.5300 1.2624 0.2612  0.2760  0.2960  58   ASN B O     
7636 C  CB    . ASN B 59  ? 1.7370 1.4606 1.1314 0.2913  0.2873  0.3111  58   ASN B CB    
7637 C  CG    . ASN B 59  ? 1.9375 1.6440 1.2801 0.3084  0.2864  0.3179  58   ASN B CG    
7638 O  OD1   . ASN B 59  ? 2.0678 1.7667 1.3823 0.3170  0.3015  0.3249  58   ASN B OD1   
7639 N  ND2   . ASN B 59  ? 1.9857 1.6868 1.3148 0.3141  0.2686  0.3158  58   ASN B ND2   
7640 N  N     . GLN B 60  ? 1.5774 1.3495 1.0526 0.2638  0.2530  0.2679  59   GLN B N     
7641 C  CA    . GLN B 60  ? 1.5814 1.3697 1.1032 0.2489  0.2515  0.2618  59   GLN B CA    
7642 C  C     . GLN B 60  ? 1.4695 1.2690 1.0000 0.2450  0.2283  0.2438  59   GLN B C     
7643 O  O     . GLN B 60  ? 1.4160 1.2211 0.9325 0.2481  0.2211  0.2316  59   GLN B O     
7644 C  CB    . GLN B 60  ? 1.6171 1.4160 1.1525 0.2457  0.2674  0.2621  59   GLN B CB    
7645 C  CG    . GLN B 60  ? 1.6859 1.5039 1.2679 0.2313  0.2647  0.2550  59   GLN B CG    
7646 C  CD    . GLN B 60  ? 1.8568 1.6869 1.4513 0.2302  0.2799  0.2556  59   GLN B CD    
7647 O  OE1   . GLN B 60  ? 1.6226 1.4460 1.1925 0.2399  0.2949  0.2627  59   GLN B OE1   
7648 N  NE2   . GLN B 60  ? 1.9372 1.7855 1.5694 0.2193  0.2762  0.2483  59   GLN B NE2   
7649 N  N     . TRP B 61  ? 1.4806 1.2825 1.0337 0.2380  0.2174  0.2423  60   TRP B N     
7650 C  CA    . TRP B 61  ? 1.4275 1.2408 0.9901 0.2342  0.1959  0.2263  60   TRP B CA    
7651 C  C     . TRP B 61  ? 1.3852 1.2155 0.9743 0.2244  0.1941  0.2144  60   TRP B C     
7652 O  O     . TRP B 61  ? 1.3811 1.2172 0.9936 0.2176  0.2077  0.2191  60   TRP B O     
7653 C  CB    . TRP B 61  ? 1.3091 1.1206 0.8917 0.2293  0.1871  0.2283  60   TRP B CB    
7654 C  CG    . TRP B 61  ? 1.4516 1.2475 1.0060 0.2409  0.1832  0.2367  60   TRP B CG    
7655 C  CD1   . TRP B 61  ? 1.5470 1.3248 1.0903 0.2458  0.1966  0.2536  60   TRP B CD1   
7656 C  CD2   . TRP B 61  ? 1.4633 1.2614 0.9971 0.2495  0.1645  0.2293  60   TRP B CD2   
7657 N  NE1   . TRP B 61  ? 1.5522 1.3194 1.0680 0.2580  0.1874  0.2574  60   TRP B NE1   
7658 C  CE2   . TRP B 61  ? 1.5450 1.3259 1.0553 0.2606  0.1674  0.2425  60   TRP B CE2   
7659 C  CE3   . TRP B 61  ? 1.4424 1.2558 0.9756 0.2486  0.1459  0.2130  60   TRP B CE3   
7660 C  CZ2   . TRP B 61  ? 1.5474 1.3281 1.0346 0.2718  0.1516  0.2401  60   TRP B CZ2   
7661 C  CZ3   . TRP B 61  ? 1.4670 1.2811 0.9785 0.2582  0.1304  0.2103  60   TRP B CZ3   
7662 C  CH2   . TRP B 61  ? 1.5411 1.3399 1.0302 0.2702  0.1331  0.2238  60   TRP B CH2   
7663 N  N     . ALA B 62  ? 1.2859 1.1250 0.8714 0.2236  0.1769  0.1991  61   ALA B N     
7664 C  CA    . ALA B 62  ? 1.3430 1.1964 0.9496 0.2154  0.1736  0.1871  61   ALA B CA    
7665 C  C     . ALA B 62  ? 1.4081 1.2699 1.0144 0.2128  0.1522  0.1718  61   ALA B C     
7666 O  O     . ALA B 62  ? 1.3973 1.2547 0.9786 0.2197  0.1411  0.1693  61   ALA B O     
7667 C  CB    . ALA B 62  ? 1.3642 1.2150 0.9522 0.2208  0.1851  0.1861  61   ALA B CB    
7668 N  N     . ILE B 63  ? 1.3442 1.2194 0.9787 0.2027  0.1468  0.1622  62   ILE B N     
7669 C  CA    . ILE B 63  ? 1.3223 1.2072 0.9600 0.1985  0.1281  0.1474  62   ILE B CA    
7670 C  C     . ILE B 63  ? 1.2849 1.1698 0.9055 0.1997  0.1271  0.1373  62   ILE B C     
7671 O  O     . ILE B 63  ? 1.3462 1.2318 0.9751 0.1982  0.1389  0.1383  62   ILE B O     
7672 C  CB    . ILE B 63  ? 1.4203 1.3182 1.0974 0.1868  0.1225  0.1430  62   ILE B CB    
7673 C  CG1   . ILE B 63  ? 1.4786 1.3730 1.1696 0.1857  0.1232  0.1522  62   ILE B CG1   
7674 C  CG2   . ILE B 63  ? 1.2720 1.1807 0.9523 0.1821  0.1047  0.1280  62   ILE B CG2   
7675 C  CD1   . ILE B 63  ? 1.4563 1.3619 1.1834 0.1746  0.1172  0.1475  62   ILE B CD1   
7676 N  N     . LEU B 64  ? 1.2490 1.1332 0.8459 0.2025  0.1132  0.1276  63   LEU B N     
7677 C  CA    . LEU B 64  ? 1.3236 1.2041 0.8994 0.2032  0.1109  0.1169  63   LEU B CA    
7678 C  C     . LEU B 64  ? 1.3190 1.2111 0.9092 0.1936  0.0950  0.1025  63   LEU B C     
7679 O  O     . LEU B 64  ? 1.3081 1.2073 0.8961 0.1921  0.0797  0.0974  63   LEU B O     
7680 C  CB    . LEU B 64  ? 1.4190 1.2877 0.9516 0.2132  0.1080  0.1166  63   LEU B CB    
7681 C  CG    . LEU B 64  ? 1.3241 1.1778 0.8317 0.2237  0.1256  0.1276  63   LEU B CG    
7682 C  CD1   . LEU B 64  ? 1.3067 1.1583 0.8260 0.2272  0.1365  0.1440  63   LEU B CD1   
7683 C  CD2   . LEU B 64  ? 1.4888 1.3316 0.9512 0.2324  0.1195  0.1234  63   LEU B CD2   
7684 N  N     . ASP B 65  ? 1.3087 1.2036 0.9137 0.1877  0.0990  0.0967  64   ASP B N     
7685 C  CA    . ASP B 65  ? 1.3107 1.2142 0.9268 0.1785  0.0859  0.0833  64   ASP B CA    
7686 C  C     . ASP B 65  ? 1.2633 1.1549 0.8513 0.1802  0.0868  0.0742  64   ASP B C     
7687 O  O     . ASP B 65  ? 1.3922 1.2776 0.9820 0.1815  0.0988  0.0750  64   ASP B O     
7688 C  CB    . ASP B 65  ? 1.4037 1.3183 1.0582 0.1703  0.0892  0.0839  64   ASP B CB    
7689 C  CG    . ASP B 65  ? 1.5360 1.4605 1.2036 0.1606  0.0752  0.0713  64   ASP B CG    
7690 O  OD1   . ASP B 65  ? 1.4578 1.3917 1.1317 0.1571  0.0621  0.0679  64   ASP B OD1   
7691 O  OD2   . ASP B 65  ? 1.5327 1.4555 1.2040 0.1570  0.0778  0.0654  64   ASP B OD2   
7692 N  N     . VAL B 66  ? 1.2667 1.1551 0.8283 0.1804  0.0742  0.0657  65   VAL B N     
7693 C  CA    . VAL B 66  ? 1.3110 1.1849 0.8404 0.1818  0.0738  0.0562  65   VAL B CA    
7694 C  C     . VAL B 66  ? 1.2618 1.1407 0.7993 0.1703  0.0613  0.0423  65   VAL B C     
7695 O  O     . VAL B 66  ? 1.3567 1.2498 0.9057 0.1635  0.0464  0.0374  65   VAL B O     
7696 C  CB    . VAL B 66  ? 1.2820 1.1478 0.7733 0.1890  0.0681  0.0557  65   VAL B CB    
7697 C  CG1   . VAL B 66  ? 1.3095 1.1586 0.7658 0.1893  0.0669  0.0444  65   VAL B CG1   
7698 C  CG2   . VAL B 66  ? 1.2567 1.1159 0.7389 0.2007  0.0820  0.0706  65   VAL B CG2   
7699 N  N     . LEU B 67  ? 1.2519 1.1190 0.7832 0.1688  0.0680  0.0364  66   LEU B N     
7700 C  CA    . LEU B 67  ? 1.2769 1.1456 0.8163 0.1578  0.0590  0.0244  66   LEU B CA    
7701 C  C     . LEU B 67  ? 1.2588 1.1093 0.7598 0.1567  0.0541  0.0126  66   LEU B C     
7702 O  O     . LEU B 67  ? 1.3051 1.1359 0.7820 0.1641  0.0659  0.0127  66   LEU B O     
7703 C  CB    . LEU B 67  ? 1.2379 1.1061 0.8016 0.1567  0.0703  0.0271  66   LEU B CB    
7704 C  CG    . LEU B 67  ? 1.3373 1.2123 0.9215 0.1453  0.0622  0.0186  66   LEU B CG    
7705 C  CD1   . LEU B 67  ? 1.5618 1.4465 1.1804 0.1454  0.0716  0.0261  66   LEU B CD1   
7706 C  CD2   . LEU B 67  ? 1.3453 1.2006 0.9035 0.1424  0.0614  0.0072  66   LEU B CD2   
7707 N  N     . ASP B 68  ? 1.2077 1.0650 0.7029 0.1474  0.0370  0.0023  67   ASP B N     
7708 C  CA    . ASP B 68  ? 1.2890 1.1306 0.7483 0.1435  0.0296  -0.0102 67   ASP B CA    
7709 C  C     . ASP B 68  ? 1.3260 1.1581 0.7902 0.1336  0.0292  -0.0202 67   ASP B C     
7710 O  O     . ASP B 68  ? 1.3513 1.1965 0.8337 0.1215  0.0174  -0.0266 67   ASP B O     
7711 C  CB    . ASP B 68  ? 1.3223 1.1787 0.7737 0.1381  0.0110  -0.0157 67   ASP B CB    
7712 C  CG    . ASP B 68  ? 1.3972 1.2384 0.8095 0.1336  0.0024  -0.0286 67   ASP B CG    
7713 O  OD1   . ASP B 68  ? 1.3561 1.1715 0.7424 0.1370  0.0123  -0.0326 67   ASP B OD1   
7714 O  OD2   . ASP B 68  ? 1.3610 1.2162 0.7685 0.1266  -0.0144 -0.0351 67   ASP B OD2   
7715 N  N     . THR B 69  ? 1.3047 1.1132 0.7515 0.1392  0.0427  -0.0212 68   THR B N     
7716 C  CA    . THR B 69  ? 1.3615 1.1576 0.8120 0.1322  0.0449  -0.0288 68   THR B CA    
7717 C  C     . THR B 69  ? 1.4269 1.2107 0.8515 0.1203  0.0317  -0.0443 68   THR B C     
7718 O  O     . THR B 69  ? 1.6485 1.4368 1.0547 0.1170  0.0197  -0.0494 68   THR B O     
7719 C  CB    . THR B 69  ? 1.4229 1.1973 0.8614 0.1439  0.0640  -0.0245 68   THR B CB    
7720 O  OG1   . THR B 69  ? 1.6120 1.3632 1.0068 0.1509  0.0677  -0.0291 68   THR B OG1   
7721 C  CG2   . THR B 69  ? 1.4091 1.1979 0.8740 0.1544  0.0768  -0.0090 68   THR B CG2   
7722 N  N     . ALA B 70  ? 1.4110 1.1789 0.8341 0.1136  0.0340  -0.0516 69   ALA B N     
7723 C  CA    . ALA B 70  ? 1.4996 1.2519 0.8987 0.1006  0.0233  -0.0666 69   ALA B CA    
7724 C  C     . ALA B 70  ? 1.7471 1.4635 1.1016 0.1072  0.0319  -0.0732 69   ALA B C     
7725 O  O     . ALA B 70  ? 1.7438 1.4476 1.0887 0.1223  0.0477  -0.0658 69   ALA B O     
7726 C  CB    . ALA B 70  ? 1.5550 1.3080 0.9763 0.0888  0.0209  -0.0708 69   ALA B CB    
7727 N  N     . GLY B 71  ? 1.7930 1.4930 1.1199 0.0952  0.0214  -0.0875 70   GLY B N     
7728 C  CA    . GLY B 71  ? 1.8458 1.5091 1.1267 0.0997  0.0278  -0.0961 70   GLY B CA    
7729 C  C     . GLY B 71  ? 2.0980 1.7357 1.3605 0.0851  0.0226  -0.1107 70   GLY B C     
7730 O  O     . GLY B 71  ? 2.3336 1.9349 1.5598 0.0892  0.0310  -0.1178 70   GLY B O     
7731 N  N     . GLN B 72  ? 2.1519 1.8071 1.4384 0.0680  0.0095  -0.1152 71   GLN B N     
7732 C  CA    . GLN B 72  ? 2.3696 2.0019 1.6410 0.0516  0.0039  -0.1288 71   GLN B CA    
7733 C  C     . GLN B 72  ? 2.4816 2.0863 1.7537 0.0564  0.0192  -0.1271 71   GLN B C     
7734 O  O     . GLN B 72  ? 2.5429 2.1227 1.7993 0.0439  0.0168  -0.1378 71   GLN B O     
7735 C  CB    . GLN B 72  ? 2.3661 2.0280 1.6664 0.0324  -0.0130 -0.1324 71   GLN B CB    
7736 C  CG    . GLN B 72  ? 2.3074 1.9930 1.6015 0.0244  -0.0307 -0.1375 71   GLN B CG    
7737 C  CD    . GLN B 72  ? 2.3164 2.0310 1.6387 0.0053  -0.0465 -0.1416 71   GLN B CD    
7738 O  OE1   . GLN B 72  ? 2.3585 2.0913 1.7176 0.0033  -0.0442 -0.1346 71   GLN B OE1   
7739 N  NE2   . GLN B 72  ? 2.2829 2.0030 1.5880 -0.0091 -0.0626 -0.1531 71   GLN B NE2   
7740 N  N     . GLU B 73  ? 2.5304 2.1399 1.8210 0.0736  0.0345  -0.1139 72   GLU B N     
7741 C  CA    . GLU B 73  ? 2.5737 2.1609 1.8673 0.0815  0.0498  -0.1102 72   GLU B CA    
7742 C  C     . GLU B 73  ? 2.5477 2.1446 1.8712 0.0683  0.0447  -0.1104 72   GLU B C     
7743 O  O     . GLU B 73  ? 2.4717 2.0592 1.8074 0.0752  0.0560  -0.1046 72   GLU B O     
7744 C  CB    . GLU B 73  ? 2.6710 2.2104 1.9167 0.0851  0.0580  -0.1205 72   GLU B CB    
7745 C  CG    . GLU B 73  ? 2.6912 2.2067 1.9351 0.1005  0.0774  -0.1144 72   GLU B CG    
7746 C  CD    . GLU B 73  ? 2.6805 2.2098 1.9361 0.1223  0.0920  -0.1002 72   GLU B CD    
7747 O  OE1   . GLU B 73  ? 2.7542 2.2948 2.0002 0.1277  0.0904  -0.0981 72   GLU B OE1   
7748 O  OE2   . GLU B 73  ? 2.5505 2.0802 1.8253 0.1338  0.1052  -0.0907 72   GLU B OE2   
7749 N  N     . GLU B 74  ? 2.6758 2.2927 2.0114 0.0498  0.0277  -0.1166 73   GLU B N     
7750 C  CA    . GLU B 74  ? 2.6233 2.2543 1.9900 0.0375  0.0228  -0.1155 73   GLU B CA    
7751 C  C     . GLU B 74  ? 2.5952 2.2549 2.0033 0.0481  0.0293  -0.1008 73   GLU B C     
7752 O  O     . GLU B 74  ? 2.5719 2.2331 2.0008 0.0456  0.0327  -0.0972 73   GLU B O     
7753 C  CB    . GLU B 74  ? 2.6068 2.2609 1.9821 0.0175  0.0038  -0.1234 73   GLU B CB    
7754 C  CG    . GLU B 74  ? 2.7391 2.3741 2.0756 0.0069  -0.0057 -0.1375 73   GLU B CG    
7755 C  CD    . GLU B 74  ? 2.8094 2.4722 2.1584 -0.0131 -0.0247 -0.1445 73   GLU B CD    
7756 O  OE1   . GLU B 74  ? 2.6920 2.3839 2.0780 -0.0196 -0.0294 -0.1392 73   GLU B OE1   
7757 O  OE2   . GLU B 74  ? 2.7960 2.4524 2.1178 -0.0220 -0.0351 -0.1553 73   GLU B OE2   
7758 N  N     . PHE B 75  ? 2.2974 1.9793 1.7167 0.0596  0.0310  -0.0922 74   PHE B N     
7759 C  CA    . PHE B 75  ? 2.1589 1.8667 1.6153 0.0700  0.0377  -0.0783 74   PHE B CA    
7760 C  C     . PHE B 75  ? 2.1650 1.8580 1.6131 0.0895  0.0554  -0.0700 74   PHE B C     
7761 O  O     . PHE B 75  ? 2.1370 1.8471 1.5971 0.1007  0.0605  -0.0604 74   PHE B O     
7762 C  CB    . PHE B 75  ? 1.9947 1.7378 1.4720 0.0687  0.0278  -0.0736 74   PHE B CB    
7763 C  CG    . PHE B 75  ? 2.0187 1.7788 1.5030 0.0510  0.0105  -0.0817 74   PHE B CG    
7764 C  CD1   . PHE B 75  ? 1.9987 1.7803 1.5160 0.0418  0.0049  -0.0798 74   PHE B CD1   
7765 C  CD2   . PHE B 75  ? 1.9592 1.7152 1.4172 0.0438  -0.0002 -0.0912 74   PHE B CD2   
7766 C  CE1   . PHE B 75  ? 1.8754 1.6746 1.4003 0.0260  -0.0102 -0.0868 74   PHE B CE1   
7767 C  CE2   . PHE B 75  ? 1.9441 1.7191 1.4107 0.0274  -0.0162 -0.0984 74   PHE B CE2   
7768 C  CZ    . PHE B 75  ? 1.8284 1.6254 1.3291 0.0187  -0.0207 -0.0959 74   PHE B CZ    
7769 N  N     . SER B 76  ? 2.2149 1.8751 1.6416 0.0938  0.0654  -0.0736 75   SER B N     
7770 C  CA    . SER B 76  ? 2.2237 1.8695 1.6423 0.1131  0.0833  -0.0658 75   SER B CA    
7771 C  C     . SER B 76  ? 2.1796 1.8523 1.6387 0.1223  0.0908  -0.0517 75   SER B C     
7772 O  O     . SER B 76  ? 2.1534 1.8238 1.6128 0.1387  0.1051  -0.0431 75   SER B O     
7773 C  CB    . SER B 76  ? 2.2556 1.8605 1.6447 0.1158  0.0919  -0.0727 75   SER B CB    
7774 O  OG    . SER B 76  ? 2.2463 1.8382 1.6274 0.1359  0.1098  -0.0651 75   SER B OG    
7775 N  N     . ALA B 77  ? 2.1343 1.8328 1.6275 0.1121  0.0816  -0.0491 76   ALA B N     
7776 C  CA    . ALA B 77  ? 2.0280 1.7555 1.5603 0.1188  0.0861  -0.0365 76   ALA B CA    
7777 C  C     . ALA B 77  ? 2.0240 1.7773 1.5694 0.1209  0.0827  -0.0306 76   ALA B C     
7778 O  O     . ALA B 77  ? 2.0722 1.8177 1.5929 0.1221  0.0806  -0.0345 76   ALA B O     
7779 C  CB    . ALA B 77  ? 1.9670 1.7099 1.5276 0.1073  0.0778  -0.0367 76   ALA B CB    
7780 N  N     . MET B 78  ? 1.9783 1.7609 1.5610 0.1218  0.0823  -0.0212 77   MET B N     
7781 C  CA    . MET B 78  ? 1.9228 1.7292 1.5209 0.1238  0.0797  -0.0145 77   MET B CA    
7782 C  C     . MET B 78  ? 1.9230 1.7222 1.5063 0.1383  0.0928  -0.0077 77   MET B C     
7783 O  O     . MET B 78  ? 1.8752 1.6924 1.4728 0.1420  0.0942  0.0005  77   MET B O     
7784 C  CB    . MET B 78  ? 1.8498 1.6633 1.4399 0.1123  0.0642  -0.0220 77   MET B CB    
7785 C  CG    . MET B 78  ? 1.9205 1.7435 1.5251 0.0973  0.0514  -0.0288 77   MET B CG    
7786 S  SD    . MET B 78  ? 1.7549 1.5929 1.3548 0.0854  0.0335  -0.0362 77   MET B SD    
7787 C  CE    . MET B 78  ? 1.3127 1.1816 0.9443 0.0912  0.0330  -0.0245 77   MET B CE    
7788 N  N     . ARG B 79  ? 2.0186 1.7902 1.5722 0.1466  0.1029  -0.0108 78   ARG B N     
7789 C  CA    . ARG B 79  ? 1.9448 1.7088 1.4824 0.1613  0.1167  -0.0043 78   ARG B CA    
7790 C  C     . ARG B 79  ? 1.9766 1.7607 1.5462 0.1709  0.1288  0.0096  78   ARG B C     
7791 O  O     . ARG B 79  ? 1.9711 1.7667 1.5461 0.1776  0.1352  0.0182  78   ARG B O     
7792 C  CB    . ARG B 79  ? 2.0969 1.8257 1.5958 0.1689  0.1257  -0.0111 78   ARG B CB    
7793 C  CG    . ARG B 79  ? 2.1906 1.8965 1.6550 0.1584  0.1142  -0.0258 78   ARG B CG    
7794 C  CD    . ARG B 79  ? 2.2587 1.9272 1.6819 0.1676  0.1251  -0.0320 78   ARG B CD    
7795 N  NE    . ARG B 79  ? 2.3771 2.0211 1.7677 0.1557  0.1140  -0.0472 78   ARG B NE    
7796 C  CZ    . ARG B 79  ? 2.3013 1.9379 1.6634 0.1516  0.1062  -0.0545 78   ARG B CZ    
7797 N  NH1   . ARG B 79  ? 2.2717 1.9222 1.6321 0.1593  0.1084  -0.0478 78   ARG B NH1   
7798 N  NH2   . ARG B 79  ? 2.4071 2.0221 1.7414 0.1392  0.0957  -0.0688 78   ARG B NH2   
7799 N  N     . GLU B 80  ? 1.9511 1.7403 1.5424 0.1713  0.1318  0.0120  79   GLU B N     
7800 C  CA    . GLU B 80  ? 1.9320 1.7423 1.5552 0.1797  0.1424  0.0247  79   GLU B CA    
7801 C  C     . GLU B 80  ? 1.8558 1.6959 1.5100 0.1736  0.1365  0.0318  79   GLU B C     
7802 O  O     . GLU B 80  ? 1.8049 1.6620 1.4803 0.1803  0.1462  0.0429  79   GLU B O     
7803 C  CB    . GLU B 80  ? 2.1506 1.9629 1.7916 0.1796  0.1433  0.0252  79   GLU B CB    
7804 C  CG    . GLU B 80  ? 2.1301 1.9577 1.7944 0.1647  0.1280  0.0214  79   GLU B CG    
7805 C  CD    . GLU B 80  ? 2.1083 1.9196 1.7496 0.1523  0.1148  0.0086  79   GLU B CD    
7806 O  OE1   . GLU B 80  ? 2.1406 1.9241 1.7462 0.1548  0.1174  0.0013  79   GLU B OE1   
7807 O  OE2   . GLU B 80  ? 2.0140 1.8408 1.6727 0.1398  0.1019  0.0057  79   GLU B OE2   
7808 N  N     . GLN B 81  ? 1.8785 1.7253 1.5357 0.1609  0.1212  0.0258  80   GLN B N     
7809 C  CA    . GLN B 81  ? 1.8443 1.7170 1.5306 0.1552  0.1152  0.0319  80   GLN B CA    
7810 C  C     . GLN B 81  ? 1.7854 1.6595 1.4618 0.1611  0.1205  0.0381  80   GLN B C     
7811 O  O     . GLN B 81  ? 1.7487 1.6381 1.4462 0.1653  0.1285  0.0488  80   GLN B O     
7812 C  CB    . GLN B 81  ? 1.8676 1.7473 1.5601 0.1413  0.0979  0.0236  80   GLN B CB    
7813 C  CG    . GLN B 81  ? 1.8596 1.7644 1.5824 0.1358  0.0916  0.0292  80   GLN B CG    
7814 C  CD    . GLN B 81  ? 1.8619 1.7842 1.6183 0.1378  0.0982  0.0380  80   GLN B CD    
7815 O  OE1   . GLN B 81  ? 1.8526 1.7737 1.6166 0.1388  0.1012  0.0374  80   GLN B OE1   
7816 N  NE2   . GLN B 81  ? 1.8334 1.7717 1.6096 0.1382  0.1005  0.0463  80   GLN B NE2   
7817 N  N     . TYR B 82  ? 1.7644 1.6226 1.4081 0.1611  0.1160  0.0316  81   TYR B N     
7818 C  CA    . TYR B 82  ? 1.6569 1.5157 1.2886 0.1671  0.1204  0.0377  81   TYR B CA    
7819 C  C     . TYR B 82  ? 1.6655 1.5132 1.2824 0.1810  0.1387  0.0449  81   TYR B C     
7820 O  O     . TYR B 82  ? 1.6233 1.4757 1.2387 0.1869  0.1461  0.0537  81   TYR B O     
7821 C  CB    . TYR B 82  ? 1.5607 1.4086 1.1622 0.1628  0.1084  0.0288  81   TYR B CB    
7822 C  CG    . TYR B 82  ? 1.5828 1.4056 1.1492 0.1623  0.1062  0.0168  81   TYR B CG    
7823 C  CD1   . TYR B 82  ? 1.6549 1.4559 1.1919 0.1735  0.1193  0.0170  81   TYR B CD1   
7824 C  CD2   . TYR B 82  ? 1.5578 1.3781 1.1193 0.1501  0.0911  0.0052  81   TYR B CD2   
7825 C  CE1   . TYR B 82  ? 1.6907 1.4658 1.1934 0.1726  0.1171  0.0053  81   TYR B CE1   
7826 C  CE2   . TYR B 82  ? 1.6123 1.4081 1.1411 0.1479  0.0887  -0.0062 81   TYR B CE2   
7827 C  CZ    . TYR B 82  ? 1.7059 1.4780 1.2046 0.1591  0.1016  -0.0064 81   TYR B CZ    
7828 O  OH    . TYR B 82  ? 1.8532 1.5980 1.3174 0.1565  0.0993  -0.0184 81   TYR B OH    
7829 N  N     . MET B 83  ? 1.7039 1.5369 1.3096 0.1870  0.1470  0.0418  82   MET B N     
7830 C  CA    . MET B 83  ? 1.6714 1.4958 1.2654 0.2016  0.1657  0.0490  82   MET B CA    
7831 C  C     . MET B 83  ? 1.6634 1.5109 1.2953 0.2059  0.1768  0.0618  82   MET B C     
7832 O  O     . MET B 83  ? 1.7040 1.5493 1.3319 0.2183  0.1934  0.0693  82   MET B O     
7833 C  CB    . MET B 83  ? 1.6644 1.4619 1.2295 0.2078  0.1709  0.0406  82   MET B CB    
7834 C  CG    . MET B 83  ? 1.6781 1.4492 1.1992 0.2055  0.1635  0.0285  82   MET B CG    
7835 S  SD    . MET B 83  ? 1.9081 1.6429 1.3926 0.2130  0.1712  0.0184  82   MET B SD    
7836 C  CE    . MET B 83  ? 1.9158 1.6256 1.3528 0.2061  0.1588  0.0040  82   MET B CE    
7837 N  N     . ARG B 84  ? 1.6513 1.5215 1.3195 0.1961  0.1682  0.0643  83   ARG B N     
7838 C  CA    . ARG B 84  ? 1.6906 1.5854 1.3967 0.1976  0.1764  0.0760  83   ARG B CA    
7839 C  C     . ARG B 84  ? 1.6547 1.5671 1.3805 0.1917  0.1739  0.0837  83   ARG B C     
7840 O  O     . ARG B 84  ? 1.7266 1.6526 1.4703 0.1960  0.1859  0.0951  83   ARG B O     
7841 C  CB    . ARG B 84  ? 1.7543 1.6614 1.4879 0.1913  0.1693  0.0734  83   ARG B CB    
7842 C  CG    . ARG B 84  ? 1.8232 1.7183 1.5476 0.2003  0.1772  0.0711  83   ARG B CG    
7843 C  CD    . ARG B 84  ? 1.8586 1.7655 1.6083 0.1939  0.1689  0.0688  83   ARG B CD    
7844 N  NE    . ARG B 84  ? 1.9870 1.8892 1.7325 0.1805  0.1517  0.0586  83   ARG B NE    
7845 C  CZ    . ARG B 84  ? 1.9333 1.8418 1.6947 0.1732  0.1426  0.0547  83   ARG B CZ    
7846 N  NH1   . ARG B 84  ? 1.9421 1.8614 1.7240 0.1780  0.1478  0.0598  83   ARG B NH1   
7847 N  NH2   . ARG B 84  ? 1.9130 1.8179 1.6695 0.1612  0.1279  0.0458  83   ARG B NH2   
7848 N  N     . THR B 85  ? 1.6280 1.5401 1.3509 0.1819  0.1590  0.0779  84   THR B N     
7849 C  CA    . THR B 85  ? 1.6202 1.5454 1.3588 0.1769  0.1560  0.0847  84   THR B CA    
7850 C  C     . THR B 85  ? 1.5188 1.4310 1.2280 0.1826  0.1598  0.0875  84   THR B C     
7851 O  O     . THR B 85  ? 1.4744 1.3943 1.1934 0.1805  0.1600  0.0949  84   THR B O     
7852 C  CB    . THR B 85  ? 1.5672 1.5009 1.3205 0.1645  0.1382  0.0778  84   THR B CB    
7853 O  OG1   . THR B 85  ? 1.5995 1.5181 1.3249 0.1621  0.1271  0.0662  84   THR B OG1   
7854 C  CG2   . THR B 85  ? 1.5215 1.4702 1.3060 0.1586  0.1350  0.0768  84   THR B CG2   
7855 N  N     . GLY B 86  ? 1.5656 1.4571 1.2381 0.1900  0.1628  0.0819  85   GLY B N     
7856 C  CA    . GLY B 86  ? 1.5664 1.4450 1.2076 0.1959  0.1652  0.0838  85   GLY B CA    
7857 C  C     . GLY B 86  ? 1.5055 1.3859 1.1471 0.2058  0.1842  0.0972  85   GLY B C     
7858 O  O     . GLY B 86  ? 1.5134 1.3942 1.1593 0.2131  0.1980  0.1011  85   GLY B O     
7859 N  N     . ASP B 87  ? 1.4651 1.3468 1.1022 0.2066  0.1854  0.1048  86   ASP B N     
7860 C  CA    . ASP B 87  ? 1.5751 1.4573 1.2098 0.2153  0.2037  0.1183  86   ASP B CA    
7861 C  C     . ASP B 87  ? 1.4609 1.3217 1.0509 0.2274  0.2122  0.1171  86   ASP B C     
7862 O  O     . ASP B 87  ? 1.4874 1.3469 1.0722 0.2369  0.2304  0.1271  86   ASP B O     
7863 C  CB    . ASP B 87  ? 1.5120 1.4031 1.1613 0.2107  0.2024  0.1281  86   ASP B CB    
7864 C  CG    . ASP B 87  ? 1.4829 1.3926 1.1728 0.1983  0.1926  0.1280  86   ASP B CG    
7865 O  OD1   . ASP B 87  ? 1.5952 1.5126 1.3026 0.1936  0.1872  0.1209  86   ASP B OD1   
7866 O  OD2   . ASP B 87  ? 1.5358 1.4510 1.2386 0.1936  0.1906  0.1349  86   ASP B OD2   
7867 N  N     . GLY B 88  ? 1.4517 1.2963 1.0093 0.2270  0.1997  0.1051  87   GLY B N     
7868 C  CA    . GLY B 88  ? 1.4932 1.3157 1.0050 0.2377  0.2058  0.1021  87   GLY B CA    
7869 C  C     . GLY B 88  ? 1.4861 1.2935 0.9710 0.2338  0.1903  0.0854  87   GLY B C     
7870 O  O     . GLY B 88  ? 1.4643 1.2793 0.9630 0.2225  0.1730  0.0778  87   GLY B O     
7871 N  N     . PHE B 89  ? 1.4241 1.2094 0.8697 0.2428  0.1968  0.0797  88   PHE B N     
7872 C  CA    . PHE B 89  ? 1.4656 1.2330 0.8825 0.2387  0.1839  0.0633  88   PHE B CA    
7873 C  C     . PHE B 89  ? 1.5642 1.3115 0.9319 0.2456  0.1828  0.0591  88   PHE B C     
7874 O  O     . PHE B 89  ? 1.5434 1.2837 0.8926 0.2576  0.1979  0.0679  88   PHE B O     
7875 C  CB    . PHE B 89  ? 1.5081 1.2638 0.9237 0.2418  0.1919  0.0570  88   PHE B CB    
7876 C  CG    . PHE B 89  ? 1.6150 1.3897 1.0757 0.2347  0.1904  0.0594  88   PHE B CG    
7877 C  CD1   . PHE B 89  ? 1.6224 1.4135 1.1142 0.2402  0.2056  0.0724  88   PHE B CD1   
7878 C  CD2   . PHE B 89  ? 1.5416 1.3188 1.0137 0.2220  0.1738  0.0487  88   PHE B CD2   
7879 C  CE1   . PHE B 89  ? 1.5820 1.3915 1.1143 0.2336  0.2032  0.0743  88   PHE B CE1   
7880 C  CE2   . PHE B 89  ? 1.5361 1.3304 1.0476 0.2160  0.1723  0.0510  88   PHE B CE2   
7881 C  CZ    . PHE B 89  ? 1.5957 1.4060 1.1368 0.2219  0.1866  0.0636  88   PHE B CZ    
7882 N  N     . LEU B 90  ? 1.5671 1.3062 0.9139 0.2375  0.1646  0.0455  89   LEU B N     
7883 C  CA    . LEU B 90  ? 1.4492 1.1704 0.7483 0.2418  0.1592  0.0390  89   LEU B CA    
7884 C  C     . LEU B 90  ? 1.5587 1.2572 0.8294 0.2376  0.1528  0.0218  89   LEU B C     
7885 O  O     . LEU B 90  ? 1.5473 1.2492 0.8229 0.2245  0.1349  0.0106  89   LEU B O     
7886 C  CB    . LEU B 90  ? 1.3938 1.1292 0.6946 0.2351  0.1414  0.0392  89   LEU B CB    
7887 C  CG    . LEU B 90  ? 1.5215 1.2500 0.7871 0.2446  0.1425  0.0445  89   LEU B CG    
7888 C  CD1   . LEU B 90  ? 1.5681 1.2981 0.8397 0.2571  0.1641  0.0618  89   LEU B CD1   
7889 C  CD2   . LEU B 90  ? 1.4145 1.1596 0.6866 0.2380  0.1234  0.0446  89   LEU B CD2   
7890 N  N     . ILE B 91  ? 1.8206 1.4955 1.0619 0.2487  0.1680  0.0198  90   ILE B N     
7891 C  CA    . ILE B 91  ? 1.7618 1.4093 0.9700 0.2459  0.1637  0.0034  90   ILE B CA    
7892 C  C     . ILE B 91  ? 1.6756 1.3104 0.8402 0.2433  0.1500  -0.0067 90   ILE B C     
7893 O  O     . ILE B 91  ? 1.6995 1.3258 0.8338 0.2545  0.1575  -0.0018 90   ILE B O     
7894 C  CB    . ILE B 91  ? 1.7145 1.3397 0.9041 0.2604  0.1856  0.0049  90   ILE B CB    
7895 C  CG1   . ILE B 91  ? 1.6742 1.3181 0.9090 0.2652  0.2004  0.0180  90   ILE B CG1   
7896 C  CG2   . ILE B 91  ? 1.7796 1.3747 0.9394 0.2564  0.1813  -0.0123 90   ILE B CG2   
7897 C  CD1   . ILE B 91  ? 1.8899 1.5424 1.1583 0.2535  0.1916  0.0128  90   ILE B CD1   
7898 N  N     . VAL B 92  ? 1.5509 1.1853 0.7122 0.2282  0.1297  -0.0204 91   VAL B N     
7899 C  CA    . VAL B 92  ? 1.6729 1.3016 0.7989 0.2230  0.1129  -0.0304 91   VAL B CA    
7900 C  C     . VAL B 92  ? 1.7466 1.3459 0.8376 0.2157  0.1066  -0.0491 91   VAL B C     
7901 O  O     . VAL B 92  ? 1.6879 1.2849 0.7966 0.2044  0.1015  -0.0569 91   VAL B O     
7902 C  CB    . VAL B 92  ? 1.6094 1.2684 0.7639 0.2104  0.0925  -0.0297 91   VAL B CB    
7903 C  CG1   . VAL B 92  ? 1.6647 1.3238 0.7846 0.2097  0.0778  -0.0349 91   VAL B CG1   
7904 C  CG2   . VAL B 92  ? 1.4776 1.1633 0.6755 0.2150  0.0996  -0.0122 91   VAL B CG2   
7905 N  N     . TYR B 93  ? 1.7881 1.3638 0.8281 0.2218  0.1071  -0.0564 92   TYR B N     
7906 C  CA    . TYR B 93  ? 1.8978 1.4430 0.8983 0.2139  0.0995  -0.0755 92   TYR B CA    
7907 C  C     . TYR B 93  ? 1.9543 1.4986 0.9176 0.2094  0.0822  -0.0842 92   TYR B C     
7908 O  O     . TYR B 93  ? 1.9694 1.5309 0.9306 0.2169  0.0803  -0.0742 92   TYR B O     
7909 C  CB    . TYR B 93  ? 2.0040 1.5130 0.9725 0.2275  0.1205  -0.0781 92   TYR B CB    
7910 C  CG    . TYR B 93  ? 2.0683 1.5601 0.9907 0.2436  0.1308  -0.0757 92   TYR B CG    
7911 C  CD1   . TYR B 93  ? 2.0120 1.5160 0.9449 0.2603  0.1486  -0.0577 92   TYR B CD1   
7912 C  CD2   . TYR B 93  ? 2.1113 1.5737 0.9785 0.2415  0.1233  -0.0915 92   TYR B CD2   
7913 C  CE1   . TYR B 93  ? 1.9804 1.4684 0.8702 0.2753  0.1591  -0.0549 92   TYR B CE1   
7914 C  CE2   . TYR B 93  ? 2.1667 1.6127 0.9895 0.2567  0.1329  -0.0895 92   TYR B CE2   
7915 C  CZ    . TYR B 93  ? 2.0998 1.5588 0.9340 0.2740  0.1512  -0.0708 92   TYR B CZ    
7916 O  OH    . TYR B 93  ? 2.1697 1.6122 0.9587 0.2894  0.1617  -0.0682 92   TYR B OH    
7917 N  N     . SER B 94  ? 1.9694 1.4929 0.9027 0.1968  0.0692  -0.1028 93   SER B N     
7918 C  CA    . SER B 94  ? 2.0963 1.6196 0.9945 0.1895  0.0499  -0.1136 93   SER B CA    
7919 C  C     . SER B 94  ? 2.2905 1.7739 1.1273 0.1983  0.0578  -0.1238 93   SER B C     
7920 O  O     . SER B 94  ? 2.4593 1.9096 1.2774 0.1978  0.0672  -0.1334 93   SER B O     
7921 C  CB    . SER B 94  ? 2.0422 1.5746 0.9523 0.1660  0.0272  -0.1281 93   SER B CB    
7922 O  OG    . SER B 94  ? 2.1426 1.6817 1.0241 0.1584  0.0070  -0.1375 93   SER B OG    
7923 N  N     . VAL B 95  ? 2.1913 1.6764 0.9951 0.2072  0.0542  -0.1215 94   VAL B N     
7924 C  CA    . VAL B 95  ? 2.3277 1.7753 1.0696 0.2163  0.0610  -0.1313 94   VAL B CA    
7925 C  C     . VAL B 95  ? 2.4571 1.8841 1.1627 0.1988  0.0416  -0.1543 94   VAL B C     
7926 O  O     . VAL B 95  ? 2.4366 1.8267 1.0887 0.2038  0.0467  -0.1657 94   VAL B O     
7927 C  CB    . VAL B 95  ? 2.2416 1.6972 0.9572 0.2319  0.0634  -0.1210 94   VAL B CB    
7928 C  CG1   . VAL B 95  ? 2.1339 1.6092 0.8849 0.2480  0.0829  -0.0978 94   VAL B CG1   
7929 C  CG2   . VAL B 95  ? 2.1916 1.6739 0.9053 0.2208  0.0367  -0.1249 94   VAL B CG2   
7930 N  N     . THR B 96  ? 2.4391 1.8887 1.1717 0.1780  0.0198  -0.1615 95   THR B N     
7931 C  CA    . THR B 96  ? 2.5370 1.9697 1.2415 0.1580  0.0010  -0.1834 95   THR B CA    
7932 C  C     . THR B 96  ? 2.5577 1.9730 1.2809 0.1440  0.0036  -0.1925 95   THR B C     
7933 O  O     . THR B 96  ? 2.6447 2.0455 1.3496 0.1247  -0.0115 -0.2105 95   THR B O     
7934 C  CB    . THR B 96  ? 2.5404 2.0112 1.2587 0.1432  -0.0265 -0.1864 95   THR B CB    
7935 O  OG1   . THR B 96  ? 2.6816 2.1357 1.3674 0.1237  -0.0450 -0.2082 95   THR B OG1   
7936 C  CG2   . THR B 96  ? 2.2601 1.7694 1.0432 0.1336  -0.0324 -0.1770 95   THR B CG2   
7937 N  N     . ASP B 97  ? 2.6396 2.0560 1.3983 0.1528  0.0222  -0.1803 96   ASP B N     
7938 C  CA    . ASP B 97  ? 2.7230 2.1225 1.5005 0.1423  0.0270  -0.1864 96   ASP B CA    
7939 C  C     . ASP B 97  ? 2.7294 2.0985 1.4966 0.1622  0.0547  -0.1797 96   ASP B C     
7940 O  O     . ASP B 97  ? 2.7246 2.1130 1.5254 0.1766  0.0696  -0.1620 96   ASP B O     
7941 C  CB    . ASP B 97  ? 2.5825 2.0219 1.4227 0.1315  0.0192  -0.1774 96   ASP B CB    
7942 C  CG    . ASP B 97  ? 2.6583 2.0811 1.5182 0.1213  0.0244  -0.1825 96   ASP B CG    
7943 O  OD1   . ASP B 97  ? 2.7661 2.1678 1.6058 0.1034  0.0132  -0.1995 96   ASP B OD1   
7944 O  OD2   . ASP B 97  ? 2.5555 1.9866 1.4509 0.1308  0.0394  -0.1694 96   ASP B OD2   
7945 N  N     . LYS B 98  ? 2.5780 1.8999 1.2985 0.1631  0.0615  -0.1941 97   LYS B N     
7946 C  CA    . LYS B 98  ? 2.5665 1.8579 1.2743 0.1831  0.0882  -0.1886 97   LYS B CA    
7947 C  C     . LYS B 98  ? 2.4871 1.7884 1.2447 0.1835  0.0986  -0.1789 97   LYS B C     
7948 O  O     . LYS B 98  ? 2.4499 1.7522 1.2224 0.2027  0.1200  -0.1650 97   LYS B O     
7949 C  CB    . LYS B 98  ? 2.6228 1.8590 1.2701 0.1823  0.0919  -0.2077 97   LYS B CB    
7950 C  CG    . LYS B 98  ? 2.5643 1.7661 1.1955 0.2039  0.1198  -0.2033 97   LYS B CG    
7951 C  CD    . LYS B 98  ? 2.5859 1.7299 1.1586 0.2011  0.1225  -0.2235 97   LYS B CD    
7952 C  CE    . LYS B 98  ? 2.6598 1.7704 1.2206 0.2232  0.1505  -0.2186 97   LYS B CE    
7953 N  NZ    . LYS B 98  ? 2.7625 1.8831 1.3173 0.2497  0.1703  -0.2034 97   LYS B NZ    
7954 N  N     . ALA B 99  ? 2.5044 1.8147 1.2887 0.1623  0.0838  -0.1856 98   ALA B N     
7955 C  CA    . ALA B 99  ? 2.4555 1.7737 1.2845 0.1618  0.0924  -0.1773 98   ALA B CA    
7956 C  C     . ALA B 99  ? 2.4138 1.7756 1.2939 0.1731  0.0999  -0.1561 98   ALA B C     
7957 O  O     . ALA B 99  ? 2.3580 1.7225 1.2670 0.1827  0.1151  -0.1456 98   ALA B O     
7958 C  CB    . ALA B 99  ? 2.3802 1.7041 1.2282 0.1358  0.0735  -0.1879 98   ALA B CB    
7959 N  N     . SER B 100 ? 2.3539 1.7497 1.2454 0.1722  0.0892  -0.1495 99   SER B N     
7960 C  CA    . SER B 100 ? 2.2805 1.7150 1.2174 0.1825  0.0963  -0.1297 99   SER B CA    
7961 C  C     . SER B 100 ? 2.2746 1.6994 1.2016 0.2069  0.1209  -0.1173 99   SER B C     
7962 O  O     . SER B 100 ? 2.2511 1.7008 1.2186 0.2159  0.1319  -0.1010 99   SER B O     
7963 C  CB    . SER B 100 ? 2.2697 1.7387 1.2163 0.1764  0.0790  -0.1260 99   SER B CB    
7964 O  OG    . SER B 100 ? 2.2714 1.7253 1.1694 0.1832  0.0770  -0.1314 99   SER B OG    
7965 N  N     . PHE B 101 ? 2.3369 1.7264 1.2111 0.2176  0.1299  -0.1248 100  PHE B N     
7966 C  CA    . PHE B 101 ? 2.3407 1.7220 1.2035 0.2414  0.1541  -0.1129 100  PHE B CA    
7967 C  C     . PHE B 101 ? 2.3595 1.7228 1.2336 0.2518  0.1739  -0.1095 100  PHE B C     
7968 O  O     . PHE B 101 ? 2.3122 1.6877 1.2063 0.2689  0.1931  -0.0940 100  PHE B O     
7969 C  CB    . PHE B 101 ? 2.3288 1.6792 1.1288 0.2502  0.1571  -0.1220 100  PHE B CB    
7970 C  CG    . PHE B 101 ? 2.2106 1.5644 1.0008 0.2732  0.1780  -0.1073 100  PHE B CG    
7971 C  CD1   . PHE B 101 ? 2.2007 1.5901 1.0386 0.2813  0.1880  -0.0872 100  PHE B CD1   
7972 C  CD2   . PHE B 101 ? 2.3286 1.6493 1.0614 0.2863  0.1879  -0.1138 100  PHE B CD2   
7973 C  CE1   . PHE B 101 ? 2.1714 1.5645 1.0014 0.3012  0.2079  -0.0731 100  PHE B CE1   
7974 C  CE2   . PHE B 101 ? 2.3724 1.6968 1.0962 0.3075  0.2082  -0.0996 100  PHE B CE2   
7975 C  CZ    . PHE B 101 ? 2.2983 1.6595 1.0716 0.3146  0.2184  -0.0790 100  PHE B CZ    
7976 N  N     . GLU B 102 ? 2.4527 1.7873 1.3144 0.2421  0.1698  -0.1234 101  GLU B N     
7977 C  CA    . GLU B 102 ? 2.4239 1.7413 1.2966 0.2527  0.1879  -0.1197 101  GLU B CA    
7978 C  C     . GLU B 102 ? 2.5098 1.8654 1.4463 0.2504  0.1891  -0.1051 101  GLU B C     
7979 O  O     . GLU B 102 ? 2.6844 2.0411 1.6399 0.2653  0.2075  -0.0946 101  GLU B O     
7980 C  CB    . GLU B 102 ? 2.4876 1.7621 1.3293 0.2422  0.1829  -0.1381 101  GLU B CB    
7981 C  CG    . GLU B 102 ? 2.7594 1.9865 1.5345 0.2494  0.1886  -0.1522 101  GLU B CG    
7982 C  CD    . GLU B 102 ? 2.7118 1.9366 1.4552 0.2333  0.1671  -0.1658 101  GLU B CD    
7983 O  OE1   . GLU B 102 ? 2.7880 2.0212 1.5443 0.2102  0.1463  -0.1750 101  GLU B OE1   
7984 O  OE2   . GLU B 102 ? 2.7285 1.9442 1.4343 0.2438  0.1710  -0.1671 101  GLU B OE2   
7985 N  N     . HIS B 103 ? 2.3641 1.7518 1.3338 0.2326  0.1697  -0.1043 102  HIS B N     
7986 C  CA    . HIS B 103 ? 2.3172 1.7407 1.3458 0.2291  0.1692  -0.0917 102  HIS B CA    
7987 C  C     . HIS B 103 ? 2.2630 1.7219 1.3224 0.2412  0.1786  -0.0730 102  HIS B C     
7988 O  O     . HIS B 103 ? 2.2484 1.7392 1.3570 0.2379  0.1774  -0.0622 102  HIS B O     
7989 C  CB    . HIS B 103 ? 2.2802 1.7234 1.3319 0.2054  0.1454  -0.0984 102  HIS B CB    
7990 C  CG    . HIS B 103 ? 2.3112 1.7239 1.3424 0.1907  0.1364  -0.1150 102  HIS B CG    
7991 N  ND1   . HIS B 103 ? 2.3753 1.7619 1.3617 0.1802  0.1247  -0.1317 102  HIS B ND1   
7992 C  CD2   . HIS B 103 ? 2.2725 1.6759 1.3212 0.1843  0.1374  -0.1172 102  HIS B CD2   
7993 C  CE1   . HIS B 103 ? 2.3237 1.6856 1.3015 0.1670  0.1192  -0.1437 102  HIS B CE1   
7994 N  NE2   . HIS B 103 ? 2.2704 1.6413 1.2850 0.1697  0.1271  -0.1348 102  HIS B NE2   
7995 N  N     . VAL B 104 ? 2.2948 1.7482 1.3260 0.2547  0.1881  -0.0690 103  VAL B N     
7996 C  CA    . VAL B 104 ? 2.2497 1.7348 1.3086 0.2655  0.1979  -0.0508 103  VAL B CA    
7997 C  C     . VAL B 104 ? 2.3098 1.8038 1.4003 0.2789  0.2182  -0.0378 103  VAL B C     
7998 O  O     . VAL B 104 ? 2.2182 1.7464 1.3571 0.2769  0.2187  -0.0250 103  VAL B O     
7999 C  CB    . VAL B 104 ? 2.2639 1.7378 1.2812 0.2774  0.2047  -0.0494 103  VAL B CB    
8000 C  CG1   . VAL B 104 ? 2.1274 1.6300 1.1719 0.2898  0.2189  -0.0294 103  VAL B CG1   
8001 C  CG2   . VAL B 104 ? 2.2084 1.6825 1.2018 0.2637  0.1825  -0.0600 103  VAL B CG2   
8002 N  N     . ASP B 105 ? 2.6175 2.0811 1.6810 0.2930  0.2349  -0.0410 104  ASP B N     
8003 C  CA    . ASP B 105 ? 2.6244 2.0971 1.7179 0.3063  0.2535  -0.0292 104  ASP B CA    
8004 C  C     . ASP B 105 ? 2.6331 2.1137 1.7619 0.2953  0.2453  -0.0312 104  ASP B C     
8005 O  O     . ASP B 105 ? 2.6770 2.1752 1.8412 0.3036  0.2568  -0.0198 104  ASP B O     
8006 C  CB    . ASP B 105 ? 2.7423 2.1795 1.7955 0.3262  0.2743  -0.0321 104  ASP B CB    
8007 C  CG    . ASP B 105 ? 2.8090 2.2007 1.8169 0.3207  0.2675  -0.0516 104  ASP B CG    
8008 O  OD1   . ASP B 105 ? 2.7805 2.1699 1.7906 0.3006  0.2468  -0.0625 104  ASP B OD1   
8009 O  OD2   . ASP B 105 ? 2.9140 2.2717 1.8837 0.3365  0.2833  -0.0560 104  ASP B OD2   
8010 N  N     . ARG B 106 ? 2.4155 1.8847 1.5356 0.2768  0.2257  -0.0451 105  ARG B N     
8011 C  CA    . ARG B 106 ? 2.3318 1.8117 1.4870 0.2647  0.2165  -0.0461 105  ARG B CA    
8012 C  C     . ARG B 106 ? 2.2183 1.7450 1.4279 0.2579  0.2099  -0.0332 105  ARG B C     
8013 O  O     . ARG B 106 ? 2.2901 1.8344 1.5381 0.2584  0.2132  -0.0256 105  ARG B O     
8014 C  CB    . ARG B 106 ? 2.3411 1.7990 1.4732 0.2454  0.1973  -0.0638 105  ARG B CB    
8015 C  CG    . ARG B 106 ? 2.3179 1.7832 1.4814 0.2315  0.1873  -0.0661 105  ARG B CG    
8016 C  CD    . ARG B 106 ? 2.2414 1.7427 1.4387 0.2133  0.1678  -0.0647 105  ARG B CD    
8017 N  NE    . ARG B 106 ? 2.4242 1.9242 1.6370 0.1966  0.1552  -0.0719 105  ARG B NE    
8018 C  CZ    . ARG B 106 ? 2.4092 1.9228 1.6580 0.1967  0.1584  -0.0647 105  ARG B CZ    
8019 N  NH1   . ARG B 106 ? 2.3326 1.8632 1.6074 0.2122  0.1732  -0.0505 105  ARG B NH1   
8020 N  NH2   . ARG B 106 ? 2.4147 1.9256 1.6737 0.1806  0.1464  -0.0718 105  ARG B NH2   
8021 N  N     . PHE B 107 ? 2.1691 1.7158 1.3817 0.2518  0.2005  -0.0306 106  PHE B N     
8022 C  CA    . PHE B 107 ? 2.0473 1.6355 1.3077 0.2473  0.1963  -0.0176 106  PHE B CA    
8023 C  C     . PHE B 107 ? 2.0478 1.6535 1.3284 0.2638  0.2161  -0.0009 106  PHE B C     
8024 O  O     . PHE B 107 ? 1.9478 1.5856 1.2734 0.2612  0.2161  0.0103  106  PHE B O     
8025 C  CB    . PHE B 107 ? 1.9226 1.5245 1.1777 0.2368  0.1803  -0.0198 106  PHE B CB    
8026 C  CG    . PHE B 107 ? 1.8703 1.4685 1.1205 0.2178  0.1586  -0.0336 106  PHE B CG    
8027 C  CD1   . PHE B 107 ? 1.8757 1.4969 1.1661 0.2047  0.1472  -0.0325 106  PHE B CD1   
8028 C  CD2   . PHE B 107 ? 1.8861 1.4592 1.0915 0.2126  0.1494  -0.0476 106  PHE B CD2   
8029 C  CE1   . PHE B 107 ? 1.8665 1.4864 1.1537 0.1871  0.1281  -0.0446 106  PHE B CE1   
8030 C  CE2   . PHE B 107 ? 1.8492 1.4217 1.0520 0.1940  0.1293  -0.0601 106  PHE B CE2   
8031 C  CZ    . PHE B 107 ? 1.8801 1.4766 1.1245 0.1814  0.1191  -0.0583 106  PHE B CZ    
8032 N  N     . HIS B 108 ? 2.1178 1.7034 1.3658 0.2803  0.2330  0.0007  107  HIS B N     
8033 C  CA    . HIS B 108 ? 2.1160 1.7198 1.3825 0.2957  0.2527  0.0171  107  HIS B CA    
8034 C  C     . HIS B 108 ? 2.1020 1.7174 1.4028 0.3026  0.2640  0.0247  107  HIS B C     
8035 O  O     . HIS B 108 ? 2.0345 1.6825 1.3768 0.3048  0.2704  0.0388  107  HIS B O     
8036 C  CB    . HIS B 108 ? 2.1912 1.7699 1.4115 0.3121  0.2684  0.0166  107  HIS B CB    
8037 C  CG    . HIS B 108 ? 2.1386 1.7365 1.3757 0.3276  0.2894  0.0337  107  HIS B CG    
8038 N  ND1   . HIS B 108 ? 2.1520 1.7455 1.3919 0.3445  0.3101  0.0399  107  HIS B ND1   
8039 C  CD2   . HIS B 108 ? 2.0784 1.7004 1.3308 0.3286  0.2933  0.0465  107  HIS B CD2   
8040 C  CE1   . HIS B 108 ? 2.1956 1.8119 1.4533 0.3544  0.3259  0.0556  107  HIS B CE1   
8041 N  NE2   . HIS B 108 ? 2.1484 1.7809 1.4134 0.3446  0.3162  0.0599  107  HIS B NE2   
8042 N  N     . GLN B 109 ? 2.2002 1.7892 1.4841 0.3061  0.2664  0.0156  108  GLN B N     
8043 C  CA    . GLN B 109 ? 2.2040 1.8038 1.5192 0.3139  0.2764  0.0229  108  GLN B CA    
8044 C  C     . GLN B 109 ? 2.1753 1.8028 1.5362 0.2981  0.2613  0.0250  108  GLN B C     
8045 O  O     . GLN B 109 ? 2.2609 1.9120 1.6599 0.3028  0.2680  0.0354  108  GLN B O     
8046 C  CB    . GLN B 109 ? 2.3878 1.9482 1.6690 0.3232  0.2836  0.0130  108  GLN B CB    
8047 C  CG    . GLN B 109 ? 2.4748 2.0097 1.7368 0.3068  0.2655  -0.0034 108  GLN B CG    
8048 C  CD    . GLN B 109 ? 2.6594 2.1529 1.8883 0.3163  0.2741  -0.0124 108  GLN B CD    
8049 O  OE1   . GLN B 109 ? 2.6674 2.1447 1.8756 0.3362  0.2932  -0.0090 108  GLN B OE1   
8050 N  NE2   . GLN B 109 ? 2.6350 2.1106 1.8585 0.3024  0.2606  -0.0235 108  GLN B NE2   
8051 N  N     . LEU B 110 ? 2.1100 1.7361 1.4677 0.2797  0.2409  0.0154  109  LEU B N     
8052 C  CA    . LEU B 110 ? 2.0323 1.6859 1.4326 0.2648  0.2266  0.0175  109  LEU B CA    
8053 C  C     . LEU B 110 ? 1.9724 1.6649 1.4118 0.2639  0.2283  0.0317  109  LEU B C     
8054 O  O     . LEU B 110 ? 1.9819 1.7005 1.4626 0.2631  0.2298  0.0403  109  LEU B O     
8055 C  CB    . LEU B 110 ? 1.9976 1.6418 1.3841 0.2460  0.2053  0.0040  109  LEU B CB    
8056 C  CG    . LEU B 110 ? 2.0211 1.6464 1.4027 0.2372  0.1969  -0.0067 109  LEU B CG    
8057 C  CD1   . LEU B 110 ? 2.2207 1.8050 1.5609 0.2487  0.2086  -0.0141 109  LEU B CD1   
8058 C  CD2   . LEU B 110 ? 1.9756 1.6003 1.3512 0.2171  0.1756  -0.0180 109  LEU B CD2   
8059 N  N     . ILE B 111 ? 1.9631 1.6590 1.3891 0.2640  0.2280  0.0341  110  ILE B N     
8060 C  CA    . ILE B 111 ? 1.9045 1.6334 1.3645 0.2624  0.2299  0.0474  110  ILE B CA    
8061 C  C     . ILE B 111 ? 1.9399 1.6847 1.4225 0.2766  0.2500  0.0614  110  ILE B C     
8062 O  O     . ILE B 111 ? 1.8946 1.6702 1.4203 0.2729  0.2507  0.0717  110  ILE B O     
8063 C  CB    . ILE B 111 ? 1.8292 1.5542 1.2645 0.2615  0.2267  0.0475  110  ILE B CB    
8064 C  CG1   . ILE B 111 ? 1.8101 1.5269 1.2303 0.2463  0.2049  0.0346  110  ILE B CG1   
8065 C  CG2   . ILE B 111 ? 1.6919 1.4466 1.1591 0.2614  0.2316  0.0625  110  ILE B CG2   
8066 C  CD1   . ILE B 111 ? 1.7973 1.5086 1.1891 0.2463  0.2002  0.0337  110  ILE B CD1   
8067 N  N     . LEU B 112 ? 2.1173 1.8418 1.5713 0.2929  0.2668  0.0619  111  LEU B N     
8068 C  CA    . LEU B 112 ? 2.0854 1.8267 1.5602 0.3076  0.2872  0.0757  111  LEU B CA    
8069 C  C     . LEU B 112 ? 2.1243 1.8809 1.6341 0.3085  0.2882  0.0787  111  LEU B C     
8070 O  O     . LEU B 112 ? 2.1926 1.9795 1.7400 0.3127  0.2975  0.0917  111  LEU B O     
8071 C  CB    . LEU B 112 ? 2.1281 1.8425 1.5610 0.3260  0.3053  0.0746  111  LEU B CB    
8072 C  CG    . LEU B 112 ? 2.2460 1.9780 1.6943 0.3430  0.3288  0.0898  111  LEU B CG    
8073 C  CD1   . LEU B 112 ? 2.1155 1.8270 1.5211 0.3557  0.3427  0.0906  111  LEU B CD1   
8074 C  CD2   . LEU B 112 ? 2.2058 1.9370 1.6652 0.3556  0.3397  0.0915  111  LEU B CD2   
8075 N  N     . ARG B 113 ? 2.0370 1.7736 1.5351 0.3042  0.2785  0.0672  112  ARG B N     
8076 C  CA    . ARG B 113 ? 2.0190 1.7684 1.5477 0.3057  0.2786  0.0702  112  ARG B CA    
8077 C  C     . ARG B 113 ? 1.9154 1.6960 1.4873 0.2888  0.2631  0.0731  112  ARG B C     
8078 O  O     . ARG B 113 ? 1.9300 1.7393 1.5412 0.2908  0.2670  0.0829  112  ARG B O     
8079 C  CB    . ARG B 113 ? 2.1093 1.8231 1.6076 0.3076  0.2751  0.0575  112  ARG B CB    
8080 C  CG    . ARG B 113 ? 2.1249 1.8490 1.6520 0.3053  0.2702  0.0587  112  ARG B CG    
8081 C  CD    . ARG B 113 ? 2.2292 1.9145 1.7231 0.3125  0.2730  0.0489  112  ARG B CD    
8082 N  NE    . ARG B 113 ? 2.3116 1.9612 1.7622 0.3030  0.2633  0.0338  112  ARG B NE    
8083 C  CZ    . ARG B 113 ? 2.2233 1.8658 1.6722 0.2846  0.2449  0.0237  112  ARG B CZ    
8084 N  NH1   . ARG B 113 ? 2.1968 1.8637 1.6829 0.2740  0.2343  0.0268  112  ARG B NH1   
8085 N  NH2   . ARG B 113 ? 2.2146 1.8258 1.6233 0.2766  0.2371  0.0101  112  ARG B NH2   
8086 N  N     . VAL B 114 ? 1.9432 1.7192 1.5082 0.2725  0.2454  0.0645  113  VAL B N     
8087 C  CA    . VAL B 114 ? 1.8328 1.6364 1.4361 0.2570  0.2307  0.0665  113  VAL B CA    
8088 C  C     . VAL B 114 ? 1.8653 1.7016 1.5020 0.2570  0.2367  0.0801  113  VAL B C     
8089 O  O     . VAL B 114 ? 1.8399 1.7042 1.5168 0.2515  0.2335  0.0866  113  VAL B O     
8090 C  CB    . VAL B 114 ? 1.7381 1.5302 1.3250 0.2412  0.2117  0.0547  113  VAL B CB    
8091 C  CG1   . VAL B 114 ? 1.7150 1.5359 1.3400 0.2266  0.1980  0.0575  113  VAL B CG1   
8092 C  CG2   . VAL B 114 ? 1.6842 1.4469 1.2445 0.2382  0.2049  0.0416  113  VAL B CG2   
8093 N  N     . LYS B 115 ? 1.8826 1.7152 1.5022 0.2627  0.2457  0.0847  114  LYS B N     
8094 C  CA    . LYS B 115 ? 1.9317 1.7925 1.5806 0.2636  0.2544  0.0987  114  LYS B CA    
8095 C  C     . LYS B 115 ? 1.9669 1.8450 1.6383 0.2765  0.2719  0.1097  114  LYS B C     
8096 O  O     . LYS B 115 ? 1.9547 1.8633 1.6632 0.2737  0.2763  0.1210  114  LYS B O     
8097 C  CB    . LYS B 115 ? 1.9016 1.7518 1.5232 0.2672  0.2605  0.1013  114  LYS B CB    
8098 C  CG    . LYS B 115 ? 1.7373 1.5835 1.3498 0.2538  0.2434  0.0953  114  LYS B CG    
8099 C  CD    . LYS B 115 ? 1.6964 1.5720 1.3508 0.2420  0.2366  0.1031  114  LYS B CD    
8100 C  CE    . LYS B 115 ? 1.6364 1.5082 1.2822 0.2303  0.2198  0.0974  114  LYS B CE    
8101 N  NZ    . LYS B 115 ? 1.5921 1.4892 1.2762 0.2198  0.2142  0.1049  114  LYS B NZ    
8102 N  N     . ASP B 116 ? 1.9906 1.8499 1.6404 0.2905  0.2819  0.1065  115  ASP B N     
8103 C  CA    . ASP B 116 ? 2.0302 1.9048 1.6983 0.3055  0.2994  0.1168  115  ASP B CA    
8104 C  C     . ASP B 116 ? 1.9742 1.8682 1.6536 0.3120  0.3157  0.1303  115  ASP B C     
8105 O  O     . ASP B 116 ? 1.9244 1.8517 1.6436 0.3129  0.3230  0.1423  115  ASP B O     
8106 C  CB    . ASP B 116 ? 2.1650 2.0667 1.8762 0.3003  0.2926  0.1203  115  ASP B CB    
8107 C  CG    . ASP B 116 ? 2.1701 2.0810 1.8926 0.3178  0.3081  0.1275  115  ASP B CG    
8108 O  OD1   . ASP B 116 ? 2.1521 2.0358 1.8469 0.3285  0.3113  0.1206  115  ASP B OD1   
8109 O  OD2   . ASP B 116 ? 2.1603 2.1057 1.9193 0.3209  0.3172  0.1403  115  ASP B OD2   
8110 N  N     . ARG B 117 ? 2.0268 1.8999 1.6702 0.3159  0.3212  0.1285  116  ARG B N     
8111 C  CA    . ARG B 117 ? 2.0144 1.9002 1.6606 0.3226  0.3377  0.1411  116  ARG B CA    
8112 C  C     . ARG B 117 ? 2.0683 1.9249 1.6677 0.3402  0.3533  0.1386  116  ARG B C     
8113 O  O     . ARG B 117 ? 2.0669 1.8906 1.6287 0.3441  0.3484  0.1258  116  ARG B O     
8114 C  CB    . ARG B 117 ? 2.0017 1.8938 1.6521 0.3082  0.3283  0.1434  116  ARG B CB    
8115 C  CG    . ARG B 117 ? 1.9859 1.9067 1.6822 0.2913  0.3149  0.1467  116  ARG B CG    
8116 C  CD    . ARG B 117 ? 1.9695 1.9260 1.7105 0.2940  0.3274  0.1606  116  ARG B CD    
8117 N  NE    . ARG B 117 ? 2.0331 2.0159 1.8161 0.2772  0.3145  0.1634  116  ARG B NE    
8118 C  CZ    . ARG B 117 ? 1.9991 2.0159 1.8254 0.2744  0.3209  0.1746  116  ARG B CZ    
8119 N  NH1   . ARG B 117 ? 1.9834 2.0155 1.8201 0.2875  0.3403  0.1849  116  ARG B NH1   
8120 N  NH2   . ARG B 117 ? 1.8637 1.9002 1.7237 0.2581  0.3076  0.1752  116  ARG B NH2   
8121 N  N     . GLU B 118 ? 2.1336 2.0020 1.7351 0.3503  0.3726  0.1511  117  GLU B N     
8122 C  CA    . GLU B 118 ? 2.1585 2.0000 1.7143 0.3677  0.3888  0.1497  117  GLU B CA    
8123 C  C     . GLU B 118 ? 2.1908 2.0016 1.7014 0.3621  0.3788  0.1398  117  GLU B C     
8124 O  O     . GLU B 118 ? 2.1949 1.9727 1.6583 0.3731  0.3839  0.1312  117  GLU B O     
8125 C  CB    . GLU B 118 ? 2.1913 2.0558 1.7626 0.3790  0.4124  0.1666  117  GLU B CB    
8126 C  CG    . GLU B 118 ? 2.2748 2.1510 1.8518 0.3695  0.4132  0.1757  117  GLU B CG    
8127 C  CD    . GLU B 118 ? 2.2727 2.1748 1.8931 0.3488  0.3965  0.1787  117  GLU B CD    
8128 O  OE1   . GLU B 118 ? 2.1844 2.1100 1.8444 0.3441  0.3919  0.1804  117  GLU B OE1   
8129 O  OE2   . GLU B 118 ? 2.2025 2.1006 1.8161 0.3377  0.3879  0.1792  117  GLU B OE2   
8130 N  N     . SER B 119 ? 2.1711 1.9920 1.6946 0.3457  0.3642  0.1406  118  SER B N     
8131 C  CA    . SER B 119 ? 2.1010 1.8982 1.5864 0.3396  0.3527  0.1324  118  SER B CA    
8132 C  C     . SER B 119 ? 1.9719 1.7877 1.4860 0.3208  0.3351  0.1342  118  SER B C     
8133 O  O     . SER B 119 ? 1.9408 1.7868 1.5010 0.3139  0.3357  0.1437  118  SER B O     
8134 C  CB    . SER B 119 ? 2.0828 1.8690 1.5355 0.3520  0.3697  0.1395  118  SER B CB    
8135 O  OG    . SER B 119 ? 2.1106 1.9261 1.5963 0.3516  0.3824  0.1568  118  SER B OG    
8136 N  N     . PHE B 120 ? 1.8807 1.6785 1.3668 0.3130  0.3194  0.1247  119  PHE B N     
8137 C  CA    . PHE B 120 ? 1.7712 1.5830 1.2792 0.2966  0.3020  0.1251  119  PHE B CA    
8138 C  C     . PHE B 120 ? 1.7501 1.5438 1.2196 0.2958  0.2950  0.1217  119  PHE B C     
8139 O  O     . PHE B 120 ? 1.6948 1.4618 1.1194 0.3038  0.2962  0.1129  119  PHE B O     
8140 C  CB    . PHE B 120 ? 1.7471 1.5611 1.2721 0.2841  0.2823  0.1135  119  PHE B CB    
8141 C  CG    . PHE B 120 ? 1.6761 1.5128 1.2378 0.2686  0.2684  0.1168  119  PHE B CG    
8142 C  CD1   . PHE B 120 ? 1.6366 1.5019 1.2441 0.2649  0.2744  0.1282  119  PHE B CD1   
8143 C  CD2   . PHE B 120 ? 1.6555 1.4854 1.2056 0.2580  0.2493  0.1085  119  PHE B CD2   
8144 C  CE1   . PHE B 120 ? 1.6150 1.4984 1.2538 0.2508  0.2619  0.1305  119  PHE B CE1   
8145 C  CE2   . PHE B 120 ? 1.6398 1.4890 1.2221 0.2451  0.2374  0.1114  119  PHE B CE2   
8146 C  CZ    . PHE B 120 ? 1.6462 1.5207 1.2719 0.2415  0.2438  0.1222  119  PHE B CZ    
8147 N  N     . PRO B 121 ? 1.7044 1.5112 1.1891 0.2870  0.2880  0.1286  120  PRO B N     
8148 C  CA    . PRO B 121 ? 1.6623 1.4536 1.1113 0.2867  0.2798  0.1259  120  PRO B CA    
8149 C  C     . PRO B 121 ? 1.6335 1.4038 1.0496 0.2828  0.2618  0.1082  120  PRO B C     
8150 O  O     . PRO B 121 ? 1.6643 1.4411 1.0974 0.2704  0.2437  0.0999  120  PRO B O     
8151 C  CB    . PRO B 121 ? 1.6731 1.4843 1.1540 0.2752  0.2711  0.1341  120  PRO B CB    
8152 C  CG    . PRO B 121 ? 1.6823 1.5169 1.2065 0.2746  0.2852  0.1469  120  PRO B CG    
8153 C  CD    . PRO B 121 ? 1.6888 1.5245 1.2218 0.2790  0.2905  0.1411  120  PRO B CD    
8154 N  N     . MET B 122 ? 1.6533 1.3984 1.0216 0.2930  0.2669  0.1023  121  MET B N     
8155 C  CA    . MET B 122 ? 1.6770 1.4002 1.0090 0.2892  0.2507  0.0852  121  MET B CA    
8156 C  C     . MET B 122 ? 1.6903 1.3957 0.9747 0.2970  0.2520  0.0849  121  MET B C     
8157 O  O     . MET B 122 ? 1.6979 1.4005 0.9695 0.3093  0.2702  0.0960  121  MET B O     
8158 C  CB    . MET B 122 ? 1.7232 1.4277 1.0406 0.2935  0.2550  0.0741  121  MET B CB    
8159 C  CG    . MET B 122 ? 1.6687 1.3887 1.0288 0.2870  0.2533  0.0738  121  MET B CG    
8160 S  SD    . MET B 122 ? 1.8991 1.5958 1.2408 0.2977  0.2653  0.0656  121  MET B SD    
8161 C  CE    . MET B 122 ? 1.7230 1.4226 1.0599 0.3178  0.2945  0.0811  121  MET B CE    
8162 N  N     . ILE B 123 ? 1.6771 1.3717 0.9356 0.2898  0.2324  0.0723  122  ILE B N     
8163 C  CA    . ILE B 123 ? 1.7169 1.3935 0.9262 0.2965  0.2301  0.0694  122  ILE B CA    
8164 C  C     . ILE B 123 ? 1.7460 1.4014 0.9210 0.2906  0.2141  0.0496  122  ILE B C     
8165 O  O     . ILE B 123 ? 1.6259 1.2893 0.8178 0.2766  0.1953  0.0403  122  ILE B O     
8166 C  CB    . ILE B 123 ? 1.6792 1.3706 0.8941 0.2931  0.2205  0.0781  122  ILE B CB    
8167 C  CG1   . ILE B 123 ? 1.6315 1.3371 0.8696 0.3003  0.2393  0.0981  122  ILE B CG1   
8168 C  CG2   . ILE B 123 ? 1.5628 1.2363 0.7253 0.2978  0.2121  0.0715  122  ILE B CG2   
8169 C  CD1   . ILE B 123 ? 1.6004 1.3139 0.8352 0.3001  0.2334  0.1080  122  ILE B CD1   
8170 N  N     . LEU B 124 ? 1.7259 1.3542 0.8525 0.3009  0.2220  0.0430  123  LEU B N     
8171 C  CA    . LEU B 124 ? 1.7329 1.3377 0.8218 0.2950  0.2075  0.0236  123  LEU B CA    
8172 C  C     . LEU B 124 ? 1.6926 1.2984 0.7546 0.2904  0.1894  0.0192  123  LEU B C     
8173 O  O     . LEU B 124 ? 1.8280 1.4345 0.8710 0.3002  0.1958  0.0290  123  LEU B O     
8174 C  CB    . LEU B 124 ? 1.7456 1.3184 0.7921 0.3082  0.2237  0.0175  123  LEU B CB    
8175 C  CG    . LEU B 124 ? 1.7817 1.3252 0.7886 0.3016  0.2111  -0.0037 123  LEU B CG    
8176 C  CD1   . LEU B 124 ? 1.8084 1.3591 0.8475 0.2853  0.1969  -0.0127 123  LEU B CD1   
8177 C  CD2   . LEU B 124 ? 1.8901 1.4009 0.8582 0.3164  0.2302  -0.0084 123  LEU B CD2   
8178 N  N     . VAL B 125 ? 1.6945 1.3014 0.7553 0.2756  0.1669  0.0051  124  VAL B N     
8179 C  CA    . VAL B 125 ? 1.7235 1.3373 0.7657 0.2695  0.1467  0.0005  124  VAL B CA    
8180 C  C     . VAL B 125 ? 1.8188 1.4079 0.8164 0.2633  0.1338  -0.0196 124  VAL B C     
8181 O  O     . VAL B 125 ? 1.7912 1.3755 0.7982 0.2506  0.1243  -0.0323 124  VAL B O     
8182 C  CB    . VAL B 125 ? 1.6951 1.3396 0.7824 0.2560  0.1295  0.0031  124  VAL B CB    
8183 C  CG1   . VAL B 125 ? 1.6660 1.3184 0.7329 0.2504  0.1078  -0.0028 124  VAL B CG1   
8184 C  CG2   . VAL B 125 ? 1.6583 1.3248 0.7864 0.2616  0.1418  0.0225  124  VAL B CG2   
8185 N  N     . ALA B 126 ? 1.9051 1.4781 0.8535 0.2717  0.1335  -0.0224 125  ALA B N     
8186 C  CA    . ALA B 126 ? 2.0111 1.5617 0.9134 0.2649  0.1190  -0.0418 125  ALA B CA    
8187 C  C     . ALA B 126 ? 2.0728 1.6453 0.9764 0.2541  0.0935  -0.0455 125  ALA B C     
8188 O  O     . ALA B 126 ? 1.9673 1.5479 0.8535 0.2624  0.0908  -0.0375 125  ALA B O     
8189 C  CB    . ALA B 126 ? 1.9489 1.4694 0.7949 0.2803  0.1326  -0.0437 125  ALA B CB    
8190 N  N     . ASN B 127 ? 1.8380 1.4209 0.7624 0.2361  0.0750  -0.0570 126  ASN B N     
8191 C  CA    . ASN B 127 ? 1.8190 1.4281 0.7532 0.2251  0.0507  -0.0600 126  ASN B CA    
8192 C  C     . ASN B 127 ? 1.8739 1.4681 0.7618 0.2165  0.0327  -0.0787 126  ASN B C     
8193 O  O     . ASN B 127 ? 1.9568 1.5186 0.8085 0.2160  0.0379  -0.0913 126  ASN B O     
8194 C  CB    . ASN B 127 ? 1.8500 1.4837 0.8378 0.2102  0.0410  -0.0604 126  ASN B CB    
8195 C  CG    . ASN B 127 ? 1.7868 1.4550 0.7977 0.2046  0.0222  -0.0556 126  ASN B CG    
8196 O  OD1   . ASN B 127 ? 1.7119 1.3894 0.7108 0.2154  0.0215  -0.0455 126  ASN B OD1   
8197 N  ND2   . ASN B 127 ? 1.7412 1.4284 0.7847 0.1884  0.0073  -0.0624 126  ASN B ND2   
8198 N  N     . LYS B 128 ? 1.8837 1.5024 0.7727 0.2100  0.0112  -0.0802 127  LYS B N     
8199 C  CA    . LYS B 128 ? 1.9400 1.5536 0.7923 0.1990  -0.0102 -0.0977 127  LYS B CA    
8200 C  C     . LYS B 128 ? 2.0159 1.6014 0.8065 0.2113  -0.0048 -0.1018 127  LYS B C     
8201 O  O     . LYS B 128 ? 2.0714 1.6349 0.8225 0.2030  -0.0141 -0.1197 127  LYS B O     
8202 C  CB    . LYS B 128 ? 1.9797 1.5809 0.8361 0.1794  -0.0186 -0.1160 127  LYS B CB    
8203 C  CG    . LYS B 128 ? 1.9426 1.5730 0.8545 0.1646  -0.0284 -0.1148 127  LYS B CG    
8204 C  CD    . LYS B 128 ? 1.9637 1.5814 0.8706 0.1438  -0.0400 -0.1343 127  LYS B CD    
8205 C  CE    . LYS B 128 ? 1.7098 1.3563 0.6701 0.1287  -0.0495 -0.1334 127  LYS B CE    
8206 N  NZ    . LYS B 128 ? 1.7236 1.3574 0.6773 0.1073  -0.0610 -0.1520 127  LYS B NZ    
8207 N  N     . VAL B 129 ? 1.9738 1.5590 0.7546 0.2307  0.0102  -0.0854 128  VAL B N     
8208 C  CA    . VAL B 129 ? 2.0136 1.5733 0.7344 0.2436  0.0156  -0.0882 128  VAL B CA    
8209 C  C     . VAL B 129 ? 2.0931 1.6678 0.7859 0.2411  -0.0080 -0.0932 128  VAL B C     
8210 O  O     . VAL B 129 ? 2.3635 1.9179 1.0021 0.2496  -0.0079 -0.0982 128  VAL B O     
8211 C  CB    . VAL B 129 ? 1.9955 1.5482 0.7133 0.2655  0.0417  -0.0685 128  VAL B CB    
8212 C  CG1   . VAL B 129 ? 1.9392 1.4951 0.7051 0.2667  0.0610  -0.0583 128  VAL B CG1   
8213 C  CG2   . VAL B 129 ? 1.9798 1.5576 0.7013 0.2751  0.0361  -0.0526 128  VAL B CG2   
8214 N  N     . ASP B 130 ? 2.0187 1.6289 0.7460 0.2301  -0.0284 -0.0921 129  ASP B N     
8215 C  CA    . ASP B 130 ? 1.9893 1.6173 0.6932 0.2258  -0.0536 -0.0986 129  ASP B CA    
8216 C  C     . ASP B 130 ? 2.1369 1.7492 0.8072 0.2088  -0.0707 -0.1230 129  ASP B C     
8217 O  O     . ASP B 130 ? 2.2707 1.8945 0.9139 0.2048  -0.0918 -0.1307 129  ASP B O     
8218 C  CB    . ASP B 130 ? 2.0181 1.6898 0.7717 0.2191  -0.0698 -0.0907 129  ASP B CB    
8219 C  CG    . ASP B 130 ? 2.0324 1.7156 0.8321 0.1998  -0.0754 -0.0989 129  ASP B CG    
8220 O  OD1   . ASP B 130 ? 1.9591 1.6191 0.7667 0.1969  -0.0593 -0.1023 129  ASP B OD1   
8221 O  OD2   . ASP B 130 ? 2.0159 1.7317 0.8435 0.1883  -0.0956 -0.1015 129  ASP B OD2   
8222 N  N     . LEU B 131 ? 2.1738 1.7601 0.8449 0.1987  -0.0623 -0.1351 130  LEU B N     
8223 C  CA    . LEU B 131 ? 2.2915 1.8579 0.9306 0.1811  -0.0768 -0.1587 130  LEU B CA    
8224 C  C     . LEU B 131 ? 2.4281 1.9454 1.0143 0.1898  -0.0595 -0.1672 130  LEU B C     
8225 O  O     . LEU B 131 ? 2.4911 1.9807 1.0753 0.1812  -0.0515 -0.1784 130  LEU B O     
8226 C  CB    . LEU B 131 ? 2.2528 1.8273 0.9344 0.1599  -0.0834 -0.1675 130  LEU B CB    
8227 C  CG    . LEU B 131 ? 2.1558 1.7780 0.8937 0.1510  -0.0982 -0.1594 130  LEU B CG    
8228 C  CD1   . LEU B 131 ? 2.0483 1.6729 0.8276 0.1332  -0.0982 -0.1657 130  LEU B CD1   
8229 C  CD2   . LEU B 131 ? 2.0947 1.7447 0.8192 0.1420  -0.1265 -0.1670 130  LEU B CD2   
8230 N  N     . MET B 132 ? 2.4189 1.9241 0.9610 0.2078  -0.0529 -0.1617 131  MET B N     
8231 C  CA    . MET B 132 ? 2.5255 1.9843 1.0153 0.2186  -0.0348 -0.1687 131  MET B CA    
8232 C  C     . MET B 132 ? 2.5760 2.0065 1.0191 0.2028  -0.0498 -0.1946 131  MET B C     
8233 O  O     . MET B 132 ? 2.6612 2.0485 1.0672 0.2072  -0.0349 -0.2042 131  MET B O     
8234 C  CB    . MET B 132 ? 2.7268 2.1814 1.1807 0.2420  -0.0238 -0.1553 131  MET B CB    
8235 C  CG    . MET B 132 ? 2.6792 2.1549 1.1739 0.2584  -0.0052 -0.1295 131  MET B CG    
8236 S  SD    . MET B 132 ? 2.7448 2.2094 1.1933 0.2858  0.0114  -0.1136 131  MET B SD    
8237 C  CE    . MET B 132 ? 2.3385 1.8184 0.7462 0.2805  -0.0206 -0.1235 131  MET B CE    
8238 N  N     . HIS B 133 ? 2.5836 2.0372 1.0275 0.1845  -0.0788 -0.2062 132  HIS B N     
8239 C  CA    . HIS B 133 ? 2.6198 2.0484 1.0233 0.1658  -0.0948 -0.2316 132  HIS B CA    
8240 C  C     . HIS B 133 ? 2.6272 2.0328 1.0499 0.1494  -0.0890 -0.2435 132  HIS B C     
8241 O  O     . HIS B 133 ? 2.6116 1.9845 0.9960 0.1358  -0.0959 -0.2646 132  HIS B O     
8242 C  CB    . HIS B 133 ? 2.5727 2.0380 0.9792 0.1492  -0.1278 -0.2397 132  HIS B CB    
8243 C  CG    . HIS B 133 ? 2.6416 2.1519 1.1154 0.1359  -0.1397 -0.2326 132  HIS B CG    
8244 N  ND1   . HIS B 133 ? 2.5755 2.1252 1.0908 0.1482  -0.1380 -0.2111 132  HIS B ND1   
8245 C  CD2   . HIS B 133 ? 2.6640 2.1851 1.1697 0.1114  -0.1527 -0.2441 132  HIS B CD2   
8246 C  CE1   . HIS B 133 ? 2.5331 2.1160 1.1024 0.1327  -0.1496 -0.2100 132  HIS B CE1   
8247 N  NE2   . HIS B 133 ? 2.5736 2.1410 1.1388 0.1102  -0.1585 -0.2295 132  HIS B NE2   
8248 N  N     . LEU B 134 ? 2.6380 2.0590 1.1177 0.1503  -0.0767 -0.2305 133  LEU B N     
8249 C  CA    . LEU B 134 ? 2.7153 2.1135 1.2144 0.1381  -0.0680 -0.2387 133  LEU B CA    
8250 C  C     . LEU B 134 ? 2.6693 2.0565 1.1934 0.1566  -0.0382 -0.2222 133  LEU B C     
8251 O  O     . LEU B 134 ? 2.6378 2.0217 1.1975 0.1489  -0.0310 -0.2219 133  LEU B O     
8252 C  CB    . LEU B 134 ? 2.6860 2.1183 1.2354 0.1142  -0.0876 -0.2425 133  LEU B CB    
8253 C  CG    . LEU B 134 ? 2.7519 2.1942 1.2819 0.0908  -0.1173 -0.2616 133  LEU B CG    
8254 C  CD1   . LEU B 134 ? 2.5607 2.0397 1.1465 0.0691  -0.1331 -0.2624 133  LEU B CD1   
8255 C  CD2   . LEU B 134 ? 2.8432 2.2339 1.3174 0.0806  -0.1173 -0.2842 133  LEU B CD2   
8256 N  N     . ARG B 135 ? 2.5153 1.8980 1.0219 0.1807  -0.0208 -0.2081 134  ARG B N     
8257 C  CA    . ARG B 135 ? 2.4764 1.8524 1.0078 0.1985  0.0075  -0.1916 134  ARG B CA    
8258 C  C     . ARG B 135 ? 2.5047 1.8310 1.0051 0.2024  0.0257  -0.2025 134  ARG B C     
8259 O  O     . ARG B 135 ? 2.5962 1.8867 1.0375 0.2053  0.0261  -0.2164 134  ARG B O     
8260 C  CB    . ARG B 135 ? 2.3336 1.7202 0.8543 0.2220  0.0206  -0.1732 134  ARG B CB    
8261 C  CG    . ARG B 135 ? 2.2494 1.6312 0.7943 0.2407  0.0504  -0.1554 134  ARG B CG    
8262 C  CD    . ARG B 135 ? 2.1266 1.5320 0.6792 0.2588  0.0593  -0.1341 134  ARG B CD    
8263 N  NE    . ARG B 135 ? 2.1050 1.5075 0.6812 0.2755  0.0878  -0.1171 134  ARG B NE    
8264 C  CZ    . ARG B 135 ? 2.0791 1.5048 0.6782 0.2890  0.0991  -0.0958 134  ARG B CZ    
8265 N  NH1   . ARG B 135 ? 2.0708 1.5230 0.6725 0.2893  0.0850  -0.0880 134  ARG B NH1   
8266 N  NH2   . ARG B 135 ? 2.0622 1.4847 0.6827 0.3024  0.1251  -0.0819 134  ARG B NH2   
8267 N  N     . LYS B 136 ? 2.5193 1.8427 1.0586 0.2030  0.0407  -0.1963 135  LYS B N     
8268 C  CA    . LYS B 136 ? 2.5420 1.8198 1.0579 0.2070  0.0581  -0.2056 135  LYS B CA    
8269 C  C     . LYS B 136 ? 2.5166 1.7879 1.0459 0.2309  0.0885  -0.1884 135  LYS B C     
8270 O  O     . LYS B 136 ? 2.5460 1.7809 1.0582 0.2377  0.1054  -0.1939 135  LYS B O     
8271 C  CB    . LYS B 136 ? 2.6616 1.9354 1.2062 0.1856  0.0490  -0.2161 135  LYS B CB    
8272 C  CG    . LYS B 136 ? 2.7386 2.0140 1.2675 0.1598  0.0204  -0.2353 135  LYS B CG    
8273 C  CD    . LYS B 136 ? 2.8193 2.0912 1.3791 0.1389  0.0137  -0.2438 135  LYS B CD    
8274 C  CE    . LYS B 136 ? 2.8888 2.1637 1.4343 0.1118  -0.0143 -0.2629 135  LYS B CE    
8275 N  NZ    . LYS B 136 ? 2.6267 1.8992 1.2036 0.0907  -0.0202 -0.2701 135  LYS B NZ    
8276 N  N     . ILE B 137 ? 2.4268 1.7321 0.9867 0.2438  0.0962  -0.1677 136  ILE B N     
8277 C  CA    . ILE B 137 ? 2.4102 1.7137 0.9840 0.2660  0.1248  -0.1504 136  ILE B CA    
8278 C  C     . ILE B 137 ? 2.4428 1.7583 0.9966 0.2828  0.1313  -0.1373 136  ILE B C     
8279 O  O     . ILE B 137 ? 2.3343 1.6855 0.9123 0.2792  0.1188  -0.1274 136  ILE B O     
8280 C  CB    . ILE B 137 ? 2.3389 1.6742 0.9821 0.2636  0.1306  -0.1353 136  ILE B CB    
8281 C  CG1   . ILE B 137 ? 2.4704 1.7885 1.1295 0.2509  0.1292  -0.1466 136  ILE B CG1   
8282 C  CG2   . ILE B 137 ? 2.2835 1.6255 0.9431 0.2860  0.1579  -0.1153 136  ILE B CG2   
8283 C  CD1   . ILE B 137 ? 2.5290 1.8648 1.2107 0.2252  0.1024  -0.1571 136  ILE B CD1   
8284 N  N     . THR B 138 ? 2.4708 1.7558 0.9800 0.3017  0.1514  -0.1370 137  THR B N     
8285 C  CA    . THR B 138 ? 2.4779 1.7697 0.9624 0.3188  0.1601  -0.1246 137  THR B CA    
8286 C  C     . THR B 138 ? 2.4532 1.7792 0.9897 0.3299  0.1759  -0.0993 137  THR B C     
8287 O  O     . THR B 138 ? 2.4759 1.8162 1.0629 0.3269  0.1834  -0.0920 137  THR B O     
8288 C  CB    . THR B 138 ? 2.7192 1.9680 1.1425 0.3366  0.1794  -0.1310 137  THR B CB    
8289 O  OG1   . THR B 138 ? 2.6583 1.8942 1.0997 0.3491  0.2056  -0.1242 137  THR B OG1   
8290 C  CG2   . THR B 138 ? 2.8176 2.0293 1.1874 0.3246  0.1636  -0.1571 137  THR B CG2   
8291 N  N     . ARG B 139 ? 2.4938 1.8323 1.0163 0.3425  0.1810  -0.0859 138  ARG B N     
8292 C  CA    . ARG B 139 ? 2.4178 1.7856 0.9844 0.3531  0.1975  -0.0616 138  ARG B CA    
8293 C  C     . ARG B 139 ? 2.5538 1.9072 1.1265 0.3694  0.2283  -0.0532 138  ARG B C     
8294 O  O     . ARG B 139 ? 2.4418 1.8187 1.0670 0.3715  0.2404  -0.0380 138  ARG B O     
8295 C  CB    . ARG B 139 ? 2.2199 1.5997 0.7642 0.3633  0.1968  -0.0494 138  ARG B CB    
8296 C  CG    . ARG B 139 ? 2.1223 1.5249 0.7018 0.3764  0.2179  -0.0240 138  ARG B CG    
8297 C  CD    . ARG B 139 ? 2.2250 1.6383 0.7818 0.3852  0.2154  -0.0119 138  ARG B CD    
8298 N  NE    . ARG B 139 ? 2.1610 1.6039 0.7455 0.3719  0.1906  -0.0096 138  ARG B NE    
8299 C  CZ    . ARG B 139 ? 2.2123 1.6859 0.8473 0.3703  0.1923  0.0080  138  ARG B CZ    
8300 N  NH1   . ARG B 139 ? 2.1887 1.6694 0.8538 0.3797  0.2169  0.0253  138  ARG B NH1   
8301 N  NH2   . ARG B 139 ? 2.1832 1.6812 0.8390 0.3590  0.1689  0.0083  138  ARG B NH2   
8302 N  N     . GLU B 140 ? 2.9538 2.2691 1.4731 0.3812  0.2412  -0.0633 139  GLU B N     
8303 C  CA    . GLU B 140 ? 2.8804 2.1816 1.4025 0.3985  0.2712  -0.0557 139  GLU B CA    
8304 C  C     . GLU B 140 ? 2.9115 2.2119 1.4732 0.3906  0.2730  -0.0607 139  GLU B C     
8305 O  O     . GLU B 140 ? 2.9869 2.2969 1.5817 0.4012  0.2945  -0.0475 139  GLU B O     
8306 C  CB    . GLU B 140 ? 2.9188 2.1771 1.3703 0.4136  0.2838  -0.0667 139  GLU B CB    
8307 C  CG    . GLU B 140 ? 3.3433 2.6013 1.7546 0.4273  0.2899  -0.0579 139  GLU B CG    
8308 C  CD    . GLU B 140 ? 3.2631 2.5264 1.6489 0.4143  0.2609  -0.0670 139  GLU B CD    
8309 O  OE1   . GLU B 140 ? 2.9900 2.2567 1.3879 0.3941  0.2361  -0.0814 139  GLU B OE1   
8310 O  OE2   . GLU B 140 ? 3.2394 2.5046 1.5933 0.4245  0.2631  -0.0593 139  GLU B OE2   
8311 N  N     . GLN B 141 ? 2.5889 1.8785 1.1479 0.3719  0.2511  -0.0790 140  GLN B N     
8312 C  CA    . GLN B 141 ? 2.5301 1.8196 1.1275 0.3632  0.2514  -0.0830 140  GLN B CA    
8313 C  C     . GLN B 141 ? 2.4703 1.8046 1.1390 0.3570  0.2499  -0.0658 140  GLN B C     
8314 O  O     . GLN B 141 ? 2.3917 1.7330 1.0979 0.3605  0.2629  -0.0589 140  GLN B O     
8315 C  CB    . GLN B 141 ? 2.5108 1.7804 1.0898 0.3427  0.2272  -0.1057 140  GLN B CB    
8316 C  CG    . GLN B 141 ? 2.4878 1.7059 1.0016 0.3478  0.2318  -0.1248 140  GLN B CG    
8317 C  CD    . GLN B 141 ? 2.4355 1.6344 0.9345 0.3251  0.2080  -0.1469 140  GLN B CD    
8318 O  OE1   . GLN B 141 ? 2.4930 1.7141 1.0048 0.3067  0.1833  -0.1513 140  GLN B OE1   
8319 N  NE2   . GLN B 141 ? 2.3765 1.5338 0.8488 0.3264  0.2159  -0.1607 140  GLN B NE2   
8320 N  N     . GLY B 142 ? 2.3903 1.7552 1.0777 0.3482  0.2340  -0.0588 141  GLY B N     
8321 C  CA    . GLY B 142 ? 2.2615 1.6671 1.0134 0.3431  0.2334  -0.0423 141  GLY B CA    
8322 C  C     . GLY B 142 ? 2.2684 1.6884 1.0395 0.3610  0.2594  -0.0211 141  GLY B C     
8323 O  O     . GLY B 142 ? 2.2727 1.7164 1.0960 0.3605  0.2677  -0.0090 141  GLY B O     
8324 N  N     . LYS B 143 ? 2.3158 1.7225 1.0449 0.3767  0.2725  -0.0161 142  LYS B N     
8325 C  CA    . LYS B 143 ? 2.2496 1.6686 0.9939 0.3939  0.2991  0.0041  142  LYS B CA    
8326 C  C     . LYS B 143 ? 2.2745 1.6828 1.0309 0.4047  0.3211  0.0054  142  LYS B C     
8327 O  O     . LYS B 143 ? 2.2195 1.6517 1.0193 0.4108  0.3377  0.0221  142  LYS B O     
8328 C  CB    . LYS B 143 ? 2.3648 1.7682 1.0556 0.4088  0.3088  0.0079  142  LYS B CB    
8329 C  CG    . LYS B 143 ? 2.3017 1.7244 0.9906 0.4037  0.2942  0.0156  142  LYS B CG    
8330 C  CD    . LYS B 143 ? 2.1653 1.6249 0.9112 0.4029  0.3017  0.0376  142  LYS B CD    
8331 C  CE    . LYS B 143 ? 2.2438 1.7137 0.9739 0.4077  0.2999  0.0504  142  LYS B CE    
8332 N  NZ    . LYS B 143 ? 2.2930 1.7579 0.9924 0.3981  0.2722  0.0375  142  LYS B NZ    
8333 N  N     . GLU B 144 ? 2.3512 1.7235 1.0694 0.4072  0.3217  -0.0120 143  GLU B N     
8334 C  CA    . GLU B 144 ? 2.4155 1.7749 1.1415 0.4193  0.3427  -0.0112 143  GLU B CA    
8335 C  C     . GLU B 144 ? 2.4095 1.7918 1.1961 0.4079  0.3371  -0.0082 143  GLU B C     
8336 O  O     . GLU B 144 ? 2.4728 1.8699 1.2939 0.4179  0.3559  0.0042  143  GLU B O     
8337 C  CB    . GLU B 144 ? 2.5251 1.8363 1.1920 0.4242  0.3435  -0.0316 143  GLU B CB    
8338 C  CG    . GLU B 144 ? 2.6968 1.9907 1.3700 0.4362  0.3627  -0.0330 143  GLU B CG    
8339 C  CD    . GLU B 144 ? 2.7484 2.0569 1.4367 0.4584  0.3931  -0.0138 143  GLU B CD    
8340 O  OE1   . GLU B 144 ? 2.7452 2.0515 1.4038 0.4707  0.4048  -0.0067 143  GLU B OE1   
8341 O  OE2   . GLU B 144 ? 2.7251 2.0486 1.4555 0.4635  0.4052  -0.0053 143  GLU B OE2   
8342 N  N     . MET B 145 ? 2.3718 1.7588 1.1723 0.3871  0.3113  -0.0193 144  MET B N     
8343 C  CA    . MET B 145 ? 2.2798 1.6901 1.1375 0.3754  0.3045  -0.0161 144  MET B CA    
8344 C  C     . MET B 145 ? 2.2076 1.6617 1.1203 0.3751  0.3096  0.0047  144  MET B C     
8345 O  O     . MET B 145 ? 2.2280 1.7019 1.1873 0.3754  0.3171  0.0134  144  MET B O     
8346 C  CB    . MET B 145 ? 2.2137 1.6210 1.0723 0.3529  0.2758  -0.0319 144  MET B CB    
8347 C  CG    . MET B 145 ? 2.2448 1.6802 1.1632 0.3390  0.2660  -0.0278 144  MET B CG    
8348 S  SD    . MET B 145 ? 2.4095 1.8309 1.3462 0.3452  0.2801  -0.0298 144  MET B SD    
8349 C  CE    . MET B 145 ? 2.4871 1.8616 1.3728 0.3347  0.2657  -0.0555 144  MET B CE    
8350 N  N     . ALA B 146 ? 2.1634 1.6322 1.0703 0.3747  0.3057  0.0130  145  ALA B N     
8351 C  CA    . ALA B 146 ? 2.1357 1.6427 1.0917 0.3737  0.3107  0.0326  145  ALA B CA    
8352 C  C     . ALA B 146 ? 2.1408 1.6558 1.1113 0.3914  0.3398  0.0485  145  ALA B C     
8353 O  O     . ALA B 146 ? 2.1249 1.6693 1.1480 0.3894  0.3464  0.0614  145  ALA B O     
8354 C  CB    . ALA B 146 ? 2.0906 1.6067 1.0315 0.3706  0.3005  0.0377  145  ALA B CB    
8355 N  N     . THR B 147 ? 2.2066 1.6969 1.1311 0.4087  0.3575  0.0478  146  THR B N     
8356 C  CA    . THR B 147 ? 2.2153 1.7132 1.1516 0.4267  0.3864  0.0623  146  THR B CA    
8357 C  C     . THR B 147 ? 2.2687 1.7612 1.2235 0.4318  0.3955  0.0582  146  THR B C     
8358 O  O     . THR B 147 ? 2.2959 1.8051 1.2776 0.4440  0.4171  0.0718  146  THR B O     
8359 C  CB    . THR B 147 ? 2.2280 1.7006 1.1071 0.4447  0.4032  0.0627  146  THR B CB    
8360 O  OG1   . THR B 147 ? 2.3121 1.7438 1.1379 0.4470  0.3966  0.0421  146  THR B OG1   
8361 C  CG2   . THR B 147 ? 2.0881 1.5686 0.9511 0.4418  0.3965  0.0701  146  THR B CG2   
8362 N  N     . LYS B 148 ? 2.3528 1.8229 1.2939 0.4229  0.3798  0.0401  147  LYS B N     
8363 C  CA    . LYS B 148 ? 2.3490 1.8122 1.3072 0.4274  0.3870  0.0363  147  LYS B CA    
8364 C  C     . LYS B 148 ? 2.2977 1.8016 1.3249 0.4197  0.3859  0.0491  147  LYS B C     
8365 O  O     . LYS B 148 ? 2.4080 1.9240 1.4615 0.4314  0.4037  0.0585  147  LYS B O     
8366 C  CB    . LYS B 148 ? 2.3914 1.8212 1.3200 0.4166  0.3686  0.0144  147  LYS B CB    
8367 C  CG    . LYS B 148 ? 2.3830 1.8034 1.3290 0.4194  0.3733  0.0099  147  LYS B CG    
8368 C  CD    . LYS B 148 ? 2.3271 1.7140 1.2442 0.4059  0.3539  -0.0114 147  LYS B CD    
8369 C  CE    . LYS B 148 ? 2.5450 1.8891 1.3924 0.4114  0.3543  -0.0261 147  LYS B CE    
8370 N  NZ    . LYS B 148 ? 2.4326 1.7440 1.2516 0.3959  0.3347  -0.0474 147  LYS B NZ    
8371 N  N     . HIS B 149 ? 2.2018 1.7276 1.2586 0.4004  0.3648  0.0495  148  HIS B N     
8372 C  CA    . HIS B 149 ? 2.2642 1.8280 1.3846 0.3912  0.3614  0.0606  148  HIS B CA    
8373 C  C     . HIS B 149 ? 2.1456 1.7424 1.2955 0.3912  0.3688  0.0791  148  HIS B C     
8374 O  O     . HIS B 149 ? 2.1171 1.7457 1.3180 0.3807  0.3629  0.0878  148  HIS B O     
8375 C  CB    . HIS B 149 ? 2.2271 1.7945 1.3643 0.3699  0.3344  0.0495  148  HIS B CB    
8376 C  CG    . HIS B 149 ? 2.2681 1.8033 1.3790 0.3670  0.3262  0.0315  148  HIS B CG    
8377 N  ND1   . HIS B 149 ? 2.2798 1.8106 1.4070 0.3729  0.3345  0.0307  148  HIS B ND1   
8378 C  CD2   . HIS B 149 ? 2.3037 1.8092 1.3730 0.3585  0.3104  0.0140  148  HIS B CD2   
8379 C  CE1   . HIS B 149 ? 2.3021 1.7993 1.3977 0.3681  0.3248  0.0136  148  HIS B CE1   
8380 N  NE2   . HIS B 149 ? 2.3162 1.7980 1.3769 0.3585  0.3100  0.0029  148  HIS B NE2   
8381 N  N     . ASN B 150 ? 2.1566 1.7452 1.2742 0.4026  0.3817  0.0853  149  ASN B N     
8382 C  CA    . ASN B 150 ? 2.1396 1.7549 1.2792 0.4034  0.3907  0.1035  149  ASN B CA    
8383 C  C     . ASN B 150 ? 2.0337 1.6677 1.1986 0.3843  0.3684  0.1045  149  ASN B C     
8384 O  O     . ASN B 150 ? 1.8749 1.5399 1.0888 0.3766  0.3684  0.1166  149  ASN B O     
8385 C  CB    . ASN B 150 ? 2.1262 1.7701 1.3114 0.4114  0.4118  0.1199  149  ASN B CB    
8386 C  CG    . ASN B 150 ? 2.0125 1.6743 1.2046 0.4181  0.4295  0.1386  149  ASN B CG    
8387 O  OD1   . ASN B 150 ? 2.1285 1.7891 1.3062 0.4125  0.4222  0.1417  149  ASN B OD1   
8388 N  ND2   . ASN B 150 ? 1.8080 1.4870 1.0226 0.4303  0.4532  0.1516  149  ASN B ND2   
8389 N  N     . ILE B 151 ? 2.1002 1.7146 1.2299 0.3768  0.3491  0.0912  150  ILE B N     
8390 C  CA    . ILE B 151 ? 2.0108 1.6395 1.1592 0.3594  0.3257  0.0891  150  ILE B CA    
8391 C  C     . ILE B 151 ? 1.9112 1.5296 1.0203 0.3612  0.3199  0.0897  150  ILE B C     
8392 O  O     . ILE B 151 ? 1.9201 1.5107 0.9769 0.3703  0.3230  0.0813  150  ILE B O     
8393 C  CB    . ILE B 151 ? 1.9192 1.5389 1.0695 0.3460  0.3041  0.0714  150  ILE B CB    
8394 C  CG1   . ILE B 151 ? 1.9775 1.6095 1.1692 0.3441  0.3091  0.0724  150  ILE B CG1   
8395 C  CG2   . ILE B 151 ? 1.9341 1.5678 1.0987 0.3294  0.2800  0.0684  150  ILE B CG2   
8396 C  CD1   . ILE B 151 ? 2.1972 1.8215 1.3938 0.3303  0.2888  0.0567  150  ILE B CD1   
8397 N  N     . PRO B 152 ? 1.8658 1.5044 0.9962 0.3535  0.3119  0.0997  151  PRO B N     
8398 C  CA    . PRO B 152 ? 1.8017 1.4307 0.8943 0.3548  0.3030  0.0994  151  PRO B CA    
8399 C  C     . PRO B 152 ? 1.7935 1.4048 0.8539 0.3465  0.2793  0.0795  151  PRO B C     
8400 O  O     . PRO B 152 ? 1.8695 1.4829 0.9485 0.3349  0.2654  0.0679  151  PRO B O     
8401 C  CB    . PRO B 152 ? 1.7381 1.3938 0.8696 0.3463  0.2970  0.1131  151  PRO B CB    
8402 C  CG    . PRO B 152 ? 1.7657 1.4427 0.9473 0.3458  0.3127  0.1252  151  PRO B CG    
8403 C  CD    . PRO B 152 ? 1.7911 1.4614 0.9792 0.3455  0.3135  0.1134  151  PRO B CD    
8404 N  N     . TYR B 153 ? 1.8722 1.4667 0.8837 0.3522  0.2748  0.0759  152  TYR B N     
8405 C  CA    . TYR B 153 ? 1.8481 1.4246 0.8222 0.3453  0.2535  0.0568  152  TYR B CA    
8406 C  C     . TYR B 153 ? 1.8172 1.4029 0.7789 0.3413  0.2365  0.0595  152  TYR B C     
8407 O  O     . TYR B 153 ? 1.9322 1.5235 0.8878 0.3503  0.2463  0.0745  152  TYR B O     
8408 C  CB    . TYR B 153 ? 1.9029 1.4455 0.8201 0.3575  0.2638  0.0465  152  TYR B CB    
8409 C  CG    . TYR B 153 ? 1.9570 1.4784 0.8305 0.3500  0.2425  0.0261  152  TYR B CG    
8410 C  CD1   . TYR B 153 ? 1.9108 1.4237 0.7905 0.3374  0.2290  0.0093  152  TYR B CD1   
8411 C  CD2   . TYR B 153 ? 2.0189 1.5286 0.8441 0.3555  0.2362  0.0238  152  TYR B CD2   
8412 C  CE1   . TYR B 153 ? 2.0103 1.5044 0.8509 0.3289  0.2096  -0.0096 152  TYR B CE1   
8413 C  CE2   . TYR B 153 ? 2.0227 1.5147 0.8082 0.3477  0.2160  0.0047  152  TYR B CE2   
8414 C  CZ    . TYR B 153 ? 2.0478 1.5323 0.8419 0.3338  0.2028  -0.0121 152  TYR B CZ    
8415 O  OH    . TYR B 153 ? 2.0606 1.5280 0.8163 0.3242  0.1826  -0.0314 152  TYR B OH    
8416 N  N     . ILE B 154 ? 1.7495 1.3369 0.7076 0.3280  0.2112  0.0452  153  ILE B N     
8417 C  CA    . ILE B 154 ? 1.7534 1.3509 0.6994 0.3243  0.1927  0.0463  153  ILE B CA    
8418 C  C     . ILE B 154 ? 1.8319 1.4219 0.7562 0.3121  0.1680  0.0255  153  ILE B C     
8419 O  O     . ILE B 154 ? 1.8253 1.4133 0.7668 0.3010  0.1613  0.0136  153  ILE B O     
8420 C  CB    . ILE B 154 ? 1.7027 1.3308 0.7004 0.3180  0.1881  0.0603  153  ILE B CB    
8421 C  CG1   . ILE B 154 ? 1.8099 1.4468 0.7913 0.3193  0.1736  0.0652  153  ILE B CG1   
8422 C  CG2   . ILE B 154 ? 1.8064 1.4499 0.8479 0.3018  0.1744  0.0518  153  ILE B CG2   
8423 C  CD1   . ILE B 154 ? 1.8046 1.4669 0.8314 0.3155  0.1715  0.0801  153  ILE B CD1   
8424 N  N     . GLU B 155 ? 1.8489 1.4346 0.7343 0.3141  0.1546  0.0215  154  GLU B N     
8425 C  CA    . GLU B 155 ? 1.9161 1.4979 0.7793 0.3019  0.1295  0.0025  154  GLU B CA    
8426 C  C     . GLU B 155 ? 1.8497 1.4604 0.7353 0.2940  0.1083  0.0065  154  GLU B C     
8427 O  O     . GLU B 155 ? 1.8020 1.4215 0.6793 0.3036  0.1094  0.0196  154  GLU B O     
8428 C  CB    . GLU B 155 ? 1.9243 1.4787 0.7217 0.3098  0.1285  -0.0075 154  GLU B CB    
8429 C  CG    . GLU B 155 ? 2.0007 1.5228 0.7705 0.3162  0.1461  -0.0161 154  GLU B CG    
8430 C  CD    . GLU B 155 ? 2.0152 1.5086 0.7201 0.3184  0.1386  -0.0323 154  GLU B CD    
8431 O  OE1   . GLU B 155 ? 1.9984 1.4995 0.6808 0.3148  0.1190  -0.0365 154  GLU B OE1   
8432 O  OE2   . GLU B 155 ? 2.0078 1.4708 0.6836 0.3241  0.1520  -0.0411 154  GLU B OE2   
8433 N  N     . THR B 156 ? 1.7725 1.3977 0.6860 0.2774  0.0898  -0.0043 155  THR B N     
8434 C  CA    . THR B 156 ? 1.8230 1.4776 0.7623 0.2695  0.0696  -0.0015 155  THR B CA    
8435 C  C     . THR B 156 ? 1.8381 1.4950 0.7600 0.2554  0.0442  -0.0208 155  THR B C     
8436 O  O     . THR B 156 ? 1.8413 1.4764 0.7371 0.2492  0.0424  -0.0368 155  THR B O     
8437 C  CB    . THR B 156 ? 1.7502 1.4273 0.7507 0.2621  0.0720  0.0066  155  THR B CB    
8438 O  OG1   . THR B 156 ? 1.6804 1.3540 0.6984 0.2483  0.0672  -0.0073 155  THR B OG1   
8439 C  CG2   . THR B 156 ? 1.7072 1.3818 0.7270 0.2738  0.0975  0.0243  155  THR B CG2   
8440 N  N     . SER B 157 ? 1.8496 1.5335 0.7867 0.2502  0.0246  -0.0191 156  SER B N     
8441 C  CA    . SER B 157 ? 1.8855 1.5801 0.8162 0.2350  -0.0010 -0.0358 156  SER B CA    
8442 C  C     . SER B 157 ? 1.8538 1.5848 0.8253 0.2302  -0.0160 -0.0286 156  SER B C     
8443 O  O     . SER B 157 ? 1.9400 1.6839 0.9059 0.2410  -0.0194 -0.0168 156  SER B O     
8444 C  CB    . SER B 157 ? 1.8074 1.4891 0.6807 0.2390  -0.0116 -0.0449 156  SER B CB    
8445 O  OG    . SER B 157 ? 1.7787 1.4826 0.6524 0.2269  -0.0386 -0.0553 156  SER B OG    
8446 N  N     . ALA B 158 ? 1.7658 1.5120 0.7765 0.2148  -0.0245 -0.0355 157  ALA B N     
8447 C  CA    . ALA B 158 ? 1.7733 1.5535 0.8264 0.2106  -0.0366 -0.0286 157  ALA B CA    
8448 C  C     . ALA B 158 ? 1.7517 1.5539 0.7911 0.2072  -0.0612 -0.0343 157  ALA B C     
8449 O  O     . ALA B 158 ? 1.7417 1.5735 0.8148 0.2042  -0.0725 -0.0295 157  ALA B O     
8450 C  CB    . ALA B 158 ? 1.5549 1.3446 0.6517 0.1951  -0.0381 -0.0348 157  ALA B CB    
8451 N  N     . LYS B 159 ? 1.7148 1.5042 0.7059 0.2083  -0.0696 -0.0441 158  LYS B N     
8452 C  CA    . LYS B 159 ? 1.7425 1.5540 0.7178 0.2050  -0.0941 -0.0502 158  LYS B CA    
8453 C  C     . LYS B 159 ? 1.8823 1.7145 0.8648 0.2208  -0.0962 -0.0324 158  LYS B C     
8454 O  O     . LYS B 159 ? 1.9875 1.8138 0.9850 0.2332  -0.0780 -0.0160 158  LYS B O     
8455 C  CB    . LYS B 159 ? 1.8756 1.6647 0.7932 0.2047  -0.1001 -0.0634 158  LYS B CB    
8456 C  CG    . LYS B 159 ? 1.9411 1.7513 0.8456 0.1921  -0.1282 -0.0778 158  LYS B CG    
8457 C  CD    . LYS B 159 ? 1.8469 1.6714 0.7867 0.1699  -0.1391 -0.0908 158  LYS B CD    
8458 C  CE    . LYS B 159 ? 1.9162 1.7639 0.8448 0.1557  -0.1670 -0.1053 158  LYS B CE    
8459 N  NZ    . LYS B 159 ? 1.8005 1.6215 0.6728 0.1515  -0.1726 -0.1208 158  LYS B NZ    
8460 N  N     . ASP B 160 ? 1.8957 1.7524 0.8682 0.2205  -0.1183 -0.0353 159  ASP B N     
8461 C  CA    . ASP B 160 ? 2.0456 1.9222 1.0240 0.2363  -0.1218 -0.0184 159  ASP B CA    
8462 C  C     . ASP B 160 ? 2.1503 2.0030 1.0995 0.2565  -0.1025 -0.0027 159  ASP B C     
8463 O  O     . ASP B 160 ? 2.1863 2.0457 1.1574 0.2681  -0.0930 0.0150  159  ASP B O     
8464 C  CB    . ASP B 160 ? 2.2231 2.1272 1.1853 0.2341  -0.1489 -0.0254 159  ASP B CB    
8465 C  CG    . ASP B 160 ? 2.4599 2.3929 1.4564 0.2145  -0.1676 -0.0386 159  ASP B CG    
8466 O  OD1   . ASP B 160 ? 1.9974 1.9374 1.0386 0.2072  -0.1606 -0.0364 159  ASP B OD1   
8467 O  OD2   . ASP B 160 ? 2.7827 2.7324 1.7616 0.2060  -0.1894 -0.0510 159  ASP B OD2   
8468 N  N     . PRO B 161 ? 2.2395 2.0641 1.1405 0.2615  -0.0952 -0.0077 160  PRO B N     
8469 C  CA    . PRO B 161 ? 2.1972 1.9971 1.0771 0.2793  -0.0718 0.0079  160  PRO B CA    
8470 C  C     . PRO B 161 ? 2.1720 1.9588 1.0863 0.2772  -0.0484 0.0144  160  PRO B C     
8471 O  O     . PRO B 161 ? 2.0662 1.8407 0.9874 0.2652  -0.0440 0.0019  160  PRO B O     
8472 C  CB    . PRO B 161 ? 2.1876 1.9607 1.0086 0.2818  -0.0710 -0.0032 160  PRO B CB    
8473 C  CG    . PRO B 161 ? 2.1238 1.9144 0.9301 0.2697  -0.0991 -0.0205 160  PRO B CG    
8474 C  CD    . PRO B 161 ? 2.1340 1.9492 0.9933 0.2525  -0.1094 -0.0270 160  PRO B CD    
8475 N  N     . PRO B 162 ? 2.3924 2.1808 1.3281 0.2888  -0.0332 0.0341  161  PRO B N     
8476 C  CA    . PRO B 162 ? 2.3429 2.1267 1.3205 0.2848  -0.0144 0.0405  161  PRO B CA    
8477 C  C     . PRO B 162 ? 2.2700 2.0253 1.2320 0.2841  0.0051  0.0354  161  PRO B C     
8478 O  O     . PRO B 162 ? 2.3944 2.1469 1.3761 0.2713  0.0057  0.0239  161  PRO B O     
8479 C  CB    . PRO B 162 ? 2.5497 2.3365 1.5400 0.2992  -0.0019 0.0629  161  PRO B CB    
8480 C  CG    . PRO B 162 ? 2.3448 2.1246 1.2861 0.3140  -0.0057 0.0689  161  PRO B CG    
8481 C  CD    . PRO B 162 ? 2.3926 2.1846 1.3117 0.3063  -0.0316 0.0515  161  PRO B CD    
8482 N  N     . LEU B 163 ? 2.1254 1.8595 1.0522 0.2988  0.0217  0.0447  162  LEU B N     
8483 C  CA    . LEU B 163 ? 2.0899 1.7961 0.9952 0.3016  0.0414  0.0410  162  LEU B CA    
8484 C  C     . LEU B 163 ? 1.9033 1.6083 0.8525 0.2973  0.0599  0.0465  162  LEU B C     
8485 O  O     . LEU B 163 ? 1.7254 1.4289 0.6925 0.2850  0.0574  0.0338  162  LEU B O     
8486 C  CB    . LEU B 163 ? 2.1390 1.8321 1.0124 0.2921  0.0293  0.0188  162  LEU B CB    
8487 C  CG    . LEU B 163 ? 2.1101 1.7705 0.9506 0.2981  0.0492  0.0143  162  LEU B CG    
8488 C  CD1   . LEU B 163 ? 1.8649 1.5098 0.6611 0.3168  0.0619  0.0258  162  LEU B CD1   
8489 C  CD2   . LEU B 163 ? 2.1543 1.8005 0.9677 0.2865  0.0364  -0.0086 162  LEU B CD2   
8490 N  N     . ASN B 164 ? 1.9476 1.6533 0.9139 0.3072  0.0782  0.0657  163  ASN B N     
8491 C  CA    . ASN B 164 ? 1.7697 1.4716 0.7696 0.3063  0.0997  0.0732  163  ASN B CA    
8492 C  C     . ASN B 164 ? 1.8152 1.5342 0.8659 0.2910  0.0920  0.0666  163  ASN B C     
8493 O  O     . ASN B 164 ? 1.7265 1.4409 0.8003 0.2874  0.1057  0.0662  163  ASN B O     
8494 C  CB    . ASN B 164 ? 1.7880 1.4643 0.7581 0.3117  0.1171  0.0677  163  ASN B CB    
8495 C  CG    . ASN B 164 ? 1.8915 1.5495 0.8089 0.3275  0.1263  0.0739  163  ASN B CG    
8496 O  OD1   . ASN B 164 ? 1.8643 1.5272 0.7770 0.3371  0.1305  0.0897  163  ASN B OD1   
8497 N  ND2   . ASN B 164 ? 1.8620 1.4972 0.7376 0.3305  0.1299  0.0616  163  ASN B ND2   
8498 N  N     . VAL B 165 ? 1.8070 1.5465 0.8758 0.2825  0.0704  0.0618  164  VAL B N     
8499 C  CA    . VAL B 165 ? 1.6542 1.4110 0.7716 0.2686  0.0636  0.0569  164  VAL B CA    
8500 C  C     . VAL B 165 ? 1.6601 1.4255 0.8186 0.2710  0.0783  0.0735  164  VAL B C     
8501 O  O     . VAL B 165 ? 1.6753 1.4421 0.8657 0.2646  0.0878  0.0730  164  VAL B O     
8502 C  CB    . VAL B 165 ? 1.6665 1.4447 0.7919 0.2597  0.0374  0.0481  164  VAL B CB    
8503 C  CG1   . VAL B 165 ? 1.5179 1.3169 0.6967 0.2492  0.0328  0.0492  164  VAL B CG1   
8504 C  CG2   . VAL B 165 ? 1.6976 1.4690 0.7949 0.2507  0.0229  0.0282  164  VAL B CG2   
8505 N  N     . ASP B 166 ? 1.6764 1.4469 0.8339 0.2803  0.0803  0.0884  165  ASP B N     
8506 C  CA    . ASP B 166 ? 1.5913 1.3674 0.7850 0.2821  0.0947  0.1044  165  ASP B CA    
8507 C  C     . ASP B 166 ? 1.6291 1.3892 0.8180 0.2886  0.1204  0.1134  165  ASP B C     
8508 O  O     . ASP B 166 ? 1.6679 1.4333 0.8938 0.2847  0.1329  0.1207  165  ASP B O     
8509 C  CB    . ASP B 166 ? 1.5060 1.2883 0.6963 0.2907  0.0905  0.1182  165  ASP B CB    
8510 C  CG    . ASP B 166 ? 1.7870 1.5885 0.9864 0.2855  0.0659  0.1107  165  ASP B CG    
8511 O  OD1   . ASP B 166 ? 2.0296 1.8325 1.1987 0.2859  0.0504  0.0998  165  ASP B OD1   
8512 O  OD2   . ASP B 166 ? 1.8550 1.6709 1.0918 0.2811  0.0621  0.1156  165  ASP B OD2   
8513 N  N     . LYS B 167 ? 1.6396 1.3813 0.7837 0.2986  0.1285  0.1129  166  LYS B N     
8514 C  CA    . LYS B 167 ? 1.6202 1.3479 0.7580 0.3064  0.1540  0.1222  166  LYS B CA    
8515 C  C     . LYS B 167 ? 1.6332 1.3599 0.7932 0.2988  0.1615  0.1132  166  LYS B C     
8516 O  O     . LYS B 167 ? 1.5901 1.3174 0.7730 0.3006  0.1809  0.1230  166  LYS B O     
8517 C  CB    . LYS B 167 ? 1.7657 1.4731 0.8470 0.3194  0.1602  0.1222  166  LYS B CB    
8518 C  CG    . LYS B 167 ? 1.7511 1.4449 0.8231 0.3294  0.1880  0.1335  166  LYS B CG    
8519 C  CD    . LYS B 167 ? 1.8910 1.5626 0.9068 0.3399  0.1931  0.1267  166  LYS B CD    
8520 C  CE    . LYS B 167 ? 2.0105 1.6700 1.0192 0.3503  0.2219  0.1374  166  LYS B CE    
8521 N  NZ    . LYS B 167 ? 1.9938 1.6308 0.9548 0.3581  0.2275  0.1259  166  LYS B NZ    
8522 N  N     . ALA B 168 ? 1.6685 1.3939 0.8223 0.2903  0.1465  0.0950  167  ALA B N     
8523 C  CA    . ALA B 168 ? 1.5945 1.3165 0.7660 0.2840  0.1531  0.0863  167  ALA B CA    
8524 C  C     . ALA B 168 ? 1.5881 1.3291 0.8156 0.2756  0.1565  0.0929  167  ALA B C     
8525 O  O     . ALA B 168 ? 1.6242 1.3645 0.8715 0.2767  0.1731  0.0974  167  ALA B O     
8526 C  CB    . ALA B 168 ? 1.5341 1.2506 0.6889 0.2749  0.1347  0.0658  167  ALA B CB    
8527 N  N     . PHE B 169 ? 1.5367 1.2955 0.7901 0.2675  0.1407  0.0934  168  PHE B N     
8528 C  CA    . PHE B 169 ? 1.5392 1.3152 0.8437 0.2597  0.1434  0.0998  168  PHE B CA    
8529 C  C     . PHE B 169 ? 1.4760 1.2533 0.7943 0.2668  0.1626  0.1188  168  PHE B C     
8530 O  O     . PHE B 169 ? 1.4784 1.2616 0.8275 0.2642  0.1760  0.1245  168  PHE B O     
8531 C  CB    . PHE B 169 ? 1.4804 1.2737 0.8058 0.2507  0.1224  0.0958  168  PHE B CB    
8532 C  CG    . PHE B 169 ? 1.4154 1.2124 0.7397 0.2402  0.1045  0.0778  168  PHE B CG    
8533 C  CD1   . PHE B 169 ? 1.5219 1.3261 0.8782 0.2299  0.1036  0.0711  168  PHE B CD1   
8534 C  CD2   . PHE B 169 ? 1.4703 1.2643 0.7618 0.2402  0.0882  0.0679  168  PHE B CD2   
8535 C  CE1   . PHE B 169 ? 1.4547 1.2613 0.8098 0.2196  0.0880  0.0553  168  PHE B CE1   
8536 C  CE2   . PHE B 169 ? 1.4405 1.2385 0.7322 0.2290  0.0720  0.0516  168  PHE B CE2   
8537 C  CZ    . PHE B 169 ? 1.4550 1.2584 0.7782 0.2185  0.0723  0.0454  168  PHE B CZ    
8538 N  N     . HIS B 170 ? 1.4744 1.2467 0.7701 0.2755  0.1642  0.1290  169  HIS B N     
8539 C  CA    . HIS B 170 ? 1.5509 1.3231 0.8586 0.2813  0.1825  0.1478  169  HIS B CA    
8540 C  C     . HIS B 170 ? 1.5970 1.3603 0.8986 0.2877  0.2059  0.1535  169  HIS B C     
8541 O  O     . HIS B 170 ? 1.5897 1.3595 0.9196 0.2870  0.2218  0.1663  169  HIS B O     
8542 C  CB    . HIS B 170 ? 1.5083 1.2732 0.7860 0.2909  0.1801  0.1575  169  HIS B CB    
8543 C  CG    . HIS B 170 ? 1.4823 1.2586 0.7738 0.2863  0.1610  0.1569  169  HIS B CG    
8544 N  ND1   . HIS B 170 ? 1.4915 1.2651 0.7736 0.2936  0.1613  0.1703  169  HIS B ND1   
8545 C  CD2   . HIS B 170 ? 1.4936 1.2840 0.8072 0.2761  0.1419  0.1451  169  HIS B CD2   
8546 C  CE1   . HIS B 170 ? 1.4547 1.2403 0.7527 0.2888  0.1430  0.1665  169  HIS B CE1   
8547 N  NE2   . HIS B 170 ? 1.5431 1.3399 0.8607 0.2780  0.1311  0.1513  169  HIS B NE2   
8548 N  N     . ASP B 171 ? 1.5572 1.3059 0.8224 0.2941  0.2085  0.1443  170  ASP B N     
8549 C  CA    . ASP B 171 ? 1.5099 1.2506 0.7697 0.3014  0.2310  0.1488  170  ASP B CA    
8550 C  C     . ASP B 171 ? 1.6454 1.3983 0.9471 0.2932  0.2354  0.1451  170  ASP B C     
8551 O  O     . ASP B 171 ? 1.6120 1.3703 0.9338 0.2962  0.2549  0.1556  170  ASP B O     
8552 C  CB    . ASP B 171 ? 1.6657 1.3854 0.8741 0.3107  0.2321  0.1384  170  ASP B CB    
8553 C  CG    . ASP B 171 ? 1.9916 1.6981 1.1561 0.3226  0.2361  0.1464  170  ASP B CG    
8554 O  OD1   . ASP B 171 ? 1.8810 1.5928 1.0555 0.3257  0.2444  0.1628  170  ASP B OD1   
8555 O  OD2   . ASP B 171 ? 1.9828 1.6725 1.1016 0.3286  0.2310  0.1361  170  ASP B OD2   
8556 N  N     . LEU B 172 ? 1.6227 1.3812 0.9382 0.2828  0.2175  0.1306  171  LEU B N     
8557 C  CA    . LEU B 172 ? 1.5070 1.2775 0.8622 0.2750  0.2202  0.1274  171  LEU B CA    
8558 C  C     . LEU B 172 ? 1.5067 1.2971 0.9088 0.2684  0.2249  0.1402  171  LEU B C     
8559 O  O     . LEU B 172 ? 1.5484 1.3491 0.9813 0.2665  0.2367  0.1448  171  LEU B O     
8560 C  CB    . LEU B 172 ? 1.5281 1.2998 0.8869 0.2646  0.1995  0.1099  171  LEU B CB    
8561 C  CG    . LEU B 172 ? 1.4742 1.2565 0.8702 0.2569  0.2006  0.1054  171  LEU B CG    
8562 C  CD1   . LEU B 172 ? 1.5440 1.3179 0.9339 0.2663  0.2208  0.1080  171  LEU B CD1   
8563 C  CD2   . LEU B 172 ? 1.4096 1.1905 0.8041 0.2468  0.1807  0.0885  171  LEU B CD2   
8564 N  N     . VAL B 173 ? 1.5185 1.3143 0.9263 0.2651  0.2158  0.1461  172  VAL B N     
8565 C  CA    . VAL B 173 ? 1.4996 1.3099 0.9469 0.2595  0.2220  0.1591  172  VAL B CA    
8566 C  C     . VAL B 173 ? 1.5058 1.3133 0.9511 0.2676  0.2461  0.1753  172  VAL B C     
8567 O  O     . VAL B 173 ? 1.5472 1.3680 1.0290 0.2626  0.2571  0.1846  172  VAL B O     
8568 C  CB    . VAL B 173 ? 1.4816 1.2946 0.9310 0.2557  0.2070  0.1614  172  VAL B CB    
8569 C  CG1   . VAL B 173 ? 1.4465 1.2704 0.9335 0.2497  0.2140  0.1747  172  VAL B CG1   
8570 C  CG2   . VAL B 173 ? 1.3905 1.2100 0.8458 0.2473  0.1840  0.1457  172  VAL B CG2   
8571 N  N     . ARG B 174 ? 1.4961 1.2873 0.8989 0.2798  0.2547  0.1789  173  ARG B N     
8572 C  CA    . ARG B 174 ? 1.5395 1.3278 0.9379 0.2881  0.2791  0.1945  173  ARG B CA    
8573 C  C     . ARG B 174 ? 1.5262 1.3207 0.9392 0.2905  0.2945  0.1934  173  ARG B C     
8574 O  O     . ARG B 174 ? 1.5384 1.3437 0.9761 0.2907  0.3128  0.2066  173  ARG B O     
8575 C  CB    . ARG B 174 ? 1.5606 1.3291 0.9065 0.3015  0.2841  0.1979  173  ARG B CB    
8576 C  CG    . ARG B 174 ? 1.5421 1.3054 0.8736 0.3019  0.2731  0.2037  173  ARG B CG    
8577 C  CD    . ARG B 174 ? 1.5234 1.2676 0.8015 0.3161  0.2790  0.2080  173  ARG B CD    
8578 N  NE    . ARG B 174 ? 1.5354 1.2749 0.7985 0.3181  0.2682  0.2142  173  ARG B NE    
8579 C  CZ    . ARG B 174 ? 1.5462 1.2806 0.7818 0.3199  0.2476  0.2037  173  ARG B CZ    
8580 N  NH1   . ARG B 174 ? 1.5884 1.3202 0.8069 0.3187  0.2354  0.1859  173  ARG B NH1   
8581 N  NH2   . ARG B 174 ? 1.5570 1.2889 0.7820 0.3230  0.2392  0.2114  173  ARG B NH2   
8582 N  N     . VAL B 175 ? 1.4984 1.2862 0.8966 0.2924  0.2877  0.1783  174  VAL B N     
8583 C  CA    . VAL B 175 ? 1.5767 1.3687 0.9866 0.2965  0.3019  0.1769  174  VAL B CA    
8584 C  C     . VAL B 175 ? 1.6534 1.4698 1.1190 0.2857  0.3030  0.1812  174  VAL B C     
8585 O  O     . VAL B 175 ? 1.7308 1.5592 1.2182 0.2888  0.3210  0.1903  174  VAL B O     
8586 C  CB    . VAL B 175 ? 1.6295 1.4061 1.0113 0.2995  0.2924  0.1589  174  VAL B CB    
8587 C  CG1   . VAL B 175 ? 1.7311 1.5119 1.1273 0.3043  0.3064  0.1575  174  VAL B CG1   
8588 C  CG2   . VAL B 175 ? 1.6007 1.3530 0.9256 0.3105  0.2931  0.1547  174  VAL B CG2   
8589 N  N     . ILE B 176 ? 1.5564 1.3817 1.0457 0.2729  0.2837  0.1747  175  ILE B N     
8590 C  CA    . ILE B 176 ? 1.6067 1.4546 1.1472 0.2619  0.2825  0.1774  175  ILE B CA    
8591 C  C     . ILE B 176 ? 1.5945 1.4553 1.1612 0.2592  0.2967  0.1950  175  ILE B C     
8592 O  O     . ILE B 176 ? 1.6205 1.5001 1.2242 0.2549  0.3064  0.2014  175  ILE B O     
8593 C  CB    . ILE B 176 ? 1.4789 1.3316 1.0346 0.2496  0.2587  0.1664  175  ILE B CB    
8594 C  CG1   . ILE B 176 ? 1.3949 1.2367 0.9292 0.2505  0.2462  0.1492  175  ILE B CG1   
8595 C  CG2   . ILE B 176 ? 1.3835 1.2587 0.9903 0.2379  0.2570  0.1699  175  ILE B CG2   
8596 C  CD1   . ILE B 176 ? 1.4730 1.3170 1.0129 0.2399  0.2228  0.1381  175  ILE B CD1   
8597 N  N     . ARG B 177 ? 1.5656 1.4163 1.1131 0.2614  0.2982  0.2034  176  ARG B N     
8598 C  CA    . ARG B 177 ? 1.5776 1.4369 1.1474 0.2578  0.3118  0.2205  176  ARG B CA    
8599 C  C     . ARG B 177 ? 1.6377 1.5012 1.2065 0.2665  0.3373  0.2325  176  ARG B C     
8600 O  O     . ARG B 177 ? 1.6186 1.4960 1.2173 0.2610  0.3503  0.2460  176  ARG B O     
8601 C  CB    . ARG B 177 ? 1.4255 1.2699 0.9711 0.2594  0.3071  0.2269  176  ARG B CB    
8602 C  CG    . ARG B 177 ? 1.3051 1.1489 0.8577 0.2506  0.2838  0.2182  176  ARG B CG    
8603 C  CD    . ARG B 177 ? 1.3293 1.1584 0.8569 0.2546  0.2808  0.2261  176  ARG B CD    
8604 N  NE    . ARG B 177 ? 1.3742 1.2035 0.9071 0.2481  0.2588  0.2180  176  ARG B NE    
8605 C  CZ    . ARG B 177 ? 1.4902 1.3086 1.0050 0.2513  0.2521  0.2231  176  ARG B CZ    
8606 N  NH1   . ARG B 177 ? 1.6037 1.4087 1.0923 0.2605  0.2651  0.2365  176  ARG B NH1   
8607 N  NH2   . ARG B 177 ? 1.5036 1.3249 1.0264 0.2460  0.2323  0.2151  176  ARG B NH2   
8608 N  N     . GLN B 178 ? 1.7658 1.6179 1.3012 0.2798  0.3451  0.2277  177  GLN B N     
8609 C  CA    . GLN B 178 ? 1.8808 1.7360 1.4112 0.2903  0.3703  0.2388  177  GLN B CA    
8610 C  C     . GLN B 178 ? 1.8564 1.7192 1.3943 0.2964  0.3765  0.2314  177  GLN B C     
8611 O  O     . GLN B 178 ? 1.9672 1.8310 1.4956 0.3081  0.3973  0.2386  177  GLN B O     
8612 C  CB    . GLN B 178 ? 1.8031 1.6351 1.2810 0.3040  0.3790  0.2429  177  GLN B CB    
8613 C  CG    . GLN B 178 ? 2.0048 1.8252 1.4668 0.3007  0.3709  0.2489  177  GLN B CG    
8614 C  CD    . GLN B 178 ? 2.0833 1.9168 1.5799 0.2917  0.3812  0.2660  177  GLN B CD    
8615 O  OE1   . GLN B 178 ? 2.0962 1.9458 1.6198 0.2906  0.3998  0.2766  177  GLN B OE1   
8616 N  NE2   . GLN B 178 ? 1.9890 1.8154 1.4847 0.2850  0.3693  0.2690  177  GLN B NE2   
8617 N  N     . GLN B 179 ? 1.8146 1.6822 1.3685 0.2897  0.3597  0.2178  178  GLN B N     
8618 C  CA    . GLN B 179 ? 1.9496 1.8226 1.5104 0.2958  0.3646  0.2108  178  GLN B CA    
8619 C  C     . GLN B 179 ? 1.9870 1.8897 1.5959 0.2927  0.3789  0.2224  178  GLN B C     
8620 O  O     . GLN B 179 ? 1.9496 1.8594 1.5628 0.3025  0.3924  0.2235  178  GLN B O     
8621 C  CB    . GLN B 179 ? 2.0166 1.8848 1.5793 0.2887  0.3420  0.1935  178  GLN B CB    
8622 C  CG    . GLN B 179 ? 2.1216 1.9890 1.6838 0.2961  0.3456  0.1849  178  GLN B CG    
8623 C  CD    . GLN B 179 ? 2.2500 2.1453 1.8636 0.2888  0.3458  0.1879  178  GLN B CD    
8624 O  OE1   . GLN B 179 ? 2.2503 2.1647 1.8999 0.2761  0.3402  0.1941  178  GLN B OE1   
8625 N  NE2   . GLN B 179 ? 2.1239 2.0207 1.7399 0.2972  0.3519  0.1835  178  GLN B NE2   
8626 O  OXT   . GLN B 179 ? 2.0665 1.9869 1.7111 0.2803  0.3771  0.2308  178  GLN B OXT   
8627 C  C2    . 5H5 C .   ? 1.2102 1.4935 1.4207 0.0638  0.0142  0.0735  1101 5H5 A C2    
8628 C  C4    . 5H5 C .   ? 1.1457 1.4116 1.3464 0.0538  0.0104  0.0655  1101 5H5 A C4    
8629 C  C6    . 5H5 C .   ? 1.0822 1.3400 1.2835 0.0530  0.0200  0.0691  1101 5H5 A C6    
8630 C  C8    . 5H5 C .   ? 1.0957 1.3397 1.2660 0.0531  -0.0016 0.0532  1101 5H5 A C8    
8631 C  C12   . 5H5 C .   ? 1.0266 1.2284 1.1353 0.0534  -0.0159 0.0347  1101 5H5 A C12   
8632 C  C15   . 5H5 C .   ? 1.0486 1.2865 1.1790 0.0401  -0.0395 0.0265  1101 5H5 A C15   
8633 C  C16   . 5H5 C .   ? 1.0705 1.3292 1.2200 0.0385  -0.0437 0.0294  1101 5H5 A C16   
8634 C  C18   . 5H5 C .   ? 1.0812 1.3269 1.2314 0.0434  -0.0296 0.0354  1101 5H5 A C18   
8635 C  C19   . 5H5 C .   ? 1.0463 1.2907 1.2035 0.0466  -0.0204 0.0412  1101 5H5 A C19   
8636 C  C21   . 5H5 C .   ? 1.1011 1.3659 1.2884 0.0478  -0.0102 0.0525  1101 5H5 A C21   
8637 C  C24   . 5H5 C .   ? 1.1441 1.4291 1.2907 0.0330  -0.0671 0.0217  1101 5H5 A C24   
8638 C  C27   . 5H5 C .   ? 1.0984 1.4075 1.2939 0.0253  -0.0594 0.0300  1101 5H5 A C27   
8639 N  N1    . 5H5 C .   ? 1.1450 1.4144 1.3371 0.0768  0.0214  0.0764  1101 5H5 A N1    
8640 O  O3    . 5H5 C .   ? 1.1899 1.4987 1.4236 0.0609  0.0110  0.0773  1101 5H5 A O3    
8641 O  O7    . 5H5 C .   ? 1.1659 1.4100 1.3417 0.0565  0.0082  0.0594  1101 5H5 A O7    
8642 C  C9    . 5H5 C .   ? 1.0525 1.2763 1.1999 0.0546  -0.0029 0.0476  1101 5H5 A C9    
8643 C  C10   . 5H5 C .   ? 1.0496 1.2733 1.1906 0.0512  -0.0116 0.0418  1101 5H5 A C10   
8644 O  O11   . 5H5 C .   ? 1.0473 1.2523 1.1671 0.0520  -0.0117 0.0370  1101 5H5 A O11   
8645 C  C13   . 5H5 C .   ? 1.0253 1.2344 1.1382 0.0448  -0.0256 0.0279  1101 5H5 A C13   
8646 N  N14   . 5H5 C .   ? 1.0593 1.2894 1.1902 0.0430  -0.0313 0.0300  1101 5H5 A N14   
8647 N  N17   . 5H5 C .   ? 1.0845 1.3491 1.2473 0.0400  -0.0378 0.0349  1101 5H5 A N17   
8648 C  C20   . 5H5 C .   ? 1.0285 1.2930 1.2086 0.0448  -0.0197 0.0464  1101 5H5 A C20   
8649 C  C22   . 5H5 C .   ? 1.1399 1.4136 1.2941 0.0351  -0.0538 0.0267  1101 5H5 A C22   
8650 N  N23   . 5H5 C .   ? 1.1624 1.4304 1.3011 0.0364  -0.0577 0.0236  1101 5H5 A N23   
8651 N  N25   . 5H5 C .   ? 1.0890 1.3905 1.2567 0.0286  -0.0693 0.0233  1101 5H5 A N25   
8652 N  N26   . 5H5 C .   ? 1.0864 1.3803 1.2591 0.0301  -0.0601 0.0269  1101 5H5 A N26   
8653 C  C28   . 5H5 C .   ? 1.0991 1.4019 1.2977 0.0134  -0.0633 0.0216  1101 5H5 A C28   
8654 C  C29   . 5H5 C .   ? 1.2717 1.6087 1.4851 0.0263  -0.0655 0.0349  1101 5H5 A C29   
8655 P  PG    . GNP D .   ? 1.6167 1.3594 0.9058 0.0829  -0.0221 -0.0992 201  GNP B PG    
8656 O  O1G   . GNP D .   ? 1.7596 1.4824 1.0340 0.0658  -0.0286 -0.1148 201  GNP B O1G   
8657 O  O2G   . GNP D .   ? 1.5520 1.3353 0.8760 0.0791  -0.0348 -0.0930 201  GNP B O2G   
8658 O  O3G   . GNP D .   ? 1.5248 1.2552 0.8240 0.0983  -0.0008 -0.0875 201  GNP B O3G   
8659 N  N3B   . GNP D .   ? 1.7363 1.4645 0.9742 0.0911  -0.0259 -0.1038 201  GNP B N3B   
8660 P  PB    . GNP D .   ? 1.4322 1.1689 0.6626 0.1110  -0.0184 -0.0896 201  GNP B PB    
8661 O  O1B   . GNP D .   ? 1.6727 1.3783 0.8737 0.1262  0.0009  -0.0861 201  GNP B O1B   
8662 O  O2B   . GNP D .   ? 1.4481 1.2189 0.7220 0.1145  -0.0200 -0.0762 201  GNP B O2B   
8663 O  O3A   . GNP D .   ? 1.7024 1.4441 0.8978 0.1061  -0.0374 -0.0993 201  GNP B O3A   
8664 P  PA    . GNP D .   ? 1.6480 1.4287 0.8605 0.1009  -0.0577 -0.0976 201  GNP B PA    
8665 O  O1A   . GNP D .   ? 1.5592 1.3554 0.7804 0.1180  -0.0521 -0.0813 201  GNP B O1A   
8666 O  O2A   . GNP D .   ? 1.7357 1.5379 0.9816 0.0830  -0.0703 -0.1039 201  GNP B O2A   
8667 O  "O5'" . GNP D .   ? 1.7887 1.5547 0.9492 0.0975  -0.0699 -0.1109 201  GNP B "O5'" 
8668 C  "C5'" . GNP D .   ? 1.8337 1.5822 0.9731 0.0809  -0.0785 -0.1284 201  GNP B "C5'" 
8669 C  "C4'" . GNP D .   ? 1.8058 1.5556 0.9066 0.0771  -0.0952 -0.1384 201  GNP B "C4'" 
8670 O  "O4'" . GNP D .   ? 1.8195 1.5491 0.8824 0.0950  -0.0853 -0.1335 201  GNP B "O4'" 
8671 C  "C3'" . GNP D .   ? 1.8146 1.6080 0.9358 0.0735  -0.1151 -0.1353 201  GNP B "C3'" 
8672 O  "O3'" . GNP D .   ? 1.9548 1.7509 1.0515 0.0579  -0.1344 -0.1513 201  GNP B "O3'" 
8673 C  "C2'" . GNP D .   ? 1.7273 1.5246 0.8340 0.0952  -0.1091 -0.1216 201  GNP B "C2'" 
8674 O  "O2'" . GNP D .   ? 1.6389 1.4661 0.7421 0.0954  -0.1279 -0.1211 201  GNP B "O2'" 
8675 C  "C1'" . GNP D .   ? 1.8259 1.5808 0.8825 0.1023  -0.0973 -0.1277 201  GNP B "C1'" 
8676 N  N9    . GNP D .   ? 1.8529 1.5979 0.8953 0.1243  -0.0814 -0.1134 201  GNP B N9    
8677 C  C8    . GNP D .   ? 1.7607 1.5041 0.8288 0.1371  -0.0617 -0.0979 201  GNP B C8    
8678 N  N7    . GNP D .   ? 1.7654 1.4996 0.8118 0.1551  -0.0504 -0.0872 201  GNP B N7    
8679 C  C5    . GNP D .   ? 1.8465 1.5755 0.8494 0.1552  -0.0632 -0.0959 201  GNP B C5    
8680 C  C6    . GNP D .   ? 1.8047 1.5229 0.7670 0.1713  -0.0592 -0.0903 201  GNP B C6    
8681 O  O6    . GNP D .   ? 1.7163 1.4271 0.6738 0.1885  -0.0423 -0.0758 201  GNP B O6    
8682 N  N1    . GNP D .   ? 1.9130 1.6300 0.8369 0.1644  -0.0782 -0.1041 201  GNP B N1    
8683 C  C2    . GNP D .   ? 1.9211 1.6469 0.8468 0.1440  -0.0980 -0.1207 201  GNP B C2    
8684 N  N2    . GNP D .   ? 1.8923 1.6169 0.7780 0.1393  -0.1152 -0.1326 201  GNP B N2    
8685 N  N3    . GNP D .   ? 1.8420 1.5775 0.8061 0.1289  -0.1007 -0.1253 201  GNP B N3    
8686 C  C4    . GNP D .   ? 1.8429 1.5792 0.8432 0.1359  -0.0831 -0.1125 201  GNP B C4    
8687 MG MG    . MG  E .   ? 1.3055 1.1112 0.6571 0.1046  -0.0199 -0.0674 202  MG  B MG    
8688 O  O     . HOH F .   ? 1.4333 1.3815 1.4061 0.0914  -0.0404 -0.1122 1201 HOH A O     
8689 O  O     . HOH F .   ? 1.2754 1.1982 1.3136 0.0447  0.0255  0.0486  1202 HOH A O     
8690 O  O     . HOH F .   ? 0.6580 0.8703 0.6775 0.0000  -0.0448 -0.0441 1203 HOH A O     
8691 O  O     . HOH F .   ? 0.8392 1.0436 0.8584 0.0037  -0.0477 -0.0412 1204 HOH A O     
8692 O  O     . HOH F .   ? 1.0595 1.2433 1.0961 0.0119  -0.0492 -0.0277 1205 HOH A O     
8693 O  O     . HOH F .   ? 1.2391 1.4537 1.2774 0.0474  -0.0551 -0.0439 1206 HOH A O     
8694 O  O     . HOH F .   ? 1.1151 1.1601 1.0463 0.2648  0.2195  0.1265  1207 HOH A O     
8695 O  O     . HOH F .   ? 1.3163 1.8950 0.8438 0.1313  0.3155  -0.0214 1208 HOH A O     
8696 O  O     . HOH F .   ? 1.3015 1.5070 0.9197 -0.0371 0.1267  0.0891  1209 HOH A O     
8697 O  O     . HOH F .   ? 1.0293 1.0225 0.9703 0.1116  0.0155  0.0646  1210 HOH A O     
8698 O  O     . HOH F .   ? 1.1807 1.1977 1.1088 0.1500  0.1050  0.0650  1211 HOH A O     
8699 O  O     . HOH F .   ? 1.1190 1.4572 1.0698 -0.0176 -0.1258 -0.0681 1212 HOH A O     
8700 O  O     . HOH F .   ? 1.0033 1.3263 0.7041 0.1012  0.0442  -0.1325 1213 HOH A O     
8701 O  O     . HOH F .   ? 1.2873 1.2434 1.2797 0.0738  -0.0426 -0.0988 1214 HOH A O     
8702 O  O     . HOH F .   ? 0.9560 1.3361 0.9727 -0.1049 -0.0977 -0.0806 1215 HOH A O     
8703 O  O     . HOH F .   ? 1.4932 1.8168 0.7104 0.1795  0.1615  -0.0919 1216 HOH A O     
8704 O  O     . HOH F .   ? 0.9944 1.1053 0.9618 0.0307  -0.0285 -0.0172 1217 HOH A O     
8705 O  O     . HOH F .   ? 1.0615 1.7244 1.5063 0.2744  0.0906  0.2235  1218 HOH A O     
8706 O  O     . HOH F .   ? 1.0223 1.3745 1.2706 0.0512  -0.0267 0.0666  1219 HOH A O     
8707 O  O     . HOH F .   ? 1.0628 1.2453 1.0965 0.0775  -0.0531 -0.0358 1220 HOH A O     
8708 O  O     . HOH F .   ? 0.9070 1.0369 0.9568 0.0375  -0.0139 0.0071  1221 HOH A O     
8709 O  O     . HOH F .   ? 1.0500 1.7194 1.4791 0.3522  0.1209  0.2520  1222 HOH A O     
8710 O  O     . HOH F .   ? 0.8833 1.5359 1.3831 0.1259  0.0619  0.1802  1223 HOH A O     
8711 O  O     . HOH G .   ? 1.1398 1.0898 0.8462 0.1333  0.0442  0.0413  301  HOH B O     
8712 O  O     . HOH G .   ? 1.6072 1.3498 0.8518 0.3197  0.2034  0.2213  302  HOH B O     
8713 O  O     . HOH G .   ? 1.5758 1.3088 0.7376 0.3229  0.1788  0.1727  303  HOH B O     
8714 O  O     . HOH G .   ? 1.9823 1.5663 1.0756 -0.0549 -0.0936 -0.2253 304  HOH B O     
# 
